Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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A0A009IHW8 | ABTIR_ACIB9 | MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQKKKIDIDNKLLKEKQNLIKEEILERKKLEVLTKKQQKDEIEHQKKLKREIDAIKASTQYITDVSISSYNNTIPETEPEYDLFISHASEDKEDFVRPLAETLQQLGVNVWYDEFTLKVGDSLRQKIDSGLRNSKYGTVVLSTDFIKKDWTNYELDGLVAREMNGHKMILPIWHKITKNDVLDYSPNLADKVALNTSVNSIEEIAHQLADVILNR | 3.2.2.-; 3.2.2.6 | null | NAD catabolic process [GO:0019677]; signal transduction [GO:0007165] | null | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135] | PF13676; | 3.40.50.10140; | null | null | null | CATALYTIC ACTIVITY: Reaction=NAD(+) = 2'cADPR + H(+) + nicotinamide; Xref=Rhea:RHEA:75299, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:194248; Evidence={ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75300; Evidence={ECO:0000269|PubMed:36048923}; CATALYTIC AC... | null | null | null | null | FUNCTION: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922). In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed 2'cADPR (v-cADPR) (PubMed:29395922, PubMed:36048923). Cleaves NADP(+), but does not cyclize the prod... | Acinetobacter baumannii (strain 1295743) |
A0A023I7E1 | ENG1_RHIMI | MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEA... | 3.2.1.39 | null | cell wall organization [GO:0071555]; polysaccharide catabolic process [GO:0000272] | cell surface [GO:0009986]; extracellular region [GO:0005576] | glucan endo-1,3-beta-D-glucosidase activity [GO:0042973]; glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group [GO:0052861]; glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group [GO:0052862] | PF17652;PF03639; | 1.10.287.1170;1.20.5.420; | Glycosyl hydrolase 81 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250|UniProtKB:P53753}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:34801773}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:34801773}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:34801773}; | FUNCTION: Cleaves internal linkages in 1,3-beta-glucan. {ECO:0000269|PubMed:34801773}. | Rhizomucor miehei |
A0A024B7W1 | POLG_ZIKVF | MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGC... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; negative regulation of innate immune response [GO:0045824]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT ca... | centrosome [GO:0005813]; extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | 4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; mRNA (nucleoside-2'-O-)-methyltransferas... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000269|PubMed:36594413}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}... | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:C... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface ... | Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV) |
A0A024SC78 | CUTI1_HYPJR | MRSLAILTTLLAGHAFAYPKPAPQSVNRRDWPSINEFLSELAKVMPIGDTITAACDLISDGEDAAASLFGISETENDPCGDVTVLFARGTCDPGNVGVLVGPWFFDSLQTALGSRTLGVKGVPYPASVQDFLSGSVQNGINMANQIKSVLQSCPNTKLVLGGYSQGSMVVHNAASNLDAATMSKISAVVLFGDPYYGKPVANFDAAKTLVVCHDGDNICQGGDIILLPHLTYAEDADTAAAFVVPLVS | 3.1.1.74 | null | null | extracellular region [GO:0005576] | cutinase activity [GO:0050525] | PF01083; | 3.40.50.1820; | Cutinase family | PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}. | SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361263}. | CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:25219509}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-7. {ECO:0000269|PubMed:25219509}; | null | FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:25219509). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:25219509). {ECO:0000269|PubMed:25219509}. | Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei) |
A0A024SH76 | GUX2_HYPJR | MIVGILTTLATLATLAASVPLEERQACSSVWGQCGGQNWSGPTCCASGSTCVYSNDYYSQCLPGAASSSSSTRAASTTSRVSPTTSRSSSATPPPGSTTTRVPPVGSGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRAL... | 3.2.1.91 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulose 1,4-beta-cellobiosidase activity [GO:0016162]; cellulose binding [GO:0030248] | PF00734;PF01341; | 3.20.20.40; | Glycosyl hydrolase 6 (cellulase B) family | PTM: Asn-334 contains mainly a high-mannose-type glycan (Hex(7-9)GlcNAc(2)) in a 3:1 ration with a single GlcNAc. Asn-313 was primarily unglycosylated with a small fraction (18%) bearing a single GlcNAc at this site. {ECO:0000269|PubMed:12499406}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07987}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000250|UniProtKB:P07987}; | null | null | null | null | FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-gluc... | Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei) |
A0A026W182 | ORCO_OOCBI | MMKMKQQGLVADLLPNIRVMKTFGHFVFNYYNDNSSKYLHKVYCCVNLFMLLLQFGLCAVNLIVESADVDDLTANTITLLFFTHSIVKICYFAIRSKYFYRTWAIWNNPNSHPLFAESNARYHAIALKKMRLLLFLVGGTTMLAAVAWTVLTFFEHPIRKIVDPVTNETEIIELPQLLIRSFYPFDAGKGITHVLVLVYQFYWVLFMLIDANSLDVLFCSWLLFACEQLQHLKQIMKPLMELSATLDTVVPNSSELFKAGSADHLRDGDNPPPPPPPQSDNMLDLDLRNIYSNRQDFTATFRPTAGMTFNGGVGPNGLTK... | null | null | antennal development [GO:0007469]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; detection of pheromone [GO:0043695]; olfactory behavior [GO:0042048]; response to pheromone [GO:0019236]; signal transduction [GO:0007165]; social behavior [GO:0035176] | plasma membrane [GO:0005886] | odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984] | PF02949; | null | Insect chemoreceptor superfamily, Heteromeric odorant receptor channel (TC 1.A.69) family, Orco subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the f... | Ooceraea biroi (Clonal raider ant) (Cerapachys biroi) |
A0A044RE18 | BLI_ONCVO | MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAF... | 3.4.21.75 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12855702}; Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958}; | dibasic protein processing [GO:0090472]; zymogen activation [GO:0031638] | extracellular region [GO:0005576]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252] | PF01483;PF00082;PF16470; | 2.60.120.260;3.30.70.850;3.40.50.200; | Peptidase S8 family, Furin subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:12855702}.; PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is probably autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound as a potent autoinhibitor. Probably following transport to the trans Golgi, a se... | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12855702}. | CATALYTIC ACTIVITY: Reaction=Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.; EC=3.4.21.75; Evidence={ECO:0000269|P... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Active from pH 7.0 to 8.5. {ECO:0000269|PubMed:12855702}; | null | FUNCTION: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. {ECO:0000269|PubMed:12855702}. | Onchocerca volvulus |
A0A059TC02 | CCR1_PETHY | MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPI... | 1.2.1.44 | null | circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699] | cytoplasm [GO:0005737] | cinnamoyl-CoA reductase activity [GO:0016621]; nucleotide binding [GO:0000166]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF01370; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily | PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000269|PubMed:25217505}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24985707}. | CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; Ph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=208.6 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:25217505}; KM=307.6 uM for feruloyl-CoA {ECO:0000269|PubMed:25217505}; KM=270.3 uM for sinapoyl-CoA {ECO:0000269|PubMed:25217505}; Vmax=1235.7 nmol/sec/mg enzyme with p-coumaroyl-CoA as substrate {ECO:0000269|PubMed:... | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:25217505}; | null | FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:24985707, PubMed:25217505). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed... | Petunia hybrida (Petunia) |
A0A060A682 | HAP2_TETTH | MKFLAFGLIYFHFCILNRCEYITSSTIQKCYNSSNEPNNCSQKAVIVLSLENGQIANTEQVVATLNQLSDSGVNKQLQNSFIFEVTKSPVTALFPLIYLQDFNSQPLEQVIATTLFSCKDGFYDSSPTCKFQYDSKGQKILDSQGYCCYCSLSDILGMGNDLSRGKVCYALNLGAGSATAHCLKFSPLWYSAFKIQQYQLYFEVNINIYTVDSQNQKNLKQTLKLSTSNPTMKSSDNSTISKIIGTFTPTQPPADLSSYYLVKPSFPATDPRVLQGISSWMFVDKTMFTLDGTQCNKIGVSYSGFRQQSSSCSQPVGSCL... | null | null | fertilization [GO:0009566]; plasma membrane fusion [GO:0045026]; single fertilization [GO:0007338] | cell-cell junction [GO:0005911]; plasma membrane [GO:0005886] | fusogenic activity [GO:0140522]; lipid binding [GO:0008289] | PF10699; | null | HAP2/GCS1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25155508, ECO:0000305|PubMed:28238660}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}. Note=Detected at the mating junction. {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}. | null | null | null | null | null | FUNCTION: During fertilization, required for the formation of intercellular membrane pores and subsequent exchange of gametic pronuclei between cells. Probably initiates the formation of intercellular membrane pores by inserting part of its extracellular domain into the cell membrane of the adjoining cell in the mating... | Tetrahymena thermophila |
A0A061ACU2 | PIEZ1_CAEEL | MTVPPLLKSCVVKLLLPAALLAAAIIRPSFLSIGYVLLALVSAVLPPIRKSLALPKLVGTFVIITFLFCLAVALGVGSYQISEQVVHKNDRTYICNRSDTTLFRSIGLVRFHPTGTFESTRAFLPEIIATSAALLTIIIVMFLSHRDEQLDVVGDVVTVRSESGREQRRQRKLAAIMWSAIGNSLRRLTNFVLFLFTAYVGIVKPSLSNSIYFLAFLFISTWWSTYTPLRHGVYNQIKKFLIFYSALHFLVLYTYQIPIVHHSWLPTGSFLPRLFGLTVLMDSSCPEWWKFPFVAPDFNDDDLIMKWPLYANPIVVLVFF... | null | null | cellular response to mechanical stimulus [GO:0071260]; detection of mechanical stimulus [GO:0050982]; flagellated sperm motility [GO:0030317]; monoatomic cation transmembrane transport [GO:0098655]; positive regulation of brood size [GO:0090727]; positive regulation of ovulation [GO:0060279]; regulation of membrane pot... | plasma membrane [GO:0005886] | mechanosensitive monoatomic ion channel activity [GO:0008381]; monoatomic cation channel activity [GO:0005261] | PF15917;PF12166; | null | PIEZO (TC 1.A.75) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32490809}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Pore-forming subunit of a mechanosensitive non-specific cation channel (By similarity). Generates currents characterized by a linear current-voltage relationship (By similarity). Plays a role in reproduction by positively regulating inter-tissue signaling to promote oocyte maturation, ovulation and fertilizat... | Caenorhabditis elegans |
A0A061AE05 | PAPSH_CAEEL | MLTPRDENNEGDAMPMLKKPRYSSLSGQSTNITYQEHTISREERAAAVGRHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENVKFIEVHVSTTLEVCEQRDPKPSELYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLPEQIPDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDLKHKVAFVGEKSD... | 2.7.1.25; 2.7.7.4 | null | 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103] | nucleus [GO:0005634] | adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; sulfate adenylyltransferase (ATP) activity [GO:0004781] | PF01583;PF01747;PF14306; | 3.40.50.620;3.40.50.300;3.10.400.10; | APS kinase family; Sulfate adenylyltransferase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16497669}. | CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|PubMed:16497669}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate... | null | PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000303|PubMed:16497669}. | null | null | FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway (PubMed:16497669). The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group fro... | Caenorhabditis elegans |
A0A061I403 | FICD_CRIGR | MPMASVIAVAEPKWISVWGRFLWLTLLSMALGSLLALLLPLGAVEEQCLAVLRSFHLLRSKLDRTQHVVTKCTSPSTELSVTSGDVGLLTVKTKTSPAGKLEAKAALNQALEMKRQGKREKAHKLFLHALKMDPGFVDALNEFGIFSEEEKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTIDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPH... | 2.7.7.108; 3.1.4.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+). {ECO:0000250|UniProtKB:Q9BVA6}; | protein adenylylation [GO:0018117]; protein deadenylylation [GO:0044602]; regulation of IRE1-mediated unfolded protein response [GO:1903894]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986] | endoplasmic reticulum membrane [GO:0005789] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087] | PF02661; | 1.10.3290.10;1.25.40.10; | Fic family | PTM: Auto-AMPylated in vitro. {ECO:0000250|UniProtKB:Q9BVA6}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV... | null | null | null | null | FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (PubMed:27918543). The side chain of Glu-231 determines which of the two ... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
A0A067CMC7 | HTP3_SAPPC | MLEVPVWIPILAFAVGLGLGLLIPHLQKPFQRFSTVNDIPKEFFEHERTLRGKVVSVTDGDTIRVRHVPWLANGDGDFKGKLTETTLQLRVAGVDCPETAKFGRTGQPFGEEAKAWLKGELQDQVVSFKLLMKDQYSRAVCLVYYGSWAAPMNVSEELLRHGYANIYRQSGAVYGGLLETFEALEAEAREKRVNIWSLDKRETPAQYKARK | 3.1.31.- | null | null | extracellular space [GO:0005615]; host cell cytosol [GO:0044164] | endonuclease activity [GO:0004519]; metal ion binding [GO:0046872] | PF00565; | 2.40.50.90; | RxLR effector family; LCL3 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29904064}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:29904064}. Note=Uptake into host cells is more efficient at a lower pH of 5.5. S.parasitica acidifies the pH of its environment, which likely leads to the exposure of a gp96 protein to the host cell surface. T... | null | null | null | null | null | FUNCTION: Effector involved in the disease saprolegniosis in salmonids and other freshwater fish, resulting in considerable economic losses in aquaculture (PubMed:29904064). Within the host fish cells, Htp3 is released from vesicles into host cytosol where it degrades nucleic acids (PubMed:29904064). {ECO:0000269|PubMe... | Saprolegnia parasitica (strain CBS 223.65) |
A0A067XGX8 | AROG2_PETHY | MALTATATTRGGSALPNSCLQTPKFQSLQKPTFISSFPTNKKTKPRTKHISAVQSPPSTTKWNLESWKTKPAFQLPDYPDKVELESVLKTLSTYPPIVFAGEARNLEEKLGEAALGNAFLLQGGDCAESFKEFSANNIRDTFRVMLQMGVVLMFGGQMPVIKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNVNGDAFDEKSRIPDPHRMVRAYTQSVATLNLLRAFASGGYAAMQRVNQWNLDFTDQSEQGDRYRELAHRVDEAMGFMTAAGLTVDHTIMTTTDFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMI... | 2.5.1.54 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512}; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423] | chloroplast [GO:0009507] | 3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; metal ion binding [GO:0046872] | PF01474; | 3.20.20.70; | Class-II DAHP synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}. | CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}. | null | null | FUNCTION: Involved in the production of volatile organic compounds (VOCs) (PubMed:24815009). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). {ECO:000... | Petunia hybrida (Petunia) |
A0A067XH53 | AROG1_PETHY | MALSTNSTTSSLLPKTPLVQQPLLKNASLPTTTKAIRFIQPISAIHSSDSSKNTPIVSAKPSSPPAATSTAAATAVTKQEWSIDSWKTKKALQLPEYPNQEELKNVLKTIEDFPPIVFAGEARHLEEKLGEAAMGRAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVIKVGRMAGQFAKPRSDNFEEKNGVKLPSYRGDNVNGDAFDLKSRTPDPQRLIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELANRVDEALGFMNAAGLTTDHPIMTTTEFWTSHECLLLPYEQS... | 2.5.1.54 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512}; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; green leaf volatile biosynthetic process [GO:0010597] | chloroplast [GO:0009507] | 3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; metal ion binding [GO:0046872] | PF01474; | 3.20.20.70; | Class-II DAHP synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}. | CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}. | null | null | FUNCTION: Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:24815009). Catalyz... | Petunia hybrida (Petunia) |
A0A067XR63 | XTH7_DIOKA | MNAEGGNLHREFEITWGDGRARIHNNGGLLTLSLDRASGSGFRSKNEYLFGRIEIQIKLVAGNSAGTVATYYLSSEGPTHDEIDFEFLGNSSGEPYTLHTNVFSQGKGNREQQFFLWFDPTMDFHTYTILWNPQRIIFYVDETPIREFKNLERHGIPFPRSQAMRVYSSMWNADDWATRGGLVKTDWTKAPFTASYRSYKADACVWSGEASSCGSQDSNPSDKWWMTEELNATRMKRLRWVQKKYMVYNYCVDKMRFPEGLAPECNIS | 2.4.1.207 | null | cell wall assembly [GO:0070726]; fruit ripening [GO:0009835]; xyloglucan metabolic process [GO:0010411] | apoplast [GO:0048046]; cytoplasm [GO:0005737] | hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; xyloglucan:xyloglucosyl transferase activity [GO:0016762] | PF00722;PF06955; | 2.60.120.200; | Glycosyl hydrolase 16 family, XTH group 2 subfamily | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27242828}. Note=Dispersed throughout the cell. {ECO:0000269|PubMed:27242828}. | CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5-6. Activity decreases sharply when the pH is lowered from 5 to 4. {ECO:0000269|PubMed:27242828}; | null | FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall assembly and synthesis in fast growing tissues and in the maintenance of firmness in mature fruits. {ECO:0000269|PubMed:27242828}. | Diospyros kaki (Kaki persimmon) (Diospyros chinensis) |
A0A067XRK9 | XTH6_DIOKA | MASSLTLPMAMAFTLLALSFASAMGGSMNSSRFDELFQPSWAFDHFVYEGEVLKMKLDNYSGAGFSSKGKYLFGKVTVQIKLVEGDSAGTVTAFYMSSDGTNHNEFDFEFLGNTTGEPYLVQTNVYVNGVGNREQRLNLWFDPTKDFHSYSLLWNQRQVVFMVDETPIRVHSNLEHRGIPFPKDQPMGVYSSIWNADDWATQGGRIKTDWSHAPFVASYQGFAIDACECPAAVAATDNARRCSSSAEKQFWWDMPTLSELSLHQSHQLIWVRANHLVYDYCTDTARFPVTPAECEHHRH | 2.4.1.207 | null | cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; fruit ripening [GO:0009835]; xyloglucan metabolic process [GO:0010411] | apoplast [GO:0048046] | hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; xyloglucan:xyloglucosyl transferase activity [GO:0016762] | PF00722;PF06955; | 2.60.120.200; | Glycosyl hydrolase 16 family, XTH group 1 subfamily | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27242828}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}. | CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6. Highly active between pH range 4.5-6.5. {ECO:0000269|PubMed:27242828}; | null | FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall restructuring during postharvest fruit softening. {ECO:0000269|PubMed:27242828}. | Diospyros kaki (Kaki persimmon) (Diospyros chinensis) |
A0A067YMX8 | XTH8_DIOKA | MAASPYSIFAVQLLLLASWMLSSSSSNFNQDFNIAWGGGRARILNNGELVTLSLDKASGSGFRSKNLYLFGKIDMQLKLVPGNSAGTVTTYYLSSEGSVRDEIDFEFLGNLTGEPYTLHTNVYSHGKGEREQQFRLWFDPAADFHTYSILWNSKTIVFYVDQTPVREFKNMESIGVPYLRQPMRLFSSIWNADEWATRGGLIKTDWTQAPFTTSYRNFRADNACVWAAKASSCGLAAGGNAWLSVELDAKSRGRLRWVRRNQMIYDYCVDGKRFPRGVPPECKLNLHI | 2.4.1.207 | null | cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; cellular response to gibberellin stimulus [GO:0071370]; fruit ripening [GO:0009835]; response to abscisic acid [GO:0009737]; xyloglucan catabolic process [GO:2000899] | apoplast [GO:0048046] | hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; polysaccharide binding [GO:0030247]; xyloglucan:xyloglucosyl transferase activity [GO:0016762] | PF00722;PF06955; | 2.60.120.200; | Glycosyl hydrolase 16 family, XTH group 2 subfamily | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27966647}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}. | CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6. Activity decreases sharply when the pH is lowered from 5 to 4. {ECO:0000269|PubMed:27966647}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 30-40 degrees Celsius. {ECO:0000269|PubMed:27966647}; | FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Overexpression in Arabidopsis transgenic plants causes accelerated dark-induced leaf senescence and higher lipid peroxidation of the leaf cells. Overexpression in tr... | Diospyros kaki (Kaki persimmon) (Diospyros chinensis) |
A0A068B6Q6 | CA18_CONBE | PDGRNAAAKAFDLITPTVRKGCCSNPACILNNPNQCG | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | PF07365; | null | Conotoxin A superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin inhibits mammalian alpha-3-beta-2/CHRNA3-CHRNB2 nAChR (IC(50)=9.4 nM (rat), IC(50)=8.8 nM (human)), as well as the subunit chimera alpha-6/alpha-3-beta-2-beta-3 nAChR (CHRNA6/CHRNA3-CHRNB2-CHRNB3)(IC(50)=2.1 nM... | Conus betulinus (Beech cone) |
A0A068J840 | UGT1_PANGI | MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVLIAKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAIFPSVIETQKTHVRDIISGMTQSESTQVVGLLADLLFINIMDIANEFNVPTYVYSPAGAGHLGLAFHLQTLNDKKQDVTEFRNSDTELLVPSFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGSFQENQVKEIAMGLERSGHRFLWSLRPSIPKGETKLQLKY... | 2.4.1.363 | null | terpenoid biosynthetic process [GO:0016114] | null | UDP-glycosyltransferase activity [GO:0008194] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-ginsenoside C-K + H(+) + UDP; Xref=Rhea:RHEA:57976, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75950, ChEBI:CHEBI:77146; EC=2.4.1.363; Evidence={ECO:0000269|PubMed:24603359, ECO:0000269|PubMed:26032089}; Physiolog... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=359 uM for protopanaxadiol {ECO:0000269|PubMed:24603359}; KM=178 uM for dammarenediol II {ECO:0000269|PubMed:24603359}; Vmax=254 nmol/min/mg enzyme with protopanaxadiol as substrate {ECO:0000269|PubMed:24603359}; Vmax=423 nmol/min/mg enzyme with dammarenediol II as... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Component of the dammarane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway (PubMed:26032089, PubMed:29378087). Glycosyltransferase that catalyzes the biosynthesis of ginsenoside F1 from protopanaxatriol (PPT) (PubMed:26032089). Triggers C20-OH glycosylation of ginsenoside Rg3 ... | Panax ginseng (Korean ginseng) |
A0A068Q5Q5 | DEPOL_BPKNT | MALIRLVAPERVFSDLASMVAYPNFQVQDKITLLGSAGGDFTFTTTASVVDNGTVFAVPGGYLLRKFVGPAYSSWFSNWTGIVTFMSAPNRHLVVDTVLQATSVLNIKSNSTLEFTDTGRILPDAAVARQVLNITGSAPSVFVPLAADAAAGSKVITVAAGALSAVKGTYLYLRSNKLCDGGPNTYGVKISQIRKVVGVSTSGGVTSIRLDKALHYNYYLSDAAEVGIPTMVENVTLVSPYINEFGYDDLNRFFTSGISANFAADLHIQDGVIIGNKRPGASDIEGRSAIKFNNCVDSTVKGTCFYNIGWYGVEVLGCSE... | 4.-.-.- | null | adhesion receptor-mediated virion attachment to host cell [GO:0098671]; symbiont entry into host cell via disruption of host cell envelope [GO:0098994]; symbiont entry into host cell via disruption of host cell glycocalyx [GO:0098996] | virus tail [GO:0098015] | lyase activity [GO:0016829] | null | 2.160.20.10; | K1-specific depolymerase family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Tail appendage. {ECO:0000305}. | null | null | null | null | null | FUNCTION: Functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (PubMed:35130876). Displays a lyase activity that specifically degrades the K1-type polysaccharides of Klebsiella pneumoniae capsule (PubMed:25001459, PubMed:35130876). {ECO:0000269|PubMed:2500145... | Klebsiella phage NTUH-K2044-K1-1 (Bacteriophage NTUH-K2044-K1-1) |
A0A072ULZ1 | GLB12_MEDTR | MEENKKTVDGSVDFTEEQEALVVKSWNAMKNNSCDLSLKFFTKILEIAPPAKQMFSFLKDSNVPLEQNPKLKPHAMSVFLMTCESAVQLRKAGKVRVRESNLKKLGATHFKTGVQDEHFEVTKQALLETIEEAIPEMWSLAMKNAWAEAHDQLANAIKVEMKEAHDQMDNANLIINMEENTGSCFTEEQEALVVKSWNAIKYNSGDLSLKFFKKILEIAPPAKQLFSFLKDSNVPLEHNPKLKPHAMSVFLMTCESAVQLRKAGKVTVRESNLKKLGATHFKTGVKDEHFEVTKQALLETIKEALPEMWSPAMENAWGEA... | 1.7.2.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:33329665}; Note=Binds 2 heme groups per subunit. {ECO:0000269|PubMed:33329665}; | response to ammonium ion [GO:0060359]; response to hypoxia [GO:0001666]; response to nitrate [GO:0010167]; response to nitric oxide [GO:0071731]; response to symbiotic bacterium [GO:0009609] | null | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825] | PF00042; | 1.10.490.10; | Plant globin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:00002... | null | null | null | null | FUNCTION: Phytoglobin that regulates the fine tuning of nitric oxide (NO) concentration in the cytosol in response to sudden changes in O(2) availability, and performs both symbiotic and nonsymbiotic functions (PubMed:33329665). Exhibits NO dioxygenase activity in the presence of O(2) but nitrite reductase (NiR) activi... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A0A072UR65 | CHT5B_MEDTR | MANILNLKHLLTLALILLALATKSSTSSSSSITRVKGIYWLENPFFPPTTVDTSLFTHIFYSFLTPNNITYKLEISSSQILSLNTFTKTFKTKSPPAATLFSIGGAGSNSSLLAFIASDPPACAAFINSTIDVARTFGFDGIDLDWEFPKNTKEMNDLGEMLFQWRKAISDEGATTGRPPLLLTAAVYFAVNFSIYGEPRMYPVNSINENLDWVNVMSYELRGPRSNKTGAPSGTFDPKSNVSVVSGLLSWIHSGVVPEKLVMGMPLYGKSWKLRDPNVHGIGAPSVGSGPGVNGLMAYFQVLDFNRQKSAKVEYDVDTA... | 3.2.1.14 | null | chitin catabolic process [GO:0006032]; defense response to fungus [GO:0050832]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576] | chitin binding [GO:0008061]; chitinase activity [GO:0004568] | PF00704; | 3.10.50.10;3.20.20.80; | Glycosyl hydrolase 18 family, Chitinase class V subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000269|PubMed:27383628}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.5 mM for (GlcNAc)6 {ECO:0000269|PubMed:27383628}; KM=8.6 mM for (GlcNAc)5 {ECO:0000269|PubMed:27383628}; | PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305}. | null | null | FUNCTION: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5 (PubMed:27383628). Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules (PubMed:27383628). Has the capacity... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A0A072VDF2 | CCR1_MEDTR | MPAATAAAAAESSSVSGETICVTGAGGFIASWMVKLLLEKGYTVRGTLRNPDDPKNGHLKKLEGAKERLTLVKVDLLDLNSVKEAVNGCHGVFHTASPVTDNPEEMVEPAVNGAKNVIIAGAEAKVRRVVFTSSIGAVYMDPNRSVDVEVDESCWSDLEFCKKTKNWYCYGKAVAEAAAWDVAKEKGVDLVVVNPVLVLGPLLQPTINASTIHILKYLTGSAKTYANATQAYVHVRDVALAHILVYEKPSASGRYLCAETSLHRGELVEILAKYFPEYPIPTKCSDEKNPRVKPHIFSNKKLKDLGLEFTPVSECLYETV... | 1.2.1.-; 1.2.1.44 | null | lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699] | cytoplasm [GO:0005737] | cinnamoyl-CoA reductase activity [GO:0016621]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF01370; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily | PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000250|UniProtKB:A0A059TC02}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}. | CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=54.5 uM for feruloyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=7.2 uM for sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=161 uM for caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|Pub... | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000250|UniProtKB:A0A059TC02}. | null | null | FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:20876124). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:20876124). Mediates the conversion of feruloyl-CoA to coniferylaldehyde (PubMed:20876124). Also ... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A0A075BSX9 | HLNO_SHIS7 | MTEKIYDAIVVGAGFSGLVAARELSAQGRSVLIIEARHRLGGRTHVVNFLGRPVEIGGAGVHWCQPHVFAEMQRYGFGFKEAPLADLDKAYMVFADGQKIDVPPATFDEEYTTAFEKFCSRSRELFPRPYSPLDNHEVSNLDGVSARDHLESLGLNELQLASMNAELTLYGGAPTTELSYPSFVKFHALASWDTITFTDSEKRYHVQGGTNALCQAIFDDCRADSEFGVPVEAVAQTDNGVTVTLADKRVFRALTCVLTLPTKVYADVRFEPPLPPEKRAFIEHAEMADGAELYVHVRQNLGNTFTFCDDPNPFNAVQTY... | 1.5.3.5 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:25002425}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:25002425}; | alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608] | null | (S)-6-hydroxynicotine oxidase activity [GO:0018531]; nucleotide binding [GO:0000166] | PF01593; | 3.50.50.60; | Flavin monoamine oxidase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-6-hydroxynicotine + H2O + O2 = 6-hydroxypseudooxynicotine + H2O2; Xref=Rhea:RHEA:11880, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58182, ChEBI:CHEBI:58682; EC=1.5.3.5; Evidence={ECO:0000269|PubMed:25002425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.019 mM for (S)-6-hydroxynicotine {ECO:0000269|PubMed:25002425}; KM=0.033 mM for 6-hydroxynornicotine {ECO:0000269|PubMed:27568381}; KM=2.03 mM for nicotine {ECO:0000269|PubMed:25002425}; Note=kcat is 7.3 sec(-1) with (S)-6-hydroxynicotine as substrate. kcat is 0.... | PATHWAY: Alkaloid degradation; nicotine degradation; 6-hydroxypseudooxynicotine from nicotine (S-isomer route): step 2/2. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Stable between pH 6.0 and 9.8. {ECO:0000269|PubMed:25002425}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Stable at temperatures lower than 50 degrees Celsius. {ECO:0000269|PubMed:25002425}; | FUNCTION: Involved in the degradation of L-nicotine (PubMed:25002425). Catalyzes the oxidation of (S)-6-hydroxynicotine (6-hydroxy-L-nicotine) to 6-hydroxypseudooxynicotine (PubMed:25002425). Oxidation of the pyrrolidine ring of (S)-6-hydroxynicotine leads to the formation of the optically inactive 6-hydroxy-N-methylmy... | Shinella sp. (strain HZN7) |
A0A075D5I4 | PINMT_RAUSE | MAEKQQAVAEFYDNSTGAWEVFFGDHLHDGFYDPGTTATIAGSRAAVVRMIDEALRFANISDDPAKKPKTMLDVGCGIGGTCLHVAKKYGIQCKGITISSEQVKCAQGFAEEQGLEKKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPIVIVSYAHRNLSPSEGSLKPEEKKVLKKICDNIVLSWVCSSADYVRWLTPLPVEDIKAADWTQNITPFYPLLMKEAFTWKGFTSLLMKGGWSAIKVVLAVRMMAKAADDGVLKFVAVTCRKSK | 2.1.1.- | null | alkaloid biosynthetic process [GO:0009821]; methylation [GO:0032259]; vindoline biosynthetic process [GO:1900985] | plant-type vacuole membrane [GO:0009705] | N-methyltransferase activity [GO:0008170] | PF13847; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, gTMT family | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:35166361}. | CATALYTIC ACTIVITY: Reaction=picrinine + S-adenosyl-L-methionine = ervincine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70505, ChEBI:CHEBI:194555; Evidence={ECO:0000269|PubMed:26848097}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for picrinine {ECO:0000269|PubMed:26848097}; KM=9.3 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:26848097}; Vmax=126.1 pmol/sec/mg enzyme with picrinine as substrate {ECO:0000269|PubMed:26848097}; Vmax=97.2 pmol/sec/mg enzyme with S-adenosyl-L-methionin... | PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:26848097}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. {ECO:0000269|PubMed:26848097}; | FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with l... | Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum) |
A0A075D657 | PINMT_VINMI | MYTCSIIIYILTFWQLSKIKKQVAAAEKQVMTVTEKQEAVAEFYDKSTDAWEVFFGEHLHDGFYEPGTTATIPGSKVAVVRMIDELLRFAGISDDPEKKPKTMLDVGCGLGGTCLHVAKKYDIKCTGITISPEQVKCAQDLAATQGLESKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPVVIAGYAARNLSPSEESLKPEEKMVLEKICDHIVLSWLCSTGDYVKWLTPLPVQDIKVWDLTQNITPFYPLCIKEAFTWKSFTSLLKMGGWSAIKVVFAVKMMAMAAEEGLLKFAAVTCRK... | 2.1.1.- | null | alkaloid biosynthetic process [GO:0009821]; methylation [GO:0032259]; vindoline biosynthetic process [GO:1900985] | cytosol [GO:0005829] | N-methyltransferase activity [GO:0008170]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF08241; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, gTMT family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35166361}. | CATALYTIC ACTIVITY: Reaction=picrinine + S-adenosyl-L-methionine = ervincine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70505, ChEBI:CHEBI:194555; Evidence={ECO:0000269|PubMed:26848097}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.1 uM for picrinine {ECO:0000269|PubMed:26848097}; KM=15.8 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:26848097}; Vmax=100.8 pmol/sec/mg enzyme with picrinine as substrate {ECO:0000269|PubMed:26848097}; Vmax=135 pmol/sec/mg enzyme with S-adenosyl-L-methion... | PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:26848097}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. {ECO:0000269|PubMed:26848097}; | FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with l... | Vinca minor (Common periwinkle) |
A0A075F7E9 | LERK1_ORYSI | MVALLLFPMLLQLLSPTCAQTQKNITLGSTLAPQGPASSWLSPSGDFAFGFRPVEGNTSFYLIAVWFNKISDKTVVWYAKNTDQDPSIVEVPSDSFLQLTNDGALSLKDRSGQEGWNPQVTGVAYASMRDTGNFVLLGADGTTKWQTFDMPSDTILPTQVIPCNKTRNKSLRARLDIDDYSSGRFLLDVQTDGNLALYLVAVPSGSKYQQYWSTDTTGNGSELVFSETGKVYFALTDGTQINISSDAGIGSMADYFHRATLDPDGVFRQYVYPKKANAGILGGETWTALSMQPQNICHAIVSDVGSGVCGFNSYCTFDGT... | 2.7.11.1 | null | defense response [GO:0006952]; phosphorylation [GO:0016310]; response to other organism [GO:0051707] | membrane [GO:0016020] | ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF01453;PF00069; | 2.90.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Involved in innate immunity. Required for the expression of defense-related genes PR1A, LOX2 and CHS1 upon biotic stresses. Required for basal resistance to the fungal blast (M.grisea), bacterial blight (O.oryzae pv. oryzae, Xoo) and the herbivorous insect brown planthopper (N.lugens, BPH). May be involved in... | Oryza sativa subsp. indica (Rice) |
A0A075F932 | SYT1_ANSCY | MVSESHHEALAAPPATTVAAAPPSNVTEPASPGGGGGKEDAFSKLKEKFMNELNKIPLPPWALIAIAIVAVLLILTCCFCLCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQDDDAETGLTDGEEKEEPKEVEKLGKIQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEYKVAMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNG... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains. {ECO:0000250|UniProtKB:P21707}; | calcium ion-regulated exocytosis of neurotransmitter [GO:0048791]; cell differentiation [GO:0030154]; cellular response to calcium ion [GO:0071277]; multicellular organismal reproductive process [GO:0048609]; positive regulation of dendrite extension [GO:1903861]; regulation of calcium ion-dependent exocytosis [GO:0017... | axon [GO:0030424]; chromaffin granule membrane [GO:0042584]; cytoplasm [GO:0005737]; dense core granule [GO:0031045]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; clathrin binding [GO:0030276]; phosphatidylserine binding [GO:0001786]; phospholipid binding [GO:0005543]; syntaxin binding [GO:0019905] | PF00168; | 2.60.40.150; | Synaptotagmin family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000250|UniProtKB:P21707}. Cytoplasmic ves... | null | null | null | null | null | FUNCTION: Calcium sensor that participates in triggering neurotransmitter release at the synapse (By similarity). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence... | Anser cygnoides (Swan goose) |
A0A075FBG7 | ELS_MARVU | MSITFNLKIAPFSGPGIQRSKETFPATEIQITASTKSTMTTKCSFNASTDFMGKLREKVGGKADKPPVVIHPVDISSNLCMIDTLQSLGVDRYFQSEINTLLEHTYRLWKEKKKNIIFKDVSCCAIAFRLLREKGYQVSSDKLAPFADYRIRDVATILELYRASQARLYEDEHTLEKLHDWSSNLLKQHLLNGSIPDHKLHKQVEYFLKNYHGILDRVAVRRSLDLYNINHHHRIPDVADGFPKEDFLEYSMQDFNICQAQQQEELHQLQRWYADCRLDTLNYGRDVVRIANFLTSAIFGEPEFSDARLAFAKHIILVTR... | 4.2.3.131; 4.2.3.189; 4.2.3.190 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q40577}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577}; | gibberellin biosynthetic process [GO:0009686]; miltiradiene biosynthetic process [GO:1901946] | chloroplast [GO:0009507] | 9,13-epoxylabda-14-ene synthase activity [GO:0106239]; magnesium ion binding [GO:0000287]; manoyl oxide synthase activity [GO:0062206]; miltiradiene synthase activity [GO:0062205]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=peregrinol diphosphate = (13R)-9,13-epoxylabd-14-ene + diphosphate; Xref=Rhea:RHEA:54512, ChEBI:CHEBI:33019, ChEBI:CHEBI:138232, ChEBI:CHEBI:138233; EC=4.2.3.189; Evidence={ECO:0000269|PubMed:24990389}; CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene; Xref=... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:24990389}. | null | null | FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to 9,13(R)-epoxy-labd-14-e... | Marrubium vulgare (White horehound) |
A0A075QQ08 | IF4E1_TOBAC | MVDEVEKPASLEESKTNTREVEEGAEEVIESDDTMSSLGNPCKAMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTVEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCASGGKWTMSFSRGKSDTCWLYTLLAMIGEQFDCGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDSIGFIFHDDAKKLDRAAKNRYSV | null | null | defense response to virus [GO:0051607]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-120-Cys-158 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm {ECO:0000250|UniProtKB:K0P2S0}. | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:15988567). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiat... | Nicotiana tabacum (Common tobacco) |
A0A075TJ05 | OTASE_ASPNG | MVRRIASATPMVQSPMSPLGTTYCVRPNPVSLNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMK... | 3.4.17.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24947135}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | carboxypeptidase activity [GO:0004180]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237] | PF01979; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Ochratoxinase amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24947135}. | CATALYTIC ACTIVITY: Reaction=H2O + ochratoxin A = L-phenylalanine + ochratoxin alpha; Xref=Rhea:RHEA:72751, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:166829, ChEBI:CHEBI:192527; Evidence={ECO:0000269|PubMed:24947135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72752; Evidence={ECO:0000269|PubMed:24947... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:24947135}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 66 degrees Celsius. {ECO:0000269|PubMed:24947135}; | FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by As... | Aspergillus niger |
A0A075TMP0 | PATD_PENEN | MASTTPSTYKQAVFKEQGAGLTLEEVALTLPKRDEILVKVEACGVCHSDHFAQTNLMGGGFPLVPGHEIIGRVAAVGEGETVWKEGDRIGGAWHGGHDGTCGACKKGFFQMCDNEQVNGISRNGGYAEYCIIRREAAVHIPDHVNAAKYAPMLCAGVTVFNAMRHMKIPPGELVAIQGLGGLGHLALQYANKFGYRVVALSRDSTKEEFARKLGAHEYIDTSREDPVAALQKLGGASLIVSTAPVPEIINPLIQGLGVMGKLLILSIVGGIEVHTGLLVGKGKSIWSWPSGHATDSEDAIAFADLHGIDCLIEEFPLDKC... | 1.1.1.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q96533}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96533}; | patulin biosynthetic process [GO:0140723] | cytosol [GO:0005829] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase (NADP+) activity [GO:0008106]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}. | CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + neopatulin = (E)-ascladiol + NADP(+); Xref=Rhea:RHEA:62224, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145111, ChEBI:CHEBI:145112; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62225; Evidence={ECO:00002... | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FUNCTION: Alcohol dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatD catalyzes the conversion... | Penicillium expansum (Blue mold rot fungus) |
A0A075TMP8 | PATI_PENEN | MDILQLAPTHLLAILLSSTSALFLITYLLRAGHRPSDLPNGPPTVPLFGNELQVPKSDAHFQFSRWAKEYGGFFTLKRYNNTTIVISDQKLIKTLLDKKSNIYSHRPASLVSHLITQSDHLLVMQYGERWRMLRKTIHQYFMEPRCERDHWKVQEAEAKQMLHDYLTMPEDHMLHPKRYSNSITNSLVFGIRTKTVHDEYMKKLFYLMDKWSLVQELGATPPVDSFALLRYVPQWMLGNWRNRAVEVGDLMQSLYQTVLDQVKERRQRGIQRDSFMDRVLDTLKQTPLSENELRFLGGVLMEGGSDTSSSLILTIIQAMT... | 1.-.-.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | patulin biosynthetic process [GO:0140723] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}. | CATALYTIC ACTIVITY: Reaction=3-hydroxybenzyl alcohol + O2 + reduced [NADPH--hemoprotein reductase] = gentisyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:62212, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:5325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI... | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatI catalyzes the co... | Penicillium expansum (Blue mold rot fungus) |
A0A075TR33 | PATO_PENEN | MRLHQSPPRLLVCILSVLQVSAGLSSNCRCMPGDSCWPSLNDWARFNTSIGGRLVDTQPLGQPCHDPFYTASECNELKQQWTHPELHDASSSSIMSAAVANETCDAFTPRSKPCTLGAMVRYAVNASSPDDFVQTIRFSQERNIRLVIRNTGHDYAGKSTGAGALSIWTHSLKEIDFLNYTSAHYTGPAVRMTAGIQGTDINPAAHKKGLVIVGGECATVGPVGGFTQGGGHSALSSRFGLAADQVLEWEVVDGMGRLLTASPTQNPDLYWALSGGGGGTFGVVYAVTVKTFPDFAVTGVVLQFENIDPSSNRFFEAVGH... | 1.-.-.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305}; | patulin biosynthetic process [GO:0140723] | fungal-type vacuole lumen [GO:0000328]; vacuole [GO:0005773] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218] | PF08031;PF01565; | 3.30.465.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}. | null | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatO acts with patJ in th... | Penicillium expansum (Blue mold rot fungus) |
A0A075TR41 | PATJ_PENEN | MAPFVPYHYSAGQSTIVKFGGLLTTEFLEPPPGRCFLFRQTYRHTIEGSIPENLRKLINSPDRPKGPPPHFHQFQTEYFRVENGVLGISVDGVVRRITPEDGEISVKAGSVHNFFIHPDSPENMTVYLSASDSGNDYQLDRVFFENWYGYWHDALLHDGGIDWIQFLAIQDGGDAYTPAPAWVPFRRQVGYWTCVIVGRWIGGLLGYKPFFREYTTDWDFAVAKMKGSFFQRHLVHAAFEEEKSWTKQAELEPKGKPENAEFEPWTEDMSPAPLSLGPVAYEQGLFHGVQPGSVNGSNGHSTGVESKLEQLGSRAQRRVV... | 1.-.-.- | null | patulin biosynthetic process [GO:0140723] | cytoplasmic vesicle lumen [GO:0060205]; fungal-type vacuole lumen [GO:0000328]; vacuole [GO:0005773] | oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218] | null | 2.60.120.10; | Oxidoreductase OpS7 family | null | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:30680886}. | null | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FUNCTION: Probable oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatJ acts with patO in the ... | Penicillium expansum (Blue mold rot fungus) |
A0A075TRC0 | PATK_PENEN | MHSVSPSTYPSGGTSPAPADTPGTEYSEYEFSNDVAVVGMACRVAGGNHNPELLWQSLLSQKSAVGEIPEMRWEPYYRRDPRNAKELKKTTSRGYFLDRLEDFDCQFFGISPKEAEQMDPQQRVSLEVASEALEDAGIPAKSLSGSDTAVFWGVNSDDYSKLVLEDLPNVEAWMGIGTAYCGVPNRISYHLNLMGPSTAVDAACASSLVAVHHGVQAIRLGESQVAIVGGVNALCGPGLTRVLDKAGAISSDGSCKSFDDDAHGYARGEGAGALVLKSLHRALLDHDNVLAVIKGSAVAQDGKTNGIMAPNAKAQQLAAR... | 2.3.1.165 | null | fatty acid biosynthetic process [GO:0006633]; patulin biosynthetic process [GO:0140723] | cytosol [GO:0005829] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; 6-methylsalicylic acid synthase activity [GO:0050641]; fatty acid synthase activity [GO:0004312]; phosphopantetheine binding [GO:0031177]; polyketide synthase activity [GO:0016218] | PF00698;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.40.50.720;3.10.129.110; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 3 CO2 + 4 CoA + H2O + NADP(+); Xref=Rhea:RHEA:12240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:36658, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; ... | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FUNCTION: 6-methylsalicylic acid synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886, PubMed:35339702). Pa... | Penicillium expansum (Blue mold rot fungus) |
A0A075TRK9 | PATE_PENEN | MRLTSGIFHAAIAVAAVGAVLPEGPSSSKTHRNEYARRMLGSSFGIPKNQTFDYLVIGGGTAGLTIATRLAEQGVGSVAVIEAGGFYELNNGNLSQIPAQDAFYVGTDLDDWQPGIDWGFHTTPQAGAYDRVSHYARGKCLGGSSARNYMAYQRGTKAAHQRWADTVGDSSYTWEQFLPFFEKSLHFTPANDALRGANASVVSDPSVLGNGDGPLSVTYPHYAQAFATWAKHAFIEIGLQIRSGFQSGALLGQSYGLYTINATTMHRESSETSFLRKGLADPNLTVFQSALAKRIRFQDKRAVGVDVETMGRAYTLSARK... | 1.1.-.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:E4QP00}; | patulin biosynthetic process [GO:0140723] | cell cortex [GO:0005938]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; vacuole [GO:0005773] | flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on CH-OH group of donors [GO:0016614]; polyketide synthase activity [GO:0016218] | PF05199;PF00732; | 3.50.50.60;3.30.560.10; | GMC oxidoreductase family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:30680886}. Vacuole {ECO:0000269|PubMed:30680886}. Secreted {ECO:0000269|PubMed:30680886}. Secreted, cell wall {ECO:0000269|PubMed:30680886}. | CATALYTIC ACTIVITY: Reaction=(E)-ascladiol + A = AH2 + patulin; Xref=Rhea:RHEA:62228, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:74926, ChEBI:CHEBI:145112; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62229; Evidence={ECO:0000269|PubMed:30680886}; | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FUNCTION: Patulin synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatE catalyzes the last step of th... | Penicillium expansum (Blue mold rot fungus) |
A0A075TRL5 | PATH_PENEN | MEPFLLLLLVLLPAIVLVRYAFTYGHRTSTMPIGPPTLPFIGNIHQITKKYTHIKFTEWAAQYGGLYMLKIGNGNMAVITDRRLVKEVLDRKSGIYSHRPHSFVSHDLITKGNHLLVMHYGDQWRTFRRLVHQHLMETMVENHHTKIVNAEAIQLVRDYMIDPEHHMAHPKRYSNSITNSIVFGIRTANREGANMRRLYKLMEEWSEVMETGATPPVDLFPWLKLLPQWLFNNYIDRAKAIGVQMETLYVDILNKVIKRREDGHNNGTFMDKVLDSQEKHNLPWHQLAFIGGVLMEGGSDTSSSLTLAIVQALIQNPDVQ... | 1.-.-.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | patulin biosynthetic process [GO:0140723] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}. | CATALYTIC ACTIVITY: Reaction=3-methylphenol + O2 + reduced [NADPH--hemoprotein reductase] = 3-hydroxybenzyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:62208, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17069, ChEBI:... | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatH catalyzes the co... | Penicillium expansum (Blue mold rot fungus) |
A0A075TXZ1 | PATG_PENEN | MAKIDVHHHFYPPAMRQALDRAGGDPSGWYIPPWTLELDQDITRQMKVTTTILSVTAPGPGIEPDVTKAAALARSCNESAAAIRDAKPQQYGFFASVPSLFDTAAVLKEIEYACTTLRADGVTLFTRYGKGSNYLGHAAFRPIWADLSRRGAVVFIHPTHPVDTQLINTWLPQPMFDYPHETGRAAMDLLTSGILQDYPGCKIILSHAGGTLPYLIHRAATMLPLMPRTLGLSTEELVEAARTFYFDTAISSNPVTLKALFEFAAPGHVLFGSDFPNAPHDAILRFTNFLEAYELPEETKRQVDSGAALELFPRLKGILD... | 4.1.1.52 | null | patulin biosynthetic process [GO:0140723] | cytosol [GO:0005829] | 6-methylsalicylate decarboxylase activity [GO:0047596]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; polyketide synthase activity [GO:0016218] | PF04909; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, ACMSD family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}. | CATALYTIC ACTIVITY: Reaction=6-methylsalicylate + H(+) = 3-methylphenol + CO2; Xref=Rhea:RHEA:23112, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17231, ChEBI:CHEBI:36658; EC=4.1.1.52; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23113; Evidence={ECO:0000269|PubMed:3... | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FUNCTION: 6-methylsalicylic acid decarboxylase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatG catalyzes... | Penicillium expansum (Blue mold rot fungus) |
A0A076FFM5 | F8H1_OCIBA | MPFPMEVLQASSLSFPLLRRHSRNNLINKFRNPTLPRIDIPRQNIDLKTFAATTPTVACPPSDPEIIPEKKEDKFDWYENWYPVATVCDLDKRRPHGRKVIGIDVVVWWDRKENAWKVFDDTCPHRLAPLSEGRIDQWGRLQCVYHGWCFDGVGACKFIPQAPHDGPPVETSKKACVKGVYPSCVRNGIVWFWPNSDPKYKDIYLTNKPHYIPELDDPSFTCTTITREVPYGYEILAENLMDPSHVPYAHYGILELEKVKESSKRDREGGHEMEISVGTIDVNGFSAKHVSADYYFVPPYVYYGRITPNAATKTKDATLP... | 1.14.15.- | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628}; | flavonoid metabolic process [GO:0009812] | chloroplast [GO:0009507]; chloroplast membrane [GO:0031969]; cytoplasm [GO:0005737] | 2 iron, 2 sulfur cluster binding [GO:0051537]; chlorophyllide a oxygenase [overall] activity [GO:0010277]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497] | PF08417;PF00355; | 2.102.10.10; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:25139498}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:25139498}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] + salvigenin = 8-hydroxysalvigenin + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:73455, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for salvigenin {ECO:0000269|PubMed:25139498}; Vmax=60.3 pmol/sec/mg enzyme with salvigenin as substrate {ECO:0000269|PubMed:25139498}; | PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Rieske-type, PAO-family oxygenase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proli... | Ocimum basilicum (Sweet basil) |
A0A078CGE6 | M3KE1_BRANA | MARQMTSSQFHKSKTLDNKYMLGDEIGKGAYGRVYIGLDLENGDFVAIKQVSLENIVQEDLNTIMQEIDLLKNLNHKNIVKYLGSLKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADVNTHSVVGTPYWMAPEVIEMSGVCAASDIWSVGCTVIELLTCVPPYYDLQPMPALFRIVQDDSPPIPDSLSPDITDFLRQCFKKDSRQRPDAKTLLSHPWIRNSRRALQSSLRHSGTIRYMKGADSSSEKDGEGSQDIAESVSAEKV... | 2.7.11.1 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; MAPK cascade [GO:0000165]; protein autophosphorylation [GO:0046777]; regulation of cell division [GO:0051302] | cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.25.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. {ECO:0000269|PubMed:11489177}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8T2I8}. Nucleus, nucleolus {ECO:0000269|PubMed:15292395}. Cell membrane {ECO:0000250|UniProtKB:Q9LJD8}. Note=Accumulates in the nucleolus during interphase (PubMed:15292395). Localized to the plasma membrane in developi... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11489177}; CATALYTIC... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells (PubMed:11489177). Required for the normal functioning of the plasma membrane in developing pollen. Involved in the regulation of cell expansion and embryo develo... | Brassica napus (Rape) |
A0A087WPF7 | AUTS2_MOUSE | MDGPTRGHGLRKKRRSRSQRDRERRSRAGLGTGAAGGIGAGRTRAPSLASSSGSDKEDNGKPPSSAPSRPRPPRRKRRESTSAEEDIIDGFAMTSFVTFEALEKDVAVKPQERAEKRQTPLTKKKREALTNGLSFHSKKSRLSHSHHYSSDRENDRNLCQHLGKRKKMPKGLRQLKPGQNSCRDSDSESASGESKGFQRSSSRERLSDSSAPSSLGTGYFCDSDSDQEEKASDASSEKLFNTVLVNKDPELGVGALPEHNQDAGPIVPKISGLERSQEKSQDCCKEPVFEPVVLKDPHPQLPQLPSQAQAEPQLQIPSPG... | null | null | actin cytoskeleton organization [GO:0030036]; axon extension [GO:0048675]; dendrite extension [GO:0097484]; innate vocalization behavior [GO:0098582]; neuron migration [GO:0001764]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of Rac protein signal transduction [GO:0035022]; positive ... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; growth cone [GO:0030426]; nucleus [GO:0005634] | chromatin binding [GO:0003682] | PF15336; | null | AUTS2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19948250, ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25533347}. Cell projection, growth cone {ECO:0000269|PubMed:25533347}. Note=Detected both in cytoplasm and nucleus (PubMed:25533347). Colocalizes with RAC1 a... | null | null | null | null | null | FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitinatio... | Mus musculus (Mouse) |
A0A087X1C5 | CP2D7_HUMAN | MGLEALVPLAMIVAIFLLLVDLMHRHQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREAMVTRGEDTADRPPAPIYQVLGFGPRSQGVILSRYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFADQAGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLPHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAKKEKAKGSPESSFNDENLRIVVGNLFLAGMVTTSTTLAWGLLL... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | arachidonic acid metabolic process [GO:0019369]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739] | aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000305|PubMed:15051713}. Mitochondrion {ECO:0000269|PubMed:18838503}. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: May be responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It may be involved in the metabolism of codeine to morphine (PubMed:15051713). However, another study could not confirm it (PubMed:18838503). {ECO:0000269|PubMed:15051713, ECO:0000269|PubMed:18838503}. | Homo sapiens (Human) |
A0A088MIT0 | BRKP2_PHYNA | MAFLKKSLFLVLFLGVVSLSFCEEEKREEHEEEKRDEEDAESLGKRYGGLSPLRISKRVPPGFTPFRSPARSISGLTPIRLSKRVPPGFTPFRSPARRISEADPGFTPSFVVIKGLSPLRGKRRPPGFSPFRVD | null | null | defense response [GO:0006952] | extracellular region [GO:0005576] | toxin activity [GO:0090729] | PF03032; | null | Frog skin active peptide (FSAP) family, Bradykinin-related peptide subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26443407}. | null | null | null | null | null | FUNCTION: [[Val1,Thr6]-bradykinyl-Ser,Pro,Ala]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). {ECO:0000250|UniProtKB:P84899}.; FUNCTION: [Bradykinin]: May produce in vitro relaxation of rat arterial smooth muscle and ... | Physalaemus nattereri (Cuyaba dwarf frog) (Eupemphix nattereri) |
A0A088MLT8 | IQIP1_MOUSE | MRLEELKRLQNPLEQVDDGKYLLENHQLAMDVENNIENYPLSLQPLESKVKIIQRAWREYLQRQDPLEKRSPSPPSVSSDKLSSSVSMNTFSDSSTPDYREDGMDLGSDAGSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDDRGYRDDGCPAREPGDVSARIGSSGSGSRSAATTMPSPMPNGNLHPHDPQDLRHNGNVVVAGRPNASRVPRRPIQKTQPPGSRRGGRNRASGGLCLQPPDGGTRVPEEPPAPPMDWEALEKHLAGLQFREQEVRNQGQAR... | null | null | axon ensheathment [GO:0008366]; negative regulation of cytoskeleton organization [GO:0051494]; positive regulation of hippo signaling [GO:0035332] | axon initial segment [GO:0043194]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886] | ankyrin binding [GO:0030506]; calmodulin binding [GO:0005516]; transmembrane transporter binding [GO:0044325] | PF15157;PF10148; | null | null | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:18550753}. Cytoplasm {ECO:0000250|UniProtKB:B3KU38}. Note=Localizes to the axon initial segments (AIS) and nodes of Ranvier of neurons and is absent from dendrites. {ECO:0000269|PubMed:18550753}. | null | null | null | null | null | FUNCTION: May play a role in action potential conduction in myelinated cells through the organization of molecular complexes at nodes of Ranvier and axon initial segments (PubMed:25950943, PubMed:25953347, PubMed:27979964). May also play a role in axon outgrowth and guidance (PubMed:25953347). {ECO:0000269|PubMed:25950... | Mus musculus (Mouse) |
A0A089QRB9 | MSL3_MYCTU | MRTATATSVAVIGMACRLPGGIDSPQRLWEALLRGDDLVGEIPADRWDANVYYDPEPGVPGRSVSRWGAFLDDVGGFDCDFFGLTEREATAIDPQHRLLLEVSWEAIEHAGVDPATLAESQTGVFVGLTHGDYELLSADCGAAEGPYGFTGTSNSFASGRVAYTLGLHGPAVTVDTACSSGLTAVHQACRSLDDGESDLALAGGVVVTLEPRKSVSGSLQGMLSPTGRCHAFDEAADGFVSGEGCVVLLLKRLPDAVRDGDRVLAIVRGTAANQDGRTVNIAAPSAQAQIAVYQQALAAAGVEASTVGMVEAHGTGTPVG... | 2.3.1.252 | null | DIM/DIP cell wall layer assembly [GO:0071770]; methyl-branched fatty acid biosynthetic process [GO:1902321]; secondary metabolite biosynthetic process [GO:0044550] | plasma membrane [GO:0005886]; polyketide synthase complex [GO:0034081] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF08240;PF00107;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765; | 3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | CATALYTIC ACTIVITY: Reaction=3 (S)-methylmalonyl-CoA + a long-chain fatty acyl-CoA + 9 H(+) + holo-[mycolipanoate synthase] + 6 NADPH = 3 CO2 + 4 CoA + 3 H2O + long-chain mycolipanoyl-[mycolipanoate synthase] + 6 NADP(+); Xref=Rhea:RHEA:50344, Rhea:RHEA-COMP:12617, Rhea:RHEA-COMP:12618, ChEBI:CHEBI:15377, ChEBI:CHEBI:1... | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305|PubMed:12207710}. | null | null | FUNCTION: Polyketide synthase involved in the biosynthesis of methyl-branched fatty acids such as mycolipanoic, mycolipenic (phthienoic) and mycolipodienoic acids required for the synthesis of a major class of polyacylated trehaloses. Catalyzes the elongation of CoA esters of long-chain fatty acids by incorporation of ... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
A0A095AMW7 | MLES_LEUME | MNTTGYDILRNPFLNKGTAFSEAERQQLGLTGTLPSQIQTIEEQAEQAYKQFQAKSPLLEKRIFLMNLFNENVTLFYHLMDQHVSEFMPIVYDPVVAESIEQYNEIYTNPQNAAFLSVDRPEDVENALKNAAAGRDIKLVVVTDAEGILGMGDWGVNGVDIAVGKLMVYTAAAGIDPATVLPVSIDAGTNNKELLHNPLYLGNKHERIAGEQYLEFIDKFVTAEQNLFPESLLHWEDFGRSNAQVILDKYKESIATFNDDIQGTGMIVLAGIFGALNISKQKLVDQKFVTFGAGTAGMGIVNQIFSELKQAGLSDDEARN... | 4.1.1.101 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16345941}; COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:16345941}; | malate metabolic process [GO:0006108]; malolactic fermentation [GO:0043464]; pyruvate metabolic process [GO:0006090] | cytosol [GO:0005829] | carboxy-lyase activity [GO:0016831]; malate dehydrogenase (decarboxylating) (NAD+) activity [GO:0004471]; malolactic enzyme activity [GO:0043883]; manganese ion binding [GO:0030145]; NAD binding [GO:0051287] | PF00390;PF03949; | 3.40.50.10380;3.40.50.720; | Malic enzymes family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-malate + H(+) = (S)-lactate + CO2; Xref=Rhea:RHEA:46276, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:16651; EC=4.1.1.101; Evidence={ECO:0000269|PubMed:16345941}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.043 mM for NAD {ECO:0000269|PubMed:16345941}; KM=16.7 mM for (S)-malate {ECO:0000269|PubMed:16345941}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.35. {ECO:0000269|PubMed:16345941}; | null | FUNCTION: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate. {ECO:0000269|PubMed:16345941}. | Leuconostoc mesenteroides |
A0A095C6S0 | OXDA2_CRYD2 | MSFDAVVIGSGVIGLSIARELDNRGLKVAMVARDLAEDSLSVGFASPWAGCNWYSFAEGGTPAAEWDAITFSKLAKLAEDHPDLCEKIPFCSVWDLPKSDSESEPWFKDLVFEYKKLKSTPGQHLAGGKKFGYSFKSYVLHAPNYIRHLSSEIRARGIPIHRYRLSSIDEAYNLPGIGKVSLVVNASGLGAKSLIGVEDEKVYSGRGQTVLVRAPGFKACIMHTEGFYADLDESGREITPPPPAYIIPRPGPEGHVVLGGVYQKDNWSTLPDLKEAERILKDCYNLAPELAGPNGKSWKDIEIISHNVGLRPAREGEPRL... | 1.4.3.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P80324}; | aspartate catabolic process [GO:0006533]; cellular detoxification [GO:1990748]; D-amino acid catabolic process [GO:0019478]; nitrogen utilization [GO:0019740] | peroxisomal matrix [GO:0005782] | D-amino-acid oxidase activity [GO:0003884]; D-aspartate oxidase activity [GO:0008445]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P80324}. | CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-ri... | null | null | null | null | FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:26132227). Enables the organism to utilize D-amino acids as a source of nutrients (PubMed:26132227). Enables the organism to utilize D-alanine, D-cysteine, D-histidine, D-leucine, D-methionine, D-phenylalanine, D-pro... | Cryptococcus deuterogattii (strain R265) (Cryptococcus gattii VGII (strain R265)) |
A0A096MJN4 | SEPT4_RAT | MIKHFLEDNSDDAELSKFVKDFPGSEPCHPTESKTRVARPQILEPRPQSPDLCDDDVEFRATLWSQPSDSQQYFCPPAPLSPSSRPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWRPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPSEVDRKKCKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALK... | null | null | brain development [GO:0007420]; cytoskeleton-dependent cytokinesis [GO:0061640]; flagellated sperm motility [GO:0030317]; hematopoietic stem cell homeostasis [GO:0061484]; negative regulation of stem cell proliferation [GO:2000647]; neuron migration [GO:0001764]; positive regulation of apoptotic process [GO:0043065]; p... | axon [GO:0030424]; axon terminus [GO:0043679]; cell division site [GO:0032153]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; motile cilium [GO:0031514]; perikaryon [GO:0043204]; septin complex [GO:0031105]; septin ring [G... | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; molecular adaptor activity [GO:0060090] | PF00735; | 3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family | PTM: Phosphorylated by DYRK1A. {ECO:0000250|UniProtKB:P28661}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28661}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:P28661}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:O43236}. Cell projection, axon {ECO:0000250|UniProtKB:P28661}. Cell projection, dendrite {ECO:0000250|UniProtKB:P28661}. Perika... | null | null | null | null | null | FUNCTION: Filament-forming cytoskeletal GTPase. Pro-apoptotic protein involved in LGR5-positive intestinal stem cell and Paneth cell expansion in the intestines, via its interaction with XIAP (By similarity). May also play a role in the regulation of cell fate in the intestine (By similarity). Positive regulator of apo... | Rattus norvegicus (Rat) |
A0A096MJY4 | MEF2C_RAT | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVTIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNIQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYG... | null | null | AMPA selective glutamate receptor signaling pathway [GO:0098990]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; B cell homeostasis [GO:0001782]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; blood vessel development [GO:0001568]; blood vessel remodeling [GO:0001974]; c... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; postsynapse [GO:0098794]; protein-containing complex [GO:0032991]; sarcomere [GO:0030017]; sarcoplasm [GO:0016528] | chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polyme... | PF12347;PF00319; | 3.40.1810.10; | MEF2 family | PTM: Phosphorylated on Ser-59; which enhances DNA binding activity. Phosphorylated on Ser-396; which is required for Lys-391 sumoylation and inhibits transcriptional activity. {ECO:0000250}.; PTM: Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivati... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15862299}. Cytoplasm, sarcoplasm {ECO:0000269|PubMed:15862299}. | null | null | null | null | null | FUNCTION: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes (PubMed:15862299). Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an e... | Rattus norvegicus (Rat) |
A0A096MK47 | MLIP_RAT | MTSCVLAGSIETTPKVSPGDSEAKPLIFTFVPTLRRLPTHIQLADTSKFLVKIPEEPTDKNPETVNRFEYSDHMTFSCESKEERDQRILDYPSEVSGKNSQRKEFNTKEPQGMQKGDLFKAEYVFIVDSDGEDEATCRQGEQGPPGATGNIATRPKSLAISSSLASDVVRPKVRGVDVKVSSHPEIPHGIAPQQKHGQLTSPTTSEQLAHKPPAFSFVSPTNQKTPPVPAKVSGTTVLEEFHIRRLDVHGASEEETATYFHTTAHDSPLPAWKGASTLVFSPSAQLPGSSLCGSNVADHTRGLAPEAQKKVSTSSALNPR... | null | null | negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of cardiac muscle hypertrophy in response to stress [GO:1903243]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; transcription by RNA polym... | cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear lumen [GO:0031981]; nucleus [GO:0005634]; PML body [GO:0016605]; sarcolemma [GO:0042383] | lamin binding [GO:0005521]; transcription corepressor activity [GO:0003714] | PF15274; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FW52}. Nucleus envelope {ECO:0000250|UniProtKB:Q5FW52}. Nucleus, PML body {ECO:0000250|UniProtKB:Q5FW52}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5FW52}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q5FW52}; Peripheral membrane protein {ECO:0000250|UniProtKB... | null | null | null | null | null | FUNCTION: Required for myoblast differentiation into myotubes, possibly acting as a transcriptional regulator of the myogenic program (By similarity). Required for cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays a role in the protect... | Rattus norvegicus (Rat) |
A0A096P8D3 | IDH_OSTTA | MTRVERGRVLARAIERAVAHRASARRWTTTTRTPAWMVTGWMGGRGVDRSTAMTRFERCGSTASSKITAAPMVYVRGEEMTAYVMDLIRSRWIEPRVDVGGWETFDLRAKNRDDTEDRVLRDVIEAGKRIKAIFKEPTVTPTADQVKRLGLRKSWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVLFERHAVGGEYSAGYKNVGKGKLTTTFTPSEGPDAGKTVVVDEREIVDEEAAVVTYHNPYDNVHDLARFFFGRCLEAKVTPYVVTKKTVFKWQEPFWQIMRTVFDEEFKAQFVAAGVMKEGEELVHLLSDA... | 1.1.1.41 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25724193, ECO:0000269|Ref.4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25724193}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000269|Ref.4}; | isocitrate metabolic process [GO:0006102]; NAD metabolic process [GO:0019674]; NADP metabolic process [GO:0006739]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; peroxisome [GO:0005777] | isocitrate dehydrogenase (NAD+) activity [GO:0004449]; isocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803] | PF00180; | 3.40.718.10; | Isocitrate and isopropylmalate dehydrogenases family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH; Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41; Evidence={ECO:0000269|PubMed:25724193}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23633; Ev... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=226 uM for NAD(+) with Mg(2+) as cofactor {ECO:0000269|PubMed:25724193}; KM=265 uM for NAD(+) with Mn(2+) as cofactor {ECO:0000269|PubMed:25724193}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 with Mn(2+) as cofactor and 8.5 with Mg(2+) as cofactor. {ECO:0000269|PubMed:25724193}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:25724193}; | FUNCTION: Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (Probable). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production (Probable). {ECO:0000305|PubMed:25724193}. | Ostreococcus tauri |
A0A097PTA8 | DEFCO_COPCI | MKLSTSLLAIVAVASTFIGNALSATTVPGCFAECIDKAAVAVNCAAGDIDCLQASSQFATIVSECVATSDCTALSPGSASDADSINKTFNILSGLGFIDEADAFSAADVPEERDLTGLGRVLPVEKRQNCPTRRGLCVTSGLTACRNHCRSCHRGDVGCVRCSNAQCTGFLGTTCTCINPCPRC | null | null | defense response to bacterium [GO:0042742] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | lipid binding [GO:0008289] | PF18251; | 3.30.30.140; | Invertebrate defensin family | PTM: Contains a unique connectivity of 6 cysteine bonds in contrast to most other CS-alpha-beta defensins which are linked by 3 or 4 disulfide bonds. {ECO:0000305}.; PTM: Disulfide bonds are essential for structural integrity and antibacterial activity, since activity is lost after treatment with reducing agents. Thank... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25342741, ECO:0000305|PubMed:28825809}. Target cell membrane {ECO:0000269|PubMed:25342741, ECO:0000305|PubMed:28825809}. Note=specific localization at active cell wall synthesis sites. {ECO:0000269|PubMed:25342741}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 1-8. {ECO:0000269|PubMed:25342741}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4-90 degrees Celsius. {ECO:0000269|PubMed:25342741}; | FUNCTION: Antimicrobial peptide that acts against Gram-positive bacteria (Listeria spp., Enterococcus spp., B.subtilis, B.anthracis, P.aeruginosa) (PubMed:25342741, PubMed:28825809). Is not active against Gram-negative bacteria (PubMed:25342741). It selectively inhibits peptidoglycan biosynthesis through complex format... | Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata) |
A0A0A0LLY1 | SRBP1_CUCSA | MASSSVEFRCFVGGLAWATDSNSLEKAFSVYGEIVEAKIVSDRETGRSRGFGFVTFLEEEAMRSAIEAMNGHILDGRNITVNEAQQRGGGGGGGYNRGGGYGGRRDGGGFSRGGGGGYGGGGGGGYGGGRDRGYGGGGGYGGGRDSRGSGGGGSEGGWRN | null | null | defense response [GO:0006952]; extracellular transport [GO:0006858]; miRNA transport [GO:1990428]; regulation of defense response to virus [GO:0050688]; regulation of RNA splicing [GO:0043484]; RNA transport [GO:0050658] | cytosol [GO:0005829]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | miRNA binding [GO:0035198]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; single-stranded RNA binding [GO:0003727]; siRNA binding [GO:0035197] | PF00076; | 3.30.70.330; | GR-RBP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31812689}. Note=Observed in the phloem translocation stream. {ECO:0000269|PubMed:31812689}. | null | null | null | null | null | FUNCTION: Possibly has a role in RNA transcription or processing during stress (By similarity). Binds sequence non-specifically to RNAs and DNAs (By similarity). Mediates cell-to-cell trafficking of RNA interference (RNAi) signals (small RNAs (sRNA), e.g. small interfering RNA (siRNA) and microRNA (miRNA)) which regula... | Cucumis sativus (Cucumber) |
A0A0A1C3I2 | HMGR1_PANGI | MDVRRRLPPKLRRPLPITESSHHHRKTPFPADVDRSPSPTPKASDALPLPLYLTNGIFFTLFFSVAYYLLHRWRDKIRSSTPLHIVTLSELAAIVSLIASFIYLLGFFGIDFVQSFVSRADVDVDIDVEPDILEADRRPCSKLMDQPPPPPVVMSSEEDEEIVKSVVSGKTPSYSLESKLGDCYRAASIRREAVQRTTGRSLLGLPLDGFDYESILGQCCEMPIGYVQIPVGIAGPLLLNGCEYVVPMATTEGCLVASTNRGCKAIYACGGATGILLKDGMTRAPVVRFSTAKRASDLKFFLEDPLNFDTLAVVFNKSSR... | 1.1.1.34 | null | coenzyme A metabolic process [GO:0015936]; response to absence of light [GO:0009646]; response to jasmonic acid [GO:0009753]; saponin biosynthetic process [GO:0016135]; sterol biosynthetic process [GO:0016126]; triterpenoid biosynthetic process [GO:0016104] | chloroplast membrane [GO:0031969]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778] | hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420] | PF00368; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:00002... | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003}; | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:24569845, PubMed:29378087). Promotes triterpenes accumulation in r... | Panax ginseng (Korean ginseng) |
A0A0A1C930 | HMR2A_PANGI | MDVRRRPVKSLSSAKTATAGEPPKSQQQHPKASDALPLPLYLTNGLFFTMFFSVMYFLLHRWREKIRNSTPLHVVTLSELAALVLLMASVIYLLGFFGIGFVRSVIRPSPDAWDILEDDNAINEEDSRREPCAEAIDCSLPPKPKIVHMVPQKALNPKSAFADMMVEQPALAIAPLTEEDEEIVKSVVTGKIPSYSLESKLGDCKKAASIRREALQRITGKSLAGLPLDGFDYKSILGQCCEMPVGYVQIPVGIAGPLLLNETEYSVPMATTEGCLVASTNRGCKAIYASGGATSVLLRDGMTRAPVVRFSTVKRAAELK... | 1.1.1.34 | null | coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; response to jasmonic acid [GO:0009753]; saponin biosynthetic process [GO:0016135]; triterpenoid biosynthetic process [GO:0016104] | chloroplast membrane [GO:0031969]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778] | hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420] | PF00368; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane pro... | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003}; | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:24569845, PubMed:29378087). {ECO:0000250|UniProtKB:P14891, ECO:000... | Panax ginseng (Korean ginseng) |
A0A0A1H8I4 | AIS_PSESP | MFPRLPTLALGALLLASTPLLAAQPVTTLTVLSSGGIMGTIREVAPAYEKATGVKLDIAAAPSMGDTPQAIPNRLARNEPADVVLMVGSALDKLVASGQVAKDSRVDLGQSFIAMAVRQGAPKPDISNMDAFKQTLEKAQSVAYSDSASGVYLSRILFPRMQLDKSFMAKARMIPAEPVGAVVARGEAQLGFQQLSELKAVPGIDIVGLIPDQAQKMTLYSGAMVSKSQHPEAARALLQYLASKDAAKAIEDSGLKPVPAQP | 5.3.3.7 | null | cellular response to calcium ion [GO:0071277]; cellular response to iron ion [GO:0071281]; cellular response to magnesium ion [GO:0071286]; cellular response to manganese ion [GO:0071287]; cellular response to nickel ion [GO:0071289]; cellular response to silver ion [GO:0071292]; response to DDT [GO:0046680]; response ... | outer membrane-bounded periplasmic space [GO:0030288] | aconitate delta-isomerase activity [GO:0047614] | PF13531; | 3.40.190.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=trans-aconitate = cis-aconitate; Xref=Rhea:RHEA:17265, ChEBI:CHEBI:15708, ChEBI:CHEBI:16383; EC=5.3.3.7; Evidence={ECO:0000269|PubMed:26293748}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.9 mM for cis-aconitic acid {ECO:0000269|PubMed:26293748}; KM=80 mM for trans-aconitic acid {ECO:0000269|PubMed:26293748}; Note=kcat and kcat/KM are 4500 sec(-1) and 760 sec(-1) mM(-1), respectively for cis-aconitic acid. kcat and kcat/KM are 15000 sec(-1) and 190... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:26293748}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:26293748}; | FUNCTION: Involved in assimilation of trans-aconitic acid. Preference for cis-aconitic acid is 14-fold higher than for trans-aconitic acid. Not active on intermediates of tricarboxylic acid (TCA) cycle including citric acid, succinic acid, fumaric acid, and 2-oxoglutaric acid or on other dicarboxilic acids including it... | Pseudomonas sp |
A0A0A1HA03 | 708C1_FAGES | MMGDLTTSFPATTLTTNDQPHVVVCSGAGMGHLTPFLNLASALSSAPYNCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSALSPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPEHIFTSFTISNAKYFSLSKGILVNTFDSFEPETLSALNSGDTLSDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELR... | 2.4.1.360 | null | null | null | UDP-glucosyltransferase activity [GO:0035251] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-oxodihydrochalcone + H(+) + UDP; Xref=Rhea:RHEA:51504, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:142482, ChEBI:CHEBI:142483; EC=2.4.1.360; Evidence={... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 uM for 2-hydroxynaringenin {ECO:0000269|PubMed:25142187}; KM=40 uM for 2-hydroxypinocembrin {ECO:0000269|PubMed:25142187}; KM=36.5 uM for 2-phenyl-2',4',6'-trihydroxyactophenone {ECO:0000269|PubMed:25142187}; KM=3.73 uM for phloretin {ECO:0000269|PubMed:3269916... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:25142187}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-50 degrees Celsius. {ECO:0000269|PubMed:25142187}; | FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin (PubMed:25142187). No activity with flavanones, flavones or flavonols (PubMed:25142187). Exhibits C-glycosylation activity toward 2... | Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum) |
A0A0A1I6E7 | NDB4S_ANDCR | MEIKYLLTVFLVLLIVSDHCQAFLFSLIPHAISGLISAFKGRRKRDLDGQIDRFRNFRKRDAELEELLSKLPIY | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | null | null | Non-disulfide-bridged peptide (NDBP) superfamily, Short antimicrobial peptide (group 4) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25332684}. Target cell membrane {ECO:0000250}. Note=Forms a helical membrane channel in the prey. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM). {ECO:000026... | Androctonus crassicauda (Arabian fat-tailed scorpion) |
A0A0A1I6N9 | NDB4T_ANDCR | MEIKYLLTVFLVLLIVSDHCQAFLFSLIPNAISGLLSAFKGRRKRNLDGQIDRFRNFRKRDAELEELLSKLPIY | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | null | null | Non-disulfide-bridged peptide (NDBP) superfamily, Short antimicrobial peptide (group 4) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25332684}. Target cell membrane {ECO:0000250}. Note=Forms a helical membrane channel in the prey. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM). {ECO:000026... | Androctonus crassicauda (Arabian fat-tailed scorpion) |
A0A0A6ZFY4 | UGT29_PANGI | MDNQNGRISIALLPFLAHGHISPFFELAKQLAKRNCNVFLCSTPINLSSIKDKDSSASIKLVELHLPSSPDLPPHYHTTNGLPSHLMLPLRNAFETAGPTFSEILKTLNPDLLIYDFNPSWAPEIASSHNIPAVYFLTTAAASSSIGLHAFKNPGEKYPFPDFYDNSNITPEPPSADNMKLLHDFIACFERSCDIILIKSFRELEGKYIDLLSTLSDKTLVPVGPLVQDPMGHNEDPKTEQIINWLDKRAESTVVFVCFGSEYFLSNEELEEVAIGLEISTVNFIWAVRLIEGEKKGILPEGFVQRVGDRGLVVEGWAPQ... | 2.4.1.365 | null | response to molecule of fungal origin [GO:0002238]; saponin biosynthetic process [GO:0016135]; terpene biosynthetic process [GO:0046246]; terpenoid biosynthetic process [GO:0016114] | null | UDP-glycosyltransferase activity [GO:0008194] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(20S)-ginsenoside F2 + UDP-alpha-D-glucose = (20S)-ginsenoside Rd + H(+) + UDP; Xref=Rhea:RHEA:58004, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:67988, ChEBI:CHEBI:77145; EC=2.4.1.365; Evidence={ECO:0000269|PubMed:25320211}; PhysiologicalDirection=left-to-right; Xr... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=149 uM for ginsenoside Rh2 (at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:25769286}; KM=311 uM for ginsenoside Rh2 (at pH 7 and 35 degrees Celsius) {ECO:0000269|PubMed:25320211}; KM=188 uM for ginsenoside F2 (at pH 7 and 35 degrees Celsius) {ECO:0000269|PubMe... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Component of the dammarane-type triterpene saponins (e.g. PPD-type ginsenosides or panaxosides) biosynthetic pathway (PubMed:25320211, PubMed:25769286, PubMed:27746309, PubMed:29378087). Glycosyltransferase that catalyzes the conversion of ginsenoside Rh2 to ginsenoside Rg3 (PubMed:25320211, PubMed:25769286, ... | Panax ginseng (Korean ginseng) |
A0A0A7EPL0 | PIAL1_ARATH | MVIPATSRFGFRAEFNTKEFQASCISLANEIDAAIGRNEVPGNIQELALILNNVCRRKCDDYQTRAVVMALMISVKSACQLGWFPERETQELLAIIDLMWNGFSCPENVTSCVNSPVTLISQVIERFYPCVKLGHILVSFEAKPESKMMMKDFHISKKMPHSPKQKVGLFVVRTEDISRSNCIVHPQGVSFLLNGKGIDKRVNISMESGPQLPTNVTALLNLGANLLQAIGCFGGSYLIAIAFMDVIPLPNKPLLKDYVHPEVVGSNSDCDIIEGPSRISLSCPISRTRIKLPVKGHVCKHLQCFDFWNYVNMNTRRPSW... | 2.3.2.- | null | positive regulation of sulfur metabolic process [GO:0051176]; protein sumoylation [GO:0016925]; regulation of gene silencing by regulatory ncRNA [GO:0060966]; response to abscisic acid [GO:0009737]; response to osmotic stress [GO:0006970]; response to salt stress [GO:0009651] | nucleus [GO:0005634] | ligase activity [GO:0016874]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; zinc ion binding [GO:0008270] | PF02891; | 3.30.40.10; | PIAL protein ligase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:25415977}. | null | null | FUNCTION: Together with MOM1 and PIAL2, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation (PubMed:27113777). E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates (Pub... | Arabidopsis thaliana (Mouse-ear cress) |
A0A0A7EQR3 | GCE_CERUI | MFKPSFVALALVSYATAQASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCLQGAAPAPARTTAAPPPPPATTAAPPPPTTSAPTGSSPVAGACGAIASTVPNYNNAKLPDPFTFANGTALRTKADWSCRRAEISALIQNYEAGTLPPKPPVVTASFSKSGNTGTLAITAGLSNSQTIKFSPTISYPSGTPPANGWPLIIAYEGGSIPIPAGVATLTYSNSDMAQQNSASSRGQGLFYQLYGSTHSASAMTAWVWGVSRIIDALEMTPTAQINTQRIGVTGCSRDGKGALMAGAFEERIALTIPQESGSGGDACWRL... | 3.1.1.117 | null | carbohydrate metabolic process [GO:0005975]; lignin catabolic process [GO:0046274] | extracellular region [GO:0005576] | carboxylic ester hydrolase activity [GO:0052689]; cellulose binding [GO:0030248] | PF00734; | 3.40.50.1820; | Carbohydrate esterase 15 (CE15) family | PTM: N-glycosylated (PubMed:25425346). {ECO:0000269|PubMed:25425346}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25425346}. | CATALYTIC ACTIVITY: Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+); Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668; EC=3.1.1.117; Evidence={ECO:0000269|PubMed:2542534... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 mM for benzyl (methyl 4-O-methyl-alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=80 mM for benzyl (methyl alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=55 mM for phenylpropyl (methyl alpha-D-glucopyranoside) uronate {ECO:... | null | null | null | FUNCTION: Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin (PubMed:25425346, PubMed:26712478... | Cerrena unicolor (Canker rot fungus) (Daedalea unicolor) |
A0A0A7GEY4 | GGPPS_GEOAI | MISEIIKDRAKLVNEKIEELLKEQEPEGLYRAARHYLKAGGKRLRPVITLLSAEALGEDYRKAIHAAIAIETVHNFTLVHDDIMDEDEMRRGVKTVHTLFGIPTAILAGDTLYAEAFEILSMSDAPPENIVRAVSKLARVCVEICEGQFMDMSFEERDSVGESEYLEMVRKKTGVLIGISASIPAVLFGKDESVEKALWNYGIYSGIGFQIHDDLLDISGKGKIGKDWGSDILEGKKTLIVIKAFEEGIELETFGKGRASEEELERDIKKLFDCGAVDYARERAREYIEMAKKNLEVIDESPSRNYLVELADYLIERDH | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:30062607}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diph... | null | PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000305}.; PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: st... | null | null | FUNCTION: Catalyzes the addition of 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGPP). Catalyzes the synthesis of geranylgeranyl pyrophosphate as a major product and of farnesyl pyrophosphate in smaller amounts. {ECO:0000269|PubMed:30062607}. | Geoglobus acetivorans |
A0A0A7HFE1 | CAS10_STRTR | MKKEKIDLFYGALLHDIGKVIQRATGERKKHALVGADWFDEIADNQVISDQIRYHMANYQSDKLGNDHLAYITYIADNIASGVDRRQSNEESDEDASAKIWDTYTNQADIFNVFGAQTDKRYFKPTVLNLKSKPNFASATYEPFSKGDYAAIATRIKNELAEFEFNQAQIDSLLNLFEAILSFVPSSTNSKEIADISLAEHSRLTAAFALAIYDYLEDKGRHNYKEDLFTKASAFYEEEAFLLASFDLSGIQDFIYNIATSGAAKQLKARSLYLDFMSEYIADSLLDKLGLNRANLLYVGGGHAYFVLANTEKTVETLVQ... | 2.7.7.-; 3.1.-.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:27105119, ECO:0000269|PubMed:28663439}; Note=Degradation of ssDNA requires Mn(2+), Co(2+) or Ni(2+); Mg(2+), Ca(2+) or Zn(2+) do not activate ssDNase activity (PubMed:27105119). Formation of cOA requires Mn(2+), Co(2+) or Zn(2+... | defense response to virus [GO:0051607] | null | ATP binding [GO:0005524]; endonuclease activity [GO:0004519]; exonuclease activity [GO:0004527]; RNA binding [GO:0003723]; transferase activity [GO:0016740] | PF20824;PF18211;PF01966; | 3.30.70.270;1.10.3210.10; | CRISPR-associated Cas10/Csm1 family | null | null | CATALYTIC ACTIVITY: Reaction=6 ATP = cyclic hexaadenylate + 6 diphosphate; Xref=Rhea:RHEA:58276, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:142456; Evidence={ECO:0000269|PubMed:28663439}; | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target ... | Streptococcus thermophilus |
A0A0A7HIF0 | CSM3_STRTR | MTFAKIKFSAQIRLETGLHIGGSDAFAAIGAIDSPVIKDPITNIPIIPGSSLKGKMRTLLAKVYNEKVAEKPSDDSDILSRLFGNSKDKRFKMGRLIFRDAFLSNADELDSLGVRSYTEVKFENTIDRITAEANPRQIERAIRNSTFDFELIYEITDENENQVEEDFKVIRDGLKLLELDYLGGSGSRGYGKVAFEKLKATTVFGNYDVKTLNELLTAEV | 3.1.-.- | COFACTOR: Name=a metal cation; Xref=ChEBI:CHEBI:25213; Evidence={ECO:0000269|PubMed:25458845}; Note=Endonucleolytic cleavage of target ssRNA by the Csm complex requires a divalent metal ion; Mg(2+) has the best activity in vitro, but Mn(2+), Ca(2+), Zn(2+), Ni(2+), and Co(2+) also support cleavage. {ECO:0000269|PubMed:... | defense response to virus [GO:0051607] | null | endonuclease activity [GO:0004519]; RNA binding [GO:0003723] | PF03787; | null | CRISPR-associated Csm3 family | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target ... | Streptococcus thermophilus |
A0A0A7HIX6 | CSM6A_STRTR | MKILISAVGTTDPISNNHDAALLHIARNYRPDKIVLVYSQEMMVKQDLINKVLLSIEGYNPIIEIDSTILNNDEVFLFDKMYEVMGQIVQKYTNDDNEIILNLSSGTPQIISALFALNRINDYNTQAIQVATPKNRANREYTALTESEIDALIMENQDNRLDFVDRSIKDKSEKFTQALVKRHLRSLIASFDYQAAEAIINRKEYNKLLSKKKIAYIREKLYDFSRVFKNQSILSDILSFPLDDSQKKALNYYLMIDVLKEREHIADVLIKAKSLAEFVIEETIKKDHEGLIVFDGNLPKLNPSFPDCEAILDDIDKKMK... | 3.1.-.- | null | defense response to virus [GO:0051607] | null | endonuclease activity [GO:0004519]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723] | PF09659; | 3.40.50.10770; | CRISPR-associated Csm6 family | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target ... | Streptococcus thermophilus |
A0A0B0QJR1 | HEPT_APHF2 | MTNIEPVIIETRLELIGRYLDHLKKFENISLDDYLSSFEQQLITERLLQLITQAAIDINDHILSKLKSGKSYTNFEAFIELGKYQILTPELAKQIAPSSGLRNRLVHEYDDIDPNQVFMAISFALQQYPLYVRQINSYLITLEEEND | 3.1.27.- | null | null | toxin-antitoxin complex [GO:0110001] | endonuclease activity [GO:0004519]; nucleotide binding [GO:0000166]; RNA nuclease activity [GO:0004540] | PF01934; | 1.20.120.580; | HepT RNase toxin family | PTM: Di-AMPylated by cognate antitoxin MntA on Tyr-109 when both are expressed in E.coli; GMPylation occurs much less often. Leads to an increase of mass of 659 Da. Di-AMPylation moves the catalytic His-107 away from the catalytic center, leading to loss of nuclease activity and thus toxicity. Probably one subunit of t... | null | CATALYTIC ACTIVITY: Reaction=(tRNA)-3'-end (ribonucleoside 5'-phosphate)-(guanosyl 5'-phosphate)-(cytosyl 5'-phosphate)-(cytosyl 5'-phosphate)-(adenosine 5'-phosphate) + H2O = GpCpCpA + H(+) + tRNA 3'-end (ribonucleotide 3'-phosphate); Xref=Rhea:RHEA:66608, Rhea:RHEA-COMP:17075, Rhea:RHEA-COMP:17076, ChEBI:CHEBI:15377,... | null | null | null | null | FUNCTION: Toxic component of a type VII toxin-antitoxin (TA) system. Upon cloning in E.coli inhibits cell growth for several hours; eventually cells recover and start growing. Cleaves the last 4 nucleotides from the tRNA acceptor stem (shown in vitro with E.coli tRNA-Glu(UUC)); only cleaves intact tRNA. Has no activity... | Aphanizomenon flos-aquae (strain 2012/KM1/D3) |
A0A0B4J1F4 | ARRD4_MOUSE | MGGEAGADGPRGRVKSLGLVFEDESKGCYSSGETVAGHVLLEAAEPVALRGLRLEAQGRATSAWGPSAGARVCIGGGSPAASSEVEYLNLRLSLLEAPAGEGVTLLQPGKHEFPFRFQLPSEPLATSFTGKYGSIQYCVRAVLERPQVPDQSVRRELQVVSHVDVNTPPLLTPMLKTQEKMVGCWLFTSGPVSLSVKIERKGYCNGEAIPIYAEIENCSSRLVVPKAAIFQTQTYLASGKTKTVRHMVANVRGNHIGSGSTDTWNGKMLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKRLMLELPLVIGTIPYSGFGR... | null | null | extracellular vesicle biogenesis [GO:0140112]; positive regulation of interferon-beta production [GO:0032728]; protein K63-linked ubiquitination [GO:0070534]; protein transport [GO:0015031]; protein ubiquitination [GO:0016567] | cytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular vesicle [GO:1903561]; plasma membrane [GO:0005886] | ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF02752;PF00339; | 2.60.40.640; | Arrestin family | null | SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:19605364}. Cell membrane {ECO:0000269|PubMed:19605364, ECO:0000269|PubMed:27462458}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:19605364}. Note=Also found in extracellular vesicles different ... | null | null | null | null | null | FUNCTION: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates (PubMed:27462458). Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (By similarity). Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extrac... | Mus musculus (Mouse) |
A0A0B4J1G0 | FCG3A_MOUSE | MWQLLLPTALVLTAFSGIQAGLQKAVVNLDPKWVRVLEEDSVTLRCQGTFSPEDNSIKWFHNESLIPHQDANYVIQSARVKDSGMYRCQTALSTISDPVQLEVHMGWLLLQTTKWLFQEGDPIHLRCHSWQNRPVRKVTYLQNGKGKKYFHENSELLIPKATHNDSGSYFCRGLIGHNNKSSASFRISLGDPGSPSMFPPWHQITFCLLIGLLFAIDTVLYFSVRRGLQSPVADYEEPKIQWSKEPQDK | null | null | antibody-dependent cellular cytotoxicity [GO:0001788]; cell surface receptor signaling pathway [GO:0007166]; cellular response to lipopolysaccharide [GO:0071222]; dendritic cell antigen processing and presentation [GO:0002468]; Fc receptor-mediated immune complex endocytosis [GO:0160006]; natural killer cell degranulat... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | IgE binding [GO:0019863]; IgE receptor activity [GO:0019767]; IgG binding [GO:0019864]; IgG receptor activity [GO:0019770]; immune receptor activity [GO:0140375] | PF13895;PF13927; | 2.60.40.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:18949059}.; PTM: Phosphorylated following receptor ligation. {ECO:0000269|PubMed:17558411}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:28389502}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG) (PubMed:16039578). Binds with intermediate affinity to both IgG2a and IgG2b (PubMed:16039578, PubMed:17558411, PubMed:19795417). Can bind to IgG2a and IgG2b monomers (PubMed:18949059). Does not display binding to IgG1 or IgG3 (PubMed:160395... | Mus musculus (Mouse) |
A0A0B4J1N3 | GP15L_MOUSE | MRLLALSGLLCMLLLCFCIFSSEGRRHPAKSLKLRRCCHLSPRSKLTTWKGNHTRPCRLCRNKLPVKSWVVPGALPQI | null | null | defense response to fungus [GO:0050832]; defense response to Gram-positive bacterium [GO:0050830]; G protein-coupled receptor signaling pathway [GO:0007186]; lymphocyte chemotaxis [GO:0048247]; mast cell degranulation [GO:0043303]; negative regulation of cell cycle G1/S phase transition [GO:1902807]; negative regulatio... | extracellular space [GO:0005615] | chemokine activity [GO:0008009]; G protein-coupled receptor binding [GO:0001664]; receptor ligand activity [GO:0048018] | PF15854; | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6UWK7}. | null | null | null | null | null | FUNCTION: Highly cationic protein that has multiple functions. Acts as a chemotactic factor that mediates lymphocytes recruitment to epithelia through binding and activation of the G-protein coupled receptor GPR15 (PubMed:28900043, PubMed:28936214). May be a tumor suppressor; together with SUSD2 has a growth inhibitory... | Mus musculus (Mouse) |
A0A0B4J2F0 | PIOS1_HUMAN | MFRRLTFAQLLFATVLGIAGGVYIFQPVFEQYAKDQKELKEKMQLVQESEEKKS | null | null | regulation of endoplasmic reticulum unfolded protein response [GO:1900101]; response to unfolded protein [GO:0006986] | mitochondrial outer membrane [GO:0005741] | null | null | null | null | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:31653868}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Plays a role in regulation of the unfolded protein response triggered by endoplasmic reticulum (ER) stress resulting from the presence of unfolded proteins in the ER lumen. {ECO:0000269|PubMed:31653868}. | Homo sapiens (Human) |
A0A0B4J2F2 | SIK1B_HUMAN | MVIMSEFSADPAGQGQGQQKPLRVGFYDIERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDSSNLEKIYREVQLMKLLNHPHIIKLYQVMETKDMLYIVTEFAKNGEMFDYLTSNGHLSENEARKKFWQILSAVEYCHDHHIVHRDLKTENLLLDGNMDIKLADFGFGNFYKSGEPLSTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPFFMSQDCESLIRRMLVVDPARRITIAQIRQHRWMRAEPCLPGPACPAFSAHSYTSNLGDYDEQALGIMQTLGVDRQ... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; | intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, AMPK subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P57059}; CATALYTI... | null | null | null | null | FUNCTION: Probable serine/threonine-protein kinase. {ECO:0000250|UniProtKB:P57059}. | Homo sapiens (Human) |
A0A0B4K692 | NEP2_DROME | MQTVIQNPNWWRRRNKLEKSLLVSLGIMFVVLATGFGLWIGKVLRTSPPSNPQATALHGDSTTINQVPTGTASKGKSGDSGDVCLTQECIHTASTVLRKMKPEVEPCDNFYEFACGTYLEEENIPDDKVSISTFSVISDKLQEQLKDIITAERPETEPKHFRLPNLLYKACMNKTLIETLGPEPITRVAERLGGWPLIKGDSWNADDSWTWQEQVKKFRTAGFSMDYIIDFSIGVDLQNSTKRLIDLDQSSLALSREYLVKGFNETLVTAYYKYMVDIAVLFGANRDLAKTELLLSLEFEMALANISWPNEKRRNSSELY... | 3.4.24.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08473}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08473}; | protein processing [GO:0016485]; proteolysis [GO:0006508]; sperm competition [GO:0046692] | extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886] | endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237] | PF01431;PF05649; | 3.40.390.10;1.10.1380.10; | Peptidase M13 family | PTM: N-glycosylated. {ECO:0000269|PubMed:17157960}.; PTM: The soluble form is probably produced by proteolytic cleavage. {ECO:0000305|PubMed:15554877, ECO:0000305|PubMed:17157960}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960}. Note=A secreted form exists that is probably produced by proteolytic cleavage (Probable). In embryos, adult Malpighian tubules and testes, detected ... | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11; Evidence={ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5 at 35 degrees Celsius. {ECO:0000269|PubMed:17157960}; | null | FUNCTION: Metalloendoprotease which cleaves peptides such as tachykinin peptide TK-2 at the amino side of hydrophobic residues (PubMed:15554877, PubMed:17157960). Functions in female fertility, embryogenesis and memory formation (PubMed:24395329, PubMed:27629706). Required in females for normal patterns of egg laying, ... | Drosophila melanogaster (Fruit fly) |
A0A0B4K7J2 | RBP2_DROME | MFTTRKEVDAHVHKMLGKLQPGRERDIKGLAVARLYMKVQEYPKAIEYLNGYLRVRDDAVGHNMIATCYSRLNPPDVTEALQHYQRSIQIDPRQSEVVIDACELLVKENNASITECARYWLDQANSLDLSGNKQVFNLRMRVNLADSNGERDDTSGGDGEQNTLEILMYKELQARPQDVNIRIQLLRSYVEKMKIDQAFNYALKTELESKNCTSQSNEWYEQIWMVLFKIEMAKDVKKNWRFWHFALHTLDRLVQLSLEGSGLADSSKQLFRLDQYLFKFSTSIERSGDAPQRDLHQACIDHFTGQLLLHAVTLIFKREV... | 2.3.2.- | null | germ cell development [GO:0007281]; juvenile hormone mediated signaling pathway [GO:0035626]; mRNA transport [GO:0051028]; NLS-bearing protein import into nucleus [GO:0006607]; nuclear pore complex assembly [GO:0051292]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expr... | annulate lamellae [GO:0005642]; cytoplasm [GO:0005737]; nuclear pore [GO:0005643] | GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; SUMO transferase activity [GO:0019789] | PF00638;PF00641; | 2.30.29.30;1.25.40.10;4.10.1060.10; | RanBP2 E3 ligase family | null | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Note=Localizes to annulate lamellae, stacked membrane sheets of the endoplasmic reticulum. Localizes to granules which travel from nurse cells into the ooplasm through ring canals connecting the cytoplasm of the two cell types. {ECO:000... | null | null | null | null | null | FUNCTION: E3 SUMO-protein ligase (By similarity). Component of the nuclear pore complex (NPC), a complex required for trafficking across the nuclear envelope (PubMed:17682050). Required for nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner, but a... | Drosophila melanogaster (Fruit fly) |
A0A0B4KEE4 | KOI_DROME | MSENTYQIETRRRSRSKTPFLRSSCDHENCEHAGEEGHVHHLKRKSAAPNVQTIIEEHIVESSISKKTRAKAFAQLTSDYSSDDMTPDAKRKQNSITATVTSILTKRSGGATSTPRNRSQLETTQNTLNSAQEKLNQSNGNLSSGNVSDYLAYIEYRDAGEYWNKTPKTDYTYSELSPHRRQLAPGIVAMPNMSRKSLENHNDRVNYMVQQNPAQEEFIRRRYQSKYTQQVNYDSADELDATFGQQKQSWWLIRLIQLVVSSITTVWSRVTNLSATETTAYQNYHAKRQQSQQVGLWWKIVQTIGGGLASLLRYLYVFIG... | null | null | double-strand break repair via homologous recombination [GO:0000724]; nuclear migration [GO:0007097]; nucleus localization [GO:0051647] | meiotic nuclear membrane microtubule tethering complex [GO:0034993]; microtubule organizing center [GO:0005815]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; perinuclear region of cytoplasm [GO:0048471] | protein-membrane adaptor activity [GO:0043495] | PF07738; | 2.60.120.260; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:32066907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18820457, ECO:0000269|PubMed:32066907}. Note=Lam is required for perinuclear localization of Ko... | null | null | null | null | null | FUNCTION: Component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (By similarity). Is required to nuclear migration in eye and to anchor klar in the nuclear membrane (PubMed:18820457). {ECO:0000250|UniProtKB:O94901, ECO:0000269... | Drosophila melanogaster (Fruit fly) |
A0A0B4KGY6 | NOVA_DROME | MESIMKVAMDKAAEQLIQQFGFDYLQQQLQLQHQNQHNSSPQQPQHQQLEPENEHLTYQYQQSKPTHMQQLACNYQPRHSTTTSSPSSTHSLASGGGSSSNSSNSSSSDSSSINISHISNISNISNIGNISNSNHSNAAYSLAVHSYQKQIESPANPSHVPHHQMDLSPLSENGSPNGTPGAQTPTATASGNTAAALASAAAAAAAATSGGNGSSITNCNSNNSSSSSNAQQQLQLGNYKTNSCWCYGESVCSGIEVEIENNNNNHIHHGETTYHMKILVPAVASGAIIGKGGETIASLQKDTGARVKMSKSHDFYPGTT... | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of RNA splicing [GO:0033120]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA binding [GO:0003729]; pre-mRNA intronic binding [GO:0097157] | PF00013; | 3.30.1370.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11784037, ECO:0000269|PubMed:28525754}. Cytoplasm {ECO:0000269|PubMed:28525754}. Note=Localizes to synaptoneuropil region of neurons. {ECO:0000269|PubMed:28525754}. | null | null | null | null | null | FUNCTION: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion (By similarity). Plays a role in long-term memory formation by processing the unspliced Orb2-isoform A (Orb2A) mRNA and thereby controlling Orb2A protein abundance (PubMed:2852575... | Drosophila melanogaster (Fruit fly) |
A0A0B4LFY9 | STING_DROME | MAIASNVVEAGNAVRAEKGRKYFYFRKMIGDYIDTSIRIVATVFLADLLLRLYRCVVEYGSNGRYYLPEDRLWIILRRSCTYNNRSIYLIVGFLLVAFFRISVTGNYRNVMPTTLFLFQMPLYWIWSFTDMDQSTLSYSHWIRDSHGLDYAAGMASNYFHGYLKLSLPERKDDGLKHRLAMYEDKNNVTFGIKRLVILIPDEMFVNGVLESHLLDKAEPLETQFINRAGVYRPFKHDVYRMNKKVNGRTYYFAVEGATPMISFFDATYSNLSGTWQMQELKREIWIKFYKHLKELITTWPETRDLVELIIYNSHDSKGNL... | null | null | antiviral innate immune response [GO:0140374]; autophagosome assembly [GO:0000045]; cellular response to virus [GO:0098586]; cGAS/STING signaling pathway [GO:0140896]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of antimicr... | autophagosome [GO:0005776]; endoplasmic reticulum membrane [GO:0005789] | 2',3'-cyclic GMP-AMP binding [GO:0061507]; 3',2'-cyclic GMP-AMP binding [GO:0140704]; cyclic-di-GMP binding [GO:0035438] | PF15009; | 3.40.50.12100; | STING family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30119996}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Facilitator of innate immune signaling that binds cyclic dinucleotides produced in response to infection by bacteria and/or viruses, and promotes the activation of the NF-kappa-B transcription factor Rel (Relish) (PubMed:29924997, PubMed:29934091, PubMed:30119996, PubMed:33262294, PubMed:34261127, PubMed:3426... | Drosophila melanogaster (Fruit fly) |
A0A0B4U9L8 | VMF1_VIPAA | MLQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPQKLTALLKGAIQQPEQKYEDAMQYEFKVNGKPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGHIQNDAHLTASISACNGLKGHFQLRGETYLIEPLKIPDSEAHAVYKYENVEKEDEGPKKCGVTQTNWKSDEPIKASQFILTPEQRAYMNANKYIKLAIVVDNVMFRKYTGNFTAIRTRIYEIVNTLNLIYTILNIHIALVFLEIWSKGDSINVQSVVDVTLNSFGEWRERDLLNRKRHDNAQLLTGINFNGDTIGFGFVGSMCIPKKSVG... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9DGB9}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9DGB9}; | envenomation resulting in modulation of blood coagulation in another organism [GO:0044468]; envenomation resulting in modulation of process in another organism [GO:0035738]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; extraorganismal space [GO:0043245]; plasma membrane [GO:0005886] | metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:25549999}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:25549999}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25549999}. | null | null | null | null | null | FUNCTION: Zinc metalloprotease that has fibrinogenolytic activity. Does not have hemorrhagic activity in rats. Cleaves insulin B chain at '38-Ala-|-Leu-39' and '40-Tyr-|-Leu-41' bonds. Hydrolyzes only partially and weakly isolated extracellular matrix (ECM) bovine fibronectin and basal membrane (BM) protein human colla... | Vipera ammodytes ammodytes (Western sand viper) |
A0A0B5A051 | PT1L_HUMLU | MELSSVSSFSLGTNPFISIPHNNNNNLKVSSYCCKSKSRVINSTNSKHCSPNNNNNNNTSNKTTHLLGLYGQSRCLLKPLSIFSCKDQRGNSIRASAQIEDRPPESGNLSALTNVKDFVSVCWEYVRPYTAKGVIICSSCLFGRELLENPNLFSWPLIFRALLGMLAILGSCFYTAGINQIFDMDIDRINKPDLPLVSGRISVESAWLLTLSPAIIGFILILKLNSGPLLTSLYCLAILSGTIYSVPPFRWKKNPITAFLCILMIHAGLNFSVYYASRAALGLAFVWSPSFSFITAFITFMTLTLASSKDLSDINGDRKF... | 2.5.1.136 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:E5RP65}; | null | chloroplast membrane [GO:0031969] | prenyltransferase activity [GO:0004659] | PF01040; | 1.10.357.140; | UbiA prenyltransferase family | null | SUBCELLULAR LOCATION: Plastid {ECO:0000269|PubMed:25564559}. Plastid, chloroplast membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: [2-acylphloroglucinol 4-prenyltransferase]: Reaction=2',4,4',6'-tetrahydroxychalcone + dimethylallyl diphosphate = desmethylxanthohumol + diphosphate; Xref=Rhea:RHEA:51876, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:77645, ChEBI:CHEBI:134302; EC=2.5.1.136; Evidence={ECO:0000269|PubMed:2976009... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.74 uM for naringenin chalcone {ECO:0000269|PubMed:29760092}; KM=75.12 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:29760092}; KM=5.01 uM for naringenin chalcone (in the presence of CHIL2) {ECO:0000269|PubMed:29760092}; KM=62.78 uM for dimethylallyl diphos... | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}. | null | null | FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the first prenylation step in the beta-bitter acid pathway (PubMed:25564559). Uses dimethylallyl diphosphate (DMAPP) as the prenyl do... | Humulus lupulus (European hop) |
A0A0B5A886 | GP_SFTSV | MMKVIWFSSLICLVIQCSGDSGPIICAGPIHSNKSAGIPHLLGYSEKICQIDRLIHVSSWLRNHSQFQGYVGQRGGRSQVSYYPAENSYSRWSGLLSPCDADWLGMLVVKKAKESDMIVPGPSYKGKVFFERPTFDGYVGWGCGSGKSRTESGELCSSDSGTSSGLLPSDRVLWIGDVACQPMTPIPEETFLELKSFSQSEFPDICKIDGIVFNQCEGESLPQPFDVAWMDVGHSHKIIMREHKTKWVQESSSKDFVCYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRCSLVHKPGEVVVSYGG... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host endosome membrane [GO:0039654]; symbiont entry into host cell [GO:0046718] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; virion membrane [GO:0055036] | null | PF19019;PF07243;PF07245; | 2.60.40.3770;2.60.98.50; | Phlebovirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins including glycoprotein C and glycoprotein N. {ECO:0000269|PubMed:27855227}.; PTM: [Glycoprotein N]: The cytoplasmic tail is Palmitoylated. {ECO:0000250|UniProtKB:P09613}.; PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProt... | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host e... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By ... | SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with thrombocytopenia virus) |
A0A0B5A8P4 | INS3A_CONGE | MTTSFYFLLVALGLLLYVCQSSFGNQHTRNSDTPKHRCGSELADQYVQLCHGKRNDAGKKRGRASPLWQRQGFLSMLKAKRNEAFFLQRDGRGIVEVCCDNPCTVATLRTFCH | null | null | glucose metabolic process [GO:0006006] | extracellular region [GO:0005576] | hormone activity [GO:0005179]; toxin activity [GO:0090729] | PF00049; | 1.10.100.10; | Insulin family | PTM: It is noteworthy that in this dimer, in contrast to Con-Ins G1, the chain B is amidated and not the chain A. {ECO:0000269|PubMed:25605914}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25605914}. | null | null | null | null | null | FUNCTION: This venom insulin, from a fish-hunting cone snail, facilitates prey capture by rapidly inducing hypoglycemic shock (PubMed:30747102). It is one of the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the insulin receptor (IN... | Conus geographus (Geography cone) (Nubecula geographus) |
A0A0B5AC19 | NSS_SFTSV | MSLSKCSNVDLKSVAMNANTVRLEPSLGEYPTLRRDLVECSCSVLTLSMVKRMGKMTNTVWLFGNPKNPLHQLEPGLEQLLDMYYKDMRCYSQRELSALRWPSGKPSVWFLQAAHMFFSIKNSWAMETGRENWRGLFHRITKGQKYLFEGDMILDSLEAIEKRRLRLGLPEILITGLSPILDVALLQIESLARLRGMSLNHHLFTSPSLRKPLLDCWDFFIPVRKKKTDGSYSVLDEDDEPGVLHGYPHLMAHYLNRCPFHNLIRFDEELRTAALNTIWGRDWPAIGDLPKEV | null | null | symbiont-mediated arrest of host cell cycle during G2/M transition [GO:0039592]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity [GO:0039540]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathwa... | host cell cytoplasmic vesicle [GO:0044161] | null | null | null | Bandavirus NS-S protein family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:24478431}. Host cytoplasmic vesicle {ECO:0000269|PubMed:24335286, ECO:0000269|PubMed:28680969, ECO:0000269|PubMed:30598516}. Note=Localizes to the viral cytoplasmic occlusion bodies. {ECO:0000269|PubMed:24335286, ECO:0000269|PubMed:27226560, ECO:0000269|PubMed:28... | null | null | null | null | null | FUNCTION: Sequesters host STAT2 into viral inclusion bodies (Probable) (PubMed:29886262). Impairs IFN-stimulated phosphorylation and nuclear translocation of host STAT2, thereby suppressing type-I IFN antiviral signaling (Probable) (PubMed:28680969, PubMed:29886262). Sequesters host TRIM25, RIGI, TBK1/IKK complex compo... | SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with thrombocytopenia virus) |
A0A0B5AC95 | INS1A_CONGE | MTTSSYFLLMALGLLLYVCQSSFGNQHTRTFDTPKHRCGSEITNSYMDLCYRKRNDAGEKRGRASPLWQRRGSLSKLKARAKRNGAFHLPRDGRGVVEHCCHRPCSNAEFKKYCG | null | null | glucose metabolic process [GO:0006006] | extracellular region [GO:0005576] | hormone activity [GO:0005179]; toxin activity [GO:0090729] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25605914}. | null | null | null | null | null | FUNCTION: This venom insulin, from a fish-hunting cone snail, facilitates prey capture by rapidly inducing hypoglycemic shock (PubMed:25605914, PubMed:27617429). It is one of the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the ins... | Conus geographus (Geography cone) (Nubecula geographus) |
A0A0B5KYT4 | MPDE2_PENBR | MESLSLTWITAIAVVLYLVQRYVRSYWRLKDIPGPVLAKLTDLQRVWWVKTGRAHEFHRDMHAMYGPIVRFGPNMVSVSDPRVIPTIYPSRPGFPKGDFYRTQKPYTRNKGAMPAVFNTQDEDLHKQLRSPIASLYSMTNVVRLEPLVDETLTVLSKQLDERFVGTNDKPFDLGDWLQYFAFDSMGTLTFSRRYGFLEQGRDMHGILQEIWNFMTRVAVMGQIPWFDEIWNKNSFITLFKRPTGFGVLKVVDNFISQRVSSRENDEKADEKDMLSQFLNIQASNPHSIMPWAPRAWTFSNVMAGSDSTANVMRTMMYNLL... | 1.-.-.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | mycophenolic acid biosynthetic process [GO:0140722]; terpenoid biosynthetic process [GO:0016114] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218] | PF00753;PF00067; | 1.10.630.10;3.60.15.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31209052}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=5-methylorsellinate + O2 + reduced [NADPH--hemoprotein reductase] = 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66668, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31209052}. | null | null | FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:31209052). MpaDE' is an endoplasmic reticulum-bound enzyme that ca... | Penicillium brevicompactum |
A0A0B5LB55 | MPAH2_PENBR | MSTEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKREGPVPDDAITFIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNEDKLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHSFGGNIITNLAYLHPRLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRANRAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPVTLTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRPEPRSTFRRLETLRPSCLW... | 3.1.1.- | null | mycophenolic acid biosynthetic process [GO:0140722]; terpenoid biosynthetic process [GO:0016114] | peroxisomal matrix [GO:0005782] | fatty acyl-CoA hydrolase activity [GO:0047617]; hydrolase activity [GO:0016787]; polyketide synthase activity [GO:0016218] | PF12697; | 3.40.50.1820; | AB hydrolase superfamily, MpaH hydrolase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:31209052}. Note=The mpaH' location in peroxisomes is required for the unique cooperation between biosynthetic and beta-oxidation catabolism machineries to produce final MPA. {ECO:0000269|PubMed:31209052}. | CATALYTIC ACTIVITY: Reaction=H2O + mycophenolyl-CoA = CoA + H(+) + mycophenolate; Xref=Rhea:RHEA:66704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:62932, ChEBI:CHEBI:167447; Evidence={ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=722.3 uM for acetyl-CoA {ECO:0000269|PubMed:31209052}; KM=351.5 uM for propionyl-CoA {ECO:0000269|PubMed:31209052}; KM=76.37 uM for malonyl-CoA {ECO:0000269|PubMed:31209052}; KM=201.9 uM for isobutyryl-CoA {ECO:0000269|PubMed:31209052}; KM=780.83 uM for isovaleryl-... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134}. | null | null | FUNCTION: Type I acyl-CoA thioesterase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:31209052, PubMed:33843134). MpaH' acts as a peroxisomal acyl-CoA hy... | Penicillium brevicompactum |
A0A0B6CGH9 | F7ODM_OCIBA | MRITLQYIKLESKNTKERDMAESKAIGRSLEVPNVQELAKGKLASVPARYVRYSDRENTTLPPLTQIPVIDMQALLHPNSFEAELNSLHKACKQWGFFQLINHGVEAAVMEKMKLEMQEFFNLPLEEKQKFRQSADDMEGYGQSFVVSDEQKLDWADGFSVISLPTYLRKPHLIPKLPAPFRDAIDAYGAQLKELAIKILGFMAEALGMDPHEMTALFEEGIQALRMNYYPPCPQPEMVSGLCPHSDAGGLTILMQVNEVEGLQVRKDGGWVPVSPLPDAFIINLGDILEIVTNGEYFSVEHQATVNGDKERLSVAAFLN... | 1.14.13.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q94LP4}; | coumarin biosynthetic process [GO:0009805]; response to molecule of fungal origin [GO:0002238] | cytoplasm [GO:0005737] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; metal ion binding [GO:0046872] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q94LP4}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + gardenin B + O2 = CO2 + formaldehyde + H(+) + nevadensin + succinate; Xref=Rhea:RHEA:73443, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:79628, ChEBI:CHEBI:192756; Evidence={ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.46 uM for gardenin B {ECO:0000269|PubMed:25378691}; KM=20.98 uM for 2-oxoglutarate {ECO:0000269|PubMed:25378691}; KM=4.02 uM for Fe(2+) {ECO:0000269|PubMed:25378691}; KM=7.651 uM for ascorbate {ECO:0000269|PubMed:25378691}; Vmax=1.267 pmol/sec/mg enzyme with gard... | PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Oxoglutarate-dependent dioxygenase (2-ODD) acting as a flavonoid 7-O-demethylase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-al... | Ocimum basilicum (Sweet basil) |
A0A0B7P3V8 | YP41B_YEAST | MATPVRDETRNVIDDNISARIQSKVKTNDTVRQTPSSLRKVSIKDEQVKQYQRNLNRFKTILNGLKAEEEKLSETDDIQMLAEKLLKLGETIDKVENRIVDLVEKIQLLETNENNNILHEHIDATGTYYLFDTLTSTNKRFYPKDCVFDYRTNNVENIPILLNNFKKFIKKYQFDDVFENDIIEIDPRENEILCKIIKEGLGESLDIMNTNTTDIFRIIDGLKNKYRSLHGRDVRIRAWEKVLVDTTCRNSALLMNKLQKLVLMEKWIFSKCCQDCPNLKDYLQEAIMGTLHESLRNSVKQRLYNIPHNVGINHEEFLIN... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; transposition [GO:0032196] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF00665; | 3.30.420.10; | null | PTM: Proteolytically processed into capsid protein (CA), Ty4 protease (PR), integrase (IN) and reverse transcriptase/ribonuclease H (RT) proteins (By similarity). Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tR... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. {ECO:0000250}.; FUNCTION: The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
A0A0B7P9G0 | UEX_DROME | MNTYFISFITIIIFANGINGTSVDTSNKLLLQKANDFNLSQNLSSSRTRRTIANSFRIVGIRLEDETVETKNGIPTVLVDKEQQFRVFGSGLEENTAITFTNEKNDYGGPCLKPATDLFTPIEVSSNGFSALYSVKFPSFINEFFICAKTAEKTTNHSKAATTTPLEHQGNSDFLKIKTFEPLIPVWLAIIIIVTCLGFSALFSGLNLGLMSMDRTELKILRNTGTEKEKKYASKIAPVRDQGNYLLCSILLGNVLVNSTFTILLDGLTSGLFAVIFSTLAIVLFGEITPQAVCSRHGLAIGAKTILVTKTVMAITAPLS... | null | null | cellular response to carbon dioxide [GO:0071244]; export across plasma membrane [GO:0140115]; intracellular manganese ion homeostasis [GO:0030026]; intracellular monoatomic ion homeostasis [GO:0006873]; long-term memory [GO:0007616]; magnesium ion homeostasis [GO:0010960]; magnesium ion transmembrane transport [GO:1903... | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | magnesium ion transmembrane transporter activity [GO:0015095]; transmembrane transporter activity [GO:0022857] | PF01595; | 3.10.580.10;2.60.120.10; | ACDP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31404830}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Probable metal transporter (By similarity). Acts downstream of PRL-1 and protects the nervous system against olfactory carbon dioxide stimulation (PubMed:31404830). {ECO:0000250|UniProtKB:Q3TWN3, ECO:0000269|PubMed:31404830}. | Drosophila melanogaster (Fruit fly) |
A0A0C3RR82 | PGMA1_PHLG1 | MSSASSDSNTGSLTIAGSGIASVRHMTLETLAHVQEADIVFYVVADPVTEAYIKKNARGPCKDLEVLFDKDKVRYDTYVQMAETMLNAVREGQKVLGIFYGHPGVFVSPSRRALSIARKEGYQAKMLPGISSEDYMFADLEFDPAVHGCCAYEATQLLLREVSLDTAMSNIIWQVGGVGVSKIDFENSKVKLLVDRLEKDFGPDHHVVHYIGAVLPQSATVQDVLKISDLRKEEIVAQFNSCSTLYVPPLTHANKFSGNMVKQLFGQDVTEVSSALCPTPKWAAGSHLGDVVEYGPREKAAVDALVEHTVPADYRVLGGS... | 2.1.1.- | null | methylation [GO:0032259] | null | methyltransferase activity [GO:0008168] | PF00590; | null | Precorrin methyltransferase family | PTM: PgiMA1 automethylates at Asp-421, Asp-434, Asp-447, Asp-460, Asp-473, Asp-486, Asp-499, Asp-512, Asp-525 and Asp-538 before being processed, probably by the M64 family peptidase found in the genes surrounding PgiMA1, to release methylated peptides which then undergos macrocyclization with the N-terminus of the mod... | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:31117659}. | null | null | FUNCTION: Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities (PubMed:31117659). Type II borosins derive from the C-terminus of the fusion pr... | Phlebiopsis gigantea (strain 11061_1 CR5-6) (White-rot fungus) (Peniophora gigantea) |
A0A0C3VJP4 | SCP1_MEDTR | MEKVSLYACLILNLSLLVIFPYSKASQADKLNEFILSRKSQNPPKTLSWEEGDALKTLFSSAAYVAPPQEELRLADKIVTLPGQPYGVNFDQYSGYVTVDPETGRELFYYFVESPCNSSTKPLVLWLNGGPGCSSLGYGAFQELGPFRVNSDGKTLYRNPYAWNEVANVLFLESPAGIGFSYSNTTSDYDKSGDKSTAKDSYVFLINWLERFPQYKTRDFYISGESYAGHYVPQLASTILHNNKLYKNTIINLKGISLGNAWIDDATSLKGLYDNLWTHALNSDQTHELIEKYCDFTKQNYSAICTNAMNMSMIEKGKID... | 3.4.16.- | null | arbuscular mycorrhizal association [GO:0036377]; proteolysis [GO:0006508]; response to symbiotic fungus [GO:0009610] | apoplast [GO:0048046]; extracellular space [GO:0005615]; vacuole [GO:0005773] | serine-type carboxypeptidase activity [GO:0004185] | PF00450; | 3.40.50.11320;6.10.250.940;3.40.50.1820; | Peptidase S10 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23662629}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:23662629}. | null | null | null | null | null | FUNCTION: Carboxypeptidase that, together with KPI106, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis). {ECO:0000269|PubMed:23662629}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A0A0C5B5G6 | MOTSC_HUMAN | MRWQEMGYIFYPRKLR | null | null | activation of protein kinase activity [GO:0032147]; negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:2001145]; osteoblast differentiation [GO:0001649]; osteoblast proliferation [GO:0033687]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; purine-co... | extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25738459}. Mitochondrion {ECO:0000269|PubMed:29983246}. Nucleus {ECO:0000269|PubMed:29983246, ECO:0000269|PubMed:33473109}. Note=Translocates to the nucleus in response to metabolic stress in an AMPK-dependent manner. {ECO:0000269|PubMed:29983246}. | null | null | null | null | null | FUNCTION: Regulates insulin sensitivity and metabolic homeostasis (PubMed:25738459, PubMed:33468709). Inhibits the folate cycle, thereby reducing de novo purine biosynthesis which leads to the accumulation of the de novo purine synthesis intermediate 5-aminoimidazole-4-carboxamide (AICAR) and the activation of the meta... | Homo sapiens (Human) |
A0A0C5CJR8 | APRA_PSEMA | MSKAKDKAIVSAAQASTAYSQIDSFSHLYDRGGNLTINGKPSYTVDQAATQLLRDGAAYRDFDGNGKIDLTYTFLTSASSSTMNKHGISGFSQFNAQQKAQAALAMQSWSDVANVTFTEKASGGDGHMTFGNYSSGQDGAAAFAYLPGTGAGYDGTSWYLTNNSYTPNKTPDLNNYGRQTLTHEIGHTLGLAHPGDYNAGEGAPTYNDATYGQDTRGYSLMSYWSESNTNQNFSKGGVEAYASGPLIDDIAAIQKLYGANYNTRAGDTTYGFNSNTGRDFLSATSNADKLVFSVWDGGGNDTLDFSGFTQNQKINLNEAS... | 3.4.24.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q03023}; Note=Binds 8 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:Q03023}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q03023}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q03023}; | collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270] | PF00353;PF00413;PF08548; | 3.40.390.10;2.150.10.10; | Peptidase M10B family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. At higher temperatures, the activity decreases rapidly. Shows high enzyme activity with casein as a substrate under the storage conditions of UHT milk. Is highly thermostable. Withstands general ultra-high temperature (UH... | FUNCTION: Peptidase able to cleave azocasein and the milk substrates beta-casein and Na-caseinate. Can withstand UHT processing of milk, and is able to spoil UHT milk over the storage period. {ECO:0000269|Ref.1}. | Pseudomonas marginalis (Pseudomonas panacis) |
A0A0C5PHQ7 | ELOV5_TACFU | MEILNQRLNQQFDSWMGPRDPRVRGWLLLDNYLPTLSFTIIYLLIVWMGPKYMRNRQPVSCRGILVVYNMALTLLSLYMFYELVTAVWQGGYNFFCQDTHSGGEADNRVINVLWWYYFSKLIEFMDTFFFILRKNNHQITFLHIYHHFTMLNIWWFVMNWVPCGHSYFGATFNSFIHVLMYSYYGLSAIPAIQPYLWWKKYITQGQLVQFVLTMIQTSCAVVWPCGFPKGWLYFQISYMITLIILFSNFYIQTYKKKGTAAKKDPRHNGIKSVNGHSNGASHTNAVKNRKARTD | 2.3.1.199 | null | fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid bi... | dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789] | fatty acid elongase activity [GO:0009922] | PF01151; | null | ELO family, ELOVL5 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000255|HAMAP-Rule:MF_03205}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0... | CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03205, ECO... | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03205}. | null | null | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that... | Tachysurus fulvidraco (Yellow catfish) (Pimelodus fulvidraco) |
A0A0C5Q4Y6 | C76H2_ROSOF | MDSFPLLAALFFILAATWFISFRRPRNLPPGPFPYPIVGNMLQLGTQPHETFAKLSKKYGPLMSIHLGSLYTVIVSSPEMAKEIMHKYGQVFSGRTVAQAVHACGHDKISMGFLPVGGEWRDMRKICKEQMFSHQSMEDSQWLRKQKLQQLLEYAQKCSERGRAIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLAIIEGFLNERVESRRTNPNAPKKDDFLETLVDTLQTNDNKLKTDHLTHLMLDLFVGGSETSTTEIEWIMWELLANPEK... | 1.14.14.-; 1.14.14.175; 1.14.14.60 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1}; | diterpenoid biosynthetic process [GO:0016102] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=abieta-8,11,13-triene + O2 + reduced [NADPH--hemoprotein reductase] = ferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48080, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30468448}. | null | null | FUNCTION: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of abietatriene to produce ferruginol (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol (PubMed:... | Rosmarinus officinalis (Rosemary) (Salvia rosmarinus) |
A0A0C5QRZ2 | C76H2_SALFT | MDPFPLVAAALFIAATWFITFKRRRNLPPGPFPYPIVGNMLQLGSQPHETFAKLSKKYGPLMSIHLGSLYTVIISSPEMAKEIMHKYGQVFSGRTIAQAVHACDHDKISMGFLPVGAEWRDMRKICKEQMFSHQSMEDSQNLRKQKLQQLLEYAQKCSEEGRGIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLGLIEGYLNERIEFRKANPNAPKKDDFLETLVDALDAKDYKLKTEHLTHLMLDLFVGGSETSTTEIEWIMWELLASPEKM... | 1.14.14.-; 1.14.14.175; 1.14.14.60 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1}; | diterpenoid biosynthetic process [GO:0016102] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=abieta-8,11,13-triene + O2 + reduced [NADPH--hemoprotein reductase] = ferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48080, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30468448}. | null | null | FUNCTION: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of abietatriene to produce ferruginol (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol (PubMed:... | Salvia fruticosa (Greek sage) |
A0A0C5XL88 | PART_SPHYB | MTTSFWRIATDARTYEADDLSGAGAKITGGRWNEVGVAIVYAASSRALACLETVVHLNSGGLPLNRYLVEIEVPDEVLASAEVATPGNLPVGWDAEPAGRVSISFGSQWAQSQRTALLLVPSVIVPEETNLLINPAHPDAKGIKARKVRKWLYDPRMIRKA | 2.4.2.- | null | null | null | glycosyltransferase activity [GO:0016757]; nucleotidyltransferase activity [GO:0016779] | PF08808; | null | MbcT/ParT/Res family | PTM: Consumes NAD(+) and auto-ADP-ribosylates on the tryptic fragment Ala-47-Arg-66 in vitro. Also auto-ADP-ribosylates using NADP(+). {ECO:0000269|PubMed:30598453}. | null | null | null | null | null | null | FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Expression in E.coli inhibits cell growth; bacteriostasis is neutralized by expression of cognate antitoxin ParS. ADP-ribosylates E.coli ribose-phosphate pyrophosphokinase (RPPK, prs) using NAD(+) in vitro; ADP-ribosylates RPPK on 'Lys-182' and 'Ser-20... | Sphingobium sp. (strain YBL2) |
A0A0C6DRW4 | DSZC1_RHOER | MTLSPEKQHVRPRDAADNDPVAVARGLAEKWRATAVERDRAGGSATAEREDLRASGLLSLLVPREYGGWGADWPTAIEVVREIAAADGSLGHLFGYHLTNAPMIELIGSQEQEEHLYTQIAQNNWWTGNASSENNSHVLDWKVRATPTEDGGYVLNGTKHFCSGAKGSDLLFVFGVVQDDSPQQGAIIAAAIPTSRAGVTPNDDWAAIGMRQTDSGSTDFHNVKVEPDEVLGAPNAFVLAFIQSERGSLFAPIAQLIFANVYLGIAHGALDAAREYTRTQARPWTPAGIQQATEDPYTIRSYGEFTIALQGADAAAREAA... | 1.14.14.21 | null | dibenzothiophene catabolic process [GO:0018896]; leucine catabolic process [GO:0006552] | cytoplasm [GO:0005737] | flavin adenine dinucleotide binding [GO:0050660]; isovaleryl-CoA dehydrogenase activity [GO:0008470]; monooxygenase activity [GO:0004497] | PF08028;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | DszC flavin monooxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|Ref.2}. | CATALYTIC ACTIVITY: Reaction=dibenzothiophene + 2 FMNH2 + 2 O2 = dibenzothiophene 5,5-dioxide + 2 FMN + 2 H(+) + 2 H2O; Xref=Rhea:RHEA:49072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23681, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90356; EC=1.14.14.21; Evidence={ECO:0000269|Ref.2}; ... | null | PATHWAY: Sulfur metabolism; dibenzothiophene degradation. {ECO:0000305|PubMed:25627402}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|Ref.2}; | FUNCTION: Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner (PubMed:11229908, Ref.2). Also acts on thioxa... | Rhodococcus erythropolis (Arthrobacter picolinophilus) |
A0A0D1DWQ2 | CMU1_USTMA | MKLSVSIFVLLAVSAFGGGSAAAVSGKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGGRAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTRPLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPTNMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVLLGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLTDHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRLFQAYLIPITTQIEAAAILDHANKCT | 5.4.99.5 | null | aromatic amino acid family biosynthetic process [GO:0009073]; chorismate metabolic process [GO:0046417]; effector-mediated suppression of host salicylic acid-mediated innate immune signaling [GO:0140502] | extracellular region [GO:0005576]; host apoplast [GO:0140593]; host cell cytosol [GO:0044164] | chorismate mutase activity [GO:0004106] | null | 1.10.590.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21976020}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:21976020}. Note=Is translocated to host plant cells and spreads to neighboring tissue. The spreading is likely to occur through plasmodesmata. {ECO:0000269|PubMed:21976020}. | CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; Evidence={ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:306516... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 mM for chorismate {ECO:0000269|PubMed:30651637}; Vmax=40.8 umol/min/mg enzyme {ECO:0000269|PubMed:30651637}; Vmax=21.1 umol/min/mg enzyme (when bound to host KWL1) {ECO:0000269|PubMed:30651637}; | null | null | null | FUNCTION: Secreted chorismate mutase that is one component of a cocktail of effectors shaping the host metabolome and acting as virulence factors. The enzyme is taken up by plant cells, can spread to neighboring cells where it affects the biosynthesis of the plant immune signal salicylic acid by channelling chorismate ... | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
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