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) |
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