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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A0A0N9E2K8 | MMP21_DANRE | MLTVIRRIFIIQTFIFITAEKIFHSRDHSDVLNNIHQAELITDTDTAQRFLSKYGFIKAAGSEESQLSESSGDLDFSLSLDLHEGGTTSGSSSSDLQFVSALRDFQRLSDLPVTGVFDDATKAAMNKPRCGVMDDDQELKDVTGSNSTRNHIRTSTNTSHNHEHQAPVRKKRHLSALLKNTSLQKRDVSKWTGHMAFSKSVLKWRLIGEGYSSQLSIQEQKYIFRLAFRMWSEISPLQFIEDLHSPLENIDIRLGFGTGRHLGCSQRFDGAGREFAHAWFLGDIHFDDDEHFTVPNTGSGISLLKVAVHEIGHVLGLPHI... | 3.4.24.- | null | collagen catabolic process [GO:0030574]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right symmetry [GO:0007368]; embryonic heart tube left/right pattern formation [GO:0060971]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; regulation of heart looping [GO:... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway. {ECO:0000269|PubMed:26429889, ECO:0000269|PubMed:26437028}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0N9HMN6 | POMT3_SINHE | MEMAPTMDLEIRNGNGYGDSGEELLAAQAHIYNHIFNFISSMALKCAVELNIPEILHNHQPKAVTLSELVQALQIPQAKSACLYRLLRILVHSGFFAITKIQSEGDEEGYLPTLSSKLLLKNHPMSMSPCLLGLVNPTMVAPMHFFSDWFKRSDDMTPFEATHGASLWKYFGETPHMAEIFNEAMGCETRLAMSVVLKECKGKLEGISSLVDVGGGTGNVGRAIAEAFPNVKCTVLDLPQVVGNLKGSNNLEFVSGDMFQFIPPADVVFLKWILHDWNDEECIKILKRCKEAIPSKEEGGKLIIIDMVVNDHNKGSYEST... | 2.1.1.323 | null | aromatic compound biosynthetic process [GO:0019438]; melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]; phenylpropanoid biosynthetic process [GO:0009699]; response to wounding [GO:0009611] | null | acetylserotonin O-methyltransferase activity [GO:0017096]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(-)-pluviatolide + S-adenosyl-L-methionine = (-)-bursehernin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49036, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90893, ChEBI:CHEBI:90896; EC=2.1.1.323; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for (-)-pluviatolide {ECO:0000269|PubMed:26359402}; Vmax=1.7 nmol/min/mg enzyme with (-)-pluviatolide as substrate {ECO:0000269|PubMed:26359402}; Note=kcat is 0.72 sec(-1) with (-)-pluviatolide as substrate. {ECO:0000269|PubMed:26359402}; | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}. | null | null | FUNCTION: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the methylation of (-)-pluviatolide to produce (-)-bursehernin (PubMed:26359402). {ECO:0000269|PubMed:26359402}. | Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum) |
A0A0N9HTA1 | DOMT1_SINHE | MDTRADAEIKAMELIGIGVLPLAMKAIIELNVLEILSKAGPDTQLTAAQIVTDIPTTNPNAGFQLDRILRLLASHSVLSSSITKSGERVYGLTPMCKYFLPDQDGVSLAPMVVTIHDKVLLQSWHYLKDSVLKQGSLPFTEAFGMSPFEYSVSDTRFNKVFNAGMFDHSTLCMRDVLQRYKGFQGLGELVDVGGGTGGSLKMILSQYPNLKGINFDLPHVVADAPSFPGVKHIGGDMFESVPSGDAIFMKWILHDWDDGRCLTLLKNCWNALPEHGKVIIVEWILPSDAATDPTSRRVFTADLMMLAFSEGGKERTLGDY... | 2.1.1.330 | null | aromatic compound biosynthetic process [GO:0019438]; methylation [GO:0032259]; phenylpropanoid biosynthetic process [GO:0009699]; response to wounding [GO:0009611] | null | O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(-)-5'-demethylyatein + S-adenosyl-L-methionine = (-)-yatein + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49040, ChEBI:CHEBI:4553, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90894; EC=2.1.1.330; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=l... | null | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}. | null | null | FUNCTION: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the methylation of (-)-5'-demethylyatein to produce (-)-yatein (PubMed:26359402). {ECO:0000269|PubMed:26359402}. | Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum) |
A0A0N9NCU6 | YOPJ_YERPU | MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV | 2.3.1.- | COFACTOR: Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130; Evidence={ECO:0000250|UniProtKB:O68718}; | negative regulation of JNK cascade [GO:0046329]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of p38MAPK cascade [GO:1903753]; peptidyl-serine O-acetylation [GO:0030919]; peptidyl-threonine O-acetylation [GO:0120258] | extracellular region [GO:0005576] | O-acetyltransferase activity [GO:0016413]; toxin activity [GO:0090729] | PF03421; | null | Acetyltransferase YopJ family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DUD0}. Note=Secreted via type III secretion system (T3SS). {ECO:0000250|UniProtKB:P0DUD0}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141025; Evidence={ECO:0000269|PubMed:16728640}; PhysiologicalDirection=left-to-righ... | null | null | null | null | FUNCTION: Serine/threonine-protein acetyltransferase translocated into infected cells, which inhibits the host immune response and induces cell death by mediating acetylation of target proteins (PubMed:10489373, PubMed:12433923, PubMed:16728640, PubMed:22563435, PubMed:26810037). Inhibits the MAPK and NF-kappa-B signal... | Yersinia pseudotuberculosis |
A0A0P0VIP0 | LRSK7_ORYSJ | MPPRCRRLPLLFILLLAVRPLSAAAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPH... | 2.7.11.1 | null | defense response to bacterium [GO:0042742]; defense response to oomycetes [GO:0002229]; pollen aperture formation [GO:0062075]; pollen development [GO:0009555]; protein autophosphorylation [GO:0046777] | cytosol [GO:0005829]; plasma membrane [GO:0005886]; pollen aperture [GO:0062074] | ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; kinase activity [GO:0016301]; protein serine/threonine kinase activity [GO:0004674] | PF00139;PF00069; | 2.60.120.200;1.10.510.10; | Leguminous lectin family; Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated at Thr-376; Ser-378; Thr-386; Thr-403 and Thr-657. {ECO:0000269|PubMed:31833176}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31833176, ECO:0000269|PubMed:32284546}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:32284546}. Note=During meiosis, localizes diffusely in the cytosol and plasma membrane of microspore mother cells (MMCs). During tetra... | 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:31833176}; Physiolog... | null | null | null | null | FUNCTION: Legume-lectin receptor-like kinase required for normal pollen development and male fertility (PubMed:31833176, PubMed:32284546). Regulates pollen exine assembly and aperture development (PubMed:31833176, PubMed:32284546). Plays a critical role in annulus formation, and may participate in the formation of the ... | Oryza sativa subsp. japonica (Rice) |
A0A0P0WGX7 | ENL1_ORYSJ | MASPPPFDICGDLDDDPTPPAPTPLAAPTPNGLNDRLLRLTRTHQRGPSQNPNPNPNPNPKPPPPPPPQEPEPAKVKLAGRRRLCKLSTAGDESAGDDDSIRDILDDLTTRLDSLSVDRPTARPRPHVSPLPCALHADPDPSQSQLNDGTKPSSSFVDCDDDDDDAGGAYGGFGVKEEVTRKVFKASSSFGGRGNDDKMKAKGAYAFDTVSRKTTTESKASKFFGDYDDEDDIDQDAENGKENHADDVGWEKTEDFKMEPTGTGVTRKPYNLPGRIFNMLYPHQREGLRWLWVLHCRGTGGILGDDMGLGKTMQVSAFLA... | 3.6.4.- | null | cell division [GO:0051301]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; reciprocal meiotic recombination [GO:0007131]; regulation of endosperm development [GO:2000014]; regulation of mitotic sister chromatid separation [GO:0010965]; transcription-coupled nucleotide-excision repair ... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787] | PF00271;PF00176; | 3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25327517}. Chromosome {ECO:0000269|PubMed:25327517}. Note=Localizes to the cytoplasm during interphase, but moves to the chromosome arms during mitosis. {ECO:0000269|PubMed:25327517}. | null | null | null | null | null | FUNCTION: DNA helicase that acts as an essential component of the spindle assembly checkpoint (By similarity). Plays an indispensable role in the development of seed endosperm (PubMed:25327517). Is required to secure sister chromosome separation during endosperm syncytial mitosis, which involves extremely rapid free nu... | Oryza sativa subsp. japonica (Rice) |
A0A0P0X9Z7 | CWZF7_ORYSJ | MLSVRRRQEDARGVGLRGGAAAGGMEDDAELEEGEACGDETAFVDPDVALSYIDEKIQDVLGHFQKDFEGAVSAENLGSKFGGYGSFLPTYQRSPLPQTRSPPKAANVSSRSPYHQPTESMSQNTLAVAAPSVSKHNGSMVPLSDDSSKKEVHQSTKVERASSTQDSLNGLSKSSDHNRFKVRIKVGSDNGLARNNAAIYSGLGLDISSPSSIEDSPDGCGSLSPEFNNVPIESPRTILQIMTCFSVPGGFLLSPLRDDLVQLTQKVVPTSKKWETNANTENVQERYEGYAAKRVKSDAKKKKAVDTKRSKSRNDVSAVM... | null | null | positive regulation of DNA-templated transcription [GO:0045893]; regulation of seed growth [GO:0080113] | nucleus [GO:0005634] | sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270] | PF07496; | 3.30.40.100; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28818372}. Note=Exhibits a speckle-like distribution in the nucleus. {ECO:0000269|PubMed:28818372}. | null | null | null | null | null | FUNCTION: Transcriptional activator that acts as a positive regulator of grain size (PubMed:31830332). Binds directly to the DNA core sequence 5'-CATTTC-3' found in the promoter of MADS1, and activates MADS1 transcription (PubMed:31830332). Increases grain width via direct up-regulation of MADS1 expression (PubMed:3183... | Oryza sativa subsp. japonica (Rice) |
A0A0P0XCU3 | SSY3A_ORYSJ | MEMALRPQSLLCPRSRLKVVIRPASSASGGGLAQYFLMTRRYTGSRIVRCMVSSSDCPNRKAKRTISLHTEVASSRGYAPRIAAESSIQEREHINSDEETFDTYNRLLRNESTEWKKLDTTEVDLSQDVSSSSMRKVDATDEAKLDILEDDLPRNLLNGVTMGEVDMLDEAGAEDDVFEVDLSALHNSTVGKMDAVNEVGTENDLFEVDLSALHSAAVGKVDVVDGAKAKEDLFEMDSLALHSVTMGKVDAINAAGAEGDKFEVDLSALASNNSMIEAVNVMDEAKAIEDTLEVDLSGNATSSSTYGEVKFEVDSLGNTS... | 2.4.1.21 | null | amylopectin biosynthetic process [GO:0010021]; endosperm development [GO:0009960]; starch biosynthetic process [GO:0019252] | amyloplast [GO:0009501]; chloroplast [GO:0009507] | alpha-1,4-glucan synthase activity [GO:0033201]; glycogen (starch) synthase activity [GO:0004373]; starch binding [GO:2001070]; starch synthase activity [GO:0009011] | PF16760;PF08323;PF00534; | 3.40.50.2000;2.60.40.10; | Glycosyltransferase 1 family, Bacterial/plant glycogen synthase subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. Plastid, amyloplast {ECO:0000305}. Note=Amyloplast or chloroplast, soluble. {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21; Evidence={ECO:0000305}; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Involved in starch synthesis in endosperm amyloplasts (PubMed:17297616, PubMed:17586688, PubMed:21417378, PubMed:21595523, PubMed:21730357). Plays an important role in the elongation of amylopectin B chains (PubMed:17297616, PubMed:17586688, PubMed:21417378, PubMed:21595523, PubMed:21730357). {ECO:0000269|Pub... | Oryza sativa subsp. japonica (Rice) |
A0A0P0XII1 | CERK1_ORYSJ | MEASTSLLVLVLAAAAFAAGTVTEAAGDGCSAGCDLALASFYVTPNQNVTNMADLFGIGAANYRSLAPYNPNIPNLDFINVGGRVNVYFTCGCRSLPGSPGATYLAGAFPFQMSRGQIYTSVAANYNNLTTAEWLQATNSYPANNIPDTAVINATVNCSCGDASISPDYGLFLTYPLRAEDTLASVAATYGLSSQLDVVRRYNPGMESATGSGIVYIPVKDPNGSYLPLKSPGKGASAGAIAGGVVAGVVVLAAIFLYIIFYRRRKAKQATLLQSSEDSTQLGTISMDKVTPSTIVGPSPVAGITVDKSVEFSYEELSNA... | 2.7.11.1 | null | innate immune response [GO:0045087]; phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; chitin binding [GO:0008061]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transmembrane receptor protein kinase activity [GO:0019199] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated; induced by chitin and derivatives. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24964058, ECO:0000269|PubMed:25335639}; Single-pass 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:0000269|PubMed:23498959}; CATALYTIC... | null | null | null | null | FUNCTION: Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses. Involved in the resistance to pathogenic fungi, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-... | Oryza sativa subsp. japonica (Rice) |
A0A0P0ZBS7 | MENC_GEOSE | MAINIEYVILRHLQMELKAPFTTSFGTFQRKELILVEVVDRDGVSGWGESVAFSAPWYSEETVKTNWHMLEDFLVPLALAEPIHHPEELSKRFSAIRQNNMAKAALEGAVWDLYAKRLGVPLSQALGGAKKDIEVGVSIGIQPTVADLLQVIERYVAQGYRRIKVKIKPSWDVDVIREVRRVFPDVPLMADANSAYTLVDADRLKALDEFGLLMIEQPLAADDLVDHARLQPLLQTPICLDESIRSYDDARKALDLGSCRIINIKIGRVGGLGEAKRIHDLCAERGAPVWCGGMLEAGVGRAHNIAITTLENFTLPGDTA... | 4.2.1.113; 5.1.1.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|PubMed:25875730}; Note=Shows highest activity in vitro with Co(2+) and Ni(2+). {ECO:0000269|PubMed:25875730}; | menaquinone biosynthetic process [GO:0009234] | null | isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; O-succinylbenzoate synthase activity [GO:0043748] | PF13378;PF02746; | 3.20.20.120;3.30.390.10; | Mandelate racemase/muconate lactonizing enzyme family, MenC type 2 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377, ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113; Evidence={ECO:0000255|HAMAP-Rule:MF_01933}; CATALYTIC ACTIVITY: Reaction=N(alpha)-acetyl-D-methionine = N(a... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.6 mM for N-formyl-D-methionine {ECO:0000269|PubMed:25875730}; KM=9 mM for N-formyl-L-methionine {ECO:0000269|PubMed:25875730}; KM=11.1 mM for N-formyl-D-norleucine {ECO:0000269|PubMed:25875730}; KM=12.5 mM for N-formyl-L-norleucine {ECO:0000269|PubMed:25875730};... | PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_01933}.; PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01933}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:25875730}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55-65 degrees Celsius. {ECO:0000269|PubMed:25875730}; | FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (By similarity). Also acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-D/L-phenylalanine (PubMed:25875730). Can catalyze the racemization of a broad range of N-acylami... | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
A0A0P6JG37 | ASAH1_HETGA | MLGRSRLTFVLLAAAVTCAEAQHAPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMVDKGPMLKIIVNSFKNMVNTFVPSGKVMQMVDQKLPDLLGQFSGPYEEEMKGIADVTEIPLGEIISFNIFYELFTMCTSIITEDKKGHLLHVRNMDFGIFLGWNINNNTWVITEELKPLTVNLDFQRNSKTVFKATSFAGYVGMLTGFKPGQFSLTLNERFSMNGGYLGLLEWILGKKDASWIGFITRSVLENATSYEEAKNILAKTKLLAPAYFILGGNQSGEGCVITRERKDSLDIYELDPKQGRWYVVQTN... | 3.5.1.23 | null | fatty acid metabolic process [GO:0006631]; sphingolipid metabolic process [GO:0006665] | extracellular region [GO:0005576]; lysosome [GO:0005764] | ceramidase activity [GO:0102121]; fatty acid amide hydrolase activity [GO:0017064]; N-acylsphingosine amidohydrolase activity [GO:0017040] | PF02275;PF15508; | null | Acid ceramidase family | PTM: N-glycosylated. {ECO:0000269|PubMed:29692406}.; PTM: Proteolytically cleaved into two chains alpha and beta that remain associated via a disulfide bond (PubMed:29692406). Cleavage gives rise to a conformation change that activates the enzyme. The same catalytic Cys residue mediates the autoproteolytic cleavage and... | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q13510}. Secreted {ECO:0000250|UniProtKB:Q13510}. Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. {ECO:0000250|UniProtKB:Q13510}. | CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine; Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate ... | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:Q13510}. | null | null | FUNCTION: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes incl... | Heterocephalus glaber (Naked mole rat) |
A0A0R4I9Y1 | R213B_DANRE | MTRKRKSGKKGKPLAQKKEAQKRGGSTSSSTTQKEGAQKGDGSSSSSTTQKDGAQKRDDSTSSSSTAQKEEGQKSDGSTSSSTTNKEGAQKRDGSTSSRLQKKGPQKRKGSTSSSRAHSRSRSKSKQTSYPSQARSRSHGQHNISTTESGPLSKEAQTQTSASLLVDKDTQTETVGQASQQTQTEINGNTETAEVSQPPQLSHEDVEMEGTVQPRTKGSESDGEKEESVKRKKRKLSEIGEPAKETEDSTKLSHECEEKVGDNQKNEDTNKHYGGDSLKDLKSVTEEPKSYAAAAATGKTGKVSKEQTNQIEANQDSTME... | 2.3.2.-; 2.3.2.27; 3.6.4.- | null | defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein K63-linked ubiquitination [GO:0070534]; regulation of lipid metabolic process [GO:0019... | cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF13923;PF20173; | 3.40.50.300;3.30.40.10; | AAA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q63HN8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) ... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}. | null | null | FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity. Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccha... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IBK5 | R213A_DANRE | MKCPKCSHEALEKAPKFCSECGHKLQSQSYETTQGTPHDKSQTPSIVPQITNAEMDETGSESKSLEIQNANVSPKRPNENTSPNPKKKKRKKRKKEKKKKSGVSEGPSSLTSDLSDISLTDKEKKMDTDQSSDSDCSSCIVEDTPTPAEPSSHLSPPENETAGPAQLSASALTTGSSKDGEESIGTTQKPVSASASKAPLGVDQQTKEEKVKCKDEGQKSLSAKAQHTPNANVDQNANVQSDANIDKDSQNVEPQKSSSVKTKPSKSTVADPKKTESEKQKSGERDNENSTQPVSSPKLKRNQTEESQKMVFGPNSAPKK... | 2.3.2.-; 2.3.2.27; 3.6.4.- | null | blood circulation [GO:0008015]; defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein K63-linked ubiquitination [GO:0070534]; regulation of ... | cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00097;PF20173; | 3.40.50.300;3.30.40.10; | AAA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q63HN8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) ... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}. | null | null | FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (By similarity). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacteria... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IDX9 | NINJ1_DANRE | MASEAMELNGGVNRRDDPGARPQQGRMSRNTPLNMNHYANKKSAAESMLDIALLMANASQLKTVLELGPSFSFYIPLITLISISLTLQIIVGILLIFIVKWNLNDSSKHYILNLLENIVTALVFIVVVVNVFITAFGVQRPDDKTS | null | null | angiogenesis [GO:0001525]; cell adhesion [GO:0007155]; heart development [GO:0007507]; heterotypic cell-cell adhesion [GO:0034113]; killing of cells of another organism [GO:0031640]; leukocyte chemotaxis involved in inflammatory response [GO:0002232]; muscle cell differentiation [GO:0042692]; positive regulation of inf... | plasma membrane [GO:0005886]; synaptic membrane [GO:0097060] | cell adhesion mediator activity [GO:0098631]; lipopolysaccharide binding [GO:0001530]; membrane destabilizing activity [GO:0140912] | PF04923; | null | Ninjurin family | null | SUBCELLULAR LOCATION: [Ninjurin-1]: Cell membrane {ECO:0000250|UniProtKB:Q92982}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q92982}. Synaptic cell membrane {ECO:0000250|UniProtKB:O70131}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Effector of necroptotic and pyroptotic programmed cell death that mediates plasma membrane rupture (cytolysis) (By similarity). Acts downstream of Gasdermin (GSDMA, GSDMB, GSDMC, GSDMD, or GSDME) or MLKL during pyroptosis or necroptosis, respectively: oligomerizes in response to death stimuli and promotes pla... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IEW8 | ELAV4_DANRE | MFEISRTLNAALLSNEGSTETQWRQADLPQLQGWAEKGLLTQPKMIISNMEPQVTNGPNSATANGPSSNSRSCPSPMQTGGSNDDSKTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGPTGGSRGVGFIRFDKRIEAEEAIKGLNGQKPSGAAEPITVKFANNPSQKTSQALLSQLYQSPNRRYPGPLHHQAQRFRLDNLLNMAYGVKRFSPITIDSMTSLVGMNI... | null | null | axonogenesis [GO:0007409]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380] | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; growth cone [GO:0030426]; perikaryon [GO:0043204]; protein-containing complex [GO:0032991]; ribonucleoprotein complex [GO:1990904] | RNA binding [GO:0003723] | PF00076; | 3.30.70.330; | RRM elav family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O09032}. Perikaryon {ECO:0000250|UniProtKB:Q61701}. Cell projection, axon {ECO:0000250|UniProtKB:Q61701}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q61701}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q61701}. | null | null | null | null | null | FUNCTION: RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs (By similarity). Plays a role in the regulation of mRNA stability, alternative splicing and translation (By similarity). Binds to AU-rich element (ARE) sequences in the 3' untranslated region (3'UTR) of target mRNAs (By simil... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IFG5 | CFA53_DANRE | MLTAQRSRIRCREITGPAHSVALKARPPLSRDIDDIFVRRRKQEATRGEVLEFTKDQSSCDVRMRWERNTQRRVVSATVNRHLQDALDQYQMGIDEKRERLRELLESEELELFKEMEAKKETVLERQAKMHERAKTLRERRESERQRVVADKLDQLFREQSEELRAVQIKRRQDQVCTERESQIRTKEEVRRVQEEEEKLFAQMWESDRLAKEERHNLELQRQRENNLQQKAVLQTQMDMAEQQRIQAKELKQEEAQLLKDQREMLRLEAEREHRQKLQDQEKRRKQLDLSLRLKMKRLTRDRQEELALDMSILEQLLAQ... | null | null | cilium assembly [GO:0060271]; cilium movement [GO:0003341]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287] | axonemal microtubule [GO:0005879]; axoneme [GO:0005930]; ciliary base [GO:0097546]; extracellular region [GO:0005576] | null | PF13868; | null | CFAP53 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25504577}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25504577}. Note=In cilia of the pronephric kidney tubules, prominent localization along the axonemes and also detected at the ciliary base (PubMed:25504577). In cil... | null | null | null | null | null | FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). Regulates motility patterns of both 9+0 and 9+2 motile cilia through differential localization and recruitment of axonemal dynein components (B... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IKJ1 | CAPAM_DANRE | MTSENHTTIKADSALVMSPTGSTSQAAPFSPSTSKPIQELPDELIQAGWSKCWSKRENRPYYFNRFTNQSLWEMPVLGQHDVISDPLGLNAAPASGEANADAGLGNGQRKRHPSEDASQAGPNSFKRPKVEIPATPTTPTVPISPSTPGVKPWVNTTTDEKQGQASTPAPAPYRPSVVYWDLDIQTNAVIRERAPADHLPPHPEIELQRAQLTTKLRQHYHELCSQREGIEPPRESFNRWLLERKVVDKGLDPLLPSECDPVISPSMFREIMNDIPIRLSRIKYKEEARKLLFKYAEAAKKMIDSRNATPESRKVVKWNV... | 2.1.1.62 | null | mRNA methylation [GO:0080009]; positive regulation of translation [GO:0045727] | nucleus [GO:0005634] | mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity [GO:0016422]; RNA polymerase II C-terminal domain binding [GO:0099122]; S-adenosyl-L-methionine binding [GO:1904047] | PF12237;PF00397; | 1.20.1270.10;2.20.70.10; | CAPAM family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4Z3}. | CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:22744, Rhea:RHEA-COMP:11518, Rhea:RHEA-COMP:11519, ... | null | null | null | null | FUNCTION: Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs (PubMed:30467178). {ECO:0000269|PubMed:30467178}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IKU3 | RECK_DANRE | MSGCLQILTVLLCCRFWALVFSQDQSCCVHHAADIPRCRDACEQLASIRSESRLRHLLHRLPSYCPETLSELWICINNSLPGASRKSDGWVGLGCCELAISAECRRDCKQASSKNDISKVCKKDTENPLYSCITKNEMGSVCCSYAGRHTTCREYCQAIFRTDSSPTVSQISAVKEYCQSVSPPLILCVENYTRLHPTHRPIDSLHCCDRAEEAHCQLACKRILRTLSTEQEIMDGLISECGSQPLPQDPLWQCFLGSAHPPANTDPESPPIAKMDSAKLHCCFKANTSICRNMCVEISTSWGTQSWQEFDQHCEYNPVE... | null | null | blood vessel maturation [GO:0001955]; canonical Wnt signaling pathway [GO:0060070]; dorsal root ganglion development [GO:1990791]; extracellular matrix organization [GO:0030198]; negative regulation of metalloendopeptidase activity [GO:1904684]; regulation of angiogenesis [GO:0045765]; regulation of canonical Wnt signa... | plasma membrane [GO:0005886]; side of membrane [GO:0098552]; Wnt signalosome [GO:1990909] | coreceptor activity [GO:0015026]; endopeptidase inhibitor activity [GO:0004866]; metalloendopeptidase inhibitor activity [GO:0008191]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF07648; | 3.30.60.30; | RECK family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26051822, ECO:0000269|PubMed:27979830}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:A0A1D5PUP4}. Note=Colocalizes with adgra2 at the plasma membrane. {ECO:0000269|PubMed:26051822}. | null | null | null | null | null | FUNCTION: Functions together with adgra2 to enable brain endothelial cells to selectively respond to Wnt7 signals (wnt7a or wnt7b) (PubMed:26051822, PubMed:26657775). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (PubMed:26051822, ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IMY7 | TRPM2_DANRE | MDEAALEPTLVQTLAVSTAKGGRYLSLSPSFQRCSLASWIKENIKKKECCFYVEDGREGICKCGYPKVQHCDEAIKPEDYMGEQWDKHRHVRETPTDAFGDISFGGLGQKTGKYVRVSSDTSCENLYQLMTEQWKLRSPNLLISVTGGAKNFYIKTHLKDKFRRGLIKVAQTTGAWILTGGTHAGVMKHVGMAVRDYTLSSGSMEGQIVVIGVAPWGVIHNRSTLIHPEGRFPAYYSLDEQGQGRLSCLDINHTHFLLVDDGTQGHYGVEIELRARLEKLISKLSLGNRESGVTIPVVCVVLDGGPGTLNTIYNSMLNHT... | null | null | calcium ion transmembrane transport [GO:0070588]; protein homotetramerization [GO:0051289]; release of sequestered calcium ion into cytosol [GO:0051209] | plasma membrane [GO:0005886] | ADP-D-ribose binding [GO:0072570]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; ligand-gated calcium channel activity [GO:0099604]; ligand-gated monoatomic cation channel activity [GO:0099094]; mono-ADP-D-ribose binding [GO:0072571]; monoatomic ion channel activity [GO:0005216] | PF00520;PF18139; | 3.90.79.10; | Transient receptor (TC 1.A.4) family, LTrpC subfamily, TRPM2 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30250252}; Multi-pass membrane protein {ECO:0000269|PubMed:30250252}. | null | null | null | null | null | FUNCTION: Nonselective, voltage-independent cation channel that mediates Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as a ligand-gated ion channel. Binding of ADP-ribose to the cytoplasmic N-terminal region causes a conformation change; the channel is primed but still requires Ca(2+) bindin... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IVA4 | CC14A_DANRE | MTLDNLKHSAILSTLFKMADDNDLLGASEFIKDRLYFATLRSKPKSTANTHYFSTDEEFVYENFYADFGPLNLAMLYRYCCKLNKKLKSFTLTRKRIVHYTSFDQRKRANAAVLIGAYAVIYLKKTPEEAYRALISGSNASYLPFRDASFGNCTYNLTVLDCLQGIRKALQHGFLNFETFDVNEYEHYERVENGDLNWITPGKLLAFSGPHPKSKVENGYPLHAPEAYFPYFRKHNVTTIVRLNKKIYDAKRFTDAGFDHYDLFFVDGSTPSDIITRRFLHICESTSGAVAVHCKAGLGRTGTLIGCYLMKHYRFTSAEA... | 3.1.3.16; 3.1.3.48 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cilium assembly [GO:0060271]; dephosphorylation [GO:0016311]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of cytokinesis [GO:0032467]; regulation of exit from mitosis [GO:0007096] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinocilium [GO:0060091]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; spindle pole [GO:0000922] | myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138] | PF00782;PF14671; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class CDC14 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, kinocil... | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVI... | null | null | null | null | FUNCTION: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. {... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IVV0 | MTP_DANRE | MMPVAGLLLCVTAVLCTSALGAGPRLDNGKLYRYSYSTEVGLNRPTGSPGGNVGFRISSDVDINLAWRNPEIQDEQLLQVKISNIQVESAGKHSRKNNIFHGSSAESILGKVRLEALQRPFLVLWKMGKIRSLYAQKAEPATVKNLKRGVASMLMMQLKSGKMSEADASGKCLVEYKVNKHQVIRTKHLETCKSQETGFTTHSPVLGISGKCAAETVITLENGIIKSADAKETHVLSINARHKAATKVLSRQSLTLKAIEAGPAEVAGKDVAGVVKALDDKFLSVGVIVEKTKPKCKGCPNLMETWKAVRSQLEPNSLSK... | null | null | cholesterol homeostasis [GO:0042632]; digestion [GO:0007586]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; long-chain fatty acid transport [GO:0015909]; medium-chain fatt... | basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794] | lipid binding [GO:0008289]; lipid transfer activity [GO:0120013]; lipid transporter activity [GO:0005319]; phosphatidylethanolamine transfer activity [GO:1904121]; phospholipid transporter activity [GO:0005548] | PF19444;PF01347; | 1.25.10.20; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:17924655}. Golgi apparatus {ECO:0000250|UniProtKB:P55157}. Note=Colocalizes with P4HB/PDI in the endoplasmic reticulum. {ECO:0000269|PubMed:17924655}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:P55157}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; Evidence={ECO:0000250|UniProtKB:P55157}; CATALYTIC ACTI... | null | null | null | null | FUNCTION: Catalyzes the transport of triglyceride between phospholipid surfaces (PubMed:17924655). Catalyzes the transport of cholesteryl ester, and phospholipid between phospholipid surfaces (By similarity). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:17924655, ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IXF6 | KAT2A_DANRE | MADPAAQSSAQPRLQQAQSSGPTGSNSNPGAGSSDPARPGLSQQQWSSQKKAQVRSFPRAKKLEKLGVFSSCKANDACKCNGWKNPNPPTAARMELQQQAASLTETCRSCGHSLAEHVSHLENVSEEEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMGKPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPKERQTMYELSKMFLLCLNYWKLETPSQFRQRAQKEDAAAYKVDYTRWLCYCHVPQSNDSLPRYETCQVFGRSLLKSIFTVTRRQLLEKFRVEKDKLPPEKRTLILTHFPKFL... | 2.3.1.-; 2.3.1.48 | null | bone morphogenesis [GO:0060349]; chromatin remodeling [GO:0006338]; epigenetic regulation of gene expression [GO:0040029]; heart development [GO:0007507]; histone succinylation [GO:0106077]; internal peptidyl-lysine acetylation [GO:0018393]; limb development [GO:0060173]; long-term memory [GO:0007616]; peptidyl-lysine ... | ATAC complex [GO:0140672]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; histone acetyltransferase complex [GO:0000123]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone acetyltransferase activity [GO:0004402]; histone glutaryltransferase activity [GO:0106229]; histone H3 acetyltransferase activity [GO:0010484]; histone H3K9 acetyltransferase activity [GO:0043992]; histone succinyltransferase activity [GO:0106078]; peptide-lysine-N-acetyltransfer... | PF00583;PF00439;PF06466; | 3.40.630.30;1.20.920.10; | Acetyltransferase family, GCN5 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92830}. Chromosome {ECO:0000250|UniProtKB:Q92830}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q92830}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:Q92830}; ... | null | null | null | null | FUNCTION: Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferasesucc, succinyltransferase or malonyltransferase, depending on the context (By similarity). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequenc... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IY06 | PLAT1_DANRE | MDNQQRRTDNMASGETDHLQCVEEPQPGDLIEIFRPAYQHWALYLGDGYIINLTPVDEGQATAVSSVKSVFSRKAVVRMQLLKEVVGADSYRINNKYDDDHTPLPVSEIIQRAQMLIGQEVSYDLLGSNCEHFVTLLRYGEGVSEQASRAIGAISLVTAAASAFSVLGLINTRSRNRPF | 2.3.1.-; 3.1.1.32; 3.1.1.4 | null | lens fiber cell differentiation [GO:0070306]; lipid catabolic process [GO:0016042]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; organelle disassembly [GO:1903008] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | N-acyltransferase activity [GO:0016410]; phospholipase A1 activity [GO:0008970]; phospholipase A2 activity [GO:0004623] | PF04970; | 3.90.1720.10; | H-rev107 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:33854238}. Mitochondrion membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; Physiologica... | null | null | null | null | FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl gro... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R4IZ84 | EST1A_DANRE | MADELERVRISAAELRAQASSFNIHGDDVKDLREEGKKQRQRDSKRPDLQLYKPGVGHPNRRMDSVEGAGSDTLIQPDGFGNDPKMSDESPTSPGCSYMPGTGNEDYLNDHSKPETNHKTDGHIGGDKHKLVDENAVKIIERAGTPKSPKQSRKMRKPDRQIYQPGGRRSQGNKEVGASKELDRDRSREEEVDGKSIETPLKCEKEEKRKNRRGKNDRKKQASVETPSANKTENAVENISNKVSNLHLETVESKDRDRQDDTNQIKHSEEGRKIQTGGANRGMGEDKKKERGNGKSRPGKEKGNNQVFDKKEEGEAGGKA... | 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q86US8}; | chordate embryonic development [GO:0043009]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184] | chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nucleolus [GO:0005730]; telomerase holoenzyme complex [GO:0005697] | endonuclease activity [GO:0004519]; telomerase RNA binding [GO:0070034]; telomeric DNA binding [GO:0042162] | PF10374;PF10373;PF13638; | 3.40.50.1010;1.25.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q86US8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q86US8}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q86US8}. | null | null | null | null | null | FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini (By similarity). Required for normal embryonic development (PubMed:19414594). {ECO:0000250|UniProtKB:Q86US8, ECO:0000269|PubMed:19414594}.; FUNCTION: Plays a role in nonsense-mediated mRNA d... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0R6Y3I5 | G5K_LEIDO | MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCQFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALEELVFGDNDRLSALVAHHFKANLLVILSDIDGYYTENPRTSTNATIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARQFLLGGSHEIGTLFYSRVSS | 2.7.2.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:29777624}; | L-proline biosynthetic process [GO:0055129]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | ATP binding [GO:0005524]; glutamate 5-kinase activity [GO:0004349]; identical protein binding [GO:0042802] | PF00696; | 3.40.1160.10; | Glutamate 5-kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11; Evidence={ECO:0000269|PubMed:29777624}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14878; Evidence={ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for L-glutamate {ECO:0000269|PubMed:29777624}; KM=0.6 mM for ATP {ECO:0000269|PubMed:29777624}; | PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000269|PubMed:29777624}. | null | null | FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate (PubMed:29777624). May be important for growth and survival (PubMed:29777624). {ECO:0000269|PubMed:29777624}. | Leishmania donovani |
A0A0S2GKZ1 | LP9A_PANSI | MKYSILGLTALSFVASAAAHTLVWGVWVNGVDQGDGRNIYIRSPPNNNPVKNLTSPDMTCNVDNRVVPKSVPVNAGDTLTFEWYHNTRDDDIIASSHHGPIAVYIAPAASNGQGNVWVKLFEDAYNVTNSTWAVDRLITAHGQHSVVVPHVAPGDYLFRAEIIALHEADSLYSQNPIRGAQFYISCAQITINSSDDSTPLPAGVPFPGAYTDSTPGIQFNIYTTPATSYVAPPPSVWSGALGGSIAQVGDASLE | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:26928935, ECO:0000269|PubMed:28364950, ECO:0000269|PubMed:29057953, ECO:0000269|PubMed:32818374, ECO:0000269|PubMed:34389999, ECO:0000269|PubMed:35204695, ECO:0000269|PubMed:36071795}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:26... | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | PTM: The catalytically essential N-terminal histidine His-20 is post-translationally modified by methylation to prevent protonation of the histidine side chain, and protect the critical active site of the enzyme from oxidative damage. {ECO:0000269|PubMed:37452022}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26928935}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:26928935, ECO:0000269|PubMed:29057953, ECO:0000269|PubMed:32818374, ECO:0000269|PubMed:34389999}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation product (PubMed:26928935, PubMed:29057953, PubMed:32818374). Catalysis by LPMOs requires the reduction of the active-... | Panus similis (Lentinoid fungus) (Lentinus similis) |
A0A0S2UWC9 | CAMT1_PETHY | MAENGAAVQENQNVIRHQEVGHKSLLQSDALYQYILETSVYPREPESMKELRELTAKHPWNLMTTSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALAIPHDGKILAMDINRENYEIGLPVIEKAGVAHKIDFREGPALPVLDQLVEDKNNHGTYDFIFVDADKDNYINYHKRIIDLVKVGGLIGYDNTLWNGSLVAPADTPMRKYVRYYRDFILELNKALAADPRIEICMLPVGDGITLGRRIS | 2.1.1.-; 2.1.1.104 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q40313}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000250|UniProtKB:Q40313}; | circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; lignin biosynthetic process [GO:0009809]; methylation [GO:0032259]; phenylpropanoid metabolic process [GO:0009698] | cytosol [GO:0005829] | caffeoyl CoA:S-adenosyl-L-methionine O-methyltransferase activity [GO:0080076]; caffeoyl-CoA O-methyltransferase activity [GO:0042409]; metal ion binding [GO:0046872] | PF01596; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family, CCoAMT subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26620524}. | CATALYTIC ACTIVITY: Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104; Evidence={ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=5.8 pmol/sec/mg enzyme with (E)-caffeoyl-CoA as substrate {ECO:0000269|PubMed:26620524}; | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26620524}. | null | null | FUNCTION: Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:26620524). Methylates caffeoyl-CoA to feruloyl-CoA, also able... | Petunia hybrida (Petunia) |
A0A0S4FKT4 | VSP1_CRODO | VIGGDECNINEHNFLVALYEYWSQSFLCGGTLINGEWVLTAAHCDRKHILIYVGVHDRSVQFDKEQRRFPKEKYFFNCRNNFTKWDKDIMLIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRVMGWGTIKSPQETLPDVPHCANINLLDYEVCRTAHPQFRLPATIRILCAGVLEGGIDTCHRDSGGPLICNGEFQGIVSWGDGSCAQPDKPALYSKVFDHLDWIQNIIAGSETVNCPS | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | potassium channel regulator activity [GO:0015459]; serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26227411}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.43 mM for TAME {ECO:0000269|PubMed:26227411}; KM=0.92 mM for S-2302 {ECO:0000269|PubMed:34506860}; Vmax=0.06 mmol/min/ug enzyme towards TAME {ECO:0000269|PubMed:26227411}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Activity is stable from pH 3.5 and 10.5. {ECO:0000269|PubMed:26227411}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. Activity is stable after incubation at 100 degrees Celsius for 30 minutes. {ECO:0000269|PubMed:26227411}; | FUNCTION: Thrombin-like snake venom serine protease (PubMed:26227411, PubMed:31131001, PubMed:34506860). Releases fibrinopeptide A and B in the conversion of fibrinogen to fibrin, with preferential activity on the alpha chain of fibrinogen (PubMed:26227411, PubMed:34506860). Also hydrolyzes N-p-toluensulfonyl arginine ... | Crotalus durissus collilineatus (Brazilian rattlesnake) |
A0A0U1QT59 | TMC_DROME | MQNDEEPAAAAGTSGLSNGESLRSPPAPAPRRPKPGILRLDIGKPRRSSGGSVDFRCVGSSSSNGNTSNVATGANSENNSGVTSPHQLSVTWAPPCDLDRGGWQMQSSADAKREFYKGQRGRRAASQEDHRSYELNDFPLQNQSSDAESCHQEPHFAHQRSPGIGFDEDGGGGDIDDEESYTISVSAIMQRRASVRGYRGKRGSRSSRRASSPMDHVLDSVERRRSSVYTTSSEEGTNQESTQEQIFENIRLHKEVIQSVKLQPWPIRKKLKLVRQAKTYVARHEGALQERFAMSRSTRDLWARFKILMAARWRHWKRET... | null | null | chemosensory behavior [GO:0007635]; detection of chemical stimulus involved in sensory perception of sweet taste [GO:0001582]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; larval locomotory behavior [GO:0008345]; perception of rate of movement [GO:0019232]; positive regulation of mechan... | dendrite [GO:0030425]; plasma membrane [GO:0005886] | mechanosensitive monoatomic ion channel activity [GO:0008381] | PF07810; | null | TMC family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:27478019}. | null | null | null | null | null | FUNCTION: Probable ion channel (PubMed:27478019, PubMed:30853433, PubMed:31184585, PubMed:32649914). Component of mechanosensitive neurons that participates in proprioception, sensing food texture, and directing egg-laying site selection (oviposition) (PubMed:27298354, PubMed:27478019, PubMed:30853433, PubMed:31184585,... | Drosophila melanogaster (Fruit fly) |
A0A0U1RPR8 | GUC2D_MOUSE | MAGLQQGCHFEGQNWTAPHWKTCLPCQGPWRLTVSHLKTVSSISVLSVVFWSVLLWADSLSLLAWARETFTLGVLGPWDCDPIFAQALPSIATQLAVDQVNQDASLLPGSQLDFKVLPTGCDTPHALATFVAHKNIVAAFVGPVNPGFCSAAALLAQGWGKSLFSWACEAPEGGGDLVPTLPSAADVLLSVMRHFGWARWAIVSSHQDIWVTTAQQLATAFRTHGLPIGLVTSLGPGEKGATEVCKQLHSVHGLKIVVLCMHSALLGGLEQTTLLHCAWEEGLTDGRLVFLPYDTLLFALPYGNRSYLVLDDHGPLQEAY... | 4.6.1.2 | null | cGMP biosynthetic process [GO:0006182]; detection of carbon dioxide [GO:0003031]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; intracellular signal transduction [GO:0035556]; olfactory behavior [GO:0042048]; olfactory learning [GO:0008355]; positive regulation of cGMP-mediated si... | ciliary membrane [GO:0060170]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; guanylate cyclase activity [GO:0004383]; natriuretic peptide receptor activity [GO:0016941]; odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672] | PF01094;PF00211;PF07714; | 3.40.50.2300;6.10.250.780;3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:9096404}; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:P51839}; | null | null | null | null | FUNCTION: Functions as an olfactory receptor activated by urine odorants, uroguanylin and guanylin and as well by the volatile semiochemicals carbon disulfide (CS2) and carbon dioxide (CO2) (PubMed:17702944, PubMed:17724338, PubMed:20637621). Has guanylate cyclase activity upon binding of the ligand (By similarity). Ac... | Mus musculus (Mouse) |
A0A0U1RRE5 | NBDY_HUMAN | MGDQPCASGRSTLPPGNAREAKPPKKRCLLAPRWDYPEGTPNGGSTTLPSAPPPASAGLKSHPPPPEK | null | null | mRNA processing [GO:0006397]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; nuclear-transcribed mRNA catabolic process [GO:0000956] | P-body [GO:0000932] | null | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:27918561}. Note=Localizes to P-bodies at low concentrations without dissociating them. {ECO:0000269|PubMed:27918561}. | null | null | null | null | null | FUNCTION: Promotes dispersal of P-body components and is likely to play a role in the mRNA decapping process. {ECO:0000269|PubMed:27918561}. | Homo sapiens (Human) |
A0A0U3BRC5 | GFDPS_LEUCN | MSHCTIFLYKYFPGKPRYQHCSFLHPLNHKLKSLFLPITGSRFLSNSTFSVSDSAHSHQAKPHVRNAQFDFKAYMLEKITAVNQALDAALPVREPVKIHEAMRYSLLLGGKRICPIVCLAACHLVGGDESTAMPSAAALEMIHAMSLMHDDLPCMDNDDLRRGRPSNHVVFGEGATVLAGYALIARAFEHIATATQGVGPGKILRVIGELAQLIGAEGVVGGQVVDLRCGGEGQMAIGLEQLEYIHLHKTAASVEASAVAGAVLGGASEEEIERLRKYSRSAGLLFQVVDDILDVTKSSEELGKTAGKDLAAGKTTYPKL... | 2.5.1.81 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14324}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324}; | response to herbivore [GO:0080027]; response to insect [GO:0009625]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; terpenoid biosynthetic process [GO:0016114] | chloroplast [GO:0009507] | farnesyltranstransferase activity [GO:0004311]; geranylfarnesyl diphosphate synthase activity [GO:0044687]; metal ion binding [GO:0046872]; transferase activity [GO:0016740] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:26941091}. | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; EC=2.5.1.81; Evidence={ECO:0000269|PubMed:26941091}; Physiological... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34.89 uM for dimethylallyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=3.04 uM for isopentenyl diphosphate (in the presence of geranylgeranyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=6.28 uM for geranyl diphospha... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30468448}.; PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:26941091}. | null | null | FUNCTION: Involved in the biosynthesis of leucosceptrane sesterterpenoids natural products, which are playing defensive roles toward herbivorus insects (e.g. Spodoptera exigua) (PubMed:26941091). Catalyzes the condensation of isopentenyl pyrophosphate (IDP) with the allylic pyrophosphates to yield geranylfarnesyl dipho... | Leucosceptrum canum (Hairy white-wand) (Clerodendron leucosceptrum) |
A0A0X1KHF9 | RPH_LISMF | MKPYVLKFQEIRPHSEALVGGKGMNLGACSNIEGVHVPAGFCLTTEAYKRTLAENNEFTQLLQRLSSLKTSDMDAIREISETIRTLIQHTQIPSEIASYMDATLLDVGGYEMPFAVRSSATAEDLPHASFAGQHDTYLNIIGKDALLQHISMCWASLFTERAIIYRIQNQFDHRKVQLAVVIQQMISPEASGILFTADPITSNRKSLSIDASFGLGEALVSGLVSADSYTVRENTITNKIIATKKLAIYSLKEGGTETRILEKSQQTKQTLTDQQIIQLAKLGRKIEAYFGKPQDIEWCLAEGAFYIVQSRPITTLYPIP... | 2.7.9.6 | null | phosphorylation [GO:0016310]; response to antibiotic [GO:0046677] | null | ATP binding [GO:0005524]; kinase activity [GO:0016301] | PF00391;PF01326; | 3.30.1490.20;3.30.470.20;3.50.30.10; | Rifampicin phosphotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O + rifampicin = 21-phosphorifampicin + AMP + 2 H(+) + phosphate; Xref=Rhea:RHEA:56304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:71365, ChEBI:CHEBI:140195, ChEBI:CHEBI:456215; EC=2.7.9.6; Evidence={ECO:0000269|PubMed:24778229, ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 uM for RIF {ECO:0000269|PubMed:24778229}; KM=0.57 uM for RIF {ECO:0000269|PubMed:27103605}; KM=27.21 uM for ATP {ECO:0000269|PubMed:24778229}; KM=8.38 uM for ATP {ECO:0000269|PubMed:27103605}; Note=kcat is 1.03 sec(-1) (PubMed:24778229). kcat is 2.87 sec(-1) w... | null | null | null | FUNCTION: Catalyzes the phosphorylation of rifampicin, also known as rifampin (RIF), leading to its inactivation (PubMed:24778229, PubMed:27001859, PubMed:27103605). Confers high level resistance to a variety of clinically used rifamycin antibiotics (PubMed:24778229). Does not show phosphoenolpyruvate (PEP) synthase ac... | Listeria monocytogenes serotype 4b (strain F2365) |
A0A125QXJ1 | ABCB6_MESAU | MVTVGNYCEAEGPLGPAWAQNGLSPCFFFTLVPSTLMALGALALVLVLPCRRRDVPSGTEELFWAADSRVAPYALQLFLATLQVALPLAGLAGRVGTARGVRLPGYLLLASMLGSLASACGLWLLVAERRQARQSLAMGVWMKFRHSSGLLLLWTVAFAAENLALVSWNSPQWWWARADLGQQVQFGLWVLRYVISGGLFILGLWAPGLRPQSYTLRVHEADQDVERNQAQSTDRTSTWRDLGRKLRLLSSYLWPRGSPALQFIVLICLGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGT... | 7.6.2.5 | null | cellular detoxification of cadmium ion [GO:0098849]; heme metabolic process [GO:0042168]; heme transmembrane transport [GO:0035351]; porphyrin-containing compound metabolic process [GO:0006778] | early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; melanosome membrane [GO:0033162]; mitochondrial outer membrane [GO:0005741... | ABC-type heme transporter activity [GO:0015439]; ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; heme binding [GO:0020037] | PF00664;PF00005;PF16185; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NP58}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}.... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate; Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344, ChEBI:CHEBI:456216; EC=7.6.2.5; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; ... | null | null | null | null | FUNCTION: ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen. May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, in turn may parti... | Mesocricetus auratus (Golden hamster) |
A0A126GUP6 | MP1_DROME | MEPHFFFTVLWMLLMGTSSTYAQEIFGYCRTPDENSGTCINLRECGYLFELLQSEEVTEQDRRFLQASQCGYRNGQVLEKHFCFTNVQICCANSRMRNQQPQWGNHPQPTQTTKPTKRSGTKLLPMAPNCGENFGDRVVGGNETTKREFPWMALIEYTKPGNVKGHHCGGSLINHRYVLTAAHCVSAIPSDWELTGVRLGEWDASTNPDCTVGKNGRRDCNEPYVDYPVEERIPHPQYPGNSRDQLNDIALLRLRDEVQYSDFILPVCLPTLASQHNNIFLGRKVVVAGWGRTETNFTSNIKLKAELDTVPTSECNQRYA... | 3.4.21.- | null | melanization defense response [GO:0035006]; proteolysis [GO:0006508]; response to fungus [GO:0009620]; Toll receptor ligand protein activation cascade [GO:0160032] | null | endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; serine hydrolase activity [GO:0017171]; serine-type endopeptidase activity [GO:0004252] | PF12032;PF00089; | 3.30.1640.30;2.40.10.10; | Peptidase S1 family, CLIP subfamily | null | null | null | null | null | null | null | FUNCTION: Serine protease which plays an essential role in the melanization immune response by acting downstream of sp7 to activate prophenoloxidase (PPO1) (PubMed:16861233). May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A in the hemol... | Drosophila melanogaster (Fruit fly) |
A0A131MCZ8 | CNNM3_CAEEL | MSKTPWALGLLIFLLTFTSPLSSSPVRSTDNSTSSKGLLNVNSSVILEPSILPSSASKPESLHLSKVRVSGLRLEAHASSTENIVLGHNKKHNVVVVPNKNVRVVLFGQNFQDIGALTFTADGSCKDLAHFFEADFSSMTPIRVVVEMSFPKTTESKDSFKLCVSEKFYANPQFVIVEDPFTMVTTEIPPVDEYMPKWLSWICLLILLCFSGLFSGLNLGLMTLSPYELQLYIASGTEQEKRDAGRILPIRKKGNQLLCTLLIGNVVVNVGVSLLMDQLVGSGFAVLVAATSCIVVFGEIIPQALCVKLGLPIGARTIPI... | null | null | determination of adult lifespan [GO:0008340]; innate immune response [GO:0045087]; intracellular manganese ion homeostasis [GO:0030026]; magnesium ion homeostasis [GO:0010960]; magnesium ion transport [GO:0015693]; positive regulation of gonad development [GO:1905941]; positive regulation of multicellular organism grow... | basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | transmembrane transporter activity [GO:0022857] | PF01595; | 3.10.580.10; | ACDP family | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:27564576}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-2, cnnm-4 and cnnm-5 to regulate Mg(2+) homeostasis. Promotes postembryonic gonad development by regulating Mg(2+) levels, probably via AMPK signaling. {ECO:0000269|PubMed:27564576}. | Caenorhabditis elegans |
A0A139GI49 | KAWA_MICA8 | MKNPTLLPKLTAPVERPAVTSSDLKQASSVDAAWLNGDNNWSTPFAGVNAAWLNGDNNWSTPFAGVNAAWLNGDNNWSTPFAADGAE | null | null | defense response to bacterium [GO:0042742] | null | null | null | null | null | PTM: Kawaguchipeptin A contains a D-Leu and 2 prenylated Trp, whereas kawaguchipeptin B only contains unmodified amino acids. {ECO:0000269|PubMed:9249979, ECO:0000269|Ref.3}.; PTM: Kawaguchipeptin A is prenylated in vivo (Ref.3). Upon expression in E.coli of the whole operon, Trp residues are prenylated by C-prenyltran... | null | null | null | null | null | null | FUNCTION: Both kawaguchipeptin A and B, which only differ by post-translational modifications, have antibacterial activities, since they inhibit the growth of the Gram-positive bacterium S.aureus at a concentration of 1 ug/mL. {ECO:0000269|PubMed:9249979}. | Microcystis aeruginosa (strain NIES-88 / KW-MA1-3) |
A0A140H546 | MAFB1_TOXGO | MWRIWRCRLSFLFATGCLLGALTAGLGSQMSDSVGRNVQAPAGVADASQEAGDVVEERTERTEEQAFALGPPRRHSSESLFPRNASVTARRRRNRRIALIATAVGVAVILAAVYVLRRRRAQRPQDPEPPAPRSVEDPEVLPEEDEASSSLPPPPPPSPPPPPPVEDPLSPESQTVDLSCLSGTTVRFFGPSHHFGGFTPLYDPAPDKRVATVDAGANALFIGGGGLNGQFAKTLLEEAEKHGIRLTPEELSQHSQRIQQSLLRRAVKSPGKLVELDTGVASPVFARSFGFVPVVPGLMWEESEVGPNVGVTFVHILKPE... | null | null | null | cytoplasmic vesicle membrane [GO:0030659]; symbiont-containing vacuole membrane [GO:0020005] | null | null | null | null | PTM: Phosphorylated. {ECO:0000269|PubMed:24781109}. | SUBCELLULAR LOCATION: Parasitophorous vacuole membrane {ECO:0000269|PubMed:24781109, ECO:0000269|PubMed:26920761, ECO:0000269|PubMed:28567444}; Single-pass type I membrane protein {ECO:0000305|PubMed:24781109}. Cytoplasmic granule membrane {ECO:0000269|PubMed:24781109}; Single-pass type I membrane protein {ECO:0000305|... | null | null | null | null | null | FUNCTION: During host cell infection by tachyzoites, required for tethering the parasitophorous vacuole to the host mitochondria (PubMed:24781109, PubMed:26920761, PubMed:28567444, PubMed:29505111, PubMed:33723040, PubMed:35025629). This process, known as host mitochondrial association (HMA), induces the formation of S... | Toxoplasma gondii |
A0A140JWS2 | PTMG_PENSI | MLFLAPGYIFPHVATPVTVAIDFAQAVKEGAYSFLDLKASPVPNPELFQPPSRVSIGMTGGREERNEEIIRGPLNYLLSLPGKDIRGKLIDALNEWFRVPEDKLSTIKEIIVILHTASLLIDDIQDSSQLRRGNPVAHRIFGVAQTINSANYAYFLAQAKLADLNDSRAFDIFTKGLLKLHRGQGMELYWRDNLICPTEEEYVEMVSCKTGGLFYLAVQLMQLNSEVTVNFSSFINLLGIIFQIRDDYMNLQSGTMTKTKGFSEDLTEGKFGYPIIHSIHAAPNDQQLIQILKLKTNDEVIKQYAVRYIESTGSFIYCRE... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:25831977}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems (PubMed:25831977). The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyro... | Penicillium simplicissimum |
A0A140LI88 | ANR31_MOUSE | MENGAEASDCDSDETVIEGSVTENEPEDEELPWRRLLLNQDTTCRSEFCFHSGVDGMQKGIHSPEIQLGLKLRKDSQEQNNKNKLLLALSEDLVLQDPQDKTAQNQVLLQTTKEFPVFTVSFPHPEVSWSHQNTGGHEAENCENLPHSKKELRENSDSPEVSLLSGTSPVAPDLVALKERLTEPVKTLAVPNTLSEPGEEVTQTMTSKETKDEESSLETFVSTLEKLLESSECTQEERLLEVMDDFNPQELFSTLSNSLGSVSVPLNAWAAQGRDELENKADAALPAKLLAAVNTGADVGPSCQGQEKSSSVSGGNGCLA... | null | null | homologous chromosome pairing at meiosis [GO:0007129]; meiotic DNA double-strand break formation involved in reciprocal meiotic recombination [GO:0010780]; positive regulation of meiotic DNA double-strand break formation [GO:1903343] | chromatin [GO:0000785]; nucleus [GO:0005634] | null | PF12796;PF18755; | 1.25.40.20; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31000436}. Chromosome {ECO:0000269|PubMed:31000436, ECO:0000269|PubMed:31003867}. Note=Localizes on chromatin between preleptotene and early pachytene (PubMed:31000436). Associates with the chromosome axes, but disappears from axes upon synaptonemal complex formation (P... | null | null | null | null | null | FUNCTION: Required for DNA double-strand breaks (DSBs) formation during meiotic recombination (PubMed:31000436, PubMed:31003867). Regulates the spatial and temporal patterns of pre-DSB recombinosome assembly and recombination activity by acting as a scaffold that anchors REC114 and other factors to specific genomic loc... | Mus musculus (Mouse) |
A0A140LIF8 | IRGM2_MOUSE | MEEAVESPEVKEFEYFSDAVFIPKDGNTLSVGVIKRIETAVKEGEVVKVVSIVKEIIQNVSRNKIKIAVTGDSGNGMSSFINALRLIGHEEKDSAPTGVVRTTQKPTCYFSSHFPYVELWDLPGLGATAQSVESYLEEMQISIYDLIIIVASEQFSLNHVKLAITMQRMRKRFYVVWTKLDRDLSTSTFPEPQLLQSIQRNIRDSLQKEKVKEHPMFLVSVFKPESHDFPKLRETLQKDLPVIKYHGLVETLYQVCEKTVNERVESIKKSIDEDNLHTEFGISDPGNAIEIRKAFQKTFGLDDISLHLVALEMKNKHFNT... | 3.6.5.- | null | cellular response to interferon-beta [GO:0035458]; defense response [GO:0006952]; defense response to protozoan [GO:0042832]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]; negative regulation of non-canonical inflammasome complex assembly [GO:0160076]; protein targeting to vacu... | cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; vacuolar membrane [GO:0005774] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF05049; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, IRG family | PTM: Ubiquitinated; polyubiquitinated in the cytosol, promoting Gbp1 recruitment to the T.gondii parasitophorous vacuole membranes. {ECO:0000269|PubMed:34078740}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:34078740}. Golgi apparatus membrane {ECO:0000269|PubMed:34078740}. Cytoplasm, cytosol {ECO:0000269|PubMed:34078740}. Note=Localizes to parasitophorous vacuole membranes. {ECO:0000269|PubMed:34078740}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:34078740}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:34078740}... | null | null | null | null | FUNCTION: Immunity-related GTPase that plays important roles in innate immunity and inflammatory response (PubMed:17641048, PubMed:33124745, PubMed:33124769, PubMed:34078740, PubMed:34338548). Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes... | Mus musculus (Mouse) |
A0A140N5J7 | KDSC_ECOBD | MSKAGASLATCYGPVSADVMAKAENIRLLILDVDGVLSDGLIYMGNNGEELKAFNVRDGYGIRCALTSDIEVAIITGRKAKLVEDRCATLGITHLYQGQSNKLIAFSDLLEKLAIAPENVAYVGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCDLLLLAQGKLDEAKGQSI | 3.1.3.45 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12639950}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:12639950}; Note=Mg(2+). The phosphatase activity is also stimulated by cobalt ions, whereas baryum, zinc, and manganese ions are less effective stimulators. {ECO:00002... | lipopolysaccharide biosynthetic process [GO:0009103] | null | 3-deoxy-manno-octulosonate-8-phosphatase activity [GO:0019143]; metal ion binding [GO:0046872] | PF08282; | 3.40.50.1000; | KdsC family | null | null | CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000269|PubMed:12639950}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=75 uM for KDO 8-P {ECO:0000269|PubMed:12639950}; Vmax=500 umol/min/mg enzyme {ECO:0000269|PubMed:12639950}; Note=kcat is 175 sec(-1). {ECO:0000269|PubMed:12639950}; | PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. {ECO:0000305|PubMed:12639950}.; PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. {ECO:0000305|PubMed:12639950}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. High catalytic activity is observed between pH 5.5 and 7.0. {ECO:0000269|PubMed:12639950}; | null | FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000269|PubMed:12639950}. | Escherichia coli (strain B / BL21-DE3) |
A0A142I5B9 | POLG_ZIKVK | MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGTDTSVGIVGLLLTTAMAVEVTRRGNAYYMYLDRSDAGEAISFPTTMGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGC... | 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 | fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression ... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell surface [GO:0044228]; membrane [GO:0016020]; viral capsid [GO:0019028]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization act... | 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:0000250|UniProtKB:P17763}. 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. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can mi... | Zika virus (isolate ZIKV/Human/Cambodia/FSS13025/2010) (ZIKV) |
A0A142ZC57 | LOS_BOTBR | MKYTDFLAHPDEIIPTIRMMYADYRLKNMEIKDPSVRFCYNMLNRVSRSFAMVIQQLPVELRDATCVFYLILRALDTVEDDMAIPKEVKIPMLRTFHEHLSDRSWKIKCGYGPYVDLMDNYPLVTDVYLRFDEGTKAVIKDITRRMGNGMADFIDLDEVLTIPQYDLYCHYVAGLCGIGMCKLFVDSGLEKEDLVAEEDLANQMGLFLQKNNIVRDYLEDINELPAPRMFWPKEIWGNYAKQLDEFKDPKNLDKAMLCLNHMVTDALRHCEVGLRSLSLLHNPNILRAVLIPQVMGVRTLTLVYNNPEVFRGVVKMRRGE... | 2.5.1.148; 2.5.1.21 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P37268}; | cholesterol biosynthetic process [GO:0006695]; ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate metabolic process [GO:0045338]; sterol biosynthetic process [GO:0016126] | endoplasmic reticulum membrane [GO:0005789] | farnesyl-diphosphate farnesyltransferase activity [GO:0004310]; farnesyltranstransferase activity [GO:0004311]; metal ion binding [GO:0046872]; squalene synthase activity [GO:0051996] | PF00494; | 1.10.600.10; | Phytoene/squalene synthase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000269|PubMed:27050299}; CATALYTIC ACTIVITY:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for geranylgeranyl diphosphate {ECO:0000269|PubMed:27050299}; KM=0.13 mM for farnesyl diphosphate {ECO:0000269|PubMed:27050299}; KM=0.11 mM for phytil diphosphate {ECO:0000269|PubMed:27050299}; | null | null | null | FUNCTION: Converts the C20 geranylgeranyl diphosphate (GGPP) to the C40 lycopaoctaene, the first committed intermediate in the production of lycopadiene (PubMed:27050299, PubMed:28813599). Converts farnesyl diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in eukaryotes (PubMed:27050299, PubMed:28813... | Botryococcus braunii (Green alga) |
A0A143ZZK9 | ATP4_PLAF7 | MSSQNNNKQGGQDINNKKDSDDIKPSVSKEDLINSLKNDELNKNTTMDQNDMKKNENMNIKKNEVLNNSNNVEDGDNENSKFMNKSKEGLNNINGEKNDDNNSIVKVEESPKSIGYNYYASESIENLCKEFGLESINTGLNSEQVKINRDKYGENFIEKDEVVPVWLIFLSQYCSPVVLLLLVAAVASLALNEVVEGVAIISIVTLNACLATYMEKSSGDAIGKLAEMASPQCTVLRNGQKVVIPSREVVVGDVVLINTGDSISADLRLFDVIELKTNESLLTGESEDIKKTIVADNLSTPFATNLCFATTSVTSGSGKG... | 7.2.2.3 | null | calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; manganese ion transport [GO:0006828] | endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886] | ABC-type sodium transporter activity [GO:0140679]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type calcium transporter activity [GO:0005388]; P-type sodium transporter activity [GO:0008554] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20813948, ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:29986883, ECO:0000269|PubMed:8813672}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:29986883, ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for ATP (in the presence of 150-153 mM of Na(+)) {ECO:0000269|PubMed:29986883}; KM=16.1 mM for Na(+) {ECO:0000269|PubMed:29986883}; | null | null | null | FUNCTION: Sodium-exporting ATPase (PubMed:23414762, PubMed:29986883, PubMed:31311978, PubMed:36180431). Required for the extrusion of Na(+) from the intraerythrocytic parasites to maintain a low cytosolic concentration of Na(+) (PubMed:23414762, PubMed:25322084, PubMed:25453091, PubMed:29555632, PubMed:36180431). {ECO:... | Plasmodium falciparum (isolate 3D7) |
A0A144A134 | ISN1_PLAF7 | MKNLDINTFDNIEDIPLGSSEQDPYDFFTLSDRNVMNSDMKKNIVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEMFIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPPTFNEVRHILNLAQILSLEEGLDLLTFDADETLYPDGHDFNDEVLASYISCLLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMGGESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVIKDFGLCAQIQRKEKSIGLVPNKIPSLN... | 3.1.3.99 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32591529}; | IMP catabolic process [GO:0006204]; inosine salvage [GO:0006190]; nicotinamide riboside biosynthetic process [GO:0071590]; nicotinic acid riboside biosynthetic process [GO:0071592] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; IMP 5'-nucleotidase activity [GO:0050483]; magnesium ion binding [GO:0000287] | PF06437; | 3.40.50.1000; | ISN1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32591529}. | CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000269|PubMed:32591529}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 mM for IMP (at pH 5, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=66 mM for IMP (at pH 8, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=6.8 mM for IMP (at pH 8, 25 degrees Celsius and in the ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5. {ECO:0000269|PubMed:32591529}; | null | FUNCTION: Specifically, catalyzes the dephosphorylation of inosine monophosphate (IMP) into inosine (PubMed:32591529). By dephosphorylating IMP, plays a role in the purine salvage pathway (PubMed:32591529). Does not have phosphotransferase activity with IMP as phosphate donor and adenosine as phosphate acceptor (PubMed... | Plasmodium falciparum (isolate 3D7) |
A0A144A2H0 | AMPP_PLAF7 | MQLNFLLFVFIFLMVFHLNIFNKGKRQNLVSAYLNHFKKSYFSGVTSGSDCVNKSEVSSDNNNNNNNNNNKIAHNFFSKKYQRNFENNNLSENQENNKNIIYSGSNIFKNIYNTEMMSNNNTVDVNMMDNNPAARLEELRTIMKKNKIDVYILINSDEHNSEIINEKDKKIVKITNYSGADGILIVTKDKPILYVNALYELQAMNELDQNLFTLRISRIDNRDEIFETISSLEFNTIAFDGKNTSVVFYEKLRKALLNAYPKKKIVEKIIYNNNFDDVNKKDDENVLNFLVLEKSLVEIKDYPVNNKTLYIHDRKYNGAC... | 3.4.11.9 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19574214}; Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000269|PubMed:27462122}; | hemoglobin catabolic process [GO:0042540]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; food vacuole [GO:0020020]; vacuolar lumen [GO:0005775] | manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006] | PF01321;PF16189;PF00557;PF16188; | 3.90.230.10;3.40.350.10; | Peptidase M24B family | PTM: The N-terminus may be proteolytically cleaved to generate a 73-kDa mature form. {ECO:0000269|PubMed:19574214}. | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. Cytoplasm {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. Note=Localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:1... | CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214, ECO:0000269|PubMed:27462122}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.51 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=0.86 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 5.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=1.4 mM for human hemogl... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 (PubMed:19574214). Active at pH 5.5-7.5 (PubMed:19574214). {ECO:0000269|PubMed:19574214}; | null | FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides (PubMed:17895246, PubMed:19574214, PubMed:27462122). In the food vacuole, involved in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides (PubMed:17895246, PubMed:19574214). In the cytop... | Plasmodium falciparum (isolate 3D7) |
A0A144LUY5 | CTCN1_ECHES | MMIKIAVVLCAVMATTMVRAKYVEEQELADLLDLLISEEVSSPDDAVALQGWWRRTVDKVRNAGRKVAGFASKACGALGHSPQEARAKVLEAFPEMKEADLDEEDIGKYCGYAHALNGR | null | null | defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640] | null | null | null | null | null | null | null | null | null | null | null | null | FUNCTION: [Centrocin 1, heavy chain]: Has antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and against fungi with minimum inhibitory concentration (MIC) between 0.78 uM and 50 uM. Shows little hemolytic activity even at a concentration of 100 uM. {ECO:0000269|PubMed:27007817}.; FUNCTION: [C... | Echinus esculentus (Sea urchin) |
A0A145P7T2 | RAM1_LOTJA | MINSMCGSSVSLKSENSRNKPQPTSPNESVLQSKKNATQSSADLEQTSLNLTPPSLNLPALKFDLDGDVEVQSPDSSMWESFFSDHLLDGDFMISSPVRNNVPSPQASTFNSNYNYAHQGIQSQSLSGCSPPRFSSPLGAFNSNKGKGLSPLHRVFNSPNNQYMQHVENLALPAIEEFLEEYQGDHGLGGGGGYSNSSNKVSSDIGSSSECFDMQNHIPSMLDSLTMQNSSRYCGSVSEDSSVHGGSSQLSQDSDFYHQMGSMASASLSQALQQERYQEKQQKQHQTQQQQQPQQQQQNLTVPIPIGMDQEQDSGLQLVH... | null | null | arbuscular mycorrhizal association [GO:0036377]; regulation of DNA-templated transcription [GO:0006355]; response to symbiotic fungus [GO:0009610] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565] | PF03514; | null | GRAS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25560877}. Cytoplasm {ECO:0000269|PubMed:25560877}. | null | null | null | null | null | FUNCTION: Transcription factor acting as a central regulator of arbuscular mycorrhiza (AM)-related genes (e.g. PT4) required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis) (PubMed:25560877, PubMed:27020747). Also involved in restricting mycorrhizal colonization of the ro... | Lotus japonicus (Lotus corniculatus var. japonicus) |
A0A151V4J3 | AA13_PYRO7 | MKWSVIQALALASGVQAHGYLTFPMSRTGLNAQAGPDTCPECTILEPVTAWPDLDSAQVGRSGPCGYNARVSVDYNQPGPRWGSAPVVTYKGGDVADVQWCVDNNGDHGGMFTYRICQDQALVDKLLTPGYLPSEAEKQAAENCFRAGTLPCTDVNGQSCGYSPDCSPGQACWRNDWFTCKGFQDTKCRGVDNAPLNSCYTSIAGGYTVSSRIKIPNYVSNHTLLSFKWNSFQTPQIYLTCADIKITAPDSQSPPTTTTTSTPASPPPTSCATPAASVAVTFRSKTTTSVGQTVKIAGSIAQLGGWDASKAPALSASQYT... | 1.14.99.55 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q7SCE9}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q7SCE9}; | polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; starch binding [GO:2001070] | PF00686; | 2.60.40.10; | Polysaccharide monooxygenase AA13 family | PTM: O-mannosylated. {ECO:0000269|PubMed:27397613}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27397613}. | CATALYTIC ACTIVITY: Reaction=starch + reduced acceptor + O2 = D-glucono-1,5-lactone-terminated malto-oligosaccharides + short-chain malto-oligosaccharides + acceptor + H2O.; EC=1.14.99.55; Evidence={ECO:0000269|PubMed:27397613}; | null | null | null | null | FUNCTION: Starch-active lytic polysaccharide monooxygenase that oxidizes the C1 position of starch substrates (PubMed:27397613). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable). {ECO:0000269|PubMed:27397613, EC... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
A0A163UT06 | SET17_CAEEL | MNIKHNYISYFQMNGIQIPGISNPEAIIPITGEKKSYKLVLDFNDGAISIIEARYLDSKLHREIQDLSDNDVTILGTEISDGAYDENLDIHCDKCNKFYRPYCRLHPLFKIPDRVLKRDESSNLSFSQQTLPILFRIEESKLPNAGLGVIAEVFIPVGMVFGPYKGRRCQKKTDFYKDGYAWLIKSGDKRFYIDGSDAERSNWLRYINSPRFEDEQNMLAFQTNGKIFYRVIKPIRINQELLVWYGSSYGNEFVESENGNKYKKPAKNPFICVGAQR | 2.1.1.-; 2.1.1.364 | null | methylation [GO:0032259]; oligodendrocyte development [GO:0014003]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 monomethyltransferase activity [GO:0140945] | PF21549; | 2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29702639}. Note=In males and hermaphrodites, localizes to foci in the nucleus of spermatocytes, which express the mono- and di-methyl states of 'Lys-4' of histone H3 (PubMed:29702639). These foci are stable nuclear structures with slow diffusion and liquid-like properti... | CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:... | null | null | null | null | FUNCTION: Histone methyltransferase that specifically mono- and di-methylates 'Lys-4' of histone H3 in vitro (PubMed:24685137). Does not tri-methylate 'Lys-4' of histone H3 in vitro (PubMed:24685137). Promotes spermatid development and fertility by positively regulating the transcription of spermatocyte-specific genes ... | Caenorhabditis elegans |
A0A166U5H3 | BMT_KITPR | MAGMKTSPSQDEEACVLAIQLATSTVLPMILKSAIELDILNTISKAGPGNYLSPSDLASKLLMSNPHAPIMLERILRVLATYKVLGCKPSELSDGEVEWLYCWTPVCKFLSNNEDGASIAPLLLVHQDQVPMKSWYHLTDAILDGGTAFNKAYGMNIFDYASQDPQFNKVFNRSMAGHSTITMKKILETYNGFEGLKSIVDVGGGSGATLNMIISKYPTIKGINFDLPHVVGDSPIHPGVEHVGGDMFASVPKGDAIFLKWIFHSWSDEDCLRILKNCYEALADNKKVIVAEFIIPEVPGGSDDATKSVVHLDAVMLAYV... | 2.1.1.69 | null | aromatic compound biosynthetic process [GO:0019438]; coumarin biosynthetic process [GO:0009805]; methylation [GO:0032259]; response to jasmonic acid [GO:0009753] | cytoplasm [GO:0005737] | 5-hydroxyfuranocoumarin 5-O-methyltransferase activity [GO:0030752]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27252733}. | CATALYTIC ACTIVITY: Reaction=bergaptol + S-adenosyl-L-methionine = bergapten + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11808, ChEBI:CHEBI:18293, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77728; EC=2.1.1.69; Evidence={ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}; Physi... | null | PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.; PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}. | null | null | FUNCTION: O-methyltransferase involved in the biosynthesis of furocoumarins natural products such as bergapten, a photosensitizer used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses (PubMed:27252733, PubMed:30934718, PubMed:31666994). Cat... | Kitagawia praeruptora (Peucedanum praeruptorum) |
A0A172J1V3 | PHZM_LYSAN | MTENNRAGAVPLSSILLQMITGYWVTQSLYVAAKLGIADLVADAPKPIEELAAKTGAKAPLLKRVLRTIASIGVFTETEPGIFGITPLAALLRSGTPDSMRPQAIMHGEEQYRAWADVLHNVQTGETAFEKEFGTSYFGYLAKHPEADRVFNEAQAGYTKQVAHAVVDAYDFSPFKTVIDIGAGYGPLLSAILRSQPEARGILFDQPHVAQAAGKRLAEAGVGDRCGTVGGDFFVEVPADGDVYILSLLLHDWDDQRSIEILRNCRRAMPAHGKLLIVELVLPEGEEPFFGKWLDLHMLVLLGAQERTADEFKTLFAASG... | 2.1.1.- | null | methylation [GO:0032259]; phenazine biosynthetic process [GO:0002047] | null | identical protein binding [GO:0042802]; O-methyltransferase activity [GO:0008171]; protein homodimerization activity [GO:0042803]; S-adenosyl-L-methionine binding [GO:1904047]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF16864;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=1,6-dihydroxyphenazine + S-adenosyl-L-methionine = 1-hydroxy-6-methoxyphenazine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72523, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192365, ChEBI:CHEBI:192366; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDir... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.6 uM for 6-hydroxy-1-methoxyphenazine N(5)-oxide (at pH 7.8 and at room temperature) {ECO:0000269|PubMed:29510028}; Vmax=2.9 umol/min/mg enzyme with 6-hydroxy-1-methoxyphenazine N(5)-oxide as substrate (at pH 7.8 and at room temperature) {ECO:0000269|PubMed:2951... | null | null | null | FUNCTION: Involved in the biosynthesis of phenazine natural products including myxin, an N(5),N(10)-dioxide phenazine antiobiotic, which has antimicrobial activity. O-methyltransferase, which converts iodinin (1,6-dihydroxyphenazine N(5),N(10)-dioxide) to myxin (1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide). Catalyz... | Lysobacter antibioticus |
A0A172U6X0 | LR3E_METSD | MAFPKRLEYGGHALVWSGDWSAAGARKAIAGAARAGYDYIEIALLDPWQIDVALTKDLLQEYNLRAHASLGLSAATDVTSTDPAIVAKGDELLRKATDVLYALGGSELCGVIYCALGKYPGPASRENRANSVAAMQRLADYAADKGINIDLEVVNRYETNIMNTGLEGLAFLDEVNRPNAFLHLDTYHMNIEENGMAKSVLAAGDRLGYVHIGESHRGYLGTGNVDFASFFAALKQIDYRGPITFESFSSEIVDPKLSNTLCVWRNLWHDSDDLAGKALEFIKQRY | 5.1.3.31 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:33838083}; | null | null | isomerase activity [GO:0016853]; metal ion binding [GO:0046872] | PF01261; | 3.20.20.150; | Hyi family | null | null | CATALYTIC ACTIVITY: Reaction=L-ribulose = L-xylulose; Xref=Rhea:RHEA:53268, ChEBI:CHEBI:16880, ChEBI:CHEBI:17399; EC=5.1.3.31; Evidence={ECO:0000269|PubMed:33838083}; CATALYTIC ACTIVITY: Reaction=D-ribulose = D-xylulose; Xref=Rhea:RHEA:51544, ChEBI:CHEBI:17140, ChEBI:CHEBI:17173; EC=5.1.3.31; Evidence={ECO:0000269|PubM... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22.4 mM for L-ribulose {ECO:0000269|PubMed:33838083}; KM=27.8 mM for L-allulose {ECO:0000269|PubMed:33838083}; Note=kcat is 4923 min(-1) with L-ribulose as substrate. kcat is 4103 min(-1) with D-allulose as substrate. {ECO:0000269|PubMed:33838083}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius with D-allulose as substrate. {ECO:0000269|PubMed:33838083}; | FUNCTION: Catalyzes the epimerization of various ketoses at the C(3) position (PubMed:33838083). Exhibits the highest enzymatic activity toward L-ribulose, followed by D-ribulose, D-allulose and D-fructose (PubMed:33838083). Shows lower activity with L-xylulose, L-tagatose, D-xylulose, D-tagatose, L-sorbose, D-sorbose,... | Methylomonas sp. (strain DH-1) |
A0A178VEK7 | DUO1_ARATH | MRKMEAKKEEIKKGPWKAEEDEVLINHVKRYGPRDWSSIRSKGLLQRTGKSCRLRWVNKLRPNLKNGCKFSADEERTVIELQSEFGNKWARIATYLPGRTDNDVKNFWSSRQKRLARILHNSSDASSSSFNPKSSSSHRLKGKNVKPIRQSSQGFGLVEEEVTVSSSCSQMVPYSSDQVGDEVLRLPDLGVKLEHQPFAFGTDLVLAEYSDSQNDANQQAISPFSPESRELLARLDDPFYYDILGPADSSEPLFALPQPFFEPSPVPRRCRHVSKDEEADVFLDDFPADMFDQVDPIPSP | null | null | cell cycle G2/M phase transition [GO:0044839]; generative cell mitosis [GO:0055047]; pollen sperm cell differentiation [GO:0048235]; positive regulation of DNA-templated transcription [GO:0045893] | generative cell nucleus [GO:0048555]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:15694308}. Note=Accumulates in sperm-cell nuclei. {ECO:0000269|PubMed:15694308}. | null | null | null | null | null | FUNCTION: Transcription activator that acts as a positive regulator of male germline development by promoting both gametic cell specification and cell cycle progression (PubMed:15618418, PubMed:15694308, PubMed:19300502, PubMed:21285328). Binds to canonical MYB sites 5'-AACCGTC-3', 5'-AAACCGC-3' and 5'-AACCGT-3' in pro... | Arabidopsis thaliana (Mouse-ear cress) |
A0A178WF56 | CSTM3_ARATH | MAQYHQQHEMKQTMAETQYVTAPPPMGYPVMMKDSPQTVQPPHEGQSKGSGGFLRGCLAAMCCCCVLDCVF | null | null | negative regulation of response to salt stress [GO:1901001]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; response to salt stress [GO:0009651]; sodium ion homeostasis [GO:0055078] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | null | PF12734; | null | CYSTM1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29272523}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29272523}. Mitochondrion {ECO:0000269|PubMed:30701352}. | null | null | null | null | null | FUNCTION: Negatively regulates salt stress responses and Na(+) homeostasis (PubMed:29272523, PubMed:30701352). Prevents Na(+) efflux, disturbs reactive oxygen species (ROS) homeostasis, and represses the expression of nuclear salt stress-responsive genes (PubMed:30701352). Involved in resistance to abiotic stress (PubM... | Arabidopsis thaliana (Mouse-ear cress) |
A0A193AU77 | GGT24_PUNGR | MGSESLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNIGEEPSPIGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKEVIPRMIKKNEEQNRPVSCLINNPFIPWVSDVAESLGLPSAMLWVQSCACFAAYYHYYHGLVPFPSESAMEIDVQLPCMPLLKHDEVPSFLYPTTPYPFLRRAIMGQYKNLDKPFCVLMDTFQELEHEIIEYMSKICPIKTVGPLFKNPKAPNANVRGDFMKADDCISWLDSKPPASVVYVSFGSVVYLKQDQWDEIAFGLLNSGLNFLWVMKPPHKDSGYQ... | 2.4.1.120; 2.4.1.136; 2.4.1.170; 2.4.1.177; 2.4.1.194; 2.4.1.81 | null | 3,4-dihydroxybenzoate metabolic process [GO:0046278]; cinnamic acid ester metabolic process [GO:0009801]; ferulate metabolic process [GO:0033494] | cytoplasm [GO:0005737] | 4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity [GO:0047250]; cinnamate beta-D-glucosyltransferase activity [GO:0050412]; flavone 7-O-beta-glucosyltransferase activity [GO:0047891]; gallate 1-beta-glucosyltransferase activity [GO:0047913]; isoflavone 7-O-glucosyltransferase activity [GO:0050004]; quercetin 3-... | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27227328}. | CATALYTIC ACTIVITY: Reaction=3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP; Xref=Rhea:RHEA:15249, ChEBI:CHEBI:15834, ChEBI:CHEBI:16918, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=3,4-dihydroxybenzoate + UDP... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.98 mM for gallic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.17 mM for 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=4.44 mM for 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsi... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:27227328}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity remains fairly constant between 20-55 degrees Celsius. Active even at 0 degrees Celsius. {ECO:0000269|PubMed:27227328}; | FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinna... | Punica granatum (Pomegranate) |
A0A193AUF6 | GGT23_PUNGR | MGSESSLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNISDQPAPVGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKVLIPQMIQKNAEQGRPVSCLINNPFIPWVSDVAETLGLPSAMLWVQSCACFLAYYHYYHGLVPFPSENAMEIDVQLPSMPLLKHDEVPSFLYPTTPYPFLRRAILGQYKNLEKPFCILMDTFQELEHEIIEYTSKICPIKTVGPLFKNPKAPNTTVKGDFMKADDCIGWLDSKPASSVVYVSFGSVVYLKQDQWDEIAYGLLNSGVNFLWVMKPPHKDSGY... | 2.4.1.120; 2.4.1.136; 2.4.1.170; 2.4.1.177; 2.4.1.194; 2.4.1.81 | null | 3,4-dihydroxybenzoate metabolic process [GO:0046278]; cinnamic acid ester metabolic process [GO:0009801]; ferulate metabolic process [GO:0033494] | cytoplasm [GO:0005737] | 4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity [GO:0047250]; cinnamate beta-D-glucosyltransferase activity [GO:0050412]; flavone 7-O-beta-glucosyltransferase activity [GO:0047891]; gallate 1-beta-glucosyltransferase activity [GO:0047913]; isoflavone 7-O-glucosyltransferase activity [GO:0050004]; quercetin 3-... | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27227328}. | CATALYTIC ACTIVITY: Reaction=3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP; Xref=Rhea:RHEA:15249, ChEBI:CHEBI:15834, ChEBI:CHEBI:16918, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=3,4-dihydroxybenzoate + UDP... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.89 mM for gallic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.19 mM for 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=2.46 mM for 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsi... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:27227328}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity remains fairly constant between 20-55 degrees Celsius. Active even at 0 degrees Celsius. {ECO:0000269|PubMed:27227328}; | FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinna... | Punica granatum (Pomegranate) |
A0A193CHJ5 | PA2BC_CROTA | MRALWIVAVLLVGVEGHLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTKWDIYPYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PIRSR:PIRSR601211-2}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000255|PIRSR:PIRSR601211-2}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; ion channel regulator activity [GO:0099106]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361236, ECO:0000305|PubMed:35737043}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:35737043}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=9.8 umol/min/mg enzyme (monomer CBc) {ECO:0000269|PubMed:35737043}; | null | null | null | FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (By similarity). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a ... | Crotalus tzabcan (Yucatan neotropical rattlesnake) (Crotalus simus tzabcan) |
A0A193KX02 | TOMT_DANRE | MVSPAIALAFLPLLLTLIIRYRYYFVLLYRAVLTRWVRDCLSGISREERAFQYILTHATPGDSQSILDTFDTWCSKVEFISNIGPKKGKILDRLLQENCPITVLELGTHCGYSTVRMARSLPIGARIYSVEMDQRNAQVAEKIIRLAGFDDDMVELIQRPSDEVIPRLREDLGVERLDLVLMDHWKRCYLPDLHLLEDSGLIGQGSIILADNVIFPGAPNFLRYARRCGLYEVRVHRATLEYMRGIPDGMAELTYIGIK | 2.1.1.6 | null | auditory behavior [GO:0031223]; catecholamine catabolic process [GO:0042424]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; developmental process [GO:0032502]; dopamine metabolic process [GO:0042417]; endocytosis [GO:0006897]; hair cell differentiation [GO:0035315]; inner ear receptor ce... | basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794] | catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; orcinol O-methyltransferase activity [GO:0102938] | PF01596; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:28534737}. Golgi apparatus {ECO:0000269|PubMed:28534737}. Basolateral cell membrane {ECO:0000269|PubMed:28534737}. Note=Enriched in an apical membrane compartment above the nucleus in the hair cells. Not detectable in the hair bundle. May be present at low... | CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000250|UniProtKB:P21964}; | null | null | null | null | FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (By similarity). Required for auditory function. Component of the hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for t... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A1B0GTW7 | CIROP_HUMAN | MLLLLLLLLLLPPLVLRVAASRCLHDETQKSVSLLRPPFSQLPSKSRSSSLTLPSSRDPQPLRIQSCYLGDHISDGAWDPEGEGMRGGSRALAAVREATQRIQAVLAVQGPLLLSRDPAQYCHAVWGDPDSPNYHRCSLLNPGYKGESCLGAKIPDTHLRGYALWPEQGPPQLVQPDGPGVQNTDFLLYVRVAHTSKCHQETVSLCCPGWSTAAQSQLTAALTSWAQRRGFVMLPRLCLKLLGSSNLPTLASQSIRITGPSVIAYAACCQLDSEDRPLAGTIVYCAQHLTSPSLSHSDIVMATLHELLHALGFSGQLFKK... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08148}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148}; | cell adhesion [GO:0007155]; establishment of left/right asymmetry [GO:0061966]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; membrane [GO:0016020] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233] | PF01457; | 3.10.170.20;3.90.132.10; | Peptidase M8 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Putative metalloproteinase that plays a role in left-right patterning process. {ECO:0000250|UniProtKB:A0A1D5NSK0}. | Homo sapiens (Human) |
A0A1B1FHP3 | DPAS_CATRO | MAGKSAEEEHPIKAYGWAVKDRTTGILSPFKFSRRATGDDDVRIKILYCGICHTDLASIKNEYEFLSYPLVPGMEIVGIATEVGKDVTKVKVGEKVALSAYLGCCGKCYSCVNELENYCPEVIIGYGTPYHDGTICYGGLSNETVANQSFVLRFPERLSPAGGAPLLSAGITSFSAMRNSGIDKPGLHVGVVGLGGLGHLAVKFAKAFGLKVTVISTTPSKKDDAINGLGADGFLLSRDDEQMKAAIGTLDAIIDTLAVVHPIAPLLDLLRSQGKFLLLGAPSQSLELPPIPLLSGGKSIIGSAAGNVKQTQEMLDFAAE... | 1.1.1.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00327}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00327}; | alcohol metabolic process [GO:0006066]; alkaloid biosynthetic process [GO:0009821]; lignin biosynthetic process [GO:0009809] | cytosol [GO:0005829] | alcohol dehydrogenase (NADP+) activity [GO:0008106]; cinnamyl-alcohol dehydrogenase activity [GO:0045551]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}. | CATALYTIC ACTIVITY: Reaction=dihydroprecondylocarpine acetate + NADP(+) = H(+) + NADPH + precondylocarpine acetate; Xref=Rhea:RHEA:58576, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142769, ChEBI:CHEBI:142770; Evidence={ECO:0000269|PubMed:29724909}; PhysiologicalDirection=right-to-left; Xref=Rh... | null | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29724909}. | null | null | FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts precondylocarpine acetate to dihydroprecondylocarpine acetate. {ECO:0000269|PubMed:2... | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
A0A1B1J8Z2 | CHIT5_LOTJA | MIIKLLVALIHYLHETMAVQSIITTPLLVILMSLRSYAFTEPSLHRQQPPSKGGVRAAYWPAWSDFSTSSIDTNYFTHIYYAFVQPAPESFNLEITESYKKWAPKYDGIHNIRPRVTTLLSIGGGGNNATLFSEMASSKQNRASFINSTIHVARKHEFNGLDLDWEWPGDEKDMSNLALLLKEWYKALVVEANTSRKSRLLLTSAVYFNSTISLIGNGPRSYPVRAIRKYLDWASPMCFDYNGAWANETGFNAALYDPNSNISTKYGIGSWIGSGVPAEKLVMGLPLYGRAWELKDPNDHGVGAKAVGPAVDTDGSMDYD... | 3.2.1.14 | null | chitin catabolic process [GO:0006032]; defense response to fungus [GO:0050832]; nodulation [GO:0009877]; 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}; | null | 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... | Lotus japonicus (Lotus corniculatus var. japonicus) |
A0A1B1WAJ0 | RAD1_LOTJA | MSPPLYSVLLEDENSVFLLDLDLSSPMGFHAYPHLPILDSSIANWSLPFSISDETFRESKKLKRTMIPISSADFSISSSSSLSVSVNSIPRLNFRDHIRTYKRYLAAEELPEDTNSSESVVGAEEDGCADGMRLVQLLIACAEAVACRDKAHASMLLSELKSNALVFGSSFQRVASCFVQGLAERLTLIQPIGSGAGVSQSMMNIMDAASEEMEEAYRLVYETCPHIQFGHFVANSTILEAFEGESFVHVVDLGMSLGLPHGHQWRGLIHSLANRASGHGRVRRLRITAIGLCIARLQAIGDELSDYANNLGINLEFSVV... | null | null | arbuscular mycorrhizal association [GO:0036377]; cellular response to phosphate starvation [GO:0016036]; detection of phosphate ion [GO:0010247]; regulation of DNA-templated transcription [GO:0006355]; response to symbiotic fungus [GO:0009610] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF03514; | null | GRAS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25560877}. | null | null | null | null | null | FUNCTION: Transcription factor acting as a regulator of arbuscular mycorrhiza (AM)-related genes (e.g. PT4, STR and RAM2) (PubMed:25560877). Required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis) (PubMed:25560877). Also involved in restricting mycorrhizal colonization o... | Lotus japonicus (Lotus corniculatus var. japonicus) |
A0A1B2CTC5 | PENN_PENTH | MYHQLESHGVFPTLGDDAAKLVRTTHVQEIAFTPISEIQRFCEAQNISCDSFYLNVWSLVLRAFAETNSVCVGFGDFRPSGARLDQALFKILQTTLSPKSSILSILQGFKQDERAFSVNHREPAHNTGVVFISEASGPLDLASLGKLKYDLLMVVSFDSKSIPISLFLVYRPSTLSQSHAENLSSNITQAMQQVLARPNSFVNDVELFSTFNKSLVLCWNGLERKAASLLEVIQGHVRSRPDHPAICAWDGTISYSQLDMLTTQWASYLQSRGVQPGCLVPIMMEHSKWAIIGEIAILKAGAAFVPIDPAHPVSRLKGIV... | 6.3.2.-; 6.3.2.40 | null | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; antibiotic biosynthetic process [GO:0017000]; heterocycle biosynthetic process [GO:0018130]; monocarboxylic acid biosynthetic process [GO:0072330]; toxin biosynthetic process [GO:0009403] | cytosol [GO:0005829] | ligase activity [GO:0016874]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF08242;PF00550; | 3.30.300.30;1.10.1200.10;3.40.50.1820;3.30.559.10;3.40.50.12780;3.30.559.30;3.40.50.150; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=anthranilate + 2 ATP + O-methyl-L-tyrosine + S-adenosyl-L-methionine = (-)-4'-methoxycyclopeptine + 2 AMP + 2 diphosphate + 2 H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74487, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57856, ChEBI:CHEBI:59... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:25859931}.; PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:25859931}.; PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25859931}. | null | null | FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group (PubMed:25859931). The first stage is catalyzed by the nonribosomal peptide synthetase penN that condenses anthranil... | Penicillium thymicola |
A0A1B4XBK0 | SDNC_SORAA | MSFDQFAPFMTLGRPDAVCDECSRPVAPNSISDDDAAVNTTETDTQHANIPEEQDVINIKLDSTFNAESSAETIDLKVEGVKLAIVSQQPTYEAITAETTSSVATSEEASSDTATSLTNLTSREPSPSSSSASSVAEECPSEEPASDDTVPAASEKNHPDGTLNPNYHDARADEVHPQHEVVQVQAPHLPPPQGVQPAATENPDHDSLFSVFTQDHNPLLSGTIVGAPADYVASTPGKKIRDKAASALNIWLQVSPDDLNQIRTVIDMLHNASLILDDVEDGSVSRRGRPATHMIFGMPQAINSAGYQINRAMMEVLKLG... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; antibiotic biosynthetic process [GO:0017000]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:27072286}. | null | null | FUNCTION: Geranylgeranyl diphosphate synthase; part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure (PubMed:27072286). First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosp... | Sordaria araneosa (Pleurage araneosa) |
A0A1C3NSL9 | AJM1_CAEEL | MSTTTPEKPEEIIDATGTSDTAEKIEVVISKEEPAEQKNEVEEPDYAQVPAESEDDAAQELAPTDSAIQVVHVLEAPQKAELVTIPLAHSEAEDHKLADADRDQEEELVFNEERRKTVTMDDNASLRSASITFDANRDEQDLLNESFASNPTDETVLMQKTKDEMDATSERPRSPLDLPPPPASVVLHPSAPPPPPPPLSSTEVVGNTTTTTTTHYAPKTWNDPSITTAPKIPVSLLSGAQPLPSVLTQRTTTSSYSAPNYSASSMSGVPSDVAPPPPLPIPNQSSSSAASYQHHHASSISKSISSSREDLLSEHATSRS... | null | null | cell-cell junction organization [GO:0045216]; embryo development ending in birth or egg hatching [GO:0009792] | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; cell-cell junction [GO:0005911]; ciliary basal body [GO:0036064]; dendrite terminus [GO:0044292]; plasma membrane [GO:0005886] | cytoskeletal protein binding [GO:0008092]; metal ion binding [GO:0046872] | null | 6.10.140.2220; | null | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}. Cell projection, cilium {ECO:0000269|PubMed:27623382}. Cell junction, adherens junction {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}. Note=grdn-1-dependent localization at sensory neuron dendritic tips (... | null | null | null | null | null | FUNCTION: Controls adherens junction integrity (PubMed:11715019). Required for the correct rate and completion of elongation of the embryos (PubMed:11715019). {ECO:0000269|PubMed:11715019}. | Caenorhabditis elegans |
A0A1C7D1B7 | ELP3_DEHMC | MKKLSRTISGVTPVAVMTKPLPCPGKCIYCPTFAATPQSYTPESPAVLRAKSCEYQAYKQVALRLRIIQDMGHPTDKVELIIMGGTFLSADITYQYGFIKDCYDALNGVVAGSLEEAKTINETAQHRCVGLCIETRPDICGKAEIQRMIDFGTTRVELGVQMLDDDIYKLVERGHRVSDVAEATCLLREYGLKVHYHWMPGLPGSSPEKDLALSRMVFEDPRFCPDGLKLYPTMVVEGTILEQWWKEGRYTPYPNGTMTGLIADIKALVPPYVRISRVLRDIPAVFISAGLKDSLRDGVRQILESRHQKCRCIRCREYGH... | 2.3.1.311 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:27455459}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q02908}; | tRNA acetylation [GO:0051391]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble uridine modification [GO:0002098] | cytoplasm [GO:0005737]; elongator holoenzyme complex [GO:0033588] | 4 iron, 4 sulfur cluster binding [GO:0051539]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; S-adenosyl-L-methionine binding [GO:1904047]; tRNA binding [GO:0000049]; tRNA uridine(34) acetyltransferase activity [GO:0106261] | PF04055;PF16199; | 3.40.630.30; | ELP3 family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:5... | null | PATHWAY: tRNA modification. {ECO:0000269|PubMed:27455459}. | null | null | FUNCTION: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:27455459). The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adeno... | Dehalococcoides mccartyi (strain CBDB1) |
A0A1C8AX29 | PIGK_MONRU | MEASDQSQAKLTLSFGGIQHAFSVPIEDLSALQDQKDAFLRSRSQASLSETREPCSPAELMLDYLEFLSCRNLPPPLTKPVLLAFSRNFLHNTEIHSLLAKPEYTPQTRRRLVRTYYMAALSAAESHVKESALLDAARQGNFQLAAVFGGQSTANPACVRELAELFAAYTPFLGDLISTAAPTLSALCRLPETKEHFCGRHIDIETWLHDPASIPDGDFIATAPVSCPVVGLLNLAHYAVTCHVLGKTPGELRSHLQGVTGHSQGIVAAVAISLSDSWESFYEAARMTVETLFWIGFECHQRSPRTSVSLDQVQDSLQNG... | 1.3.1.9; 2.3.1.38; 2.3.1.39; 2.3.1.86; 3.1.2.14; 4.2.1.59 | null | long-chain fatty acid biosynthetic process [GO:0042759] | fatty acid synthase complex [GO:0005835] | (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity [GO:0004317]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0004318]; fatty acid synthase activity [GO:000... | PF00698;PF08354;PF17951;PF17828;PF13452;PF01575;PF16073; | 1.20.1050.120;1.20.930.70;3.30.1120.100;6.10.140.1400;6.10.60.10;6.20.240.10;3.20.20.70;3.10.129.10;3.40.366.10; | Fungal fatty acid synthetase subunit beta family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChE... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:26946170, ECO:0000269|PubMed:28959415}. | null | null | FUNCTION: Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants (PubMed:26946170, PubMed:28959415, PubMed:34220766). PigJ and pigK form the two subuni... | Monascus ruber (Mold) |
A0A1C9ZP88 | LP9A_GLOTR | HGYVDQVTIGGQVYTGYQPYQDPYESPVPQRIERAIPGNGPVEDLTLLDIQCNGSGGSGTKPAALIASAAAGDEIAFHWTTWPSSHVGPVITYMGKVPSNTDITSYSPTGSDVIWFKIDEAGYENGKWAATDIMSAQNSTWTVTIPKALAPGQYIVRHEIIALHQAETYPGAQFYPDCFQVQVTGPGTETPTSQALVSFPGGYTPTTPGITFNVYSGSITSYPIPGPPVWTSNEAFSGGSSSSAAASSTAVASSTADSSSSAAATQSSSAAASGSAAPSSSAIGTSTASSAAASGTAIVDANTCMNNYNKCIDAGQPDPD... | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q1K8B6}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q1K8B6}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:27590806}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (PubMed:27590806). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to... | Gloeophyllum trabeum (Brown rot fungus) (Agaricus trabeus) |
A0A1D5AG16 | PIGJ_MONRU | MAVRKLVPETAPVVDDAPASTSVDHKRSLAHKLLIELLSYQLALPVRWIETQNELLQWPETIQRYVEVGPRTTLVTMAKKTAARRASSQIVSASKLSTLKFLCTSDNTAEIYYEYPQESGAPVEEEGSKSDAAAPALAVSGSSRTATTAKATVTTPSSSSPETAPPAASTPSQGTPAGGSTTPDIPLSAKHVVLAMIAQKFRRAFDNIPTQKTVQELSGGKSTLQNEIMGDLAVEFGQLPDGGEYIPLDALGDALQGNFPGKPGKQMSSLITKLISRKMPGGFNQAAMQNHLEREWGFSKAHGQVVICLAITVEPESRLE... | 1.1.1.100; 2.3.1.41; 2.3.1.86 | null | heterocycle biosynthetic process [GO:0018130]; long-chain fatty acid biosynthetic process [GO:0042759]; organic cyclic compound biosynthetic process [GO:1901362] | fatty acid synthase complex [GO:0005835] | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; holo-[acyl-carrier-protein] synthase activity [GO:0008897]; magnesium ion binding [GO:0000287] | PF01648;PF18325;PF18314;PF00109;PF02801; | 3.30.70.2490;3.40.47.10;3.90.25.70;6.10.140.1410;3.90.470.20;3.40.50.720; | Thiolase-like superfamily, Fungal fatty acid synthetase subunit alpha family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChE... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:26946170, ECO:0000269|PubMed:28959415}. | null | null | FUNCTION: Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants (PubMed:26946170, PubMed:28959415, PubMed:34220766). PigJ and pigK form the two subun... | Monascus ruber (Mold) |
A0A1D5NS60 | ZN16L_DANRE | MSRKRNHCYMETGASSESQGAFVDSAGPFSRDEEDFSELEPDEQLVCSVTEITEHLGRNITVVLESALSEIRKLVGVRIRVLKMELREKSDEIELLKAKLESAEKDGRVSNFSSLDFRKSEHQKYGAEPKKAKTGTPVVKKENINAICDYLMKDKNQRGAAEVESDHSNQAFGSERDVRTEAQPHGSLSLWPDSGPADTDAETDIFSMLPSASKRMYDYEWMTGVELNSAEFKGDSETKCEDVPPMDEEDENEDSEEGRGSLRSVSDHFPLDTQGSPGEDRSSPAEDSMDRMEPGQQFTSHTFICPFCGTLCPDSSFLEE... | null | null | central nervous system myelination [GO:0022010]; positive regulation of myelination [GO:0031643]; positive regulation of oligodendrocyte differentiation [GO:0048714]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Probable transcription factor (Probable). Important for development and migration of oligodendrocyte precursor cells, and normal myelination of axons in the central nervous system (CNS) (PubMed:26459222). Functions autonomously in oligodendrocytes to promote CNS myelination (PubMed:26459222). Seems to act in ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A1D5NSK0 | CIROP_DANRE | MSFLLCIGILLLPWFPCVCGKCIFDQIQRSVNVVSPPTAQYASAYRFKTQRSKRHIMPMDNLQPIRIKIWIPSESPALSDWEREKLMSAVGEAVSEVSSLLSVKRVKDRLLLNRDVNKYCKFIWRNSSTLNHMKCGRAHENYRFESCLGVIIPDEHLDGCSVYPNPEHPVPTVLRPRGPGVPDADFLLYVFTHNTEKCRAESSVLAYTAHCQTGSDGRPLAGTMVICRETLKKERYTYQHFVKVTTVIHELFHVLGFSKELLSNWKDFGVDCWSHGQVTSTDQTGQVRLYSPTVIRAMQKHFNSTHTDLGAPLENKDAAL... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08148}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148}; | cell adhesion [GO:0007155]; determination of heart left/right asymmetry [GO:0061371]; establishment of left/right asymmetry [GO:0061966]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; membrane [GO:0016020] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233] | PF01457; | 3.10.170.20;3.90.132.10;2.30.34.10; | Peptidase M8 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Plays an essential role for patterning the left-right axis. Requires solely on the left side, downstream of the leftward flow, but upstream of dand5, a nodal inhibitor involved in left-right patterning. {ECO:0000269|PubMed:34903892}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A1D5NSM8 | SVEP1_DANRE | MMVTLRLALTLRLTVLLLYWSGCTCWPSHAQQFSLQSLRQTSQARQNLSESAESKVERLGQVFRKNVRLLRERGGCLDLVFLVDESSSVGASNFKSELRFVRKMLSDFPVAPEATRVALVTFSSKSHVVTRADYVSAPKAHQHKCSLFSKEIPSITYRGGGTYTRGAFQRAAQILRQSRENATKVIFLITDGYSNGGDPRPVAAALRERGVEIFTLGIWQGNIRELHEMASQPKDQHCFFVHNFAEFEALARRALHEDLPSGNYIQEDLAQCSSLCDGGKDCCDLMASCKCGTHTGQYDCVCEKGYYGKGLQHECTACPS... | null | null | cell migration [GO:0016477]; epidermal cell differentiation [GO:0009913]; epidermis development [GO:0008544]; epithelial cell-cell adhesion [GO:0090136]; lymph vessel development [GO:0001945]; lymph vessel morphogenesis [GO:0036303]; negative regulation of complement activation, classical pathway [GO:0045959] | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | calcium ion binding [GO:0005509] | PF00008;PF12947;PF07699;PF12661;PF02494;PF00354;PF00084;PF00092; | 2.60.120.200;2.10.70.10;2.10.25.10;2.10.50.10;3.40.50.410; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A2AVA0}. Nucleus {ECO:0000250|UniProtKB:Q4LDE5}. Cytoplasm {ECO:0000250|UniProtKB:Q4LDE5}. Membrane {ECO:0000250|UniProtKB:Q4LDE5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q4LDE5}. | null | null | null | null | null | FUNCTION: Required for embryonic lymphatic vascular development, via promotion of parachordal lymphangioblast development, cell alignment and migration both dorsally and ventrally (PubMed:28179430, PubMed:28179432, PubMed:37097004). Required for the formation of facial lymphatic structures and formation of brain lympha... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A1D5NY17 | TM182_CHICK | MKLSVGIFFGGLFAALGVLLFLVAFGTDYWLLATEIGRCSKAPEDAGTEKATFHHEGFFWRCWFSGNVREHNTSMWKFWYTNQSPSKNCTHAYLSPFPHIRDEHNSTSYDSAVIYRGFWTVLMLLGVITIVMASFLIICAAPFASHILYKAGGGFYILAGVLFSLVVVMYVIWVQAMADLENYTNMKKMDCPDFAVYVRYGWSFMLAPIGVFFALLAGMLFLLVGRAIYLNSD | null | null | muscle organ development [GO:0007517]; myotube cell development involved in skeletal muscle regeneration [GO:0014906]; myotube differentiation involved in skeletal muscle regeneration [GO:0014908]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myoblast fusion [GO:1901740] | plasma membrane [GO:0005886] | null | PF13903; | 1.20.140.150; | TMEM182 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34427057}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Negatively regulates myogenesis and skeletal muscle regeneration via its association with ITGB1 (PubMed:34427057). Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and inhibiting ITGB1-mediated intracellular signaling during myogenesis (PubMed:34427057). {ECO:0000269|PubMed:34427057}. | Gallus gallus (Chicken) |
A0A1D5PPP7 | CASP6_CHICK | MSGAERRPAAGRVQLDSKPTPTTTADGNQNITEVDAFDKRQTFDPAVQYKMNHQRRGVALIFNHEHFFWHLRLPDRRGTLADRNNLKRSLTDLGFEVRIFDDLKAEDVLKKVFEASRDDYSNADCFVCVFLSHGENDHVYAYDAQIKIETITNMFRGDKCQSLVGKPKIFIIQACRGDKHDDPVLVQDSVDSKDETTVNQTEVDAAGVYTLPAGADFIMCYSVAQGYFSHRETVNGSWYIQDLCEALGKHGSSLEFTELLTVVNRKVSHRKVDICRDINAIGKKQIPCFASMLTKKLYFHPKSK | 3.4.22.59 | null | activation of innate immune response [GO:0002218]; apoptotic chromosome condensation [GO:0030263]; apoptotic DNA fragmentation [GO:0006309]; apoptotic nuclear changes [GO:0030262]; apoptotic process [GO:0006915]; hepatocyte apoptotic process [GO:0097284]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type peptidase activity [GO:0008234] | PF00656; | 3.40.50.1460; | Peptidase C14A family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}. | CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59; Evidence={ECO:0000250|UniProtKB:P55212}; | null | null | null | null | FUNCTION: Cysteine protease that plays essential roles in programmed cell death, development and innate immunity (PubMed:11953316). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein lamin-A/LMNA thereby inducing nuclear shrinkage and fragme... | Gallus gallus (Chicken) |
A0A1D5PRR9 | FANCM_CHICK | MSGGRQRTLPEAWRRAAGPALQAGRDADGNDDDDDELLAAAAAELDPDPNPNVDPNPGPGPEAAAGGFCAAAGALWIYPTNRPERPYQLRMARAALFANTLLCLPTGLGKTFVAAVVMYNFYRWFPSGKVLFLAPTKALVAQQMEACAQLMGIPGRDMAEMTGGTQALSRRELWASRRVFFLTPQIMVNDLSRGTCPAVEVKCLVVDEAHKALGNHAYCQVVKELSRYTTQFRVLALTATPGSDTKAVQQVVSNLLIAQIELCSEDSPEIQPYSHERQVEKIVVPLGEELGGIQRAYIHVLETFAGRLIKLGVLARRDVP... | 3.6.4.13 | null | double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; interstrand cross-link repair [GO:0036297] | nucleus [GO:0005634] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; four-way junction DNA binding [GO:0000400]; four-way junction helicase activity [GO:0009378]; nuclease activity [GO:0004518]; RNA helicase activity [GO:0003724] | PF00270;PF02732;PF16783;PF00271; | 3.40.50.10130;1.10.150.20;1.20.1320.20;3.40.50.300; | DEAD box helicase family, DEAH subfamily, FANCM sub-subfamily | PTM: Phosphorylated; hyperphosphorylated in response to genotoxic stress. {ECO:0000269|PubMed:19465393}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19465393}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q8IYD8}; | null | null | null | null | FUNCTION: DNA-dependent ATPase component of the Fanconi anemia (FA) core complex (By similarity). Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal break... | Gallus gallus (Chicken) |
A0A1D5PUP4 | RECK_CHICK | MAAAVAAWPWALFCLAAVPPLLSPGAAGLSCCYHAKDNLMCRDVCEQILSSKSDSRLKHLLQRAPEYCPESMGEVWGCINSSLPGVLKKSDGWVGLGCCELAIAVECRQACKQASSKNDILKVCRKEYENALFSCINRNEMGSICCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDYACQTACKRILMSMKTELEIVDGLIEGCKTMPLPQDPLWQCFLESSRSVHPGVTVHPPPSTGLDGAKLHCCSKANSSTCRELCTKLYSTSWGSSQSWQEFDRFC... | null | null | blood vessel maturation [GO:0001955]; canonical Wnt signaling pathway [GO:0060070]; extracellular matrix organization [GO:0030198]; negative regulation of metalloendopeptidase activity [GO:1904684]; regulation of angiogenesis [GO:0045765]; regulation of establishment of blood-brain barrier [GO:0090210]; sprouting angio... | extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; Wnt signalosome [GO:1990909] | coreceptor activity [GO:0015026]; endopeptidase inhibitor activity [GO:0004866]; metalloendopeptidase inhibitor activity [GO:0008191]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF07648; | 3.30.60.30; | RECK family | PTM: Localizes to the plasma membrane via its GPI-anchor (PubMed:23329048). Released from the plasma membrane following cleavage of the GPI-anchor by GDPD5/GPE2 (PubMed:23329048). {ECO:0000269|PubMed:23329048}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23329048}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23329048}. | null | null | null | null | null | FUNCTION: Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (By similarity). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Acts as a Wnt7-speci... | Gallus gallus (Chicken) |
A0A1D5PXA5 | TRPV4_CHICK | MADPEDPRDAGDVLGDDSFPLSSLANLFEVEDTPSPAEPSRGPPGAVDGKQNLRMKFHGAFRKGPPKPMELLESTIYESSVVPAPKKAPMDSLFDYGTYRQHPSENKRWRRRVVEKPVAGTKGPAPNPPPILKVFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLTENGHKQADLRRQDSRGNTVLHALVAIADN... | null | null | actin filament organization [GO:0007015]; calcium ion import across plasma membrane [GO:0098703]; intracellular calcium ion homeostasis [GO:0006874]; osmosensory signaling pathway [GO:0007231] | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cilium [GO:0005929]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; calcium channel activity [GO:0005262]; calmodulin binding [GO:0005516]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; monoatomic cation channel activity [GO:0005261]; phosphatidylinositol binding [GO:0035091]; SH3 domain binding [GO:0017124] | PF00023;PF00520; | 1.10.287.70;1.25.40.20; | Transient receptor (TC 1.A.4) family, TrpV subfamily, TRPV4 sub-subfamily | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000305|PubMed:11081638, ECO:0000305|PubMed:19864432}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9EPK8}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9EPK8}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11081638, ECO:0000269|PubMed:19864432}; | null | null | null | null | FUNCTION: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:11081638, PubMed:19864432). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:11081638). Also activated by phorbol esters (PubMed:19864432)... | Gallus gallus (Chicken) |
A0A1D6E0S8 | WAK17_MAIZE | MPSRSPACRPRGRNRRSAADAVARPLALALILVSTLPRAAHSQDLALPPVQPRGVRRTMTCDNIPEPFGTRSRGASRLPGFEVTCGPNREAMLSIGGDAYMIDFVSVSGSYVVVFAEPITQVCYDGKGKPTPDTGTGAKSSEGTTTTFTWSLEGTPFTFSKSNKLVNFGCNRTLMANFFIVPGDSSPLYTSCTTTCNTLQISGSCLGEACCEAPMDQVNGAKAFSLSFERTTANGTGEEDGTCSAAFFLDKDETVFTFSGDEVRPLKTALLPPGERRMVLDWAIGSTSCEQTQSYTFEKLCKYGTCVDAPTGAGYLCKCP... | 2.7.11.1 | COFACTOR: [Isoform 1]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q1MX30}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q1MX30}; | cell surface receptor signaling pathway [GO:0007166]; detection of symbiotic fungus [GO:0009603]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; positive regulation of plant-type hypersensitive response [GO:0034052] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 2.10.25.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:36577386}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:36577386}; Peripheral membrane protein {ECO:0000305|PubMed:36577386}. Note=Associates with the plasma membrane via inte... | CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q1MX... | null | null | null | null | FUNCTION: [Isoform 1]: Kinase that contributes to activation of the hypersensitive response, a form of programmed cell death, upon fungal infection. {ECO:0000269|PubMed:36577386}.; FUNCTION: [Isoform 2]: Secreted protein that contributes to activation of the hypersensitive response, a form of programmed cell death, upo... | Zea mays (Maize) |
A0A1D6EFT8 | EDSB_MAIZE | MAPSNIVVQSSSTPPVAGGDEEFAPSVWGDFFVTYATPVSQASEQRMSERAELLKAQVRQAFDAASMDVAGLITYVDTLERLGLDNHFRDLIGAALERIGAEELPEHGGGLHIVALRFRLLRQHGIWVSTDVFDAFREDAGGFCSSLCSDDPRGLLSLYNAAHMAVPGEVVLDDAIAFARGRLLDIISKGEVRSPVSEQITRALDIPLPRFTRRLETMHYIAEYEHEEAHDGLLLELARLNFVLVRALHLRELKDLSLWWRELYNTVKLPYARDRMVEIYFWTCGMLHEEEYSLARMFFAKTFGMVSLMDDTFDVHATLD... | 4.2.3.197 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | defense response to fungus [GO:0050832]; diterpenoid biosynthetic process [GO:0016102]; sesquiterpene biosynthetic process [GO:0051762]; terpene biosynthetic process [GO:0046246] | cytoplasm [GO:0005737] | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}. | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 2 H2O = 7-epi-ent-eudesmane-5,11-diol + diphosphate; Xref=Rhea:RHEA:58164, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:142536, ChEBI:CHEBI:175763; EC=4.2.3.197; Evidence={ECO:0000269|PubMed:29570233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30187155}. | null | null | FUNCTION: Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Dihydroxylated sesquiterpenoid synthase that generates dually hydroxylated products directly from (E,E)-farnesyl diphosphate, primarily eudesmane-2,11-diol, along with two closely related structural isomers (PubMed:29570233). {ECO:000... | Zea mays (Maize) |
A0A1D6HSP4 | C92C5_MAIZE | MELASTMSVAMALAAAIFVVLCSVVASARGRREKALKLPPGPRGWPVLGSLGALAGALPPHRALAALAARHGPLMHLRLGSYHTVVASSADAARLVLRTHDSALADRPDTAAGEITSYGYLGIVHTPRGAYWRMARRLCATELFSARRVESFQDVRAQEMRALARGLFGCAAGRRAVAVREHVAGATMRNILRMAVGEKWSGCYGSPEGEAFRRSLDEAFAATGAVSNVGEWVPWLGWLDVQGFKRKMKRLHDLHDHFYEKILVDHEERRRLAQASGGEFVATDLVDVLLQLSEESTKLESESEARLPRDGVKALIQDII... | 1.14.14.58; 1.14.14.59 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | defense response [GO:0006952]; response to herbivore [GO:0080027]; terpenoid biosynthetic process [GO:0016114] | membrane [GO:0016020] | 4,8,12-trimethyltrideca-1,3,7,11-tetraene synthase activity [GO:0097007]; DMNT synthase activity [GO:0102171]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; terpene synthase activity [GO:0010333] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(6E,10E)-geranyllinalool + O2 + reduced [NADPH--hemoprotein reductase] = (3E,7E)-4,8,12-trimethyltrideca 1,3,7,11-tetraene + but-3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:13545, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.2 uM for (E)-nerolidol {ECO:0000269|PubMed:27662898}; KM=5.6 uM for (6E,10E)-geranyllinalool {ECO:0000269|PubMed:27662898}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30187155}. | null | null | FUNCTION: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps) (By similarity). Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Converts mainly nerolidol to dimethylnonatriene (DMNT) and, to a lower exte... | Zea mays (Maize) |
A0A1D6IEG9 | CRP1_MAIZE | MPASLLPPTFLPHHLRRLAPAGCTTSSVTSSSVSIPASRYDFEPLLAYLSSPSVSASLTSPSPPASVPAPEHRLAASYSAVPSHEWHALLRDLAASDASLPLAFALLPFLHRHRLCFPLDLLLSSLLHSLSVSGRLLPHSLLLSFPPSLSDPPSPLLLNSLLAASAAASRPAVALRLLSLLREHDFLPDLASYSHLLASLLNTRDPPDAALLERLLGDLRESRLEPDAPLFSDLISAFARAALPDAALELLASAQAIGLTPRSNAVTALISALGTAGRVAEAEALFLEFFLAGEIKPRTRAYNALLKGYVRIASLKNAEQ... | null | null | chloroplast mRNA processing [GO:0010239]; chloroplast organization [GO:0009658]; mRNA processing [GO:0006397]; positive regulation of translation [GO:0045727] | chloroplast [GO:0009507]; chloroplast nucleoid [GO:0042644]; chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; thylakoid membrane [GO:0042651] | mRNA binding [GO:0003729]; single-stranded RNA binding [GO:0003727] | PF01535;PF13041;PF13812;PF17177; | 1.25.40.10; | PPR family, P subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:10228173}. | null | null | null | null | null | FUNCTION: Required for the translation of the chloroplast petA and petD mRNAs. Required for the processing of the petD mRNA from a polycistronic precursor (PubMed:8039510). Binds with high affinity to the 5'-UTR of the chloroplastic petA transcript (PubMed:18669444). Activates psaC and petA translation by binding their... | Zea mays (Maize) |
A0A1D6K6U5 | CPPS2_MAIZE | MVLSSSCTTVPHLSSLAVVQLGPWSSRIKKKTDAVAVPAAAGRWRARARAQDTSESAAVAKGSSLTPIVRTDAESRRTRWPTDDDDAEPLVDEIRAMLTSMSDGDISVSAYDTAWVGLVPRLDGGEGPQFPAAVRWIRNNQLPDGSWGDAALFSAYDRLINTLACVVTLTRWSLEPEMRGRGLSFLGRNMWKLATEDEESMPIGFELAFPSLIELAKSLGVHDFPYDHQALQAIYSSREIKVKRIPKEVMHTVPTSILHSLEGMPGLDWARLLKLQSSDGSFLFSPAATAYALMNTGDDRCFSYIDRTVKKFNGGVPNVY... | 5.5.1.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q38802}; | defense response [GO:0006952]; diterpene phytoalexin biosynthetic process [GO:0051502]; diterpenoid biosynthetic process [GO:0016102]; gibberellin biosynthetic process [GO:0009686] | chloroplast [GO:0009507] | ent-copalyl diphosphate synthase activity [GO:0009905]; isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397; | 1.50.10.160;1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsc subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl diphosphate; Xref=Rhea:RHEA:14841, ChEBI:CHEBI:58553, ChEBI:CHEBI:58756; EC=5.5.1.13; Evidence={ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842; Evidence={ECO:0000269|P... | null | PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Involved in gibberellin biosynthesis (PubMed:16307364). Catalyzes the conversion of geranylgeranyl diphosphate to the gibberellin precursor ent-copalyl diphosphate (ent-CPP) (PubMed:16307364). Involved in the production of antifungal dolabralexin phytoalexins in response to biotic and abiotic stresses (PubMed... | Zea mays (Maize) |
A0A1D6L709 | VP8_MAIZE | MPHSVLARLPPGSVRLVAAFGLLLLVSLLVLHRRPGRPHVAAAAASDRLTDPSRSRLFLSQSPGANASIAADLRALTAGPHLAGTPASAGAAAHVLARLRAAGLQTLTREYEPLLSYPGHASLALLRPDGSLLARLSLEEPADEGRRVVPPYHAYAPSGGAVAEAVFVNLGREEDYVVLERLGVGVRGRVAVARRGGGYRGGVVARAADKGAVAVLIAGNADGGVERGVVLLGGPGDPLTPGWAATSGAERLKFDDKAVKQRFPSIPSMPVSAKTAAAIIRSLGGPAIPAEWKDGLGVDTGGLGPGPTLVNFTYQEDRKF... | 3.4.17.21 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q04609}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q04609}; | embryo development ending in seed dormancy [GO:0009793]; flower development [GO:0009908]; leaf vascular tissue pattern formation [GO:0010305]; maintenance of meristem identity [GO:0010074]; photomorphogenesis [GO:0009640]; proteolysis [GO:0006508]; regulation of floral meristem growth [GO:0010080]; regulation of inflor... | plasma membrane [GO:0005886] | carboxypeptidase activity [GO:0004180]; metal ion binding [GO:0046872]; metallocarboxypeptidase activity [GO:0004181] | PF04389;PF04253; | 3.50.30.30;1.20.930.40;3.40.630.10; | Peptidase M28 family, M28B subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.; EC=3.4.17.21; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Involved in the regulation of meristem development and seed maturation processes. Mediates regulation of embryonic regulatory genes and genes controlling abscisic acid (ABA) biosynthesis and turnover in developing seeds. May be required for the synthesis of small signaling molecules that integrates meristem a... | Zea mays (Maize) |
A0A1D6LAB7 | RH3B_MAIZE | MASLTLPALALALSNPGAVRLRAAAFRCWALRRRGWAAAGALASPNSVLSEHAFKRLQLGSDDEDGEGPYGSDADEGFEAGEGDNEELAIARLGLPDELVATLEKRGITHLFPIQRAVLIPALEGRDLIARAKTGTGKTLAFGIPMIKQLIEQDDGRITRRGRTPRVLVLAPTRELAKQVEKEIKESAPKLGTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVQYLVLDEADQMLAVGFEEDVETILQQLPAGRQSMLFSATMPSWVKKLSRRYLNNPLTIDLVGDQDEKLAEGIKLYAIPLTTTS... | 3.6.4.13 | null | chloroplast organization [GO:0009658]; Group II intron splicing [GO:0000373]; ribosome biogenesis [GO:0042254] | chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; zinc ion binding [GO:0008270] | PF00270;PF08152;PF00271;PF00098; | 3.40.50.300;4.10.60.10; | DEAD box helicase family, DDX21/DDX50 subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:22576849}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit. Required for normal development of... | Zea mays (Maize) |
A0A1D6LTV0 | TPS26_MAIZE | MAGITGVMNMKLAARPSSGRHSRGCRPAVVPSAGKQMLLVRRHPPGSASWPTRATGGGGGGVPAGATAADSSGQAKEEEEEDRASRNTSSFEPSIWGDFFLTYSSPLATSSAQKARMVHRAEQLKKQVAKLIAASGACSLYHRIHLVDALERLCLDYLFEDEINDMVTQIHNVDVSGCDLQTVAMWFYLLRNHGYRVSSDVVFAKFRDEQGGFAANNPRDLLNLYNAACLRTHGETILDEAASFTSKCLKSLAPYTYMEASLASEIKRALEIPLPRSVRIYGAKSRIAEYGNQTEANELVLELAKLNYNLVQLQHQEELK... | 4.2.3.-; 4.2.3.111; 4.2.3.113; 4.2.3.114; 4.2.3.15; 4.2.3.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:B2C4D0}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B2C4D0}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q5GJ60}; | diterpenoid biosynthetic process [GO:0016102]; response to wounding [GO:0009611]; terpenoid biosynthetic process [GO:0016114] | chloroplast [GO:0009507] | (4S)-limonene synthase activity [GO:0050552]; gamma-terpinene synthase activity [GO:0102903]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18218975}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol + diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.111; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552; Evidence={ECO... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30187155}. | null | null | FUNCTION: Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Mediates the synthesis of a blend of monoterpenes. Converts mainly geranyl diphosphate to alpha-terpineol. Triggers also the biosynthesis of minor monoterpenes including limonene, gamma-terpinene, beta-myrcene, terpinolene and 4-terpi... | Zea mays (Maize) |
A0A1D8EJF9 | IF4E1_SOLPI | MAAAEMERTMSFDAAEKLKAADGGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDNPTTKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLIMGADFHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRAKGEKIALWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV | 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-129-Cys-167 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:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}. Note=Binds to potyvirus viral genome-linked protein (VPg) in the nucleus and with potyvirus nuclear inclusion protein A (NIa-Pro) and nuclear inclusion protein B (NIb) in the cytoplasm. {ECO:0000250|UniProtKB:C6ZJZ3}... | 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 (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... | Solanum pimpinellifolium (Currant tomato) (Lycopersicon pimpinellifolium) |
A0A1D8PCL1 | HGT1_CANAL | MSSKIERIFSGPALKINTYLDKLPKIYNVFFIASISTIAGMMFGFDISSMSAFIGAEHYMRYFNSPGSDIQGFITSSMALGSFFGSIASSFVSEPFGRRLSLLTCAFFWMVGAAIQSSVQNRAQLIIGRIISGIGVGFGSAVAPVYGAELAPRKIRGLIGGMFQFFVTLGIMIMFYLSFGLGHINGVASFRIAWGLQIVPGLCLFLGCFFIPESPRWLAKQGQWEAAEEIVAKIQAHGDRENPDVLIEISEIKDQLLLEESSKQIGYATLFTKKYIQRTFTAIFAQIWQQLTGMNVMMYYIVYIFQMAGYSGNSNLVASS... | null | null | carbohydrate transport [GO:0008643]; cellular response to heat [GO:0034605]; cellular response to neutral pH [GO:0036244]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to heat [GO:0036168]; filamentous growth of a population of unicellular organisms in respons... | extracellular vesicle [GO:1903561]; membrane [GO:0016020]; plasma membrane [GO:0005886] | carbohydrate:proton symporter activity [GO:0005351]; glucose transmembrane transporter activity [GO:0005355] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: High-affinity glucose transporter (PubMed:10612724, PubMed:12187386). Acts as a multifunctional complement-evasion molecule that causes down-regulation of complement activation by acquisition of human complement factors FH and C4BP (PubMed:21844307). Functions also as a human immunodeficiency virus (HIV) rece... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PDV7 | VPS34_CANAL | MATLSQPQSALPKTKIATTFGLSKDLKSPISVKVCYLECTRNNVSLVPLSTKFEDPTVFKKLSQIYKNSDLFVEIRVYDGKNNNLISTPVRTSYKAFNNKGRTWNQQLKLNIDYNQISIDAYLKFSICEIIDTKPSVFGVSYLSLFSHDSSTLRSGSHKIPVFMEDDPQYSKNIQYGTLIGLTDLEKRLIDYENGKYPRLNWLDKMVLPKVDATFLKTNNKDHDYYLYIELPQFEFPIVYSDIIYQIPTIEPITETTSKIPPDDTLNSNIIINSIDIPMATSHDPSIMKVYDPDFHITANNHLNPNATTFDPVELKYRKL... | 2.7.1.137 | null | ascospore-type prospore membrane formation [GO:0032120]; autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to osmotic stress [GO:0071470]; cellular response to starvation [GO:0009267]; endocytosis [GO:0006897]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellul... | cytoplasm [GO:0005737]; endosome [GO:0005768]; endosome membrane [GO:0010008]; fungal-type vacuole membrane [GO:0000329]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus-vacuole junction [GO:0071561]; peroxisome [GO:0005777]; phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kinase complex, cla... | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; ATP binding [GO:0005524]; protein kinase activity [GO:0004672] | PF00454;PF00792;PF00613; | 2.60.40.150;1.10.1070.11;1.25.40.70; | PI3/PI4-kinase family | PTM: Autophosphorylated. {ECO:0000269|PubMed:15632428}. | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}. Endosome membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269... | null | null | null | null | FUNCTION: Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis (PubMed:15632428, PubMed:15861817). Plays an important role in protein transport and virulence (PubMed:11223944, PubMed:15632428). Component of the autophagy-specific VPS34 PI3-k... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PFP2 | ROB1_CANAL | MTPSSTKKIKQRRSTSCTVCRTIKRKCDGNTPCSNCLKRNQECIYPDVDKRKKRYSIEYITNLENTNQQLHDQLQSLIDLKDNPYQLHLKITEILESSSSFLDNSETKSDSSLGSPELSKSEASLANSFTLGGELVVSSREQGANFHVHLNQQQQQQQPSPQSLSQSSASEVSTRSSPASPNSTISLAPQILRIPSRPFQQQTRQNLLRQSDLPLHYPISGKTSGPNASNITGSIASTISGSRKSSISVDISPPPSLPVFPTSGPTLPTLLPEPLPRNDFDFAPKFFPAPGGKSNMAFGATTVYDADESMVMNVNQIEER... | null | null | DNA-templated transcription [GO:0006351]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:1900445]; regulation o... | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270] | PF04082;PF00172; | 4.10.240.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}. | null | null | null | null | null | FUNCTION: Transcription factor that mediates conventional biofilm formation and plays a key role in microcolony formation under both flow and static conditions and to epithelial surfaces (PubMed:22265407, PubMed:23637598, PubMed:28793308, PubMed:30252918, PubMed:36847358). Modulates infection of mammalian hosts (PubMed... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PHA3 | CYT1_CANAL | MFRTAYKTMNQSMVQKFIAGGVGVTGLTASYLLYQDSMTADAMTAAEHGLHPPAYNWPHNGMFETFDHASIRRGFQVYREVCAACHSLDRIAWRNLVGVSHTTSEAKAMAEELEYDDEPDDEGKPRKRPGKLADYIPGPYENEQAARAANQGAYPPDLSLIVKARHGGSDYIFSLLTGYPDEPPAGVVLPEGSNYNPYFPGGAIAMGRVLFDDLVEYEDGTPATTSQMAKDVSTFLNWASEPEHDDRKKWGLKALVVLSSLYLLSIWVKRFKWTPIKNRKFRFDPPKK | 7.1.1.8 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:P07143}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000250|UniProtKB:P07143}; | mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial respiratory chain complex III [GO:0005750]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF02167; | 1.10.760.10;1.20.5.100; | Cytochrome c family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07143}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation (PubMed:34525326, PubMed:36923588). The complex plays an important role in the uptake of multiple carbon sources presen... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PJA8 | TOS1_CANAL | MKFSSTTLLAGLSSLTATVSAGCSFEGGNYYCSETKKVIYKGIGFSGTYMDVTNMDESTGKCTQQSYSFSGNLSPLDEELSVHFRGPLTLLQFGVYYPSSSGNSKRQIDDQDCNVKHVHHKHKRATEVVQVTQTVFVDGNGNTVTSQALQTSTVESSPAVSSAAADDNANSGSGSGSSAGSGSGYGSVSALDGEGKAYRSDISTKSAPTSTSAQPSSSETASVDGAWTRDSYYTPGSTDNCVFLNYHGGSGSGVWSAKFGNSLSYANADNSGGSSTPVPLEETTIKSGEEYIIFSGSKCGSSSDCGYYRKGTVAYHGFKG... | 3.2.1.39 | null | cell wall organization [GO:0071555]; metabolic process [GO:0008152] | cell surface [GO:0009986]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; hyphal cell wall [GO:0030446] | hydrolase activity, acting on glycosyl bonds [GO:0016798] | PF10287;PF10290; | 2.60.120.200; | PGA52 family | PTM: Cleaved by KEX2 in vitro. {ECO:0000269|PubMed:18625069}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26453650, ECO:0000303|PubMed:17905924}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000250|UniProtKB:P38288}; | null | null | null | null | FUNCTION: Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling (By similarity). Plays a role in engulfment by host macrophages (PubMed:26087349). {ECO:0000250|UniProtKB:P38288, ECO:0000269|PubMed:26087349... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PJX3 | RIP1_CANAL | MSSLAFRTLRNGLGLKSSVRALSTTTTTLSNYQQPDYSSYLNNKSGQGSRNFTYFMVGSMGLLSAAGAKSTVEAFLSSFAASADVLAMAKVEVKLGAIPEGKNVIIKWQGKPVFIRHRTADEIEEANQVDIKTLRDPQNDADRVKKPEWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPEYDFTDDETLLVG | 7.1.1.8 | 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}; | mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial respiratory chain complex III [GO:0005750]; plasma membrane [GO:0005886] | 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF00355;PF02921; | 2.102.10.10;1.20.5.270; | Rieske iron-sulfur protein family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08067}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08067}. | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation (PubMed:34525326, PubMed:36923588). The complex plays an important role in the uptake of multiple carbon sources presen... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PN96 | TAC1_CANAL | MDTSSSSGTHPSTFNNLTKQQELTGNDPNDTNRKRIRVACDSCRRKKIKCNGSYPCGNCIQAKNTSNCHFTERPVRKKLKPTKQDNKSTANSNGVSKRKYNDTFSGNSINIKTEKQENTTFGINDNKSSDLESRLSRIENSMSRMMHTLENFSQNFMTQAIRNNHSNSSMFNNNSLSPTPSEDFNKSAFDSEEQQTSHSYKNLKDRVKDANELLKLRNWDEFVGTHSITCIFSRESLDWMEKTLGSYGEEYLTPIRNLPLVFHSELKPYIMKWIDPPVVDKLQRKKLLESPFPTDSKLISKLIDLYYEETSMINILVDES... | null | null | cellular response to oxidative stress [GO:0034599]; cellular response to steroid hormone stimulus [GO:0071383]; DNA-templated transcription [GO:0006351]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; positive regulation of filam... | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270] | PF04082;PF00172; | 4.10.240.10; | null | PTM: Phosphorylated (PubMed:30104273). Phosphorylation leads to hyperactivation (PubMed:30104273). {ECO:0000269|PubMed:30104273}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:15590837, ECO:0000269|PubMed:19561319}. | null | null | null | null | null | FUNCTION: Transcriptional activator of drug-responsive genes including the ABC-type transporters CDR1 and CDR2, as well as HSP12 and RTA3 (PubMed:15590837, PubMed:17905926, PubMed:19561319, PubMed:30104273). Binds the cis-acting regulatory drug-responsive elements (DREs) with the consensus sequence 5'-CGGAWATCGGATATTTT... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PNR5 | DUR31_CANAL | MAQLSSQGNNAIIYLSYAFMLATGLFLAWKFSSNKDFLSSNGTQRGIPLALNFVASAMGVGIITTYAQIANIAGLHGLLVYTICGAIPIVGFAVVGPVIRRKCPDGFILTEWVRHRFGMVTALYLSAFTCLTMFLFMVGELSAIRSAIETLTGLNALGAVIVECVVTTIYTFFGGFRVSFITDNFQGVCVLLLLIICAAGMGSYIEIDTSKIGPSGLLKANKLGWQLVYILFVAIVTNDCFMSGFWLRTFASKTDKDLWIGTSIAAFVTFAICTLIGTTGFLAVWSGDLIVGDENGYDAFFILLSKMPRWLVAFVLIFCI... | null | null | cellular response to metal ion [GO:0071248]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growt... | membrane [GO:0016020] | spermidine transmembrane transporter activity [GO:0015606] | PF00474; | 1.20.1730.10; | Sodium:solute symporter (SSF) (TC 2.A.21) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000269|PubMed:22033918}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35041; Evidence={ECO:0000269|PubMed:22033918}; | null | null | null | null | FUNCTION: Spermidine transporter that is also used by salivary gland-secreted histatin 5 (Hst 5) to enter into candidal cells (PubMed:22033918, PubMed:23613860, PubMed:24247141). A major component of host nonimmune defense systems is salivary histatins, a family of small (3-4 kDa), histidine-rich, cationic proteins sec... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PPK1 | EBP1_CANAL | MTIESTNSFVVPSDTELIDVTPLGSTKLFQPIKVGNNVLPQRIAYVPTTRFRASKDHIPSDLQLNYYNARSQYPGTLIITEATFASERGGIDLHVPGIYNDAQAKSWKKINEAIHGNGSFSSVQLWYLGRVANAKDLKDSGLPLIAPSAVYWDENSEKLAKEAGNELRALTEEEIDHIVEVEYPNAAKHALEAGFDYVEIHGAHGYLLDQFLNLASNKRTDKYGCGSIENRARLLLRVVDKLIEVVGANRLALRLSPWASFQGMEIEGEEIHSYILQQLQQRADNGQQLAYISLVEPRVTGIYDVSLKDQQGRSNEFAYK... | 1.6.99.1 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q02899}; | steroid metabolic process [GO:0008202] | cell surface [GO:0009986]; cytosol [GO:0005829]; fungal-type vacuole [GO:0000324]; hyphal cell wall [GO:0030446] | estrogen binding [GO:0099130]; FMN binding [GO:0010181]; hormone binding [GO:0042562]; NADPH dehydrogenase activity [GO:0003959]; steroid binding [GO:0005496] | PF00724; | 3.20.20.70; | NADH:flavin oxidoreductase/NADH oxidase family | null | null | CATALYTIC ACTIVITY: Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1; Evidence={ECO:0000250|UniProtKB:P43084}; | null | null | null | null | FUNCTION: Oxidoreductase that binds mammalian estrogens with high affinity. {ECO:0000250|UniProtKB:P43084}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PQ86 | ALS9_CANAL | MLPQFLLLLLYLTVSTAKTITGVFNSFDSLTWTRSVEYVYKGPETPTWTAVLGWSLNSTTADAGDTFTLIMPCVFKFITSQTSVDLTADGVSYATCDFNAGEEFTTFSSLSCTVNSVSVSYDKASGTVKLPITFNVGGTGSSVDLTDSKCFTAGKNTVTFMDGDTKISTTVDFDASPVSPSGYITSSRIIPSLNKASSLFVSPQCENGYTSGIMGFVTSQGATIDCSNINIGISKGLNDWNFPVSSESFTYTKTCSSSGIIVEYENVPAGYRPFVDAYISSENVEQYTLTYANEYTCKNGNTVVDPFTLTWWGYKNSEAD... | null | null | cell adhesion [GO:0007155]; cell adhesion involved in multi-species biofilm formation [GO:0043710]; cell adhesion involved in single-species biofilm formation [GO:0043709]; cell-cell adhesion [GO:0098609] | extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | cell adhesion molecule binding [GO:0050839] | PF05792;PF11766; | 2.60.40.1280;2.60.40.2430; | ALS family | PTM: N-glycosylated and O-glycosylated.; PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI gly... | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted, cell wall. Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. {ECO:0000305|PubMed:12845604}. | null | null | null | null | null | FUNCTION: Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections (PubMed:17510860, PubMed:22321066, PubMed:22429754). Allele ALS9-2 contributes to endothelial cell adhesion, whereas ALS9-1 does not (Pub... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PQB9 | ALS4_CANAL | MLLQFLLLSLCVSVATAKVITGIFDSFNSLTWTNAASYSYRGPANPTWTAVIGWSLDGATASAGDTFTLDMPCVFKFITDQTSIDLVADGRTYATCNLNSAEEFTTFSSVSCTVTTTMTADTKAIGTVTLPFSFSVGGSGSDVDLANSQCFTAGINTVTFNDGDTSISTTVDFEKSTVASSDRILLSRILPSLSQAVSLFLPQECANGYTSGTMGFSTAGTGATIDCSTVHVGISNGLNDWNYPISSESFSYTKTCTSTSVLVTYQNVPAGYRPFVDAYVSATRVSSYAMRYTNIYACVGAASVDDSFTHTWSGYSNSQA... | null | null | adhesion of symbiont to host [GO:0044406]; cell adhesion involved in multi-species biofilm formation [GO:0043710]; cell adhesion involved in single-species biofilm formation [GO:0043709]; cell-cell adhesion [GO:0098609]; cellular response to temperature stimulus [GO:0071502]; hyphal growth [GO:0030448] | extracellular region [GO:0005576]; extracellular vesicle [GO:1903561]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; yeast-form cell wall [GO:0030445] | cell adhesion molecule binding [GO:0050839] | PF05792;PF11766; | 2.60.40.1280;2.60.40.2430; | ALS family | PTM: N-glycosylated and O-glycosylated. {ECO:0000305}.; PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its li... | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:12845604}. Secreted, cell wall {ECO:0000269|PubMed:22106872}. Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer (Probable). Covers the surface of yeast-form cells (PubMed:22106872).... | null | null | null | null | null | FUNCTION: Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections. {ECO:0000269|PubMed:22321066, ECO:0000269|PubMed:22429754}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PS71 | PHYA_CANAL | MVSVSKLINNGLLLTSQSVFQDVATPQQASVQQYNILNFLGGSAPYIQRNGYGISTDIPAGCEIAQIQLYSRHGERYPSKSNGKSLEAIYAKFKNYNGTFKGDLSFLNDYTYFVKDQSNYAKETSPKNSEGTYAGTTNALRHGAAFRAKYGSLYKENSTLPIFTSNSNRVHETSKYFARGFLGDDYEEGKTVKFNIISEDADVGANSLTPRSACSKNKESSSSTAKKYNTTYLNAIAERLVKPNPGLNLTTSDVNNLFSWCAYEINVRGSSPFCDLFTNEEFIKNSYGNDLSKYYSNGAGNNYTRIIGSVILNSSLELLK... | 3.1.3.-; 3.1.3.8 | null | hyphal growth [GO:0030448] | cell surface [GO:0009986]; cell wall-bounded periplasmic space [GO:0030287]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277] | 4-phytase activity [GO:0008707]; acid phosphatase activity [GO:0003993] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.8; Evidence={ECO:0000269|PubMed:29216308}; PhysiologicalDirection=left-to-right; Xref=... | null | null | null | null | FUNCTION: Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate (PubMed:29216308). Myo-inositol 2-monophosphate is the en... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.