Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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A0A2N6JFX7 | TRTA_HERS1 | MIRIDATPYPYQFHPRSTALVVIDMQRDFIEEGGFGSALGNDVRPLAAIVPTVAALLQLAREAGMLVVHTRESHLPDLSDCPRSKRLRGNPTLGIGDVGPMGRILVQGEPGNQILPQLAPVEGELVIDKPGKGAFYATDLHAQLQERRITHLLVAGVTTEVCVQTSMREANDRGYECLVIEDACASYFPDFHRITLEMLTAQGGIVGWRTPLAQLQAGVAAYTGENP | 3.5.1.- | null | amide catabolic process [GO:0043605] | null | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF00857; | 3.40.50.850; | Isochorismatase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + triuret = 1-carboxybiuret + NH4(+); Xref=Rhea:RHEA:75199, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:36955, ChEBI:CHEBI:142864; Evidence={ECO:0000269|PubMed:33172891}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for triuret (at pH 6.5 and 25 degrees Celsius) {ECO:0000269|PubMed:33172891}; Note=Catalytic efficiency, kcat/KM, is 5.3 X 10(5) M(-1)sec(-1). {ECO:0000269|PubMed:33172891}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:33172891}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: The melting temperature (Tm) is 65 degrees Celsius. {ECO:0000269|PubMed:33172891}; | FUNCTION: Involved in the degradation of triuret (carbonyldiurea), an impurity in agricultural urea fertilizer, and an intermediate of uric acid oxidation endogenously found in human urine and in prokaryotic metabolism. Catalyzes the hydrolysis of triuret to 1-carboxybiuret and ammonia. The product, carboxybiuret, chan... | Herbaspirillum sp. (strain BH-1) |
A0A2P1GIW2 | CS_CATRO | MNSSTDPTSDETIWDLSPYIKIFKDGRVERLHNSPYVPPSLNDPETGVSWKDVPISSQVSARVYIPKISDHEKLPIFVYVHGAGFCLESAFRSFFHTFVKHFVAETKVIGVSIEYRLAPEHLLPAAYEDCWEALQWVASHVGLDNSGLKTAIDKDPWIINYGDFDRLYLAGDSPGANIVHNTLIRAGKEKLKGGVKILGAILYYPYFIIPTSTKLSDDFEYNYTCYWKLAYPNAPGGMNNPMINPIAENAPDLAGYGCSRLLVTLVSMISTTPDETKDINAVYIEALEKSGWKGELEVADFDADYFELFTLETEMGKNMF... | 4.-.-.- | null | alkaloid metabolic process [GO:0009820] | cytosol [GO:0005829]; nucleus [GO:0005634] | hydrolase activity [GO:0016787]; lyase activity [GO:0016829] | PF07859; | 3.40.50.1820; | 'GDXG' lipolytic enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}. Nucleus {ECO:0000269|PubMed:29724909}. | CATALYTIC ACTIVITY: Reaction=dihydroprecondylocarpine acetate = acetate + catharanthine + H(+); Xref=Rhea:RHEA:58580, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:142675, ChEBI:CHEBI:142770; Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58... | null | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102}. | null | null | FUNCTION: Component of iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. tabersonine and catharanthine) biosynthesis pathway from 19E-geissoschizine. Catalyzes the conversion of O-acetylstemmadenine (OAS) to catharanthine. {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}. | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
A0A2P1GIW3 | TS_CATRO | MGSSDETIFDLPPYIKVFKDGRVERLHSSPYVPPSLNDPETGGVSWKDVPISSVVSARIYLPKINNHDEKLPIIVYFHGAGFCLESAFKSFFHTYVKHFVAEAKAIAVSVEFRLAPENHLPAAYEDCWEALQWVASHVGLDISSLKTCIDKDPWIINYADFDRLYLWGDSTGANIVHNTLIRSGKEKLNGGKVKILGAILYYPYFLIRTSSKQSDYMENEYRSYWKLAYPDAPGGNDNPMINPTAENAPDLAGYGCSRLLISMVADEARDITLLYIDALEKSGWKGELDVADFDKQYFELFEMETEVAKNMLRRLASFIK | 4.-.-.- | null | alkaloid metabolic process [GO:0009820] | cytosol [GO:0005829]; nucleus [GO:0005634] | hydrolase activity [GO:0016787]; lyase activity [GO:0016829] | PF07859; | 3.40.50.1820; | 'GDXG' lipolytic enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}. Nucleus {ECO:0000269|PubMed:29724909}. | CATALYTIC ACTIVITY: Reaction=dihydroprecondylocarpine acetate = (-)-tabersonine + acetate + H(+); Xref=Rhea:RHEA:58584, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57893, ChEBI:CHEBI:142770; Evidence={ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:5... | null | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909}. | null | null | FUNCTION: Component of iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. tabersonine and catharanthine) biosynthesis pathway from 19E-geissoschizine. Catalyzes the conversion of O-acetylstemmadenine (OAS) to tabersonine, a precursor of vindoline. {ECO:0000269|PubMed:29511102, ECO:0000269|PubMed:29724909... | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
A0A2R2JFI5 | OPHMA_OMPOL | METSTQTKAGSLTIVGTGIESIGQMTLQALSYIEAAAKVFYCVIDPATEAFILTKNKNCVDLYQYYDNGKSRLNTYTQMSELMVREVRKGLDVVGVFYGHPGVFVNPSHRALAIAKSEGYRARMLPGVSAEDCLFADLCIDPSNPGCLTYEASDFLIRDRPVSIHSHLVLFQVGCVGIADFNFTGFDNNKFGVLVDRLEQEYGAEHPVVHYIAAMMPHQDPVTDKYTVAQLREPEIAKRVGGVSTFYIPPKARKASNLDIIRRLELLPAGQVPDKKARIYPANQWEPDVPEVEPYRPSDQAAIAQLADHAPPEQYQPLAT... | 2.1.1.- | null | methylation [GO:0032259] | null | methyltransferase activity [GO:0008168] | PF00590; | null | Precorrin methyltransferase family | PTM: OphMA automethylates at Val-401, Val-403, Val-404, Gly-405, Val-406, Ile-407, Gly-408, Ile-410, Gly-411 and Val-413 before being processed by the prolyloligopeptidase ophP which likely forms a peptidyl ester upon removal of the follower propeptide, which then undergoes macrocyclization with the N-terminus of the m... | null | null | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:28715095, ECO:0000269|PubMed:30151425, ECO:0000269|PubMed:32491837}. | null | null | FUNCTION: Fusion protein of the methyltransferase ophM and the omphalotin core peptide; part of the gene cluster that mediates the biosynthesis of omphalotin A, a highly methylated cyclic dodecapeptide with nematodicidal activity (PubMed:28715095, PubMed:30151425, PubMed:32491837, PubMed:33574430). Omphalotin A derives... | Omphalotus olearius (Jack o'lantern) |
A0A2R4QKX7 | TPS3_PIPNI | MGFSFVTNAAIAAHMPPSKQEIIRRDAKFHPTIWGDHFIQYLDTPIDPPQKVVERMEELKKQVRAMLRDTNLDISLIDWIQRTGIAYHFEEQIAETLKHVYEASTLTTDSSKYLEHFDLRHIALRFRLSRQQGYHASTDVFKRFMDEGDKFKQSIANDIEGMLSLYEASFMSVKGEAILDEALAFTGKNLEATLPNLTGSLAQQVECALEIPLRRCTDLVKARRSISCYENKNGRNEVVLELAKLDFNLLQAVHQRELALLTSWWNELGASTNLPFTRNRVVELYFWVLEVLSKPEHARAREIMVKSIIMASILDDVYDV... | 4.2.3.-; 4.2.3.133 | 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}; | alpha-copaene biosynthetic process [GO:1901931]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; sesquiterpene biosynthetic process [GO:0051762] | null | alpha-copaene synthase activity [GO:0102877]; germacrene-D synthase activity [GO:0052577]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + germacrene D; Xref=Rhea:RHEA:68716, ChEBI:CHEBI:33019, ChEBI:CHEBI:49045, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68717; Evidence={ECO:0000269|PubMed:29248443}; CATALYTIC AC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.152 uM for (2E,6E)-farnesyl diphosphate {ECO:0000269|PubMed:29248443}; Note=kcat is 0.185 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate. {ECO:0000269|PubMed:29248443}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29248443}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds that contribute to the characteristic flavors of black pepper (PubMed:29248443). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into alpha-copaene and germacrene D (PubMed:29248443). {ECO:0000269|PubMed:29248443}. | Piper nigrum (Black pepper) |
A0A2R6W0K6 | PGMP1_MARPO | MAFSAAASASTNLVPAVASGRGGAAASASQHGETARLARFGVSSSACANALSLSSSRSCASMGEVLWANGGAVRLAARRTLRVRAAGAGTIVQPEGFQITSVPTTPIDGQKTGTSGLRKKVKEFQSPNYLANWIQALFDSLPAEDVKGSTLVLGGDGRYFNKEASQIIIKIAAGNGVGKILVGREGIASTPAVSAIIRARKANGGFVMSASHNPGGPKYDWGIKFNYSSGQPAPESITDKIYGNTLSIKEIKQADIPDVNLSELGVHKFGDFSVEVIDPVADYLNLLEEVFDFDLLKGLLTSKDFRFKFDAMHAVTGAYA... | 5.4.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00949}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949}; | carbohydrate metabolic process [GO:0005975]; detection of gravity [GO:0009590]; glucose metabolic process [GO:0006006]; response to cold [GO:0009409]; starch biosynthetic process [GO:0019252]; sucrose biosynthetic process [GO:0005986] | chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; stromule [GO:0010319] | magnesium ion binding [GO:0000287]; phosphoglucomutase activity [GO:0004614] | PF02878;PF02879;PF02880; | 3.40.120.10;3.30.310.50; | Phosphohexose mutase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000250|UniProtKB:Q9SCY0}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + O-phospho-L-seryl-[protein] = alpha-D-glucose 1,6-bisphospha... | null | null | null | null | FUNCTION: Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (By similarity). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (By similarity). This enzyme participates in both the breakdown and synthesis of glucose (By similarity). ... | Marchantia polymorpha (Common liverwort) (Marchantia aquatica) |
A0A2R6XIK6 | PRAF_MARPO | MVVREAMIVPQTVQGGGKGVNGCSLVSNYQNSRDLCLQSAAMEQKSKGVIENCNLGPHDVGVGWKRNSSEGSISSMDSLPCGETVFSPSDPHNSVFRKPRRLGVSESDDESVIDQSQEESLLRKSKRSVMGGTVQPHSAMAQSVDEAAPDHSSTPSDDGKDFPSSRVKFMCSFGGKILPRPSDQQLRYVGGQTRIIGINRDVNFSELRNKMRESFGQCYTFKYQLPDEDLDALVTVSSDEDLENMMEEYDKLEADGSSRLRVFLFPADQDATSFDIDSTGDLRNSEQRYVDAVNGIAESSTRRISDGVLGASPVSSDLLG... | 2.7.11.1 | null | cellular response to auxin stimulus [GO:0071365]; phosphorylation [GO:0016310]; regulation of auxin mediated signaling pathway [GO:0010928]; regulation of photosynthesis [GO:0010109]; response to absence of light [GO:0009646]; response to auxin [GO:0009733]; response to blue light [GO:0009637]; response to red light [G... | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674] | PF00564;PF07714; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Hyperphosphorylated in response to auxin (PubMed:38128538). Its phosphorylation state is also rapidly stimulated by photosynthetic activity (e.g. in response to blue light and red light irradiation); dephosphorylated in the darkness (PubMed:31851335). {ECO:0000269|PubMed:31851335, ECO:0000269|PubMed:38128538}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:38128538}. Note=Broadly distributed to both membrane-associated and intracellular punctate structures. {ECO:0000269|PubMed:38128538}. | 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:0000255|PROSITE-ProRule:PRU10027}; ... | null | null | null | null | FUNCTION: RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming (PubMed:38128538). Required for general growth and developmental process (PubMed:3185... | Marchantia polymorpha (Common liverwort) (Marchantia aquatica) |
A0A2R8Q1W5 | KEP1B_DANRE | MTECKAEVTPSASNGHRVFSYTLESHTAAAFAIMNELRRERQLCDVTLRVRYCPLDTHVDFVAHKVVLASSSPVFRAMFTNGLKECGMEVVPIEGIHPKVMGRLIEFAYTASISVGEKCVIHVMNGAVMYQIDSVVQACCDFLVEQLDPSNAIGIASFAEQIGCTELHQKAREYIYMNFSQVATQEEFFTLSHCQLVTLISRDELNVRCESEVFHACVAWVQYDREERRPYVQALLQAVRCHSLTPHFLQRQLEHFEWDAQSKDYLSQIFRDLTLHKPTKVIPLRTPKVPQLIYTVGGYFRQSLSFLEAFNPCSGAWLRL... | null | null | cellular response to oxidative stress [GO:0034599]; cellular response to prostaglandin stimulus [GO:0071379]; cellular response to xenobiotic stimulus [GO:0071466]; protein ubiquitination [GO:0016567]; regulation of autophagy [GO:0010506]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; inclusion body [GO:0016234]; nucleus [GO:0005634] | null | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | KEAP1 family | PTM: Non-enzymatic covalent modifications of reactive cysteines by electrophile metabolites inactivate the BCR(KEAP1) complex. {ECO:0000250|UniProtKB:Q9Z2X8}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z2X8}. Nucleus {ECO:0000250|UniProtKB:Q9Z2X8}. Note=Mainly cytoplasmic. {ECO:0000250|UniProtKB:Q9Z2X8}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9Z2X8}. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting nfe2l2/nrf2 for ubiquitination (PubMed:18057000). Keap1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A2R8QCI3 | DAPLE_DANRE | MDITVSELMSNFMDSPLVVWVKTFGPLGFSSEDKLSMFMDLVDGVFLHKIMTHIDPSPMNQRVNKQVNNDVNLRIQNLNTVIRHIKNYYQEHLQQLIVMNLPNVLAIAKDPLSGKSMEEMKRMLLLILGCAVQCDRKEEIIEKIKLLDIETQAAIVTHIQEVTHNQENVLDLQWMEVAEIPAEQLDPLSRTMAFHLRKLIDERDESAELVIELTQERDYLQSQQPSGLLGFPSPERTSLSPITLLSKEDRQHLAVELADTKAKLRRSRQELEEKTEQLIDAKNEIERLDSDIQKLKQENTQLLAEARSVRAYRDEVDSLR... | null | null | apical constriction [GO:0003383]; cytoplasmic microtubule organization [GO:0031122]; cytoskeleton-dependent intracellular transport [GO:0030705]; neural tube formation [GO:0001841]; small GTPase-mediated signal transduction [GO:0007264]; Wnt signaling pathway [GO:0016055] | anchoring junction [GO:0070161]; cell junction [GO:0030054]; centrosome [GO:0005813]; cytoplasm [GO:0005737] | dynein light intermediate chain binding [GO:0051959]; G-protein alpha-subunit binding [GO:0001965]; guanyl-nucleotide exchange factor activity [GO:0005085]; microtubule binding [GO:0008017] | PF19047; | 1.10.287.1490;6.10.250.3110;1.10.418.10; | CCDC88 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9P219}. Cell junction {ECO:0000250|UniProtKB:Q9P219}. Note=Enriched at apical cell junctions. {ECO:0000250|UniProtKB:Q9P219}. | null | null | null | null | null | FUNCTION: Positive regulator of Wnt signaling, acting synergistically with dvl2 (By similarity). Functions upstream of ctnnb1/beta-catenin in the canonical Wnt pathway, and also activates jnk in the Wnt/planar cell polarity (PCP) pathway (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which b... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A2R8VHR8 | DT3UO_MOUSE | MLKMSGWQRQSQNNSRNLRRECSRRKCIFIHHHT | null | null | artery development [GO:0060840]; cell redox homeostasis [GO:0045454]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER overload response [GO:0006983]; gene expression [GO:0010467]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; negative regulation of fat ... | CHOP-ATF3 complex [GO:1990622]; CHOP-ATF4 complex [GO:1990617]; CHOP-C/EBP complex [GO:0036488]; cytoplasm [GO:0005737]; late endosome [GO:0005770]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H6Z9}. Cytoplasm {ECO:0000250|UniProtKB:Q9H6Z9}. Note=Colocalizes with WDR83 in the cytoplasm. {ECO:0000250|UniProtKB:Q62630}. | null | null | null | null | null | FUNCTION: [Isoform AltDDIT3]: Product of the upstream open reading frame (uORF) of DDIT3/CHOP that is specifically produced in absence of stress, thereby preventing translation of downstream stress effector DDIT3/CHOP. {ECO:0000269|PubMed:21285359}. | Mus musculus (Mouse) |
A0A2R9YJI3 | GPR22_DANRE | MESMPSSLTHQRFGLLNKHLTRTGNTREGRMHTPPVLGFQAIMSNVTVLDNIEPLDFEMDLKTPYPVSFQVSLTGFLMLEIVLGLSSNLTVLALYCMKSNLVSSVSNIVTMNLHVLDVLVCVGCIPLTIVVVLLPLEGNNALICCFHEACVSFASVATAANVLAITLDRYDISVRPANRVLTMGRAVALLGSIWALSFFSFLVPFIEEGFFSQAGNERNQTEAEEPSNEYYTELGLYYHLLAQIPIFFFTAVVMLVTYYKILQALNIRIGTRFHSVPKKKPRKKKTISMTSTQPESTDASQSSAGRNAPLGMRTSVSVII... | null | null | cell projection organization [GO:0030030]; cellular response to hormone stimulus [GO:0032870]; determination of digestive tract left/right asymmetry [GO:0071907]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right asymmetry in lateral mesoderm [GO:0003140]; determination of left/right... | plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930]; peptide binding [GO:0042277] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D4A3U0}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Orphan G-protein coupled receptor that regulates cilia length and structure in the Kupffer's vesicle leading to the left-right asymmetry development by establishing a directional fluid flow. {ECO:0000269|PubMed:25335082}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A2S1XB67 | ASO_CATRO | MIKKVPIVLSIFCFLLLLSSSHGSIPEAFLNCISNKFSLDVSILNILHVPSNSSYDSVLKSTIQNPRFLKSPKPLAIITPVLHSHVQSAVICTKQAGLQIRIRSGGADYEGLSYRSEVPFILLDLQNLRSISVDIEDNSAWVESGATIGEFYHEIAQNSPVHAFPAGVSSSVGIGGHLSSGGFGTLLRKYGLAADNIIDAKIVDARGRILDRESMGEDLFWAIRGGGGASFGVIVSWKVKLVKVPPMVTVFILSKTYEEGGLDLLHKWQYIEHKLPEDLFLAVSIMDDSSSGNKTLMAGFMSLFLGKTEDLLKVMAENFP... | 1.21.3.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O64743}; | alkaloid metabolic process [GO:0009820] | endoplasmic reticulum [GO:0005783]; vacuole [GO:0005773]; vesicle [GO:0031982] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491] | PF08031;PF01565; | 3.30.465.10;3.40.462.20;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:29724909}. Vacuole {ECO:0000269|PubMed:29724909}. Vesicle {ECO:0000269|PubMed:29724909}. Note=First targeted to endoplasmic reticulum (ER) and progressively secreted to vacuole by ER-derived vesicles. {ECO:0000269|PubMed:29724909}. | CATALYTIC ACTIVITY: Reaction=O-acetyl-15alpha-stemmadenine + O2 = H2O2 + precondylocarpine acetate; Xref=Rhea:RHEA:58572, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:142673, ChEBI:CHEBI:142769; Evidence={ECO:0000269|PubMed:29724909, ECO:0000269|PubMed:30256480}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHE... | null | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29724909, ECO:0000269|PubMed:30256480}. | 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 O-acetylstemmadenine (OAS) to reactive acetylated intermediates, likely dihydropreco... | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
A0A2S3R7M0 | MARTX_VIBVL | MGKPFWRSVEYFFTGNYSADDGNNSIVAIGFGGEIHAYGGDDHVTVGSIGATVYTGSGNDTVVGGSAYLRVEDTTGHLSVKGAAGYADINKSGDGNVSFAGAAGGVSIDHLGNNGDVSYGGAAAYNGITRKGLSGNVTFKGAGGYNALWHETNQGNLSFAGAGAGNKLDRTWFNRYQGSRGDVTFDGAGAANSISSRVETGNITFRGAGADNHLVRKGKVGDITLQGAGASNRIERTRQAEDVYAQTRGNIRFEGVGGYNSLYSDVAHGDIHFSGGGAYNTITRKGSGSSFDAQGMEYAKAEDIVLTAAQMHGLSIDNGN... | 2.3.1.-; 3.4.22.-; 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9KS12}; Note=Binds 2 Mg(2+) ions per subunit. Mg(2+) is required for actin cross-linking activity. Can also use Mn(2+) ions instead of Mg(2+). {ECO:0000250|UniProtKB:A0A0H3AIG7}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | acyltransferase activity [GO:0016746]; cysteine-type peptidase activity [GO:0008234]; ligase activity [GO:0016874]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF00561;PF11647;PF11713;PF20899;PF07634;PF21735; | 1.20.140.180;3.40.50.11050;3.40.50.11550;3.40.50.1820;2.60.120.260; | null | null | SUBCELLULAR LOCATION: [Multifunctional-autoprocessing repeats-in-toxin]: Secreted {ECO:0000250|UniProtKB:Q9KS12}. Host cytoplasm, host cytosol {ECO:0000250|UniProtKB:Q9KS12}. Note=Secreted via the type I secretion system. {ECO:0000250|UniProtKB:Q9KS12}.; SUBCELLULAR LOCATION: [N-epsilon-fatty acyltransferase F2]: Host ... | CATALYTIC ACTIVITY: [N-epsilon-fatty acyltransferase F2]: Reaction=hexadecanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein] = CoA + H(+) + N(6)-hexadecanoyl-L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59768, Rhea:RHEA-COMP:17936, Rhea:RHEA-COMP:17953, ChEBI:CHEBI:15... | null | null | null | null | FUNCTION: [Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessin... | Vibrio vulnificus |
A0A2S4N3N0 | OMPA_SHIFL | MKKTAIAIAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFIPNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGDNINGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKANVPGGASFKDHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDANTIGTRPDNGLLSLGVSYRFGQGEAAPVVAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRA... | null | null | monoatomic ion transmembrane transport [GO:0034220] | cell outer membrane [GO:0009279]; pore complex [GO:0046930] | porin activity [GO:0015288] | PF00691;PF01389; | 2.40.160.20;3.30.1330.60; | Outer membrane OOP (TC 1.B.6) superfamily, OmpA family | null | SUBCELLULAR LOCATION: Extracellular vesicle. Note=(Microbial infection) Upon infection with phage Sf6 is found in extracellular vesicles that associate with the tails of mature phage particles. {ECO:0000269|PubMed:22386055}.; SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250|UniProtKB:P0A910, ECO:0000255|HAMAP-Rul... | null | null | null | null | null | FUNCTION: With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. {ECO:0000255|HAMAP-Rule:MF_00842}.; FUNCTION: Required for conjugation w... | Shigella flexneri |
A0A2T4VDM4 | GSDM_VITXG | MGLCSDPAITYLKRLGYNVVRLPREGIQPLHLLGQQRGTVEYLGSLEKLITQPPSEPPAITRDQAAAGINGQKTENLSFSIGINILKSVLAQFGAGAGIEAQYNQARKVRFEFSNVLADSVEPLAVGQFLKMAEVDADNPVLKQYVLGNGRLYVITQVIKSNEFTVAAEKSGGGSIQLDVPEIQKVVGGKLKVEASVSSQSTVTYKGEKQLVFGFKCFEIGVKNGEITLFASQPGAIAMALDAAGGVMPSDSALLDEGGLLDLEGF | null | null | defense response to virus [GO:0051607] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | null | null | null | Bacterial gasdermin family | PTM: Palmitoylation helps stabilize the inactive state; may self palmitoylate. {ECO:0000269|PubMed:35025633}. | SUBCELLULAR LOCATION: [Gasdermin bGSDM]: Cytoplasm {ECO:0000305|PubMed:35025633}.; SUBCELLULAR LOCATION: [Gasdermin bGSDM, N-terminus]: Cell inner membrane {ECO:0000250|UniProtKB:P0DV48}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: [Gasdermin bGSDM]: Precursor of a pore-forming protein involved in defense against bacteriophages (By similarity). Expression of bGSDM and the neighboring protease gene (Ga0334635_1659) is toxic in E.coli (PubMed:35025633). Cleavage of this precursor by its dedicated protease releases the active moiety (gasde... | Vitiosangium sp. (strain GDMCC 1.1324) |
A0A2T5Y4G4 | CAP12_SPHFK | MKKRIFIGSSSEQLTILNEIVDLLGDDVECIPWTDAFALNKSGLDSLIKQTRLADYSILIATKDDLTKQRGESLTKPRDNVVFEFGLFLGAAGPEKCYLIAEEDTDLPTDLDGITVAKFTRNSGQYNSLDKIVESIRTHLVKIAEMSQLGLLPSTALAIGYYNSFIKRVCEEIHGSECVELEGKKIKVKSFRVDVVIPETLDDNGVGNFTTLYNKRYGLSKATTCTNPALLGTRGFPFHFKVDPPDANQESPVDIHLLDIPSTLSTIVESLKLYLPSNQVGQDFDMDYLEMRELENFAKVLKYLIGRNAATKGYVNVLTN... | 3.2.2.5 | null | defense response to virus [GO:0051607] | null | NAD+ nucleosidase activity [GO:0003953]; nucleotide binding [GO:0000166] | PF10137;PF20300; | null | Bacterial STING family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5; Evidence={ECO:0000269|PubMed:32877915, ECO:0000269|PubMed:35859168}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=27 uM for NAD(+) {ECO:0000269|PubMed:32877915}; Note=kcat is 2.3 sec(-1). {ECO:0000269|PubMed:32877915}; | null | null | null | FUNCTION: Effector protein of a CBASS antiviral system with NAD(+) hydrolase activity (PubMed:32877915). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second m... | Sphingobacterium faecium (strain DSM 11690 / JCM 21820 / NBRC 15299 / NCIMB 13408 / KS 0470) |
A0A2U1LIM9 | NCPR1_ARTAN | MQSTTSVKLSPFDLMTALLNGKVSFDTSNTSDTNIPLAVFMENRELLMILTTSVAVLIGCVVVLVWRRSSSAAKKAAESPVIVVPKKVTEDEVDDGRKKVTVFFGTQTGTAEGFAKALVEEAKARYEKAVFKVIDLDDYAAEDDEYEEKLKKESLAFFFLATYGDGEPTDNAARFYKWFTEGEEKGEWLEKLQYAVFGLGNRQYEHFNKIAKVVDEKLVEQGAKRLVPVGMGDDDQCIEDDFTAWKELVWPELDQLLRDEDDTSVATPYTAAVAEYRVVFHDKPETYDQDQLTNGHAVHDAQHPCRSNVAVKKELHSPLS... | 1.6.2.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03212}; Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_03212}; Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; | sesquiterpene biosynthetic process [GO:0051762] | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789] | flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; NADP binding [GO:0050661]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity [GO:0016491] | PF00667;PF00258;PF00175; | 3.40.50.360;3.40.50.80;2.40.30.10; | NADPH--cytochrome P450 reductase family; Flavodoxin family; Flavoprotein pyridine nucleotide cytochrome reductase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}. | CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 uM for cytochrome P450 {ECO:0000269|PubMed:16612385}; KM=23 uM for NADPH {ECO:0000269|PubMed:16612385}; | null | null | null | FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes (By similarity). It can also provide electron transfer to heme oxygenase and cytochrome B5 (By similarity). Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (PubMed:16612385). Acts as a redox part... | Artemisia annua (Sweet wormwood) |
A0A2U8QPE6 | OXLA_MICMP | MNVFFMFSLVFLAAFGSCADDTRPLGECFREADYEEFLEIARNGLKKTSNPKHVVVVGAGMSGLSAAYVLAKAGHKVTLLEASEGVGGRVKTYRNKQEGWYINLGPMRLPERHRIVREYIRKFHLPLSEFVQENENTWYYIKNIRKRVSEVKKNPDLFEYPVNPSEKGKSASQLYQESLEKVIDELKRTNCNHILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSSFYLSFIESLKSDDIFSYEKRFDEIVGGFDQLPISMYQAIAEMVHLNAQVIKIQHNAKKVIVTYQTPAKTLPSVTADYVIVCSTSRAARHI... | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | amino acid catabolic process [GO:0009063]; apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-amino-acid oxidase activity [GO:0001716]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29900074}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:29900074, ECO:0000269|PubMed:31129208}; CAT... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:29900074}; | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:29900074, PubMed:31129208). Shows activity on L-Leu, L-Trp, and L-Tyr (PubMed:29900074, PubMed:31129208). Is not ... | Micrurus mipartitus (Red-tailed coral snake) |
A0A2U9GGW3 | THS2_PAPSO | MAPLGVSGLVGKLSTELEVDCDAEKYYNMYKHGEDVKKAVPHLCVDVKIISGDPTSSGCIKEWNVNIDGKTIRSVEETTHDDETKTLRHRVFEGDVMKDFKKFDTIMVVNPKPDGNGCVVTRSIEYEKTNENSPTPFDYLQFGHQAIEDMNKYLRDSESN | 4.2.99.24 | null | alkaloid metabolic process [GO:0009820]; defense response [GO:0006952] | null | carbon-oxygen lyase activity [GO:0016835]; protein homodimerization activity [GO:0042803] | PF00407; | 3.30.530.20; | MLP family | null | null | CATALYTIC ACTIVITY: Reaction=(7S)-O-acetylsalutaridinol = acetate + H(+) + thebaine; Xref=Rhea:RHEA:56908, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57672, ChEBI:CHEBI:59953; EC=4.2.99.24; Evidence={ECO:0000269|PubMed:29807982}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56909; Evidence={ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=3.2 nmol/min/ug enzyme {ECO:0000269|PubMed:29807982}; | PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000269|PubMed:29807982}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:29807982}; | null | FUNCTION: Catalyzes the formation of thebaine from (7S)-salutaridinol 7-O-acetate at the expense of labile hydroxylated by-products, which are preferentially produced by spontaneous allylic elimination. No visible activity toward (7S)-salutaridinol (at pH 7). {ECO:0000269|PubMed:29807982}. | Papaver somniferum (Opium poppy) |
A0A2V5GX43 | PYVA_ASPV1 | MDPQQRLLLEVVFEAFEDAGISLEEMNGSRTSVLCGAFTNDYNAMLTKDLEYYPKYTVTGTGNAILANRISYAFNLKGMSLTIDTACSSSLVGFHLGAQAILNGDCEMAIIVGSALHFDPNIFITMTDLGMLSQEGRCRAFDAGGKGYARGEGICAVILRGQMQAEMHGDHIRALVRATGSNHDGMTQGITLPSSEAQEALIRRTYQSCGLDPADTQYVEAHGTGTARGDPLEMRAIGACFSSPRRSDPLYVGSVKSNIGHAEGASGLAGLIKASMALEKGQIPPNMHFKHPNPEIAFADWQIEVPTRVIDFPSNAQGTR... | 2.3.1.-; 6.3.2.- | null | fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; secondary metabolite biosynthetic process [GO:0044550] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00107;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.90.180.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110; | NRP synthetase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:33117309}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranoviolin A, a pyranonigrin analog with a C-3 methoxy group (PubMed:33117309). Initially, the PKS portion of pyvA synthesizes C-10 carbon chain from 5 molecules of malonyl-CoA, which is then condensed with the thiolation... | Aspergillus violaceofuscus (strain CBS 115571) |
A0A2Y9GHM3 | APOE_NEOSC | MKVLWAALVVALLAGCWADVEPESPLQGKPEPELEPELEPKRELEQEVEAEAGWQAGQPWELALARFWDYLRWVQTLSDQVQEDMLSNQVTQELTTLMEETMKEIKAYRAELEEQLGPMASETQARVAKELQAAQARLRSDMEDVRTRLTQYRGEVQAMLGQSTEELRARFASHMRKLRKRVLRDAEDLQKRLAVYRAGVREGAERSVSSIRERLWPLLEQARTRHANLATQPLRERVDALGQQLRGRLEEVGSRARSHLDEVREQMEEVQAKMEEQANQMRQQVEAFQARLKSWFEPLVEDMQRQWAGLVEKVQVAVGT... | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi) |
A0A2Z4HPY4 | EFUA_HORCR | MPSYHNTDKTLLGDARQSLQQAVDYSLGCQQPDGHWVAPVMADATFTAQYVFFKHQIPELSLDEDGPEIQRWLLGEQTADGSWTLAPDLPGNLSTTVEAYLALRILGVPKSDQAMLRARDFVVRNGGVEGVRFFTRFFLATFGLVPWTAIPQMPAELILLPTFMFLNIYVLSSWARSTLIPILLVRHHEPVYALPNGQSANNNFLDELWCNPGEKNIPFALPLWDLLRRYQWIEFAFTLLDHILALFGGLRRWPCRHMALKRCTAWLLEHQEESGDWAGFFPPIHGSIWALLLDGFSFQSEVIRLGMEALERLVVIDPKG... | 2.4.1.-; 5.4.99.- | null | carbohydrate metabolic process [GO:0005975]; cellular glucuronidation [GO:0052695]; lipid glycosylation [GO:0030259]; triterpenoid biosynthetic process [GO:0016104] | endoplasmic reticulum [GO:0005783]; lipid droplet [GO:0005811]; membrane [GO:0016020] | enzyme binding [GO:0019899]; intramolecular transferase activity [GO:0016866]; sterol 3-beta-glucosyltransferase activity [GO:0016906] | PF06722;PF03033;PF13243;PF13249; | 1.50.10.20;3.40.50.2000; | Terpene cyclase/mutase family; Glycosyltransferase 28 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30051576}. | null | null | FUNCTION: Terpene cyclase-glycosyl transferase fusion protein; part of the gene cluster that mediates the biosynthesis of enfumafungin, a glycosylated fernene-type triterpenoid with potent antifungal activity, mediated by its interaction with beta-1,3-glucan synthase and the fungal cell wall (PubMed:30051576). The path... | Hormonema carpetanum |
A0A2Z5D854 | C71Z4_PASSA | MDPAAIFLILAIPIASVYLLFYHKKRVNGLSSPPGPRGLPFIGHFYQIYKSECAHEYISNLSKQYGSLMTLHLGSVPALVVSSPKMAQEVLKTQDLVFCSRAQMTGSGKLSYNGLEMAFAPYGEHWRNVRKMCTLELFTQKRAQFNFRPVREDEVSRMVGRLSEAAAASEDVNAYECFTNFATSIISRVAFGKRYDEDNLGKEKFQRMVADIEAMFAAFFVSDFFPMFGWIDRLSGVKAVLDRNFNEMDTFYQELIDEHLKPDRPESLNGDLIDVMLKNKGSFLTMDSIKAILLNVFSGGIGTTGSALVFAMTALLRNQR... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1}; | coumarin biosynthetic process [GO:0009805]; response to wounding [GO:0009611] | endoplasmic reticulum [GO:0005783]; membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=O2 + psoralen + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + xanthotoxol; Xref=Rhea:RHEA:68548, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15709, ChEBI:CHEBI:27616, ChEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.3 uM for psoralen (at pH 7.4 and 28 degrees Celsius) {ECO:0000269|PubMed:29971079}; KM=9.5 uM for 6-methoxycoumarin (at pH 7.4 and 28 degrees Celsius) {ECO:0000269|PubMed:29971079}; KM=762.2 uM for scopoletin (at pH 7.4 and 28 degrees Celsius) {ECO:0000269|PubMe... | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29971079}. | null | null | FUNCTION: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes (PubMed:29971079). Catalyzes the conversion o... | Pastinaca sativa (Wild parsnip) (Anethum pastinaca) |
A0A2Z5QKZ7 | ORS_RHODA | MALVNHRENVKGRAQILAIGTANPKNCFRQVDYPDYYFRVTKSDHLIDLKAKFKRMCEKSMIEKRYMHVNEEILEQNPSMNHGGEKMVSSLDVRLDMEIMEIPKLAAEAATKAMDEWGQPKSRITHLVFHSTLGTVMPGVDYELIKLLGLNPSVKRFMLYHLGCYGGGTVLRLAKDLAENNPGSRVLVLCCEMMPSGFHGPPSLQHAHLDILTGHAIFGDGAGAVIVGCVDPSGGTNGVVERGVRRYEQPLFEIHSAYQTVLPDSKDAVGGRLREAGLIYYLSKRLSNDVSGKIDECCLAEAFSAAIKDNFEDWNSLFWI... | 2.3.1.- | null | aromatic compound biosynthetic process [GO:0019438]; orcinol biosynthetic process [GO:0046197]; polyketide biosynthetic process [GO:0030639]; terpenoid biosynthetic process [GO:0016114] | null | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF02797;PF00195; | 3.40.47.10; | Thiolase-like superfamily, Chalcone/stilbene synthases family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA = 4 CO2 + 4 CoA + orcinol; Xref=Rhea:RHEA:63072, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16536, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384; Evidence={ECO:0000269|PubMed:27729920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.6 uM for tetraacetic acid lactone (with acetyl-CoA as cosubstrate) {ECO:0000269|PubMed:27729920}; KM=11.7 uM for triacetic acid lactone (with acetyl-CoA as cosubstrate) {ECO:0000269|PubMed:27729920}; KM=9.98 uM for orcinol (with acetyl-CoA as cosubstrate) {ECO:0... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:27729920}. | null | null | FUNCTION: Involved in the biosynthesis of acetate-derived aromatic tetraketides natural products, precursors of daurichromenic acid, an anti-human immunodeficiency viruses (HIV) meroterpenoid consisting of sesquiterpene and orsellinic acid (OSA) moieties (PubMed:27729920). Accepts acetyl-CoA as starter substrate and pr... | Rhododendron dauricum (Azalea daurica) |
A0A2Z5XAU0 | PHM7_PYRSX | MSEPTSSSSLDITSNCIIETPLQPSDFLPKSANLFPKFPERISVDSWELWEFDTFDTNGSVAFGCSLYRDARGVEQGGFHAEVNALWPDGTHWGETLYFAVSEVVENSDGTTGGKWLSKDGGSITFHIASDYTAAALDFNVPGKVSGTMELRNHANVSPTSNLPASDAEAQLCPGVYYTFPMGPVATSVTATFSSVGANGESRELFISSGYGGMVRGWSARPWPTFMNDAYYVVAQVGPYMLQILRTLGSVFVQHKPFAVARLYLDGSLVSAANTVVGDELTAHADDVKGDAVRLTKVQPDEKSQGLSGKFRDGNVGYVL... | 5.5.1.- | null | null | null | isomerase activity [GO:0016853] | null | null | Diels-Alderase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29972614}. | null | null | FUNCTION: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of the trans-fused decalin-containing tetramic acid phomasetin, the stereochemical opposite of the HIV-1 integrase inhibitor equisetin (PubMed:29972614). The PKS module of phm1 together with the enoylreductase phm4 catalyze the formation ... | Pyrenochaetopsis sp |
A0A2Z5Z9X0 | ACT1_CRIJA | MNRLIILCLVAATIYSTIALPMKEDISNEERPTSVNEKPVKKSVAVAGAVIQGAALAFQVLDKILTSLGGIGRKIAIGVDNESGMKWAARNVYFYSGTSDTVLPYSVPHSKAFLYGARKTRGSVRGAVGVLAYSMSDGNTLGILFSVPYDYNWYSNWWNIKVYRGYKRANKWMYHDLYYYARPHKGNNEWHEKSLGYGLKSKGFMTSSGQTKLEIRVSRA | null | null | cytolysis in another organism [GO:0051715]; monoatomic cation transport [GO:0006812]; pore complex assembly [GO:0046931] | extracellular region [GO:0005576]; nematocyst [GO:0042151]; other organism cell membrane [GO:0044218]; pore complex [GO:0046930] | channel activity [GO:0015267]; toxin activity [GO:0090729] | PF06369; | 2.60.270.20; | Actinoporin family, Sea anemone subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29649486}. Nematocyst {ECO:0000250|UniProtKB:P07845}. Target cell membrane {ECO:0000305|PubMed:29649486}. Note=Forms an alpha-helical membrane channel in the prey. {ECO:0000250|UniProtKB:B9W5G6}. | null | null | null | null | null | FUNCTION: Probably acts in predation (PubMed:29649486). Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cytolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aro... | Cribrinopsis japonica (Deep-sea anemone) |
A0A336U966 | TYRP_ASPTE | MGFYRNLVLVAASCTQALGLCPAPRCDSPDIRHEWGELSREDRLSYISAVQCMKDRPPELSVEEVPAVRSRYDDFTAVHINYTLQIHNSGIFLPWHRHFIWLWEKALREECGFTGTLPYWDWVMWPNLAASPLFDGTETSLSGDGEFNATEQPTELNPEPGLTITIPRGAGGGCVRTGPFKDWVINMGPFAFNESYEPALPDHAFDYNPRCLVRSLNDWVIQTYNNQTVVDTLLDSPDIVEFQNIMGGFPNPPIPIGPHAMGHRSLGPDMLDFFASPQDPAFWQHHGMVDRLWTVWQDADEPWRRFALNGSSTTWYKDDT... | 1.14.18.- | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q9ZP19}; Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19}; | null | endoplasmic reticulum lumen [GO:0005788]; Golgi lumen [GO:0005796] | metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF00264; | 1.10.1280.10; | Tyrosinase family | PTM: Glycosylated. {ECO:0000269|PubMed:27133313}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. Golgi apparatus lumen {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. Note=The oxidizing environment of Golgi or endoplasmic reticulum (ER) is required for tyrP to be active. {ECO:0000269|PubMed:292... | CATALYTIC ACTIVITY: Reaction=aspulvinone E + O2 = (5Z)-3-(3,4-dihydroxyphenyl)-5-[(3,4-dihydroxyphenyl)methylidene]-5-oxo-2,5-dihydrofuran-3-olate; Xref=Rhea:RHEA:74195, ChEBI:CHEBI:15379, ChEBI:CHEBI:58240, ChEBI:CHEBI:193114; Evidence={ECO:0000269|PubMed:27133313}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-7. {ECO:0000269|PubMed:27133313}; | null | FUNCTION: Tyrosinase; part of the gene cluster that mediates the biosynthesis of Asp-melanin, a pigment that confers resistance against UV light and hampers phagocytosis by soil amoeba (PubMed:27133313, PubMed:29270299). The nonribosomal peptide synthase melA converts 4-hydroxyphenylpyruvate (4-HPPA) to aspulvinone E (... | Aspergillus terreus |
A0A343URW6 | TEX1_CATRO | MEFVVSLFAFVVSCFILLKVAKNSKNPKRNTNLELPPGPKQLPIIGNLHQLGGGLAHHVLRNLGKQYGPLMHLKIGELSTIVVSSTEIAKEVFKTHDIHFSNRPSHILVFKIVSYDYKDIVLSQYGKYWRELRKVCNLELLSPNRVQSFRSIREDAVLNMMKSISSNDGKVVNLSEMILSLIYGITARAAFGVWSKKHEEFIRLESEIQRLATTFVLADMFPSIKFLGALSGLRYKVEKVHKKVDDILEGILKEHRRQNNNMTEENGKKDLVDVLLNIQKNGDMETPFTDQHIKAIIFDMFSAGTLTSTIAVDWAMAEMM... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | indole alkaloid biosynthetic process [GO:0035835] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29934299}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(-)-tabersonine + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + lochnericine + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:61056, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:5789... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.08 uM for tabersonine (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:29934299}; Vmax=0.254 pmol/sec/ug enzyme with tabersonine as substrate (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:29934299}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:31009114}. | null | null | FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications (PubMed:31009114). Cytochrome P450 catalyzing the conversion of tabersonine to l... | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
A0A348FUE1 | PVCPS_TALVE | MSPMDLQESAAALVRQLGERVEDRRGFGFMSPAIYDTAWVSMISKTIDDQKTWLFAECFQYILSHQLEDGGWAMYASEIDAILNTSASLLSLKRHLSNPYQITSITQEDLSARINRAQNALQKLLNEWNVDSTLHVGFEILVPALLRYLEDEGIAFAFSGRERLLEIEKQKLSKFKAQYLYLPIKVTALHSLEAFIGAIEFDKVSHHKVSGAFMASPSSTAAYMMHATQWDDECEDYLRHVIAHASGKGSGGVPSAFPSTIFESVWPLSTLLKVGYDLNSAPFIEKIRSYLHDAYIAEKGILGFTPFVGADADDTATTIL... | 2.5.1.29; 5.5.1.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 4 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | isomerase activity [GO:0016853]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659] | PF00348; | 1.50.10.160;1.50.10.20;1.10.600.10; | Terpene synthase family; FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464}... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for DMAPP (for prenyltransferase activity) {ECO:0000269|PubMed:31978464}; KM=190 uM for IPP (for prenyltransferase activity) {ECO:0000269|PubMed:31978464}; | null | null | null | FUNCTION: Bifunctional terpene synthase that possesses both prenyltransferase and type II terpene cyclase activity, converting isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into geranylgeranyl diphosphate (GGPP) and further converting GGPP into copalyl diphosphate, respectively. {ECO:0000269|PubMe... | Talaromyces verruculosus (Penicillium verruculosum) |
A0A383ZFX3 | ASAH1_BALAS | MLGRSRLTFVLLSVTVTCSVAQHVPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMVDKAPALKVIVNYLKNMINAFEPSGKIVQLVDQKLPGLLGSFPGPFEEEMKGIAAVTEIPLGEIILFNIFYEFFTICTSIITEDKEGHLLHARNMDFGVFLGWNVNNNTWVVTEELKPLTVNLDFQRNSKTVFKAAGFAGYVGMLTGFKPGLFSLTLNERFSTNGGFMGVIEWILGKKDAKWIGFIIRSVLENSTSYEEAKTILTKSKILAPAYFILGGSKSGEGCVITRDRVQSLDIYELDPKQGIWYVVQTN... | 3.5.1.-; 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... | Balaenoptera acutorostrata scammoni (North Pacific minke whale) (Balaenoptera davidsoni) |
A0A384E129 | O16A_CONMB | MKLTCVVIVAVLFLTACQLITADDSRSTQRHRALRSTTKLSMSTRCKPPGSKCSPSMRDCCTTCISYTKRCRKYYN | null | null | null | extracellular region [GO:0005576] | calcium channel regulator activity [GO:0005246]; ion channel inhibitor activity [GO:0008200]; toxin activity [GO:0090729] | PF02950; | null | Conotoxin O1 superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30194442}. | null | null | null | null | null | FUNCTION: [Omega-conotoxin MoVIA]: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). This toxin potently blocks mammalian N-type calcium channels (Cav2.2/CACNA1B) (IC(50)=330 nM on human channels). It is 9-fold more potent in displacing radiolabeled omega-conotoxin... | Conus moncuri (Sea snail) |
A0A386CAB9 | NLRP1_DANRE | MSSDYTDRNNLASAIKTLGDMLEKDEAFQRLMYNASTKGEINRGRVNKVFLKALLSAGDKVGEFLNELIDHLNLFKVLGDFSWNPPVLKEAELNERTSQLRTQQHKYVERVSGFSHYGFGETGTPARGDITSPRGPQVASIEEDLATSKLAELLLAVGDHLEKIEKKGQFLPENVERFSLDCFITSESVKLSSEAVELAPCYTEPVIIQRSKEQTEKYCQEYVRSPHTSSHLLSNDKTQSIRIGQLFSPDSDGNTPKTVILCGDSGRGKSFVLEKIILDWVHLEHHFENFDAVFLLKYEELKCLSEEMSLTELLSRSCSL... | 3.4.-.- | null | inflammatory response [GO:0006954]; innate immune response [GO:0045087]; pattern recognition receptor signaling pathway [GO:0002221]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; programmed cell death [GO:0012501]; proteolysis [GO:0006508]... | canonical inflammasome complex [GO:0061702]; cytoplasm [GO:0005737]; NLRP1 inflammasome complex [GO:0072558] | ATP binding [GO:0005524]; peptidase activity [GO:0008233] | PF00619;PF13553;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1 homolog]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating pro-inflammatory caspases (caspa and/or caspb) binding.... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30150286}. Note=Co-localizes with pycard, caspa and caspb in the cytoplasm. {ECO:0000269|PubMed:30150286}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1, C-terminus]: Inflammasome {ECO:0000269|PubMed:30150286}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the nlrp1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (PubMed:30150286). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other dama... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A386KZ50 | DABA_PSEMU | MKFATSIVAAIATTGAAFTVIPQKLSHPSQLNALNTMGSISSITAESPKEVLSRVQDAGLTLTNPNDLYWMVDFLKEKYYDNGDYYYPIKTVCDGESIDVKFYCPFEPSLSPHYLELYGSRDERASIYETTMKKYNRINSEKTSAICTPYSSYGDTQIVAYFYSMMYYINDQTAHLKLPESEIESELIDILNDDILIYLNEFMSIFEPEDAQDLERIWDFLDFYQPYFSKVDGKIVLDEKYLVRTPSQMPLIKTICEYVSEQFAPSKNITQVIWEVVRYIKGVKDEIHIRGDKSFTLSLQEYDDFRDKVTASPMAHAVSD... | 2.5.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32457155}; Note=Can also use Mn(2+) ions as cofactors with a lower efficiency. {ECO:0000269|PubMed:32457155}; | cellular response to carbon dioxide [GO:0071244]; cellular response to phosphate starvation [GO:0016036] | null | metal ion binding [GO:0046872]; transferase activity [GO:0016740] | PF19086; | 1.10.600.10; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + L-glutamate = diphosphate + N-geranyl-L-glutamate; Xref=Rhea:RHEA:68156, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:172365; Evidence={ECO:0000269|PubMed:30262498, ECO:0000269|PubMed:32457155}; PhysiologicalDirection=left-to-right; Xref=Rh... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.33 uM for geranyl diphosphate {ECO:0000269|PubMed:32457155}; KM=21 mM for L-glutamic acid {ECO:0000269|PubMed:32457155}; Note=kcat is 4.3 min(-1) with geranyl diphosphate as substrate (PubMed:32457155). kcat is 4.8 min(-1) with L-glutamic acid as substrate (PubMe... | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:30262498}. | null | null | FUNCTION: Magnesium-dependent glutamate N-prenyltransferase: part of the gene cluster that mediates the biosynthesis of domoic acid (DA) and derivatives, natural products with neurochemical activity acting as ionotropic glutamate receptor (iGluR) agonists, thus being neurotoxins causing amnesic shellfish poisoning (ASP... | Pseudo-nitzschia multiseries (Marine planktonic diatom) (Nitzschia pungens f. multiseries) |
A0A396GMX6 | DELA2_MEDTR | MKREHKLEHEDMSSGSGKSGVCWEDDGGGMDELLAVVGYKVKSSDMAEVAQKLEQLEQAMMGNNFHDHDESTIAQHLSNDTVHYNPSDISNWLQTMLSNFDPQPNNPSVNSDDNDLNAIPGKAIYAADEFTSRKRVKRNESVTVTTESTTTRPIMVVETQEKGIRLVHSLMACAEAVEQNNLKMAEALVKQIGYLAVSQEGAMRKVATYFAEGLARRIYGVFPQHSVSDSLQIHFYETCPNLKFAHFTANQAILEAFQGKSSVHVIDFSINQGMQWPALMQALALRPGGPPAFRLTGIGPPASDNSDHLQQVGWRLAQFA... | null | null | arbuscular mycorrhizal association [GO:0036377]; cellular response to phosphate starvation [GO:0016036]; gibberellic acid mediated signaling pathway [GO:0009740]; hyperosmotic salinity response [GO:0042538]; jasmonic acid mediated signaling pathway [GO:0009867]; negative regulation of gibberellic acid mediated signalin... | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF12041;PF03514; | 1.10.10.1290; | GRAS family, DELLA subfamily | PTM: Ubiquitinated. Upon GA application it is ubiquitinated, leading to its subsequent degradation. {ECO:0000250|UniProtKB:Q7G7J6}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A396IUP1}. | null | null | null | null | null | FUNCTION: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway (By similarity). Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes (By similarity). Upon GA application, it is degraded by the proteasome, allowin... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A0A396IUP1 | DELA1_MEDTR | MKREHQESFGGGVISNNNKTNTNHLNSSKNINFGECSSMQNTNTKQNMWREEKETNGGGMDELLAALGYKVRSSDMADVAQKLEQLEMVMGSAQEEGINHLSSDTVHYDPTDLYSWVQTMLTELNPDSSQINDPLASLGSSSEILNNTFNDDSEYDLSAIPGMAAYPPQEENTAAKRMKTWSEPESEPAVVMSPPPAVENTRPVVLVDTQETGVRLVHTLMACAEAIQQKNLKLAEALVKHISLLASLQTGAMRKVASYFAQALARRIYGNPEETIDSSFSEILHMHFYESSPYLKFAHFTANQAILEAFAGAGRVHVID... | null | null | arbuscular mycorrhizal association [GO:0036377]; cellular response to phosphate starvation [GO:0016036]; gibberellic acid mediated signaling pathway [GO:0009740]; hyperosmotic salinity response [GO:0042538]; jasmonic acid mediated signaling pathway [GO:0009867]; negative regulation of gibberellic acid mediated signalin... | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF12041;PF03514; | 1.10.10.1290; | GRAS family, DELLA subfamily | PTM: Ubiquitinated. Upon GA application it is ubiquitinated, leading to its subsequent degradation. {ECO:0000250|UniProtKB:Q7G7J6}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24297892}. | null | null | null | null | null | FUNCTION: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway (By similarity). Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes (By similarity). Upon GA application, it is degraded by the proteasome, allowin... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A0A396JG59 | EX70I_MEDTR | MHKKQLMALLMVPQTSDSQDATITKLESAYSDLESLLRSSKQMEQNIETMETRFDLLHGSITTASRRVHPLQSLSMSRKALDTRINRAISPALALLETFKLAESLQNNLLNLSSKLSTEKTHQKRLSKLLDYMDCVDQLNEAINSISEVVEPVIMRLQEVVEFISRTKAADQYRTQRLREALITLKALYETEVDEMRFEGLLDQALLHMQDEFEVLLLKLKHRKLGDMSHMQNGGEDCDDHFEVSFELGSELEIEVLRRISNTLAANDCLDICIDIYVKVRYKRAAKALMKLNPDYLRTYTPEGIDEMEWENLETSITLW... | null | null | arbuscular mycorrhizal association [GO:0036377]; exocytosis [GO:0006887]; protein transport [GO:0015031]; response to symbiotic bacterium [GO:0009609]; response to symbiotic fungus [GO:0009610] | exocyst [GO:0000145]; periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF03081; | 1.20.1280.170; | EXO70 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26234213}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=During arbuscule branching, restricted to zones adjacent to the periarbuscular membrane (PAM) around the arbuscule hyphal tips. {ECO:0000269|PubMed:26234213}. | null | null | null | null | null | FUNCTION: Component of an exocyst subcomplex specifically required for periarbuscular membrane (PAM) biogenesis during arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme), especially critical during the early branching phase of arbuscule development; probably involved in STR and STR2 delivery i... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A0A3B6UES5 | VINC_OSCPE | MPVKFHTKTLESVIDPVAQQVGQLVLFHEQAESGLLKEDLTPLVQGVGIAVTNLVQVAASMVETSNDEDFKAELPPSMQEVQQAAVFLSDAARLLKADQGSPEGKRKLLDGARGVINGMSDLLMCADRSEVRKMVKVCRSVQEYLDVAKVIDVEADLATFLQNLTPGMTSMMKVVEQRHPELTNLAHAQMLKSELGTVREQIPILISSIRVCCLVIVKDGSSGMKDAAFGRDYVIQKLFIAIEEIIRVLQLTTTFEEEEVGGAGAASAASLAHMFHQAQDALASGDISRSTLDAVRKCISEGRRVAALAATDETRAKLLA... | null | null | cell adhesion [GO:0007155] | adherens junction [GO:0005912]; cell-cell contact zone [GO:0044291]; cortical cytoskeleton [GO:0030863]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013] | PF01044; | 1.20.120.230;1.20.120.810; | Vinculin/alpha-catenin family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:29880641}. Cell projection, filopodium {ECO:0000269|PubMed:29880641}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:29880641}. Note=Localizes to points of cell-cell contact in the pinacoderm. Localizes to the base of the microvillar collar in choanocytes. D... | null | null | null | null | null | FUNCTION: Actin filament (F-actin)-binding protein which may play a role in cell-cell adhesion. {ECO:0000269|PubMed:29880641}. | Oscarella pearsei (Sponge) |
A0A3B6UEU3 | INLPE_STRC4 | MQIDEQPGNAIGAAVEGFDHATASDADIDALKSTIYTKKIAVLKGQDLSPQQFLALGKRLGRPEAYYEPMYQHPEVTEIFVSSNVPENGKQIGVPKTGKFWHADYQFMPDPFGITLIYPQVIPEKNRGTYFIDMGRAYDRLPEDLKKEISGTYCRHSVRKYFKIRPHDVYRPISEIIEEVERKTPAVVQPTTFTHPMTGETVLYISEGFTVGIEDQDGKPLDEELLKRLFDATGQLDESFEHDNIHLQSFEQGDLLVWDNRSLIHRARHTTTPEPTVSYRVTVHDERKLHDGIQAA | 1.14.11.78 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:29906336, ECO:0000269|PubMed:32074393, ECO:0000269|PubMed:33361191}; | heterocycle metabolic process [GO:0046483]; organic cyclic compound metabolic process [GO:1901360] | null | dioxygenase activity [GO:0051213]; metal ion binding [GO:0046872] | PF02668; | 3.60.130.10; | TfdA dioxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + a (3R)-3-[(carboxymethyl)amino]fatty acid + 2 O2 = a (3R)-3-isocyanyl-fatty acid + 3 CO2 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:74931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:193080, ChEBI:CHEBI:193084; EC=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=286 uM for (3R)-3-[(carboxymethyl)amino]butanoate {ECO:0000269|PubMed:29906336}; KM=20.9 uM for 2-oxoglutarate {ECO:0000269|PubMed:29906336}; Note=kcat is 21.9 min(-1) with (3R)-3-[(carboxymethyl)amino]butanoate as substrate. {ECO:0000269|PubMed:29906336}; | null | null | null | FUNCTION: Involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs) (PubMed:28634299). Catalyzes the conversion of (3R)-3-[(carboxymethyl)amino]fatty acids such as (3R)-3-[(carboxymethyl)amino]butanoate (CABA) to (3R)-3-isocyanylbutanoate (INBA) through an oxidative decarboxylation mechanism, th... | Streptomyces coeruleorubidus |
A0A3L7I2I8 | PLPL9_CRIGR | MQFFGRLVNTLSSVTNLFSNPFRVKEISVADYTSHERVREEGQLILFQNASNRTWDCILVSPRNPHSGFRLFQLESEADALVNFQQFSSQLPPFYESSVQVLHVEVLQHLSDLIRSHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDNSQVLQLLGKNASAGLNQVNKQGLTPLHLACQMGKQEMVRVLLLCNARCNVMGPSGFPIHTAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCDVDSTSAAGNTA... | 3.1.1.4; 3.1.1.5; 3.1.2.2 | null | antibacterial humoral response [GO:0019731]; cardiolipin acyl-chain remodeling [GO:0035965]; cardiolipin biosynthetic process [GO:0032049]; phosphatidic acid metabolic process [GO:0046473]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylethanolamine catabolic process [GO:0046338]; platelet activating f... | extracellular space [GO:0005615]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143] | 1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; calcium-independent phospholipase A2 activity [GO:0047499]; identical protein binding [GO:0042802]; long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]... | PF12796;PF01734; | 1.25.40.20;3.40.1090.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60733}. Cell membrane {ECO:0000250|UniProtKB:O60733}. Mitochondrion {ECO:0000250|UniProtKB:P97819}. Cell projection, pseudopodium {ECO:0000250|UniProtKB:O60733}. Note=Recruited to the membrane-enriched pseudopods upon MCP1/CCL2 stimulation in monocytes. {ECO:00002... | 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:9079687}; PhysiologicalD... | null | null | null | null | FUNCTION: Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity resp... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
A0A3Q0KDV9 | SEP10_SCHMA | MTADVLKALPPDVRTLKLSGHVGFDSLPDQLVNKAISQGFVFNILCVGETGIGKSTLLETLFNQKFDFSPSNHDLTDPKLKAVTYDLKEANVKLKLTVVETCGYGDQINKENNIKPVVDYIDNQFENYLQEELKMKRSMQAFHDTRVHVCLYFIAPTGHSLKSIDLVAMKKLENKVNVIPVIAKSDTITKSELQKFKARILSEIQSNEIGIYQFPTDDEAVSETNSVMNQHIPFAVVGSSEEVKINGKTVRVRQYPWGSVQVENENHCDFVRLREMLLRVNMEDLRERTHGVHYETYRRQRLIEMGFRDDEKMSLQETYE... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24464615}; Note=Mg(2+) is essential for the GTP-binding, but GDP-binding does not require a metal cofactor. {ECO:0000269|PubMed:24464615}; | cytoskeleton-dependent cytokinesis [GO:0061640]; protein homooligomerization [GO:0051260] | cell division site [GO:0032153]; microtubule cytoskeleton [GO:0015630]; septin complex [GO:0031105]; septin ring [GO:0005940]; vesicle [GO:0031982] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; molecular adaptor activity [GO:0060090]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF00735; | 3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8C1B7}. Note=Colocalizes with actin in the longitudinal and circular muscles of the sporocyst. {ECO:0000269|PubMed:24367716}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Stable at wide pH range from 4 to 9. {ECO:0000269|PubMed:27687162}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Temperature-sensitive. Stable at 15 degrees Celsius. Starts to aggregate at 37 degrees Celsius. {ECO:0000269|PubMed:27687162}; | FUNCTION: Filament-forming GTP-binding protein. Lacks GTPase activity, which is likely due to absence of an essential threonine residue important for hydrolytic activity in septins. May be involved in membrane remodeling, potentially by its nucleotide-dependent cellular membrane association/dissociation ability (PubMed... | Schistosoma mansoni (Blood fluke) |
A0A3Q0KR05 | NPRS_SCHMA | MPQSTAQLKSPLLHTLLENLTQSSICTSTAIWHVPNPVNFVCNHNENSFDNKNNSVTTITTTDVSTNNHKNTNYDYEQQEQWSNEEINSNQESNEIYTMTFLKLNNAANRVAMNLANYLERKWSSITNKINRTQLNQHSLSIDEPIELRNQSDTVIALFMPPGIDRIVVQIACMKLHLAYMPLDRNVPAGRITQILHKLKPILILIDKDYYDFIYDDDHNDNDKMSDLSSSIDNNNKSLLSRKLSSNDFIIGNLNQLKLTFQLFDVKVYEYIKLMKLSKYYSRSDIYTASIPIRVCLFPFESDPIVLVLFTSGSTSSGPK... | 6.3.2.- | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258}; | amino acid adenylylation by nonribosomal peptide synthase [GO:0043042]; female genitalia development [GO:0030540] | null | beta-alanyl amine synthase activity [GO:0003833] | PF00501;PF00550; | 3.30.300.30;3.40.630.30;3.40.50.12780; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + beta-alanine + tryptamine = AMP + beta-alanyl-tryptamine + diphosphate + H(+); Xref=Rhea:RHEA:73335, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57887, ChEBI:CHEBI:57966, ChEBI:CHEBI:192794, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:35385687}; Physiolog... | null | null | null | null | FUNCTION: Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT) (PubMed:35385687). Beta-alanyl-tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing (PubMed:35385687). {ECO:0000269|PubMed:35385687}. | Schistosoma mansoni (Blood fluke) |
A0A3Q0NBH7 | PGDA_LISMG | MKIRWIRLSLVAILIIAVVFIGVIGFQKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQ... | 3.5.1.104 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8DP63}; | autolysis [GO:0001896]; carbohydrate metabolic process [GO:0005975]; cell wall modification [GO:0042545]; evasion of host innate immune recognition [GO:0141043]; negative regulation of lysozyme activity [GO:1903591] | extracellular region [GO:0005576]; Gram-positive-bacterium-type cell wall [GO:0009275]; plasma membrane [GO:0005886] | chitin deacetylase activity [GO:0004099]; lysozyme inhibitor activity [GO:0060241]; N-acetylglucosamine deacetylase activity [GO:0050119]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF01522; | 3.20.20.370; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8Y9V5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8Y9V5, ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:Q8Y9V5}. Secreted, cell wall {ECO:0000305|PubMed:19809250}. | CATALYTIC ACTIVITY: Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate.; EC=3.5.1.104; Evidence={ECO:0000269|PubMed:19809250}; | null | null | null | null | FUNCTION: Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan (PG). Deacetylates also N-acetylated PG. Does not deacetylate N-acetylmuramic acid (PubMed:19809250). Confers host lysozyme resistance. Critical for virulence and escape from innate immune response of the host. Required for ... | Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness) |
A0A3Q2TTB3 | PRIPO_CHICK | MKRKWEERVKKVEELASYYERNPLPTVYKPRLSKPLQPSRVWKIFCRQADAFRFVKTCKEDVHVFALERNTQNGQRFYLVTTYQELWYYYTKGYKTSLMHCYEVIPEKDACKLYFDLEFYKAANPGADGKDMVAKLIELVSQKLKELYDVNCSARDVLNLDSSTDEKFSRHLIFLPCKTVFKDNIHVGNFVRTILQPAIRLVGSNVAAPIAEGGAGYTSQCSAPTVELDGPLTNLTAVEDASKGWPAIADQRKETETSHHGENSEFSFLIVNNKEGDKQLFVDLGVYTRNRNFRMYKSSKAGKNVILTIAEDNKFVPNCE... | 2.7.7.102; 2.7.7.7 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q96LW4}; Note=Can act both with Mn(2+) and Mg(2+) as cofactor in vitro, but Mn(2+) is the preferred cofactor in vivo. {ECO:0000250|UniProtKB:Q96LW4}; | error-prone translesion synthesis [GO:0042276]; mitochondrial DNA repair [GO:0043504]; mitochondrial DNA replication [GO:0006264]; R-loop processing [GO:0062176]; replication fork processing [GO:0031297]; response to UV [GO:0009411]; translesion synthesis [GO:0019985] | DNA-directed RNA polymerase complex [GO:0000428]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634]; replication fork [GO:0005657] | chromatin binding [GO:0003682]; DNA primase activity [GO:0003896]; DNA-directed DNA polymerase activity [GO:0003887]; manganese ion binding [GO:0030145]; zinc ion binding [GO:0008270] | PF03121; | null | Eukaryotic-type primase small subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96LW4}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q96LW4}. Chromosome {ECO:0000250|UniProtKB:Q96LW4}. | CATALYTIC ACTIVITY: Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.; EC=2.7.7.102; Evidence={ECO:0000269|PubMed:30478192}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChE... | null | null | null | null | FUNCTION: DNA primase and DNA polymerase required to tolerate replication-stalling lesions by bypassing them (PubMed:26626482, PubMed:30478192). Required to facilitate mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able ... | Gallus gallus (Chicken) |
A0A3Q7FGP1 | IF4E2_SOLLC | MADELNKAALEEYKSSSVEDRGEEGEIVGESDDTASSLGKQITMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTAEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCANGGKWTMNFSRGKSDTCWLYTLLALIGEQFDYGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDTIGFIFHDDAKKLDRAAKNRYSV | 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-119-Cys-157 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}. | 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 lycopersicum (Tomato) (Lycopersicon esculentum) |
A0A3Q7GYG2 | MOMT2_SOLLC | MASNNNICAYELIEAEAQSWDYILSYLRPSCIKCAIQLGIPDILHKNADPIMSLSDLIAALPNLNPSKTTFIPILMRVLVDFGLFNYHQQQGDGYSLTTVGRLLVENHHFGNRSFFLFAQHPVVLNTAASVGDWLKDDLRTAFETADGKSHWDYCGADPEFNGVFNDAMAGDSRLMSNLLISDCCAGVFEGLTSLVDIGGGTGAVAMAIAGAFPSLKCIVLDLPHVIADRKGSGNLEFVAGSMFDKIPHANAILLKWILHNWDDEDCVKLLKKCKESISSRENGGKVIIIDMIMEDNYNNKQLVQSQHLMDLIMRITYAS... | 2.1.1.-; 2.1.1.155; 2.1.1.82 | null | aromatic compound biosynthetic process [GO:0019438]; flavonoid biosynthetic process [GO:0009813]; methylation [GO:0032259] | 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 | null | null | CATALYTIC ACTIVITY: Reaction=quercetin + S-adenosyl-L-methionine = H(+) + rhamnetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73115, ChEBI:CHEBI:15378, ChEBI:CHEBI:57694, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192706; Evidence={ECO:0000250|UniProtKB:F2YTN5}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | null | PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:22711283}. | null | null | FUNCTION: Flavonoid 7/4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-a... | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
A0A3Q7HJG4 | CURE1_SOLLC | MGNIKFLLLVFFLIVVVVNGCWEEERNALLELQTNIMSSNGELLVDWAGYNAAHFVDCCFWDRVKCSLETGRVIKLDLEADFGTGDGWLFNASLFLPFKSLQVLLLSSQNIIGWTKNEGFSKLRQLPNLKEVDLQYNPIDPKVLLSSLCWISSLEVLKLGVDVDTSFSIPMTYNTNMMSKKCGGLSNLRELWFEGYEINDINILSALGELRNLEKLILDDNNFNSTIFSSLKIFPSLKHLNLAANEINGNVEMNDIIDLSNLEYLDLSDNNIHSFATTKGNKKMTSLRSLLLGSSYSNSSRVIRSLKSFSSLKSLSYKNS... | null | null | activation of innate immune response [GO:0002218]; cell surface pattern recognition receptor signaling pathway [GO:0002752]; defense response to parasitic plant [GO:0002242]; immune response-regulating cell surface receptor signaling pathway [GO:0002768]; pathogen-associated molecular pattern receptor signaling pathway... | cell surface [GO:0009986]; plasma membrane [GO:0005886] | pattern recognition receptor activity [GO:0038187] | PF00560;PF13855; | 3.80.10.10; | RLP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27471302}; Single-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:27471302}. Cell surface {ECO:0000305|PubMed:27471302}. | null | null | null | null | null | FUNCTION: Involved in plant defense. Contributes to resistance against parasitic plant C.reflexa (PubMed:27471302, PubMed:33082345). Acts as a receptor for the 11 kDa glycine-rich protein (GRP) of C.reflexa inducing immune responses such as emission of stress-related phytohormone ethylene, reactive oxygen species (ROS)... | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
A0A3Q7HRZ6 | MYC2_SOLLC | MTEYSLPTMNLWNNSTSDDNVSMMEAFMSSDLSFWATNNSTSAAVVGVNSNLPHASSNTPSVFAPSSSTSASTLSAAATVDASKSMPFFNQETLQQRLQALIDGARETWTYAIFWQSSVVDFSSPSVLGWGDGYYKGEEDKAKRKLSVSSPAYIAEQEHRKKVLRELNSLISGAPPGTDDAVDEEVTDTEWFFLISMTQSFVNGSGLPGQALYSSSPIWVAGTEKLAASHCERVRQAQGFGLQTIVCIPSANGVVELGSTELIVQSSDLMNKVRVLFNFSNDLGSGSWAVQPESDPSALWLTDPSSSGMEVRESLNTVQT... | null | null | defense response [GO:0006952]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF14215;PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Transcriptional activator that binds to the G-box motif (5'-AACGTG-3') found in the promoter of the jasmonate-induced gene LAPA1 (PubMed:15231736). Acts as a negative regulator of blue light-mediated photomorphogenesis and positively regulates root growth (PubMed:24483714). Promotes growth in response to the ... | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
A0A3Q7HYF0 | MOMT3_SOLLC | MALSMDNIVISNEEEIYMMKAMHIPCGLYLNMVLRAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSFLTCNITKNDDGNVHTSYNLTPLSQSLILDKDGTSIAPFLLLATDPVAVNSWFHFKDAILEGEIPFNKAHGVHAFEYHGKDSRFNGVFNKAMQNVTCIDMKRVLECYNGFEGVKEIIDVGGGLGISLASIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMFKSVPQRELILLKAILHDWDDECCVKILKNCWRALPKDGKVVVIEQMQPEYPEINLISKNSFSVDMLMMT... | 2.1.1.-; 2.1.1.76 | null | aromatic compound biosynthetic process [GO:0019438]; flavonoid biosynthetic process [GO:0009813]; methylation [GO:0032259] | null | 3',4',5'-trimethylmyricetin 3-O-methyltransferase activity [GO:0102440]; kaempferol 3-O-methyltransferase activity [GO:0102449]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; quercetin 3-O-methyltransferase activity [GO:0030755]; S-adenosylmethionine-dependent methyltransferase ... | PF08100;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=3',4',5'-O-trimethylmyricetin + S-adenosyl-L-methionine = 3,3',4',5'-O-tetramethylmyricetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74771, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:194070, ChEBI:CHEBI:194076; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to... | null | PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:25128240}. | null | null | FUNCTION: Flavonoid 3-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-athe... | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
A0A3Q7I7R4 | IFI4E_SOLLC | MATEAPVEATEIPSVAAAETVEKQPHKLERKWTFWFDNQSKPKQGVAWGSSLRKAYTFETVEEFWSLYDQIFKPSKVTVNADFHLFKAGIEPKWEDPECANGGKWTATSSRKANLETMWLETLMALVGEQFDESEDICGVVASVRRSQDKLSLWTKTATNEAAQMGIGRKWKEIIDAEKISYSFHDDSKRERSAKSRYTV | null | null | response to virus [GO:0009615]; translational initiation [GO:0006413] | eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-99-Cys-138 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}. Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}. | 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 lycopersicum (Tomato) (Lycopersicon esculentum) |
A0A3Q8GL18 | NEPS1_NEPRA | MASTANPMQVMKKKLEGKVVIVTGGASGIGQTAARVFAQHGARAVVIADIQSEVGKSVAKSIGDPCCYVQCDVSDEEEVKSMIEWTASAYGGLDMMFSNVGIMSKSAQTVMDLDLLEFDKVMRVNARGMAACLKHAARKMVELGTRGTIICTTTPLSSRGGQSMTDYAMSKHAVMGLVRSASIQLGAHGIRVNCVTPSVVLTPLAQRMGLATPDDFHTHFGNFTSLKGVYLTPEQVAEAVVYLASDDAAFITGHDLVLDGGLLCLPFFAPS | 1.1.1.419; 5.5.1.34 | null | isoprenoid metabolic process [GO:0006720] | null | isomerase activity [GO:0016853]; oxidoreductase activity [GO:0016491] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-8-oxocitronellyl enol = cis-trans-nepetalactol; Xref=Rhea:RHEA:61416, ChEBI:CHEBI:71494, ChEBI:CHEBI:144481; EC=5.5.1.34; Evidence={ECO:0000269|PubMed:30531909, ECO:0000269|PubMed:30664302}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61417; Evidence={ECO:0000269|PubMed:3053190... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for cis-trans-nepetalactol (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:30531909}; KM=4.9 uM for cis-cis-nepetalactol (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:30531909}; KM=3.5 uM fo... | null | null | null | FUNCTION: Bifunctional enzyme that possesses cyclase and dehydrogenase activities (PubMed:30531909, PubMed:30664302). Functions as a non-oxidoreductive cyclase to promote the formation of cis-trans-nepetalactol (PubMed:30531909, PubMed:30664302). Functions as dehydrogenase to oxidize cis-cis-nepetalactol and cis-trans-... | Nepeta racemosa (Catmint) (Raceme catnip) |
A0A3S5YBC7 | EGCSE_RHOH1 | MRKTVVAFAAAIAACSAVLSSTTTSAAPPATPITTLQADGTHLVDGYGRTVLLHGVNNVDKDAPYLPAGETLTPQDIDILVRHGFNTVRLGTSFDALMPQRGQIDEAYLDRLTGVVDALTARGMHVLLDNHQDGLSKAWGGNGFPEWAIESRPREWEPNPGFPLYYLMPSLNAGWDEVWGNTHGALDHLGTALGALAERVEGKPGVMGIELLNEPWPGSRFLSCFPNGCPDFDRTYQAAMQKLTDAVRAQNPTIPVYWEPNVTWNQMMPSNLFAPPVTPALTTADVVFAPHDYCIPSQLAIYLGLPQALRGLCVPQQDLT... | 3.2.1.123 | null | galactosylceramide catabolic process [GO:0006683] | extracellular region [GO:0005576]; membrane [GO:0016020] | endoglycosylceramidase activity [GO:0047876] | PF00150;PF18564; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 5 (cellulase A) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28179425}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | CATALYTIC ACTIVITY: Reaction=an oligoglycosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O = an N-acyl-sphingoid base + an oligoglycosyl-(1->4)-D-glucose; Xref=Rhea:RHEA:22288, ChEBI:CHEBI:15377, ChEBI:CHEBI:83273, ChEBI:CHEBI:136875, ChEBI:CHEBI:156536; EC=3.2.1.123; Evidence={ECO:0000269|PubMed:28179425}; Physiologi... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for monosialotetrahexosylganglioside (GM1) {ECO:0000269|PubMed:28179425}; Note=kcat is 10.5 sec(-1) with monosialotetrahexosylganglioside as substrate. {ECO:0000269|PubMed:28179425}; | null | null | null | FUNCTION: Hydrolyzes glycosphingolipids; exhibits broad substrate specificity including monosialodihexosylganglioside (GM3), monosialotetrahexosylganglioside (GM1), fucosyl-GM1, lactosylceramide, globotriosylceramide, globotetraosylceramide, ganglioside GD1a, and ganglioside GD1b (PubMed:28179425). No activity towards ... | Rhodococcus hoagii (strain 103S) (Rhodococcus equi) |
A0A3S7WQS5 | SPCS_LEIDO | MDDRSLKLAEDFVSARYIEAGRESLRATARIMRSILAQRCCPDEGLTDAAIELILRQLSLMDTNNLAHHVGGGEREGRVVSALVRMRHFHLTHGIGRSGDLFSEQPKAAGSSLLYKITNVLMLDLIRQAGAPSTAAAVVVPMATGMTLALVLRCVAKTHMKELMKEAEAVQLQRTVTKDSTSATSAAPVQEPPMSEADRDRHDRTSLPVPATPRYVIWPRIDQKTALKCIDAAGLVPVPVQLRPAVPLARSAAPCVSTNRDSLDRGQDSIGSPSTPTSSSSLFLECHVDDVAAAVNAVGGPSQVVCVLSTTSCFAPRLPD... | 2.9.1.2 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|PIRNR:PIRNR017689, ECO:0000255|PIRSR:PIRSR017689-50}; | conversion of seryl-tRNAsec to selenocys-tRNAsec [GO:0001717]; selenocysteine incorporation [GO:0001514] | cytoplasm [GO:0005737] | O-phosphoseryl-tRNA(Sec) selenium transferase activity [GO:0098621]; selenotransferase activity [GO:0016785]; tRNA binding [GO:0000049] | PF05889; | 3.40.640.10; | SepSecS family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + 2 phosphate; Xref=Rhea:RHEA:25041, Rhea:RHEA-COMP:9743, Rhea:RHEA-COMP:9947, ChEBI:CHEBI:15377, ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78551, ChEBI:CHEBI:78573; EC=2.9.1.2; Evidence={ECO:0000255|P... | null | PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 2/2. {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}. | null | null | FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}. | Leishmania donovani |
A0A411EZW9 | PA21_AGKPL | MRTLWIMAVLLLGVEGDLMQFETLIMKIAKRSGMFWYSAYGCYCGWGGQGRPQDATDRCCFVHDCCYGKVTGCDPKLDSYTYSVENGDVVCGGNDPCKKEICECDRAAAICFRDNKVTYDNKYWRFPPQNCKEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:28063838}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418}; | 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]; 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:0000269|PubMed:28063838}. | 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:28063838}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.75 mM for 4-nitro-3-(octanoyloxy) benzoic acid (NOBA) {ECO:0000269|PubMed:28063838}; Vmax=25.9 nM/min/mg enzyme {ECO:0000269|PubMed:28063838}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:28063838}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:28063838}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that triggers a high neuromuscular toxicity in chick biventer cervicis preparations, but not in mouse phrenic nerve-diaphragm (PND) preparations, suggesting a selective neurotoxin activity towards birds (PubMed:28063838). Does not induce myotoxic, coagulant, anticoagulant, ... | Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias leucostoma) |
A0A411KUP8 | UCSA_ACRSP | MGPPSQATAANEPIAVIGSGCRFPGSASSPSKLWQLLSQPRDVLSEIPKSRFDPHGFYNKNGETGGHSNVLHSYVLDEDIRAWDADFFKVSASEAAAIDPQQRLLMETVYEALEAGGQQIHALRGSDTAVYVGLMGEEYSDIQGRELDMMPTYHATGTARSIVSNRISYFFDWHGASMTIDTACSSSLVAVHQCVQAIRSGYSRVAVAAGTNLCLGPEPYISESTFHMLSPRGRSHMWDASADGYGRGEGVAAVILKKLSDAIADGDHIECVIRETGVNQDGRTNGITVPSPDAQVALIQDTYRRAGLDLARPEDQPQFF... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; antibiotic biosynthetic process [GO:0017000]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:190156... | null | fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08241;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:29373009}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties (PubMed:29373009). These compounds share a hemiaminal-containing pyrroli... | Acremonium sp |
A0A411MR89 | SZNF_STRC2 | MSHVPPHVPFELSGAELRDAIVQYATNPIYHDNLDWLNHDNPYRRQLRPQVLPHLDYDKVPGRENILNYASLAVQRLLTSVYEADLVFFPKSGLKGKEEDFRAFYSPANRALGERIRPALERYAFGFLDDEVETSGTWTAQSLDAYLDSLDTAGGAEQSPVEKAILGSADRERAARMWLVQFAPDFLSEASPMMRNVLGYYGPAQSEWFKVVIDEYGYGVHDTKHSTLFERTLESVGLESDLHRYWQYYLNSSLLLNNYFHYLGKNHELFFRYVGALYYTESSLVDFCRRADHLLREVFGDTVDTTYFTEHIHIDQHHGR... | 1.14.13.250 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:30763082, ECO:0000269|PubMed:32511919, ECO:0000269|PubMed:33468680}; Note=Binds 3 Fe(2+) ions per subunit (PubMed:33468680). Two Fe(2+) bind the HO-like central domain and one Fe(2+) binds the C-terminal cupin domai... | antibiotic biosynthetic process [GO:0017000] | null | metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497] | PF07883;PF14518; | 1.20.910.10;2.60.120.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + N(omega)-methyl-L-arginine + 2 NADH + 3 O2 = 3 H2O + N(delta)-hydroxy-N(omega)-methyl-N(omega)-nitroso-L-citrulline + 2 NAD(+); Xref=Rhea:RHEA:69052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:114953, ChEBI:CHEBI:143209;... | null | PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:30728519, ECO:0000269|PubMed:30763082}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Stable and active at pH 3-8, but loses its activity above pH 9 (PubMed:30763082). Shows reduced activity in phosphate buffer at pH 4-6 (PubMed:30763082). {ECO:0000269|PubMed:30763082}; | null | FUNCTION: Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN) (PubMed:30728519, PubMed:30763082). Catalyzes a complex multi-step reaction: the overall reaction is an oxidative rearrangement of the guanidine group of N(omega)-methyl-L-arginine (L-NMA), generating an N-nitrosourea ... | Streptomyces achromogenes subsp. streptozoticus |
A0A445AGS0 | IFI4E_ARAHY | MATETAGAVVESSSAATVPSPAPEAGSKHKLERKWTFWFDNQSKPKQGAAWGTSLREVYTFDTVEEFWCLYDQVFKPSKLPGNADFHLFKTGIEPKWEDPECAKGGKWTVTSNRKANLDNMWLETMMALIGEQFDDAEDICGVVASVRQRQDKLSLWTKTAANEAAQMGIGRKWKEIIDVTDKIIYNFHDDSRTRSSKSRYSV | null | null | defense response to virus [GO:0051607] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-102-Cys-141 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus {ECO:0000269|PubMed:28344571}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus {ECO:0000269|PubMed:28344571}. Note=(Microbial infection) Binds to potyvirus viral genome-linked protein (VPg) in the nucleus and with viral helpe... | 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... | Arachis hypogaea (Peanut) |
A0A452E9Y6 | PERL_CAPHI | MLVCLHLQVFLASVALFEVAASDTIAQAASTTTISDAVSKVKTQVNKAFLDSRTRLKTALSSEAPTTRQLSEYFKHAKGRTRTAIRNGQVWEESLKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRL... | 1.11.1.7 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:... | antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979]; thiocyanate catabolic process [GO:0046265] | basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; peroxidase activity [GO:0004601]; thiocyanate peroxidase activity [GO:0036393] | PF03098; | 1.10.640.10; | Peroxidase family, XPO subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068}. Cytoplasm {ECO:0000250|UniProtKB:Q5SW46}. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000250|UniProtKB:P80025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137; Evidence={ECO... | null | null | null | null | FUNCTION: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By simila... | Capra hircus (Goat) |
A0A455R4Z0 | ASCI_ACREG | MPQLAGKLILAGLIPLGAWVLHGFASCNGLIQMFEDFGKQTVLSDGVTDYTGAFTGLEGLDRLLRTLLNFFWPVANGHDWALSLHAFMFAGQGVPLLVLNMLEGARPGNKSLVVSYVTVFGILYMVVGLAIMAPLYLFLHLLTSRTATAPSKAKVAVDPNTAKAVGFGVFVGYVLPTIFMSLPHPSLLSTDTKVLSVVFWQAVPLWASVCAYFASTALGQSATSRSSSNLPSALGAVYAASLIIATATHVATFAISANLSDTWSGIFTFLIPPNPFNTDMRISSFLEGATWFLQWDYTMMSLAYMVWAIGIRHGVEVPRS... | 5.4.99.- | null | terpenoid biosynthetic process [GO:0016114] | membrane [GO:0016020] | isomerase activity [GO:0016853] | null | null | Membrane-bound ascI terpene cyclase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=16-hydroxy-ilicicolin A epoxide = ascofuranol; Xref=Rhea:RHEA:63108, ChEBI:CHEBI:146158, ChEBI:CHEBI:146159; Evidence={ECO:0000269|PubMed:30952781, ECO:0000269|PubMed:35418536}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63109; Evidence={ECO:0000269|PubMed:30952781, ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50.4 uM for the product of ascH {ECO:0000269|PubMed:30952781}; Vmax=129 nmol/min/mg enzyme toward the product of ascH {ECO:0000269|PubMed:30952781}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:30952781, ECO:0000269|PubMed:35418536}. | null | null | FUNCTION: Epoxide hydrolase; part of the asc-2 gene cluster that mediates the biosynthesis of ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis (PubMed:30952781, PubMed:35418536). The first step in the pathway is performed by the ... | Acremonium egyptiacum (Oospora egyptiaca) |
A0A481NV25 | TYRDC_ENTFC | MKDMDIKAVFIGDKAENGPVYKMLLNKMVDEHLGWRENYIPSDMPAISEGDKLTPDYLATRDHMIEVLDEVSQRLRAGSIPWHSAGRYWGQMNAETLMPALLAYNYAMLWNPNNVALESSMATSQMEAEVGQDFASLFNMADGWGHIAADGSIANLEGLWYARCIKSIPLAVKEVLPEKVKNMSEWALLNLSVEEILEMTESFTDEEMDEVKAASSRSGKNIQKLGKWLVPQTKHYSWMKALDICGVGLDQMVAIPVQEDYRMDINALEKTIRELADQKIPILGVVAVVGTTEEGQVDSVDKIIQLREKLKDEGIYFYLH... | 4.1.1.-; 4.1.1.25 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305|PubMed:30659181}; | L-dopa metabolic process [GO:1903184] | null | L-dopa decarboxylase activity [GO:0036468]; pyridoxal phosphate binding [GO:0030170]; tyrosine decarboxylase activity [GO:0004837] | PF00282;PF21391; | 3.40.640.10; | Group II decarboxylase family, Tyrosine decarboxylase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315, ChEBI:CHEBI:327995; EC=4.1.1.25; Evidence={ECO:0000269|PubMed:30659181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346; Evidence={ECO:0000305|PubMed:30659181}; CAT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for L-tyrosine (at pH 5.0) {ECO:0000269|PubMed:30659181}; KM=0.4 mM for L-dopa (at pH 5.0) {ECO:0000269|PubMed:30659181}; Vmax=4.4 umol/min/mg enzyme for the decarboxylation of L-tyrosine (at pH 5.0) {ECO:0000269|PubMed:30659181}; Vmax=3.4 umol/min/mg enzyme... | PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:30659181}. | null | null | FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:30659181). Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastroint... | Enterococcus faecium (Streptococcus faecium) |
A0A481WNP4 | TRAA_PENCR | MVLPQPEPIAIVGSGCRFPGSSSSPSSLWDLLEKPRDVSKEPTNERFELRGYYHPNGAHHGTMNVQRAYMLDEDVGTFDATFFNISPNEAESIDPQQRLLMEVVYEALEAGGHRLDILRGSDTAVYVGTMSVDYNDIMLRDINSIPTYFSTGTSRAILANRISYFFDWHGPSMTIDTACSSSMVALHQSVQALRSGESRVAIAGGTELLLGPEQFVGESKMNLLSPTGQSRMWDASANGYARGDGIAAIVLKKLSDAIADGDHIECLIRQTGINQDGKSTGLTVPSSAAQADLIRSTYTKGGLDIDNPRDWPQFFEAHGT... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; lactone biosynthetic process [GO:1901336]; methylation [GO:0032259]; organonitrogen compound biosynthetic process [GO:1901566]; polyketide biosynthetic process [GO:0030639]; toxin biosynthetic process [GO:0009403] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:30811183}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the tra gene cluster that produces terrestric acid (PubMed:30811183). The clavatol biosynthesis cluster cla and the terrestric acid cluster tra are both involved in the production of peniphenones and penilactones (PubMed:30811183). The non-reducing PKS claF is responsible f... | Penicillium crustosum (Blue mold fungus) |
A0A482A9N4 | LP9A_TALVE | MPSTKVAALSAVLALASTVAGHGYVQNIVIDGESYSGYIVTQFPYESNPPAVIGWATTATDLGYVDPTEYTNADIICHKNATPGALSAPVAAGGTVELQWTTWPDSHHGPVISYLANCNGNCSTVDKTKLDFVKIDASGLIDDTTVPGTWASDQLIAANNSWTVTIPETIAPGNYVLRHEIIALHSAENTDGAQNYPQCINLEITGSGTASPTGTPGEELYTPTDPGILVNIYQSLSTYVIPGPTLWSGAANNAVASATAAASATATPTTLVTSVASATDSPSTVAPASSTTATSVLTSVVPSVTSFVPVVTVTDVVTVT... | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|Ref.3}; Note=Binds 1 copper ion per subunit. {ECO:0000269|Ref.3}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; monooxygenase activity [GO:0004497] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | PTM: The catalytically essential N-terminal histidine His-22 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:0000250|UniProtKB:G3XAP7}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30847851}. | 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:30847851, ECO:0000269|PubMed:31672609}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:31672609}; | 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 and C4 oxidation products (PubMed:30847851, PubMed:31672609). Catalysis by LPMOs requires the reduction of the active-site cop... | Talaromyces verruculosus (Penicillium verruculosum) |
A0A482D308 | CS12F_UNCAX | MAKNTITKTLKLRIVRPYNSAEVEKIVADEKNNREKIALEKNKDKVKEACSKHLKVAAYCTTQVERNACLFCKARKLDDKFYQKLRGQFPDAVFWQEISEIFRQLQKQAAEIYNQSLIELYYEIFIKGKGIANASSVEHYLSDVCYTRAAELFKNAAIASGLRSKIKSNFRLKELKNMKSGLPTTKSDNFPIPLVKQKGGQYTGFEISNHNSDFIIKIPFGRWQVKKEIDKYRPWEKFDFEQVQKSPKPISLLLSTQRRKRNKGWSKDEGTEAEIKKVMNGDYQTSYIEVKRGSKIGEKSAWMLNLSIDVPKIDKGVDPS... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30337455, ECO:0000269|PubMed:32246713}; Note=Mg(2+) is required for dsDNA cleavage (PubMed:32246713). Mg(2+) and Mn(2+) support ssDNA cleavage equally (PubMed:30337455). {ECO:0000269|PubMed:30337455, ECO:0000269|PubMed:32246713}; COFACTOR: Name... | defense response to virus [GO:0051607] | null | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF07282; | null | CRISPR-associated endonuclease Cas12f family | null | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature for dsDNA cleavage is 46 degrees Celsius and occurs between 37-52 degrees Celsius, no cleavage at 55 degrees Celsius (PubMed:32246713). Optimum temperature for ssDNA cleavage is 45-55 degrees Celsius (PubMed:30337455). {ECO:0000269|PubMed:30337... | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading ... | Uncultured archaeon |
A0A482N9V7 | ICCA_TALVA | MAANDSNNQTKPQLPEEPVAIVGSSCRFPGSSNSPSKLWDLLRQPRDVLKEFDPDRLNLKRFYHPDGDTHGSTDVTNKSYLLEEDSRLFDASFFTINPAEAAGMDPQQRILLETVYEAFESAGMTLEQLRGSLTAVHVGTMTNDYAGIQLRDLETIAKYNATGTANSIVSNRISYVFDLKGPSETIDTACSSSLVALHHAARGLLNGDCETAVVAGVNLIYDAASYIAESKLHMLSPDSQSRMWDKSANGYARGEGAAALLLKPLSRALRDGDHIEGVIRATGVNSDGQSPGITMPFAPTQAALIRQTYRRAGLDPVKDR... | 2.3.1.-; 6.3.2.- | null | fatty acid biosynthetic process [GO:0006633]; ilicicolin H biosynthetic process [GO:0140781]; methylation [GO:0032259] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; non-ribosomal peptide synthetase activity [GO:1904091]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]; polyke... | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 8 AH2 + ATP + 4 H(+) + holo-[ACP] + L-tyrosine + 7 malonyl-CoA + 2 S-adenosyl-L-methionine = 8 A + AMP + 7 CO2 + 8 CoA + diphosphate + 6 H2O + N-[(4E,6E,10S,12Z,14E)-6,10-dimethyl-3-oxohexadeca-4,6,12,14-tetraenoyl]-L-tyrosyl-[ACP] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:... | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:30905148}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:30905148). IccA assembles the backbone of ilicicolin H (PubMed:30905148)... | Talaromyces variabilis (Penicillium variabile) |
A0A482PDI9 | NLEB_CITRO | MLSPLNVLQFNFRGETALSDSAPLQTVSFAGKDYSMEPIDEKTPILFQWFEARPERYGKGEVPILNTKEHPYLSNIINAAKIENERVIGVLVDGDFTYEQRKEFLSLEDEHQNIKIIYRENVDFSMYDKKLSDIYLENIHEQESYPASERDNYLLGLLREELKNIPYGKDSLIESYAEKRGHTWFDFFRNLAVLKGGGLFTETGKTGCHNISPCGGCIYLDADMIITDKLGVLYAPDGIAVYVDCNDNRKSLENGAIVVNRSNHPALLAGLDIMKSKVDAHPYYDGVGKGLKRHFNYSSLQDYNVFCNFIEFKHKNIIPN... | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B7UI21}; | symbiont-mediated perturbation of host defense response [GO:0052031]; symbiont-mediated perturbation of host defense-related programmed cell death [GO:0034053]; symbiont-mediated suppression of host NF-kappaB cascade [GO:0085034] | extracellular region [GO:0005576]; host cell [GO:0043657] | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362]; toxin activity [GO:0090729] | null | 3.90.550.20; | Glycosyltransferase NleB family | PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins. {ECO:0000250|UniProtKB:B7UI21}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16552063}. Host cell {ECO:0000269|PubMed:16552063}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:16552063}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP; Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322... | null | null | null | null | FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:16552063, PubMed:23955153, PubMed:24025841, PubMed:28522607). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a... | Citrobacter rodentium |
A0A494BA31 | B3A4_MOUSE | MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKL... | null | null | bicarbonate transport [GO:0015701]; monoatomic anion transport [GO:0006820]; regulation of intracellular pH [GO:0051453]; saliva secretion [GO:0046541]; sodium ion transmembrane transport [GO:0035725]; transmembrane transport [GO:0055085] | apical part of cell [GO:0045177]; basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886] | chloride:bicarbonate antiporter activity [GO:0140900]; sodium,bicarbonate:chloride antiporter activity [GO:0140892]; sodium:bicarbonate symporter activity [GO:0008510] | PF07565;PF00955; | 1.10.287.570; | Anion exchanger (TC 2.A.31) family | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12225984, ECO:0000269|PubMed:23610411, ECO:0000305|PubMed:34585968}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the basolateral membrane of the cortical collecting duct (CCD)and submandibular gland (SMG) duct. {ECO:0000269|PubMed:1222... | CATALYTIC ACTIVITY: Reaction=chloride(in) + 2 hydrogencarbonate(out) + Na(+)(out) = chloride(out) + 2 hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72739, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:25745107, ECO:0000269|PubMed:27114614}; CATALYTIC ACTIVITY: Reaction=chlori... | null | null | null | null | FUNCTION: Electroneutral Cl(-)/HCO3(-) antiporter that favors chloride ion entry and efflux of hydrogencarbonate and sodium ion across the basolateral membrane and may participate in salivary secretion (PubMed:25745107, PubMed:27114614). Also mediates Cl(-)/HCO3(-) exchange activity in the presence of K(+) as well as C... | Mus musculus (Mouse) |
A0A499UB99 | OXDA_TALEM | MATNNIVVLGAGVSGLTTAWLLSKDPSNKITVAAKHMPGDYDIEYCSPWAGANYLPVGAENSRVGQWERATWPHLRDIAQNHPEAGIHFQDTVVYNRTKDQGSTTGQWFSELVKPNPWYGKVLPNFRELSKDELPPGIDNANRFTSVCINTAVYLPWLVGQCRKNGVVFKRAVFKHVAEAANAHHSGQKADLVVNCTGLSSRKLGGVQDNTLLPARGQIVVVRNDPGLMCSISGTDDGDDEVTYMMTRAAGGGTILGGTYQKHNWDSLPDPNLAVRIMKRCIELCPSLVAPGQGIEGLDIIRHGVGLRPVREDGPRIEKE... | 1.4.3.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:31420577, ECO:0000269|PubMed:33135670}; | D-amino acid catabolic process [GO:0019478]; D-amino acid metabolic process [GO:0046416]; nitrogen utilization [GO:0019740] | peroxisomal matrix [GO:0005782] | D-amino-acid oxidase activity [GO:0003884]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | PTM: The disulfide bond might contribute to the high thermal stability of the protein. {ECO:0000269|PubMed:33135670}. | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q9HGY3}. | CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:31420577}; PhysiologicalDirection=left-to-ri... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.213 mM for D-methionine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=0.628 mM for D-valine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:31420577}; KM=2.7 mM for D-alanine (at 55 degrees Celsius and at pH 8.0) {ECO:0000269|P... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:31420577}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:31420577}; | FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:31420577). Enables the organism to utilize D-amino acids as a source of nutrients (By similarity). Unusually, has high activity on D-glutamate (PubMed:31420577). {ECO:0000250|UniProtKB:Q9HGY3, ECO:0000269|PubMed:3142... | Talaromyces emersonii (Thermophilic fungus) (Rasamsonia emersonii) |
A0A4P8DY91 | COMTS_KITPR | MTTTELIPPTIQVDEEEEEACMFAMQLASASVLPMVLKSAIELDLLESIAKAGPGAYVSPSELAAKLPSSQPDTPVMLDRILRLLASYSVLKCKVQDLPQGGVERLYALAPVCKFLTKNSDGVSMAPLLLMNQDKILMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGKDPRFNKVFNLGMSNHSTITMKKILQTYNGFAGLKTVVDVGGGTGATLNMIISKYPNIKGINFDLPHVVEDAPSYPGVEHVGGDMFVSVPEGDAIFMKWICHDWSDAHCLSFLKNCYKALPQNGKVILAECILPEAPDSKLTTKNVIHIDVI... | 2.1.1.-; 2.1.1.69; 2.1.1.70 | null | aromatic compound biosynthetic process [GO:0019438]; coumarin biosynthetic process [GO:0009805]; methylation [GO:0032259]; response to hydrogen peroxide [GO:0042542]; response to UV [GO:0009411] | null | catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; O-methyltransferase activity [GO:0008171]; orcinol O-methyltransferase activity [GO:0102938]; 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=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:30934718}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11809; Evi... | null | PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:30934718}.; PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:30934718}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:30934718}; | null | FUNCTION: O-methyltransferase involved in the biosynthesis of methoxylated coumarins natural products such as isoscopoletin, scopoletin, xanthotoxin and bergapten, photosensitizers used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses (PubM... | Kitagawia praeruptora (Peucedanum praeruptorum) |
A0A4P8WAE5 | PYIS_PYRGI | MAATFSEPVAIIGTGCRFPGQCNTPSKLWELLQTPKDLLKEIPENRFSTEAFYHPQNYHHGTCNVRHSYFLEEDLRGFDAQFFGINPVEAHSVDPQQRLLLETVYESLEAAGLSMKEMQGSDTAVYVGVMSADFTDMIGRDPETFPTYFATGTARSILSNRLSFFFDWRGPSMTIDTACSSSLIEPRTGANKPDCAEQVAGSNLILGSEQYIAESKLQMLSPTGRSRMWDADADGYARGEGVAAIVLKKLSQAIADGDHIECIIRETGANQDGRTPGITMPSATAQEALIRTTYKKAGLDISKRSDRPQFFEAHGTGTPA... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31099577}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology (Probable) (PubMed:31099577)... | Pyricularia grisea (Crabgrass-specific blast fungus) (Magnaporthe grisea) |
A0A4V8GZX0 | TXNA1_OMOSC | ECKGFGKSCVPGKNECCSGLTCSNKHKWCKVLL | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 14 (Hntx-1) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30784059}. | null | null | null | null | null | FUNCTION: Potently and reversibly inhibits some human voltage-gated sodium channels (Nav1.1/SCN1A (IC(50)=72.0 nM), Nav1.2/SCN2A (IC(50)=75.5 nM), Nav1.6/SCN8A (IC(50)=115.0 nM), Nav1.7/SCN9A (IC(50)=52.7-129.5 nM), Nav1.3/SCN3A (IC(50)=306.6 nM)) (PubMed:30784059). The hNav1.7/SCN9A channel inhibition occurs without a... | Omothymus schioedtei (Malaysian earth tiger tarantula) (Cyriopagopus schioedtei) |
A0A4X1UM84 | PCKGC_PIG | MPPQLSNGLNHSAKVVRGTLDSLPQAVRDFVESSAKLCQPDQIHICDGSEEENQQLLSHMEEEGVIKRLKKYDNCWLALTDPRDVARIESKTVIITQEQRDAVPIPRSGLSQLGRWMSPEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGSAVLDALGAGEFIKGLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRMASRLAKEEGWLAEHMLILGVTNPEGQKKYFAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDQQ... | 2.7.11.-; 4.1.1.32 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P35558}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P35558}; | cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucose stimulus [GO:0071333]; cellular response to insulin stimulus [GO:0032869]; cellular response to potassium ion starvation [GO:0051365]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycer... | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783] | carboxylic acid binding [GO:0031406]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; phosphoenolpyruvate carboxykinase (GTP) activity [GO:0004613]; protein serine kinase activity (using GTP as donor) [GO:0106264] | PF00821;PF17297; | 3.90.228.20;3.40.449.10;2.170.8.10; | Phosphoenolpyruvate carboxykinase [GTP] family | PTM: Acetylated (By similarity). Lysine acetylation by p300/EP300 is increased on high glucose conditions and promotes ubiquitination by UBR5, acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2 (By similarity). Deacetylated by SIRT1 (By similarity). {ECO:0000250|UniProtKB:P35558, ECO:0000250|UniProt... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35558}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35558}. Note=Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P35558}. | CATALYTIC ACTIVITY: Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate; Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; Evidence={ECO:0000269|PubMed:26792594}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389; Evidenc... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=240 uM for phosphoenolpyruvate {ECO:0000269|PubMed:26792594}; KM=27.4 uM for GDP {ECO:0000269|PubMed:26792594}; KM=13.1 uM for oxaloacetate {ECO:0000269|PubMed:26792594}; KM=45.9 uM for GTP {ECO:0000269|PubMed:26792594}; Note=kcat is 6.8 sec(-1) with phosphoenolpyr... | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000250|UniProtKB:Q9Z2V4}. | null | null | FUNCTION: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:26792594). Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediate... | Sus scrofa (Pig) |
A0A4Y1WBN6 | YYCJ_BACAN | MGLHFSVLASGSTGNMLYVGTDEKKLLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTWNAMEHLIGNIPTDQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHNNNRKLALITDTGYVSDRMKGVIKGANAFVFESNHDVEMLRMGRYPWSIKRRILSDVGHVCNEDAALAMADVITDETKHIYLAHLSLDNNMKELARMSVSQVLEEKGFGVGEAFEIHDTDPKMPTKIQYV | 3.1.11.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q8ZRM2}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8ZRM2}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23491602}; Note=Binds 2 metal ions per subunit. The endogenous metal is unknown. {ECO:00... | null | null | exonuclease activity [GO:0004527]; metal ion binding [GO:0046872] | PF12706; | 3.60.15.10; | Metallo-beta-lactamase superfamily | null | null | null | null | null | null | null | FUNCTION: 5'->3' double-stranded DNA exonuclease (PubMed:23491602). May play a role in mutation mismatch repair (MMR) (PubMed:23491602). Required for accurate coordination of cell division with DNA replication (By similarity). May play a role in cell wall metabolism (By similarity). {ECO:0000250|UniProtKB:C0SP91, ECO:0... | Bacillus anthracis |
A0A4Y6HUD7 | PALY2_PLEOS | MTILSGTTAAPRVNGTTMNGHSKPHTNGVHLNGHAPKATTESPWPQSEEKTLLDKFVEAYYEFESYKSGQTVKVDGKTLSLAGVVAAARHHAKISLDDSASIKDKVVKSRKVIADKVASGASVYGLSTGFGGSADTRTDQPLSLGHALLQHQHVGVLPSSSQPLDVLPLSDPMSATSMPEAWVRAAMLIRMNSLIRGHSGVRWELIEKIAEIFDANITPVVPLRSSISASGDLSPLSYIAGTVVGNPSIRVFDGPAAFGAREMVPSAKALASHGIDPLPLASKEPLGILNGTAFSAAVGALALNEAVHFAMLAQVCTAMG... | 4.3.1.24 | null | cinnamic acid biosynthetic process [GO:0009800]; L-phenylalanine catabolic process [GO:0006559] | cytoplasm [GO:0005737] | phenylalanine ammonia-lyase activity [GO:0045548] | PF00221; | 1.20.200.10;1.10.275.10; | PAL/histidase family | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. {ECO:0000250|UniProtKB:Q68G84}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-phenylalanine = (E)-cinnamate + NH4(+); Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; EC=4.3.1.24; Evidence={ECO:0000269|PubMed:31655558}; | null | PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and a free ammonium ion (PubMed:31655558). Facilitates the commitment step in phenylpropanoid pathways that produce secondary metabolites such as lignins, coumarins and flavonoids (By similarity). {ECO:0000250|UniProtKB:P11... | Pleurotus ostreatus (Oyster mushroom) (White-rot fungus) |
A0A4Z3 | A3LT2_RAT | MALEGLRAKKRLLWRLFLSAFGLLGLYHYWFKIFRLFEVFIPMGICPMAIMPLLKDNFTGVLRHWARPEVLTCTSWGAPIIWDETFDPHVAEREARRQNLTIGLTVFAVGRYLEKYLEHFLVSAEQYFMVGQNVVYYVFTDRPEAVPHVALGQGRLLRVKPVRREKRWQDVSMARMLTLHEALGGQLGREADYVFCLDVDQYFSGNFGPEVLADLVAQLHAWHFRWPRWMLPYERDKRSAAALSLSEGDFYYHAAVFGGSVAALLKLTAHCATGQQLDREHGIEARWHDESHLNKFFWLSKPTKLLSPEFCWAEEIGWRP... | 2.4.1.87 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P14769}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769}; | carbohydrate metabolic process [GO:0005975]; cellular response to manganese ion [GO:0071287]; glycosphingolipid biosynthetic process [GO:0006688]; lipid glycosylation [GO:0030259] | Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; vesicle [GO:0031982] | alpha-1,3-galactosyltransferase activity [GO:0001962]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; N-acetyllactosaminide 3-alpha-galactosyltransferase activity [GO:0047276] | PF03414; | null | Glycosyltransferase 6 family | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:17206613, ECO:0000269|PubMed:18630988}; Single-pass type II membrane protein {ECO:0000269|PubMed:17206613, ECO:0000269|PubMed:18630988}. Note=Also found in numerous large vesicles throughout the cytoplasm of the soma. | CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:13013, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI... | null | null | null | null | FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group on the glycosphingolipid isoglobotrihexosylceramide or isogloboside 3 (iGb3) by catalyzing the transfer of galactose from UDP-Galactose to its acceptor molecule Gal-beta-1,4-Glc-ceramide. Can also catalyze the addition of galactose to iGb3 itself to form po... | Rattus norvegicus (Rat) |
A0A509ADH4 | YOP1_PLABA | MRMSKLYKNKEKENEKPSNEPPIKQDSLKRMSSKFLGNSLNSFDLSGKLEQVDEYLKKYPFIIEFGYKLGIKPSYIVVFGGSALFISLVLGWGAALICNLVGFAYPAYQSFKAVESQGHAETKLWLTYWVVFSLFFFIEYLIDIILFWIPFYYVIKLLFLLYLYMPQVRGAETVYNYIIRPILLKHEKTIDDTVHKISQTATNHLNQFTGNIAEKLVQEGVRRRNV | null | null | endoplasmic reticulum tubular network membrane organization [GO:1990809]; vacuole organization [GO:0007033] | endoplasmic reticulum membrane [GO:0005789] | null | PF03134; | null | DP1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:32432369}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Required to generate and maintain the structure of the tubular endoplasmic reticulum network and the digestive (food) vacuole (PubMed:27484902, PubMed:32432369). Induces high curvature in membranes and causes membrane tubule formation (PubMed:27484902). {ECO:0000269|PubMed:27484902, ECO:0000269|PubMed:3243236... | Plasmodium berghei (strain Anka) |
A0A509AFG4 | CDPK3_PLABA | MNQLCVERNLSISTAYIKSKPKKYIERIKKKKSSNKSIKSQHKFEGSKIANKNNELKDIKSKDPKHYENHINKNTKHKDILLKSKRSDNFKFSRRGFILSFTGNLEDFYNLSEEPLGKGTYGCVYKATDKLLKIQRAVKVVSKKKLKNIPRFRQEIDIMKNLDHPNVIKLLETFEDEEQIYLIMDLCTGGELFDKIIKKGSFVEMYASFIMKQIFSVLNYLHIRNICHRDIKPENFLFYDKSTESLIKIIDFGLAAYFNDIDYEMKTKAGTPYYVAPQVLTGCYDYKCDLWSAGVLFYIILCGYPPFYGESDHEILSMVK... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IBS5}; | intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cell migration [GO:0030335]; positive regulation of cell motility [GO:2000147] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019] | PF13499;PF00069; | 1.10.238.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16430692}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q8IBS5}; CATALYTI... | null | null | null | null | FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). In the mosquito midgut, regulates the gliding motility of the ookinete which is essential for the ookinete to invade the midgut epitheli... | Plasmodium berghei (strain Anka) |
A0A509AH51 | EIK2_PLABA | MLNMVDQKKGINNGSSTGVINNINGKIKNEFIFMYLIAAGGFSCVYKIKKKKSNKFYALKKIKFSANESNYEKKVLLNLREIECLRKLKNHPNIVSMNDFWLEVVQTLSKSKRERRGRRKEQQREQMGDKRREKRQQQRREKRKEQNTNTKKRVLITLSDHKKKKLKHLSCPENALNISNITNNERNVLKKDNWKNLILLKNFKKEKHNYNFNHQIELNKYNIMCLWKILNQMCVCKNEKKNIESLLPEQLIKNFKNFLFEKYILAIYDDCSYLNNKNNKTFIFFNNNLGNILHYLWWSYLGKNGKEKKNDIFKLLKYVS... | 2.7.11.1 | null | chromosome segregation [GO:0007059]; dormancy maintenance of symbiont in host [GO:0085015]; microtubule-based process [GO:0007017]; negative regulation of translation [GO:0017148]; peptidyl-serine phosphorylation [GO:0018105]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998] | centrosome [GO:0005813]; cortical microtubule [GO:0055028]; membrane [GO:0016020]; nucleus [GO:0005634] | ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily | PTM: Auto-phosphorylated. {ECO:0000250|UniProtKB:Q8I265}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-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:0000305|PubMed:20584882}; Physiolog... | null | null | null | null | FUNCTION: Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules. {ECO:0000269|PubMed:20584882}. | Plasmodium berghei (strain Anka) |
A0A509AHB6 | CDPK1_PLABA | MGCNQSKSANDVRGNKVNHVNSKKKNNKREDTNDGEEIAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCKEKNGHSEKAIKVIKKSQFDKGRYSDDNKNIEKFHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKNSLLNIKIVDFGLSSFFSKDYKLRDRLGTAYYIAPEVLKKKYNEKCDVWSCGVIMYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISDEAKELIKLMLTYDYNKRCTAEEALN... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P62344}; | intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cell motility [GO:2000147]; positive regulation of translation [GO:0045727] | cytoplasm [GO:0005737]; host cell plasma membrane [GO:0020002]; motile cilium [GO:0031514]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; symbiont-containing vacuole membrane [GO:0020005] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683] | PF13499;PF00069; | 1.10.238.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily | PTM: Myristoylated. Myristoylation and palmitoylation are required for the localization to the parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.; PTM: Palmitoylated. Palmitoylation increases in merozoites in response to low level of extracellular K(+) in the host blood. Myristoylation and palmitoylation... | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cell membrane {ECO:0000269|PubMed:22817984}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}; Cytoplasmic side {ECO:0000250|UniProtKB:P62344}. Parasitophorous vacuole membrane {ECO:0000250|UniProtKB:P62344}; Lipid-an... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P62344}; CATALYTI... | null | null | null | null | FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK... | Plasmodium berghei (strain Anka) |
A0A509AJA5 | ICP_PLABA | MKSITFFVFNICSILALLSHCEDNDIYSFDIVNETNWLKIAKNIFKGKSPSNFTIIPFNNTGSSNDNESNKEESVLLIRKKIKSNKNHDSSIISGDTVNGDISDLNYTASNFSDNSEDIEDNQKYPTTSYNSFNHLNSNIAFNEESEYIEINSESDLENKIKDINIKSNLEENNTMNESGKVDSKYELTGDEKCGKSLKLGNISNQTNQETITQSLSVGEILCIDLEGNAGTGYLWVLLGIHKDEPIINPENFPTKLTKKSFFSEEISVTQPKKYKIDEHDSSKNVNREIESPEQKESDSKPKKPQMQLLGGPDRMRSVI... | null | null | null | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; microneme [GO:0020009]; transport vesicle [GO:0030133] | cysteine-type endopeptidase inhibitor activity [GO:0004869] | PF12628; | 2.60.40.2020; | Protease inhibitor I71 family | PTM: During the liver stage, proteolytically cleaved. {ECO:0000269|PubMed:20361051}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20361051}. Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000269|PubMed:20361051}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:20361051}. Host cytoplasm {ECO:0000269|PubMed:20361051}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:20361051}. ... | null | null | null | null | null | FUNCTION: Cysteine protease inhibitor (PubMed:20361051, PubMed:21742259). Required for the invasion of host erythrocytes by merozoites (By similarity). In the mosquito vector, essential for the gliding motility of hemocoel sporozoites and, therefore, for salivary gland invasion and the subsequent transmission from the ... | Plasmodium berghei (strain Anka) |
A0A509AKL0 | KGP_PLABA | MDDDEIIPKKNHPSNERNKKKAILSHEDFTGEDSLMENHLELRDKLTEDIVTIKASLKNNLVCSTLNENEILALSNYMQFFVFKSGDMVIKQGEKGSYFFIINSGKFDVYVNDKKVKTLTKGSSFGEAALIHNTQRSATIKAGTNGTLWGVQRSTFRATLKQLSNRNFNENRSFIDSVSVFDMLTEAQKNMITNACVIQNFKPGETIVKQGDYGDVLYILKDGKATVYINDEEIRVLEKGSYFGERALLYDEPRSATIIAKEVTSCASICRKLLNVVLGNLQVVLFRNIMTEALQQSEIFKQISPDQLNDLADTAIVRDY... | 2.7.11.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8I719}; | phosphorylation [GO:0016310]; signal transduction [GO:0007165] | cAMP-dependent protein kinase complex [GO:0005952]; endoplasmic reticulum membrane [GO:0005789] | ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; cGMP binding [GO:0030553]; cGMP-dependent protein kinase activity [GO:0004692]; metal ion binding [GO:0046872] | PF00027;PF00069; | 2.60.120.10;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cGMP subfamily | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q8I719}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19779564, ECO:0000269|PubMed:27425827}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8I719}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8I719}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8I719}. Note=Predominantly localizes to the cytoplasm during sch... | 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=2.7.11.12; Evidence={ECO:0000250|UniProtKB:Q8I719}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine protein kinase which acts as a downstream effector of the second messenger cGMP (By similarity). Controls the release of Ca(2+) from intracellular stores by regulating phosphoinositide biosynthesis (PubMed:24594931). Ca(2+) signals are essential for merozoite and sporozoite invasion and egres... | Plasmodium berghei (strain Anka) |
A0A509ALD0 | ADA_PLABA | MEIPNEEIKFLKKEDIKNINLNGMNKKERYEIWKKIPKVELHCHLDLTFSGKFFLKWVRKYNLQPNMTDDQVLDHYLFTKEGKSLAEFIRKAISVSDIYRDYDILEDLAKWAVIEKYKEGVVLMEFRYSPTFVSSSHGLDIELIHKAFVKGIKNATEMLNNKIYVALICISDTGHSAASIKHSGDFAIKHKHDFVGFDHGGREIDLKDHKDVYHSVRNHGLHLTVHAGEDATLPNLNTLYTAINILNVERIGHGIRVSESEELIELVKKNNILLEVCPISNLLLNNVKSMDTHPIRKLFDAGVKVSVNSDDPGMFLTDIN... | 3.5.4.31; 3.5.4.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:A5KE01}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:A5KE01}; | adenosine catabolic process [GO:0006154]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; purine ribonucleoside salvage [GO:0006166] | cytosol [GO:0005829]; external side of plasma membrane [GO:0009897] | 2'-deoxyadenosine deaminase activity [GO:0046936]; 5'-methylthioadenosine deaminase activity [GO:0090614]; adenosine deaminase activity [GO:0004000]; metal ion binding [GO:0046872] | PF00962; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:19728741}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=57 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=4.4 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 4.7 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.35 sec(-1) with 5'-methylthioadenosine... | PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000305|PubMed:19728741}. | null | null | FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741). Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741). Plays an essential rol... | Plasmodium berghei (strain Anka) |
A0A509AMC3 | PK4_PLABA | MYNKGINICLNEDNKCIILLHIIFNKCIVSFVASHILVEGKICFLNRIKNSKIFRRFGNINNHRRNNVKEYYKFVGRINKGKEKRNKCRIKLHRFYEYAKSYILKQIKWVLNKSKYIYFNIIYHLKTICYLKNAFFLQYTQRKYFSQNIENYIINSLPKHIQSFNPIKWSYYNNNEYASNYIIINNLNFIKYKNKYEKQYDIEMEEDINCKGANDIFYNSYNYCNNNNSNSKCDEKIEKNIVDKNIENKYNIKEYDKTNKSILFPIEEEFKKIIQIENNIERNYMVPNESNKNILYNIKNILEKIRNIEAISNINNYIDM... | 2.7.11.1 | null | negative regulation of translation [GO:0017148]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998] | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634] | ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29241041}; Multi-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:29241041}; Physiolog... | null | null | null | null | FUNCTION: During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition (PubMed:29241041). Plays a role in trophozoite differentiation into schizonts (PubMed:29241041). {ECO:0000269|PubMed:29241041}. | Plasmodium berghei (strain Anka) |
A0A509APX1 | GCYB_PLABA | MKETDKIKSEVLNLMQLDGKREHINKNNKLYRKVIINPTSEDDLQKFCKNYFRIYQFSLYNFIRRLISLDAVIVYTLFMTVYIFSEISQGITKKYLFVDTAISLFLNIGILVVIESLFELKLLKDIKNANSQHYLRIVPKMSYFEKVMTKDIKVGNIIRVFQGEEFPADVVILYSKKNTNAVVDSFKIDGLYNKSIKYPVEKYKIDRDYLKMLSEINGVIKCELPNKNVFCFQGTYKLDKHPRSLHLSYENFALQSSILKGAEYIDGVVVYTGADTKKNLNIPRKIEENMTFCIKMNNVVYYLIFMYILFVLLSIIIKAI... | 4.6.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IDA0}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8IDA0}; Note=Binds 2 magnesium ions per subunit (By similarity). Is also active with manganese (in vitro) (By similarity). {ECO:0000250|UniProtKB:P30803, ECO:0000... | intracellular signal transduction [GO:0035556]; phospholipid translocation [GO:0045332]; positive regulation of cell motility [GO:2000147] | plasma membrane [GO:0005886] | ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; guanylate cyclase activity [GO:0004383]; metal ion binding [GO:0046872] | PF00211;PF16212; | 2.70.150.10;3.40.50.1000;3.30.70.1230; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily; Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | 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:Q8IDA0}; | null | null | null | null | FUNCTION: Catalyzes the synthesis of the second messenger cGMP from GTP (By similarity). Probably by regulating cGMP production, required for ookinete gliding motility, which is necessary for the ookinete to traverse the midgut epithelium of the mosquito (PubMed:17030505, PubMed:19779564). {ECO:0000250|UniProtKB:Q8IDA0... | Plasmodium berghei (strain Anka) |
A0A509AQ68 | ENO_PLABA | MAHVITRINAREILDSRGNPTVEVDLETTLGIFRAAVPSGASTGIYEALELRDNDKSRYLGKGVQQAIKNINEIIAPKLIGLDCREQKKIDNMMVQELDGSKTEWGWSKSKLGANAILAISMAICRAGAAANKTSLYKYLAQLAGKNTEKMILPVPCLNVINGGSHAGNKLSFQEFMIVPVGAPSFKEAMRYGAEVYHTLKSEIKKKYGIDATNVGDEGGFAPNILNAHEALDLLVASIKKAGYENKVKIAMDVAASEFYNIETKTYDLDFKTPNNDKSLVKTGQELVDLYIELVKKYPIISIEDPFDQDDWENYAKLTE... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IJN7}; Note=Binds 2 Mg(2+) ions per subunit (By similarity). Mg(2+) is required for catalysis and for stabilizing the dimer (By similarity). Unlike for mammalian and yeast enolases, Mg(2+) is dispensable to form an active closed conformati... | glycolytic process [GO:0006096] | cell surface [GO:0009986]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886]; vacuole [GO:0005773] | magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21949403}. Nucleus {ECO:0000269|PubMed:21949403}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:W7JLR6}. Cell surface {ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}. Cell membrane {ECO:0000250|UniProtKB:Q7RA60}; Peripheral membrane protein {ECO:0000305}; ... | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000250|UniProtKB:W7JLR6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO:0000250|UniProtKB:W7JLR6}; Phys... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:Q8IJN7}. | null | null | FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (By similarity). In addition to glycolysis, involved in various processes such as parasite development and invasion (PubMed:21949403, PubMed:24474798). Plays an essential role during ookinete invasion of the mosquito ... | Plasmodium berghei (strain Anka) |
A0A509AQE6 | CDPK5_PLABA | MCEHKANNKNDGEFVNLKEKNENNHCGNTKSTIADCDDDYSIITLCTKCLSTKTEVNKNKIILDSKALKDSRTKRRSSVNINIDILNNNLNLSPYFDRSQIVQETILMNNDDLEKLYELDKYKLGKGSYGNVVKAINKKTGQAKAIKIIDKKRINNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCTGGELFDKIVKHGSFSEYETYKIMKQIFSALAYCHSKNIIHRDLKPENILYVDSSDDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILKGKYDKKCDIWSSGVIMYILLCGYPPFNGKNND... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A5K1K8H0}; | intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cell motility [GO:2000147] | cytoplasmic vesicle [GO:0031410]; microneme membrane [GO:0033163]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019] | PF13499;PF00069; | 1.10.238.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily | PTM: May be palmitoylated. {ECO:0000250|UniProtKB:A0A5K1K8H0}.; PTM: Autophosphorylated in vitro. {ECO:0000250|UniProtKB:A0A5K1K8H0}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A5K1K8H0}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000250|UniProtKB:A0A5K1K8H0}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0A5K1K8H0}; Cytoplasmic side {ECO:0000250|UniProtKB:A0A5K1K8H0}. Cell membrane {ECO:0000250|UniProtKB:A0A... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A0A5K1K8H0}; CATA... | null | null | null | null | FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). Plays a central role in host erythrocytes and hepatocytes infection cycles (PubMed:32866196). During the liver stage, involved in sporoz... | Plasmodium berghei (strain Anka) |
A0A517FNB9 | C9B52_PARPY | MEGLLLLLPTAIIALYLYISLIRRSRKKHNLPPGSDGWPFLGETFSYLKPHSAISIGRFMEDHISRYGKIYRSNLFGEPTIVSADAELNRFVLQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRMISLNFMSAARLRTRLMPEVERQTLLVLRSWREGSTFSAQEEAKKFTFNLMAKHIMSMDPGEPETEMLRREYITFMKGVVSAPLNFPGTPYWKALKSRSSILAVIERKMEERIGRRDRGDGGVEDDDLLGWAMNQSNLLKEQILDLLLSLLFAGHETSSMALALAIYFLESCPEAVRDLRDEHLAISMSGK... | 1.14.14.- | null | brassinosteroid biosynthetic process [GO:0016132]; cholesterol metabolic process [GO:0008203]; steroid biosynthetic process [GO:0006694] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69839, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:... | null | PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:31324795}. | null | null | FUNCTION: Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation. {ECO:0000269|PubMed:31324795}. | Paris polyphylla (Daiswa polyphylla) |
A0A517FNC5 | C90G4_PARPY | MAPVVILFFLFPTLLVLVVAVLGLRGGDDSWKKRGLKVPPGSMGWPLLGETIAFRRLHPCTSLGEYMEEHVNKYGKIYRSNLFGAPTIVSADAELNRFVLMNDERLFEPCFPKSVADILGHTSMLVLTGEMHRYMKSLSVNFMGIARLRNNFLGDSELYITQNFNRWKENIPFPAKEEACKVTFNLMVKNILSLNPGEPESEHLRKLYMSFMKGVVAIPLNLPGTAYKKAIQSRATILKMIEKLMEERIRNKKAGTDKIGEADLLGFILEQSNLDAEQFGDLLLGLLFGGHETSATAITLVIYFLYDCPKAVDHLREEHL... | 1.14.14.- | null | cholesterol metabolic process [GO:0008203]; saponin biosynthetic process [GO:0016135]; steroid biosynthetic process [GO:0006694] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=cholesterol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (16S,22S)-dihydroxycholesterol + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:72191, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI... | null | PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:31324795}. | null | null | FUNCTION: Involved in the biosynthesis of spiroketal steroid and saponin natural products from cholesterol such as diosgenin and analogs (e.g. furostanol and spirostanol), plant defense compounds used as main precursors for the industrial production of steroid hormones (PubMed:31324795). During the 5,6-spiroketalizatio... | Paris polyphylla (Daiswa polyphylla) |
A0A517FNC6 | C9B51_TRIFG | MSDSDITFYCLSSILSVLLIFIFILIKRKQAKPKLNLPPGKMGWPFLGETIGYLKPYSATTLGEFMDQHIARYGKIYKSKLFGEPAIVSADAGLNRFILQNEGKLFECSYPRSIGGILGKWSMLVLVGDMHRDMRLISLNFLSHARLRTHLLKEVEKHTRLVISSWKENSTFAAQDEAKKFTFNLMAEHIMSLQPGKIETEKLKKEYVTFMKGVVSAPLNFPGTAYWKALKSRGTILKFIEGKMEERIKRMKEGNENLEEDDLLNWVLKHSNLSTEQILDLILSLLFAGHETSSVSIALAIYFLPGCPQAILQLREEHKE... | 1.14.14.- | null | brassinosteroid biosynthetic process [GO:0016132]; cholesterol metabolic process [GO:0008203]; steroid biosynthetic process [GO:0006694] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69839, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:... | null | PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:31324795}. | null | null | FUNCTION: Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation. {ECO:0000269|PubMed:31324795}. | Trigonella foenum-graecum (Fenugreek) |
A0A5B8NIM2 | CMU_ERYQU | MDAAVDLLDPSKALNLKHIRQQLIRMEDTITFQLIERVQFPLNRTVYEPGAVKIPNSNLSFLDWTLREREKTDSLIRRYQSPDEHPFFPDALLKPILQPLIYPKILHRNNINLNDKIKKYFTDQVLPSICHDFGREDRGEQAENYGSTVTADIQCLQTLSRRIHFGKWVAESKYIDDPQGFAKLIKAGDRQAIGKAITKPAVELQVLERIRLKSRTYSTDPCESDDPEPKINVDAVVAMYRDCVIPLTKEVEIDYLMQRLSD | 5.4.99.5 | null | chorismate metabolic process [GO:0046417]; effector-mediated suppression of host salicylic acid-mediated innate immune signaling [GO:0140502]; L-phenylalanine biosynthetic process [GO:0009094]; tyrosine biosynthetic process [GO:0006571] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430] | chorismate mutase activity [GO:0004106] | null | 1.10.590.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:33010586}. Secreted {ECO:0000305|PubMed:33010586}. Host cytoplasm {ECO:0000305|PubMed:33010586}. Note=Appears to be secreted despite an apparent lack of a secretory signal. {ECO:0000305|PubMed:33010586}. | CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:33010586}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; Evidence={ECO:0000269|PubMed:33010586}; | null | PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. {ECO:0000305|PubMed:33010586}. | null | null | FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate (PubMed:33010586). May function both as an effector during plant infection and in the fungal tyrosine and phenylalanine biosynthesis pathways (PubMed:33010586). During infection it channels chorismate into the phenylpropanoid pathway, thereby dec... | Erysiphe quercicola (Hevea powdery mildew) |
A0A5B9 | TRBC2_HUMAN | DLKNVFPPKVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSESYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDSRG | null | null | adaptive immune response [GO:0002250]; alpha-beta T cell activation [GO:0046631]; antibacterial humoral response [GO:0019731]; complement activation, classical pathway [GO:0006958]; T cell receptor signaling pathway [GO:0050852] | alpha-beta T cell receptor complex [GO:0042105]; blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; immunoglobulin complex, circulating [GO:0042571]; plasma membrane [GO:0005886] | antigen binding [GO:0003823]; immunoglobulin receptor binding [GO:0034987] | PF07654; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:20452950}. | null | null | null | null | null | FUNCTION: Constant region of T cell receptor (TR) beta chain (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed b... | Homo sapiens (Human) |
A0A5C2A2T2 | COP1_CONPU | MKLLAPVLWAMAALGVTWLVAVDSKESCTKHSNGCSTPLRLPCQEYFRPACDIHDNCYHCGTIFGISRKECDDAFLKDMNTLCKKLGSNSATCPARGKREVTSHRATSIAHSRLWKTALDQKSFLNRKARQAILLTPNSCLYWANNFYMAVHVFGARSYSRTTDPKDCQGLKHCLPNH | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:30765458}; | arachidonic acid secretion [GO:0050482]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | phospholipase A2 activity [GO:0004623]; toxin activity [GO:0090729] | null | 1.20.90.10; | Phospholipase A2 family, Group IX subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30765458}. | 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:30765458}; | null | null | null | null | FUNCTION: Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:30765458}. | Conus purpurascens (Purple cone) |
A0A5E4M3Q4 | SYD9_CAEEL | MSVCVSPLVQATILMTEESLTCPQCPKSFSSTKLLQQHQQMFHTDKSVLLSLKSTDAPVGMDRAFICETCGKAFRFRSNLAEHRSVHTALKPYVCKFCGKSSRLKGNLTKHILKHHKKEQNEAIAKDDIIVKKAPKIVTKDNGPTTNGSTPTTSTATPSVITVSSALASSNGHNNNNNNHAVNNNLRTIKMELEDPDYNLIAKSAPTPVVSKIVATHTVTPRSRPTPKDIKEILETIAPSVGVSETPEEMCLLPKDASSESDRSVLISLGFDFGSTLSLNHQQLQQVVRELKGELSISPDTVQSDHSDDFEQDSPPPMAI... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nuclear speck [GO:0016607]; 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; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16803962}. Nucleus speckle {ECO:0000269|PubMed:16803962}. | null | null | null | null | null | FUNCTION: Plays a role in regulating synaptic function, probably by modulation of endocytosis (PubMed:16803962). May be dispensable in muscle for normal locomotion (PubMed:16803962). May be involved in post-transcriptional mRNA processing, in parallel with unc-75 (PubMed:16803962). {ECO:0000269|PubMed:16803962, ECO:000... | Caenorhabditis elegans |
A0A5F8MPU3 | CTSRT_MOUSE | MELPPPGNRRVSINNPQETSGRVPTTSAGFPTQSSKISLKRSTYAYRPSMMSNRSSGGQSLLPSSILQKTSLNPPGSLQSKPSNLSSVHYADEEGKPLTDKNKDKDKGRGKGKGTGTRLLTMLRKTLQGSQSDEMAIANQTPNLIPFGDVVGCLAIHIKSCRQFSQRFLGQQRFNLFMRVSINNIVKCTKIRHLKAVNNEKNLVLRFGEMKYFSVQVPRRQDDERNFIYLELMHDGGDPESPPIPLGGAESHLYEVIQKGCFTEVMHLMHKNSSICRVEVEFMFSYGNFGYGFSHQLKPLQKAIEPSMFMNIAPPPERTD... | null | null | flagellated sperm motility [GO:0030317]; sperm capacitation [GO:0048240]; spermatogenesis [GO:0007283]; vesicle-mediated transport to the plasma membrane [GO:0098876] | CatSper complex [GO:0036128]; sperm principal piece [GO:0097228] | null | PF15729; | null | null | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:34998468}. Note=Specifically located in the principal piece of the sperm tail. {ECO:0000269|PubMed:34998468}. | null | null | null | null | null | FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CatSper complex targeting and trafficking into the quadrilinear nanodomains.... | Mus musculus (Mouse) |
A0A5K1K8H0 | CDPK5_PLAF7 | MKETEVEDMDTNRKDGKIKKKEKIVNMKNEEVKSTTKSTLADSDEDYSIITLCTKCLSKKLEDNKNRIILDSKAFKDNRLKGRCSVSSNEDPLDNKLNLSPYFDRSQIIQEIILMNNDELSDVYEIDRYKLGKGSYGNVVKAVSKRTGQQRAIKIIEKKKIHNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCDGGELFDKIVKYGSFSEYEAYKIMKQIFSALYYCHSKNIMHRDLKPENILYVDNTEDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILRGKYDKRCDIWSSGVIMYILLCGYPP... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20466936}; | intracellular signal transduction [GO:0035556]; positive regulation of regulated secretory pathway [GO:1903307]; protein phosphorylation [GO:0006468] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; extrinsic component of membrane [GO:0019898]; microneme membrane [GO:0033163]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019]; protein serine kinase activity [GO:01063... | PF13499;PF00069; | 1.10.238.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily | PTM: May be palmitoylated. {ECO:0000303|PubMed:12368867}.; PTM: Autophosphorylated in vitro. {ECO:0000269|PubMed:20466936}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29487234}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:29487234}; Peripheral membrane protein {ECO:0000269|PubMed:29487234}; Cytoplasmic side {ECO:0000269|PubMed:29487234}. Cell membrane {ECO:0000269|PubMed:20466936, ECO:0000269|PubM... | 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:20466936, ECO:000026... | null | null | null | null | FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (PubMed:20466936, PubMed:31915223). Plays a central role in host erythrocytes and hepatocytes infection cycles (PubMed:20466936, PubMed:29487234). During... | Plasmodium falciparum (isolate 3D7) |
A0A5K7RLP0 | MEIOS_MOUSE | MLGSDKFSCFSDQHRARSPSPTDRKDKKNHTNKLRELALLIPVTMKTRDKKYTKKEILLRVLHYIQYLQRNIDMTKALLKLHSSNGKGRFVGPGLNPSAGQTQQQHSTPSSSQKPSLWSTSSKPRKKKFTRVSEHPSWPYNPRRSLALDQAENPNTIHPGLKEENEECATYPGVLSPSTYPTTEPSVSEGDGQGAQLVFLDMAQNIFAYDILSDHAVEVQGGEPNADIKVQRSFFLTRAQPCVSSCRQKLFLCTSSEADKEAPDSDPWLPVWTSEDSPNGSPLALGSSQINTWHVADYLNEILGVSSSLFSSPSKILPDH... | null | null | activation of meiosis [GO:0090427]; cellular response to retinoic acid [GO:0071300]; meiotic cell cycle [GO:0051321]; oogenesis [GO:0048477]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283] | nucleus [GO:0005634] | DNA binding [GO:0003677]; protein dimerization activity [GO:0046983] | PF00505; | 1.10.30.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32032549}. | null | null | null | null | null | FUNCTION: Gatekeeper of meiotic initiation in both male and female germ cells (PubMed:32032549). In complex with STRA8, directly activates the transcription of a subset of critical meiotic genes playing a central role in cell-cycle switching from mitosis to meiosis. Temporal expression of MEIOSIN is required for meioti... | Mus musculus (Mouse) |
A0A5P3XKQ1 | PMP1_PARBF | MLQIRVFNYNDPIDGENIVELRYHNRSPVKAFQIVDGIWIIPERYNFTNDTKKVPDDRALTILEDEVFAVRENDYLTTDVNEKNSFLNNITKLFKRINSSNIGNQLLNYISTSVPYPVVSTNSIKARDYNTIKFDSIDGRRITKSANVLIYGPSMKNLLDKQTRAINGEEAKNGIGCLSDIIFSPNYLSVQTVSSSRFVEDPASSLTHELIHALHNLYGIQYPGEEKFKFGGFIDKLLGTRECIDYEEVLTYGGKDSEIIRKKIDKSLYPDDFVNKYGEMYKRIKGSNPYYPDEKKLKQSFLNRMNPFDQNGTFDTKEFK... | 3.4.24.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P0DPI0}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07953;PF07952; | 2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10; | Peptidase M27 family | null | null | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000269|PubMed:31253776}; | null | null | null | null | FUNCTION: [Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion; expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. ... | Paraclostridium bifermentans (Clostridium bifermentans) |
A0A5R8T042 | BLC15_ECO25 | MVKKSLRQFTLMATATVTLLLGSVPLYAQTADVQQKLAELERQSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAAAAVLKKSESEPNLLNQRVEIKKSDLVNYNPIAEKHVNGTMSLAELSAAALQYSDNVAMNKLIAHVGGPASVTAFARQLGDETFRLDRTEPTLNTAIPGDPRDTTSPRAMAQTLRNLTLGKALGDSQRAQLVTWMKGNTTGAASIQAGLPASWVVGDKTGSGGYGTTNDIAVIWPKDRAPLILVTYFTQPQPKAESRRDVLASAAKIVTDGL | 3.5.2.6 | null | beta-lactam antibiotic catabolic process [GO:0030655]; response to antibiotic [GO:0046677] | null | beta-lactamase activity [GO:0008800] | PF13354; | 3.40.710.10; | Class-A beta-lactamase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34310213}. Note=Type I secretion system (T1SS) probably involved in secretion process. {ECO:0000269|PubMed:34310213}. | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:28069651, ECO:0000269|PubMed:29941650, ECO:0000269|PubMed:35515906, ECO:0000269|PubMed:35563620}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42 uM for amoxicillin (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:29941650}; KM=19 uM for amoxicillin (at pH 6.4 and 20 degrees Celsius) {ECO:0000269|PubMed:28069651}; KM=197 uM for ampicillin (at pH 7.4) {ECO:0000269|PubMed:35563620}; KM=141 uM for desf... | null | null | null | FUNCTION: Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, third and fourth-generation cephalosporins (PubMed:11470367, PubMed:28069651, PubMed:29941650, PubMed:34310213, PubMed:35515906, PubMed:35563620). Has cefotaxime- and ceftazidime-hydrolyzing activity (Pu... | Escherichia coli O25b:H4 |
A0A5S9I252 | TATC6_HYPAT | MGQPTTTSLFMRDVMFHRMTGTSQAVNDVATLSGERREIIRRALNKKILVPNILELMPAWPSEFQPNIDEVNVEIDEWLKTVNVAKEKKLKHRARGNYTLLAGIYYPHCRKEKMLALSQFLYWIFFWDDEIDTGGELTEDREGTILCCAETNKCINDCLGPEPNYTPPPGSRGTVEMLYPILRDLRAGLSPVSTMRLKQELHDYVNGVKNQQKVRQEDHLPNPWDHFQMRVDDVGVIPSITQNEYAMDFTLPDWIRRHEAMEEIVLQCTKLTILLNEILSLQKEFRVSQLENLCLLFMNTYDMSIEQSIHKVLGLLKDHY... | 4.2.3.-; 4.2.3.104; 4.2.3.137; 4.2.3.157; 4.2.3.182; 4.2.3.57 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UR08}; Note=Binds 3 Mg(2+) ions per monomer. {ECO:0000250|UniProtKB:Q9UR08}; | null | null | (-)-E-beta-caryophyllene synthase activity [GO:0080016]; alpha-humulene synthase activity [GO:0080017]; metal ion binding [GO:0046872] | PF19086; | 1.10.600.10; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + trichobrasilenol; Xref=Rhea:RHEA:66644, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:167379, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:31418991}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66645; Evidence={ECO:0000269|... | null | PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:31418991}. | null | null | FUNCTION: Terpene cyclase that is able to convert FPP into a mixture of sesquiterpene hydrocarbons and alcohols (PubMed:31418991). The main product is trichobrasilenol (PubMed:31418991). Additionally, side products include alpha-humulene, caryophyllene, 2-epi-caryophyllene, african-3-ene, african-1-ene, isoafricanol an... | Hypocrea atroviridis (Trichoderma atroviride) |
A0A5S9MMK5 | FPEB1_CAEEL | MMTTTVQKNCWRLDQTMLGLEKPGSSDISSSSTDTSAISPISVSSMPLSPDKEKKKISFVRYNPDIPQIVTSFKGYQKLMYQGYRYNIYQIAPERNFKSWRCVCAKKMHDGQWCKCRAETTMDNKNACTKGSHNHPPRHHVAEIEFIKSQLYSAALENPDHDAGDLVNQASMYLSDGVMFDNKESIKKSLVVARNKDGKPKKPRSKRMMKFEVDDDDENEYKMPKLETDISCFLPFINNMVKVEPPFSHTPTIQIPQPIPTPIQHQQQEQSNLLQPATLNGMNNPWMGMEDHLAMIWAANAMLNPGLDVLSTIAALSKHQ... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleus [GO:0005634] | metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF04500; | 2.20.25.240; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11203704, ECO:0000269|PubMed:15165844}. Note=Localization to nucleus dependent, in part, on FLYWCH-type domain. {ECO:0000269|PubMed:15165844}. | null | null | null | null | null | FUNCTION: Putative transcription factor (PubMed:11203704). Binds to specific sequence motif 5'-[TC][AGT]TGCC[GA][AT]-3' in regulatory elements of target genes such as myosin myo-2 (PubMed:11203704, PubMed:15165844). May modulate gene expression, perhaps acting in opposition to transcription factor pha-4 (PubMed:1120370... | Caenorhabditis elegans |
A0A644F0Y1 | TBG_GIAIC | MPREVITIQCGQCGNQIGEVFWNRLCTEHGINPDGTLRPEAYTFNDRKDVFFYQSDDEHYVPRAILLDTEPGVISHIRNGPIKELINPENVYIDSTGGGAGNIWTKGFQCGEAGFEKIVEIIDREADGADSLAGFSLTHSIAGGTGSGMGSFLLDRLSDRYPKALLQTYSVFPNTTADIIVQPYNSILTLQRLALCADAVVVLDNTALDRIITNHIPNELLTNPFEHVNSLVSTVMAASTSTLRLPGFMSNDLLSLVSSLVPTPRLHFLMSSYTPITSSSLNVKEHTKDQEAGSGAVAGAAAGATRRQVHTDSIVQLVKR... | null | null | cytoplasmic microtubule organization [GO:0031122]; meiotic spindle organization [GO:0000212]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle organization [GO:0007052] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; gamma-tubulin complex [GO:0000930]; microtubule [GO:0005874]; motile cilium [GO:0031514]; nucleus [GO:0005634]; spindle [GO:0005819] | GTP binding [GO:0005525]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, spindle {... | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules (Potential). The gamma chain is found at microtubule organizing centers (MTOC) such as the centrosome (PubMed:30318753). Component of the gamma-tubulin small complex (gamma-TuSC) involved in microtubule nucleation for the formation of median bodies and in the b... | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A0A644F649 | IFT88_GIAIC | MTQNWRPQSRLQTMTFAGTARPMTSMTAAGFTKNPLATAGVASIFDKLPPEPPKDSPEQKADQMEINIFKLLRDGMSAASCKDYVTALGRIREAIKLEQKVSQHRTMNGLADSINLDLRTCIWMHWAQIQALGGQPEMALSTYEKIVKTAEGATLAQIRFNMGNINHNLGKYNEALKNFRMAIDQASPSLPRFRQKIASHMAQSCIKLHRWQDAVDRIEEYLIKQYTLASSVGTDVERQNFYAMTTRFDPLYTVLIGYYALGVPEKMIDAYSRLIDSSILISDHPDSLEIDDHHNGISSKQIAMADAELCNMSNDDELDD... | null | null | cilium assembly [GO:0060271]; inner ear receptor cell stereocilium organization [GO:0060122]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735]; kidney development [GO:0001822]; non-motile cilium assembly [GO:1905515] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary pocket collar [GO:1990900]; ciliary tip [GO:0097542]; intraciliary transport particle B [GO:0030992]; non-motile cilium [GO:0097730] | kinesin binding [GO:0019894] | PF13174;PF13181; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:31855176}. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eigh... | null | null | null | null | null | FUNCTION: Component of the intraflagellar transport complex B (IFT-B) involved in flagellar assembly (Probable). {ECO:0000305|PubMed:31855176}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
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