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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B9DGI8 | BZP63_ARATH | MEKVFSDEEISGNHHWSVNGMTSLNRSASEWAFNRFIQESSAAADDGESTTACGVSVSSPPNVPVDSEEYRAFLKSKLNLACAAVAMKRGTFIKPQDTSGRSDNGGANESEQASLASSKATPMMSSAITSGSELSGDEEEADGETNMNPTNVKRVKRMLSNRESARRSRRRKQAHLSELETQVSQLRVENSKLMKGLTDVTQTFNDASVENRVLKANIETLRAKVKMAEETVKRLTGFNPMFHNMPQIVSTVSLPSETSNSPDTTSSQVTTPEIISSGNKGKALIGCKMNRTASMRRVESLEHLQKRIRSVGDQ | null | null | cellular response to abscisic acid stimulus [GO:0071215]; cellular response to glucose stimulus [GO:0071333]; cellular response to starvation [GO:0009267]; entrainment of circadian clock [GO:0009649] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; protein heterodimerization activity [GO:0046982]; protein self-association [GO:0043621] | PF00170;PF12498; | 1.20.5.170; | BZIP family | PTM: Phosphorylated. The phosphorylation at Ser-29, Ser-294 and Ser-300 by KIN10 strongly enhances its ability to form homo- as well as heterodimers and are then essential for its transcriptional activity (PubMed:26263501). {ECO:0000269|PubMed:20047775, ECO:0000269|PubMed:26263501}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:16957775}. | null | null | null | null | null | FUNCTION: Transcription factor involved in controlling responses to starvation (PubMed:26263501). BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to up-regulate its transcription (PubMed:29348240). {ECO:0000269|PubMed:26263501, ECO:0000269|PubMed:29348240}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DGT7 | TBA2_ARATH | MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVSILLDNEAIYDICRRSLSIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPVISAEKAFHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects ... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Arabidopsis thaliana (Mouse-ear cress) |
B9DGU7 | TPK1_ARATH | MSAMDVMIHSSSFLLPCDETSTGTRYALVVLNQSLPRFTPLLWEHAKLRLCADGGANRIYDELPLFFPNEDALAIRNRYKPDVIKGDMDSIRRDVLDFYINLGTKVIDESHDQDTTDLDKCILYIRHSTLNQETSGLQILATGALGGRFDHEAGNLNVLYRYPDTRIVLLSDDCLIQLLPKTHRHEIHIQSSLEGPHCGLIPIGTPSAKTTTSGLQWDLSNTEMRFGGLISTSNLVKEEKITVESDSDLLWTISIKKTGLSIQDHTP | 2.7.6.2 | null | phosphorylation [GO:0016310]; thiamine diphosphate biosynthetic process [GO:0009229]; thiamine metabolic process [GO:0006772] | cytosol [GO:0005829] | 8-oxo-dGDP phosphatase activity [GO:0044715]; ATP binding [GO:0005524]; kinase activity [GO:0016301]; thiamine binding [GO:0030975]; thiamine diphosphokinase activity [GO:0004788] | PF04265;PF04263; | 3.40.50.10240;2.60.120.320; | Thiamine pyrophosphokinase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17611796}. | CATALYTIC ACTIVITY: Reaction=ATP + thiamine = AMP + H(+) + thiamine diphosphate; Xref=Rhea:RHEA:11576, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385, ChEBI:CHEBI:30616, ChEBI:CHEBI:58937, ChEBI:CHEBI:456215; EC=2.7.6.2; Evidence={ECO:0000269|PubMed:17611796}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11577; Evidence=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.28 uM for thiamine {ECO:0000269|PubMed:17611796}; Vmax=9.6 pmol/min/mg enzyme with thiamine as substrate {ECO:0000269|PubMed:17611796}; | PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1. {ECO:0000269|PubMed:17611796}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. Active between pH 6 and pH 8. {ECO:0000269|PubMed:17611796}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:17611796}; | FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate (TPP) (PubMed:17611796). TPP is an active cofactor for enzymes involved in glycolysis and energy production (PubMed:17611796). Plant leaves require high levels of TPP for photosynthesis and carbohydrate metabolism (PubMed:17611796). {ECO:0000... | Arabidopsis thaliana (Mouse-ear cress) |
B9DGY1 | AB1K7_ARATH | MAALLASQSCCYGGETARVTKAIGFSSSLENHFTGEATQCYGSKSKRFRIEMRQSELPSKVGINGRSVKMVPASEVVKRKDGVNGSAGKGVNGASLVSSRNINGAASTLVKAPKKTTESYLPPPVEGVRVLPSDEGFSWADENYSSLQRSIDVWSFVISLRIRILFDNSKWAYVGGFTEEKQKSRRRETASWLRESVLQLGPTFIKLGQLSSTRSDLFPREFVDELSKLQDRVPAFSPEKAKRFIEAELGAPISVMYKEFEEQPIAAASLGQVHRAVLHNGEKVVVKVQRPGLKKLFDIDLRNLKLIAEYFQKSESFGTN... | 2.7.11.1 | null | cellular response to oxidative stress [GO:0034599]; membrane lipid biosynthetic process [GO:0046467]; phosphorylation [GO:0016310]; regulation of response to reactive oxygen species [GO:1901031]; response to iron ion starvation [GO:1990641]; response to oxidative stress [GO:0006979] | chloroplast thylakoid membrane [GO:0009535]; plastoglobule [GO:0010287] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF03109; | null | Protein kinase superfamily, ADCK protein kinase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:24117441}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:22274653, ECO:0000305|PubMed:22694836}. | 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:Q9MA15}; CATALYTI... | null | null | null | null | FUNCTION: Involved in resistance to oxidative stress. Influences responses to reactive oxygen species (ROS) production. Regulates plastoglobules formation in thylakoids. Together with OSA1, regulates iron distribution within the chloroplast and mediates the oxidative stress response (PubMed:24117441). Together with ABC... | Arabidopsis thaliana (Mouse-ear cress) |
B9DHQ0 | TBA5_ARATH | MREIISIHIGQAGIQVGNSCWELYCLEHGIQPDGMMPSDTTVGVAHDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTVGKEIVDLCLDRVRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQIISSLTTSLRFDGAINVDITEFQTNLVPYPRIHFMLSSYAPVISAAKAYHEQLSVPEITNAVFEPASMMAKCDPRHGKYMACCLMYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Arabidopsis thaliana (Mouse-ear cress) |
B9DHT4 | ARIA_ARATH | MDQQPERREGRSFPERKGQKRKLEEGAAAVEDREISAVSTDGGQALLSEVAAQVSVLNSAFSWQESDRAAAKRATQVLAELAKNEDLVNVIVDGGAVPALMTHLQAPPYNDGDLAEKPYEHEVEKGSAFALGLLAIKPEYQKLIVDKGALPHLVNLLKRNKDGSSSRAVNSVIRRAADAITNLAHENSSIKTRVRVEGGIPPLVELLEFSDSKVQRAAAGALRTLAFKNDDNKNQIVECNALPTLILMLGSEDAAIHYEAVGVIGNLVHSSPHIKKEVLTAGALQPVIGLLSSCCPESQREAALLLGQFASTDSDCKVHI... | null | null | negative regulation of seed germination [GO:0010187]; protein ubiquitination [GO:0016567]; response to abscisic acid [GO:0009737]; response to salt stress [GO:0009651] | nucleus [GO:0005634]; plasma membrane [GO:0005886] | null | PF00514;PF00651; | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15516505}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2... | Arabidopsis thaliana (Mouse-ear cress) |
B9E972 | OLHYD_MACCJ | MYYSNGNYEAFARPKKPEGVDNKSAYLVGSGLASLAAASFLIRDGQMKGENIHILEELDLPGGSLDGILNPERGYIMRGGREMENHFECLWDLFRSVPSLEVEDASVLDEFYWLNKEDPNYSKCRVIENRGQRLESDGKMTLTKKANKEIIQLCLMKEEQLNDVKISDVFSKDFLDSNFWIYWKTMFAFEPWHSAMEMRRYLMRFIHHIGGLADFSALKFTKFNQFESLVMPLIEHLKAKNVTFEYGVTVKNIQVECSKESKVAKAIDIVRRGNEESIPLTENDLVFVTNGSITESTTYGDNDTPAPPTSKPGGAWQLWE... | 4.2.1.53 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:22203098}; Note=Binds 1 FAD per subunit. FAD does not seem to be involved in catalysis but rather in the structural stabilization of the enzyme. {ECO:0000269|PubMed:22203098}; | fatty acid metabolic process [GO:0006631]; response to toxic substance [GO:0009636] | null | FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; oleate hydratase activity [GO:0050151]; protein homodimerization activity [GO:0042803] | PF06100; | 3.30.9.80;3.50.50.60; | Oleate hydratase family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O; Xref=Rhea:RHEA:21852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15683, ChEBI:CHEBI:30823; EC=4.2.1.53; Evidence={ECO:0000305|PubMed:22203098}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21854; Evidence={ECO:0000305|PubMed:22203098}; CAT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=340 uM for oleate {ECO:0000269|PubMed:22203098}; KM=300 uM for myristoleate {ECO:0000269|PubMed:22203098}; KM=570 uM for palmitoleate {ECO:0000269|PubMed:22203098}; KM=390 uM for linoleate {ECO:0000269|PubMed:22203098}; KM=320 uM for alpha-linolenate {ECO:0000269|P... | PATHWAY: Lipid metabolism; fatty acid metabolism. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with oleate as substrate. {ECO:0000269|PubMed:22203098}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius with oleate as substrate. After 120 minutes, the enzyme activity is nearly unchanged at 25 degrees Celsius, but is reduced to only 25% at 35 degrees Celsius. {ECO:0000269|PubMed:22203098}; | FUNCTION: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate, probably in the (R) configuration. Cannot catalyze the reverse reaction. Is not active with saturated fatty acids and trans-, cis-5-, cis-6-, cis-8-, cis-11-, cis-13-, cis-14-, and cis-15-double bond unsaturated fatty... | Macrococcus caseolyticus (strain JCSC5402) (Macrococcoides caseolyticum) |
B9EHT4 | CLIP3_MOUSE | MTKTDPAPMAPPPRGEEEEEEEEDEPVPEAPSPTQERRQKPVVHPSAPAPLPKDYAFTFFDPNDPACQEILFDPKTTIPELFAIVRQWVPQVQHKIDVIGNEILRRGCHVNDRDGLTDMTLLHYACKAGAHGVGDPAAAVRLSQQLLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVLLKGARPRVVNSTCSDFNHGSALHIAASNLCLGAAKCLLEHGANPALRNRKGQVPAEVVPDPMDMSLDKAEAALVAKELRTLLEEAVPLSCTLPKVTLPNYDNVPGNLMLSALGLRLGDRVLLDGQKTGTLRFCGTTEFAS... | null | null | cytoplasmic microtubule organization [GO:0031122]; fat cell differentiation [GO:0045444]; membrane biogenesis [GO:0044091]; negative regulation of microtubule polymerization [GO:0031115]; peptidyl-L-cysteine S-palmitoylation [GO:0018230]; positive regulation of apoptotic process [GO:0043065]; positive regulation of end... | cell cortex [GO:0005938]; early endosome membrane [GO:0031901]; Golgi stack [GO:0005795]; membrane raft [GO:0045121]; microtubule plus-end [GO:0035371]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:003258... | ganglioside binding [GO:0035594]; microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010] | PF12796;PF01302; | 1.25.40.20;2.30.30.190; | null | PTM: Palmitoylation by ZDHHC17 regulates association with the plasma membrane. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Note=Localized to Golgi stacks as well as on tubulovesicular elements juxtaposed to Golgi cisternae. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. May modulate the cellular compartmentalization of AKT kinase family and promote its cell membrane localization, thereby playing a role in glucose transport in adipocytes (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
B9EJ57 | MTF1B_MOUSE | MASRNIWCVRRNFLFDLRGWMLQYSAEVFLKSISFRTFSVECDSKDKESLEEEREDLLSNLVTMGVDIDMARRRQPGVFNKAVTNEQELKIFLLSKGASDKVIGSIISRYPRAITRTPESLSKRWDLWRKIMASDLEIVNILERSPESFFRSNNNLNLENNIKFLCSVGLTHKCLCRLLTNAPRTFSNSLNLNKQMVEFLQETGMSLGHNDPRDFVRKIISKNPSILIQSTKRVKTNIEFLQSTFNLNKQDLLLLICGPGARILDLSNDCTKKNYTNIRERLLSLGCSEEEVQRFVLSYLNMVFLSEKKFNDKIDCLIEE... | null | null | regulation of DNA-templated transcription [GO:0006355]; termination of mitochondrial transcription [GO:0006393]; transcription initiation at mitochondrial promoter [GO:0006391] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | double-stranded DNA binding [GO:0003690]; nucleic acid binding [GO:0003676]; sequence-specific DNA binding [GO:0043565] | PF02536; | 1.25.70.10; | MTERF family | PTM: Phosphoprotein with mostly four phosphate groups. While the DNA-binding activity is unaffected by the phosphorylation state, only the phosphorylated form of the protein is active for termination activity. Functioning seems to be regulated by phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q99551}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99551}. | null | null | null | null | null | FUNCTION: Transcription termination factor. Binds to a 28 bp region within the tRNA(Leu(uur)) gene at a position immediately adjacent to and downstream of the 16S rRNA gene; this region comprises a tridecamer sequence critical for directing accurate termination. Binds DNA along the major grove and promotes DNA bending ... | Mus musculus (Mouse) |
B9EJ80 | PDZD8_MOUSE | MGLLLLILASAVLGSFLTLLAQFLLLYRRQPEPRADEAARAGDGFRYLKPVPGLPLREYLYGGGAEELAACSSEAGASSTPTPDSPAPPTLETCYFLNATILFLFRELRDTALARRWVTKKIKVEFEELLQTKTAGRLLEGLSLRDVFLGDTVPFIKTIRLVRPVVASGTGEPDDPDGDALPATCPEELAFEAEVEYNGGFHLAIDVDLVFGKSAYLFVKLSRVVGRLRFVLTRVPFTHWFFSFVEDPLIDFEVRSQFEGRPMPQLTSIIVNQLKKIIKRKHTLPSYKIRFKPFFPYQALQGFEEDEELIHIQQWALTEG... | null | null | cytoskeleton organization [GO:0007010]; lipid transport [GO:0006869]; mitochondrial calcium ion homeostasis [GO:0051560]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; regulation of cell morphogenesis [GO:0022604] | endoplasmic reticulum membrane [GO:0005789]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; mitochondrion [GO:0005739] | lipid binding [GO:0008289]; metal ion binding [GO:0046872] | PF00130;PF17820; | 2.30.42.10;3.30.60.20; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29097544}; Single-pass membrane protein {ECO:0000255}. Note=Localizes at mitochondria-endoplasmic reticulum contact sites. {ECO:0000269|PubMed:29097544}. | null | null | null | null | null | FUNCTION: Molecular tethering protein that connects endoplasmic reticulum and mitochondria membranes (PubMed:29097544). PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for endoplasmic reticulum-mitochondria Ca(2+) transfer (PubMed:29097544). In neurons, involved in the regulation of d... | Mus musculus (Mouse) |
B9EJ86 | OSBL8_MOUSE | MEAALADGEPDRSSLLGDSKDVLGPSTVVANSDEPQHLTPGKMSQRQGRDANPTPTRDLPQPSLSPASLHSQGFERGKEDISQNKDDSSLSMSKSKSESKLYNGSEKDSSTSSKLTKKESLKVQKKNYREEKKRATKELLSTITDPSVIVMADWLKIRGTLKSWTKLWCVLKPGVLLIYKTQKNGQWVGTVLLNACEIIERPSKKDGFCFKLFHPLEQSIWAVKGPKGEAVGSITQPLPSSYLIIRATSESDGRCWMDALELALKCSSLLKRTMVREGKEHDLSISSDSTHVTLYGLLRANNLHSGDNFQLNDSEIERQH... | null | null | fat cell differentiation [GO:0045444]; negative regulation of cell migration [GO:0030336]; negative regulation of sequestering of triglyceride [GO:0010891]; phospholipid transport [GO:0015914]; positive regulation of glucose import [GO:0046326]; positive regulation of insulin receptor signaling pathway [GO:0046628]; po... | cortical endoplasmic reticulum [GO:0032541]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear membrane [GO:0031965] | cholesterol binding [GO:0015485]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylserine binding [GO:0001786]; phosphatidylserine transfer activity [GO:0140343]; sterol transporter activity [GO:0015248] | PF01237;PF00169; | 1.10.287.2720;2.40.160.120;3.30.70.3490;2.30.29.30; | OSBP family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BZF1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9BZF1}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BZF1}. Note=The presence of the N-terminus extension contains an overall negative charge that may explain the weak localization to t... | null | null | null | null | null | FUNCTION: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1... | Mus musculus (Mouse) |
B9EJA2 | CTTB2_MOUSE | MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKK... | null | null | regulation of modification of postsynaptic actin cytoskeleton [GO:1905274]; regulation of synapse organization [GO:0050807] | cell cortex [GO:0005938]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; postsynaptic actin cytoskeleton [GO:0098871]; synaptic vesicle [GO:0008021] | SH3 domain binding [GO:0017124] | PF12796;PF09727; | 1.25.40.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}. Cell projection, dendritic spine {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}. Note=Remains associated with dendritic spines even after glutamate stimulation. {ECO:0000269|PubMed:22262902, ECO:0000269|... | null | null | null | null | null | FUNCTION: Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance (PubMed:22262902). Associates with the striatin-interacting phosphatase and kinase (STRIPAK) core complex to regulate dendritic spine distribution of th... | Mus musculus (Mouse) |
B9EJV3 | GRB1L_MOUSE | MGNSYAGQLKSARFEEALHNSIEASLRCSTAVPRPIFSQLYLDPDQHPFSTADVKPKVEDLDKDLVHPYTQNGSVDFSHNVAMNEMEDDEDEEEMSDSNSPPIPYSQKPAPEGSCTTDGFCQAGKDLRLVSLCMEQIDIPAGFLLVGAKSPNLPEHILVCAVDKRFLPDDHGKNALLGFSGNCIGCGERGFRYFTEFSNHINLKLTTQPKKQKHLKYYLVRTSQGVLSKGPLICWKECRSRQSSALCHSTKPISSVSSAVAPENGTANGYKAGFTVTEAANGTSGHGGKSSSCSSTPSRPGNYSLSPRPTFTSVDQANMF... | null | null | branching involved in ureteric bud morphogenesis [GO:0001658]; cardiac ventricle development [GO:0003231]; epithelial tube morphogenesis [GO:0060562]; kidney development [GO:0001822]; male genitalia development [GO:0030539]; mesonephric duct development [GO:0072177]; metanephros development [GO:0001656]; paramesonephri... | membrane [GO:0016020] | null | PF20692;PF20688;PF20267;PF15782;PF20691; | null | GREB1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Plays a major role in early metanephros and genital development. {ECO:0000269|PubMed:29100091}. | Mus musculus (Mouse) |
B9EKI3 | TMF1_MOUSE | MSWFNASQLSSFAKQALSQAQKSIDRVLDIQEEEPSAWAEAIPYGEPGISPPVSGGWDTSTWGLNSTSSEPQSPPTASQAITKPVRRTVVDESENFFSAFLSPSDAHTIQKSPVVSKPPSKSQRPEEEVKSSLQESSSPGQSRVSETAEVRDSVCVSGETSAVGTPSPVPEDKHEETAGEESEVKVPTVRLKASENVVNVNTTEDVSTTSTQSLTAETKDMALEPKEQKHEDRQSNTPSPPVSSFSSGTSTTSDIEVLDHESVISESSASSRQETSDAKSSLHLMQTSFQLLSASACPEYSRLDDFQKLNESCCSSDAFE... | null | null | acrosome assembly [GO:0001675]; androgen receptor signaling pathway [GO:0030521]; apoptotic process [GO:0006915]; cellular response to organic cyclic compound [GO:0071407]; defense response to bacterium [GO:0042742]; epithelial cell apoptotic process [GO:1904019]; flagellated sperm motility [GO:0030317]; Leydig cell di... | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | DNA binding [GO:0003677]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374] | PF12329;PF12325; | null | null | PTM: Phosphorylated by FER. {ECO:0000269|PubMed:9742951}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Concentrated at the budding structures localized at the tips of cisternae. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Potential coactivator of the androgen receptor. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER (By similarity). Mediates STAT3 degradation. {ECO:0000250, ECO:0000269|PubMed:15467733}. | Mus musculus (Mouse) |
B9EKR1 | PTPRZ_MOUSE | MRILQSFLACVQLLCLCRLDWAYGYYRQQRKLVEEIGWSYTGALNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLSGGLSEKVFKASKITFHWGKCNVSSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMDYLQNNFREQQYKFSRQVFSSYTGKEEIHEVVCSSEPENVQA... | 3.1.3.48 | null | axonal fasciculation [GO:0007413]; axonogenesis [GO:0007409]; hematopoietic progenitor cell differentiation [GO:0002244]; learning or memory [GO:0007611]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of dendrite devel... | axon [GO:0030424]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; perineuronal net [GO:0072534]; ... | fibroblast growth factor binding [GO:0017134]; integrin binding [GO:0005178]; phosphatase activity [GO:0016791]; protein tyrosine phosphatase activity [GO:0004725] | PF00194;PF00041;PF00102; | 3.10.200.10;2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 5 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21969550}; Single-pass type I membrane protein {ECO:0000269|PubMed:21969550}. Secreted {ECO:0000269|PubMed:21969550}. Note=A secreted form is apparently generated by shedding of the extracellular domain. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMe... | null | null | null | null | FUNCTION: Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a... | Mus musculus (Mouse) |
B9EXM2 | CARB_ORYSJ | MATSLSSAPTQLRPSPSPSHHRLLHRSSLLPFPRRHHHRRRRCGALSIARASASAKDGVTVRRFPAAPTEGGRLAGVRKIMILGAGPIVIGQACEFDYSGTQACKALAEEGYEVVLVNSNPATIMTDPDLAHRTYIGPMTPPLVERIIAAERPDALLPTMGGQTALNLAVSLADSGALDRLGVRLIGASLPAIRAAEDRQLFKQAMDRIGLKTPPSGIGTTLEECISIAEDIGEFPLIVRPAFTLGGTGGGIAYNRAEFEDICRAGLAASHTQQVLVEKSLLGWKEYELEVMRDMADNVVIICSIENIDPMGVHTGDSIT... | 6.3.4.16; 6.3.5.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; | arginine biosynthetic process [GO:0006526]; glutamine metabolic process [GO:0006541]; pyrimidine nucleotide biosynthetic process [GO:0006221] | chloroplast [GO:0009507]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; metal ion binding [GO:0046872] | PF02786;PF02787;PF02142; | 3.40.50.20;3.30.1490.20;3.30.470.20;1.10.1030.10;3.40.50.1380; | CarB family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI... | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000250|UniProtKB:P03965}. | null | null | FUNCTION: Large subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, hydrogencarbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea... | Oryza sativa subsp. japonica (Rice) |
B9F1C0 | SHOC1_ORYSJ | MRTRFLATDYFAPSSSSAAGKALALEFFSFPSLPVPALPPDPHFLPFTSADELPAATVADDGLGPLPIASALSDFLAAVIPQALPVPTVPAADEVLDDFLYDRGGYGEDFSSWEFGAFRIPKASEGYGVINREKDEKGEGSRSDGLEISSVMKRWEQLKELRFEVVEVDLLMALQEDIASFGEEESGGGVTLLLRVPDMKIHLDFIDIETDIKIRYQSDLPESVYQVEKVPVKDNDGNGHSSLREDCCLEIAALDHGAVIPRLEVSRNSWELDDCLTETDRYGVFDNVVRHLDEAQIQHSVFKSTEFLRSTDMDMLTFVC... | null | null | reciprocal meiotic recombination [GO:0007131]; resolution of meiotic recombination intermediates [GO:0000712] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | null | null | null | XPF family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:31266799}. Nucleus {ECO:0000269|PubMed:30589140, ECO:0000269|PubMed:31266799}. Cytoplasm {ECO:0000269|PubMed:30589140}. Cell membrane {ECO:0000269|PubMed:30589140}. Note=Predominantly localized in the nucleus (PubMed:30589140). Localized in punctuate foci onto meiocy... | null | null | null | null | null | FUNCTION: Essential for normal crossover (CO) formation during meiosis (PubMed:30589140, PubMed:31266799). Essential component for the formation of class I meiotic COs (PubMed:31266799). Interacts with PTD, another meiotic component, to regulate CO formation, possibly by stabilizing the recombination intermediates duri... | Oryza sativa subsp. japonica (Rice) |
B9FDE0 | BSK3_ORYSJ | MGGRVSKAVACCCCRSQHHGVVVESSEKTAEEDHGESYELPAFQEFSFEQLRLATSGFAVENIVSEHGEKAPNVVYKGKLDAQRRIAVKRFNRSAWPDPRQFLEEAKSVGQLRSKRLANLLGCCCEGDERLLVAEYMPNDTLAKHLFHWEAQAMKWPMRLRVVLYLAEALEYCTSKGRALYHDLNAYRVLFDDDCNPRLSCFGLMKNSRDGKSYSTNLAFTPPEYMRTGRITPESVIYSFGTLLLDVLSGKHIPPSHALDLIRDRNFNMLTDSCLEGQFSNEEGTELVRLASRCLHYEPRERPNVRSLVQALAPLQKDLE... | 2.7.11.1 | null | brassinosteroid mediated signaling pathway [GO:0009742]; phosphorylation [GO:0016310]; positive regulation of brassinosteroid mediated signaling pathway [GO:1900459] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF07714; | 1.25.40.10;1.10.510.10; | null | PTM: Phosphorylated at Ser-213 and Ser-215 by BRI1. Phosphorylation at Ser-215 is required for its function in the regulation of brassinosteroid signaling. Phosphorylation by BRI1 disrupts the interaction between its TPR and kinase domains, thereby increasing the binding between its kinase domain and BSL1. {ECO:0000269... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26697897}; Lipid-anchor {ECO:0000305|PubMed:26697897}. Note=Plasma membrane localization is required for its function in the regulation of brassinosteroid signaling. {ECO:0000269|PubMed:26697897}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Probable serine/threonine kinase that acts as a positive regulator of brassinosteroid (BR) signaling downstream of BRI1. {ECO:0000269|PubMed:26697897}. | Oryza sativa subsp. japonica (Rice) |
B9FMJ3 | KN13A_ORYSJ | MGDSGDAVMARWLQSAGLQHLAASSTSSSSASTAGGGVDPRGGGGVGVGALGGGAGGGSLLPSLLMQGYGPQSIEEKQRLYMLLRSLNFNGETAPPSISEPYTPTAQSFGGGNSLEGFYSPELRGELGAGLLDLHAMDDTELLSEDVASEPFEPSPFIPKEMDEDDDDMLPGSQPGPSDNYNAVANEKESTARENNVAKIKVVVRKRPLNRKEVSRKEEDIITVHDSSSLTVYEPKLKVDLTAYVEKHEFCFDAVLDEQVSNDEVYRETVEPIIPIIFQRTKATCFAYGQTGSGKTYTMQPLPLRAAQDMVRLLHQPVYR... | null | null | metaxylem development [GO:0090058]; microtubule depolymerization [GO:0007019]; microtubule-based movement [GO:0007018]; plant-type secondary cell wall biogenesis [GO:0009834]; regulation of cell wall organization or biogenesis [GO:1903338]; trichome morphogenesis [GO:0010090] | endoplasmic reticulum [GO:0005783]; Golgi stack [GO:0005795]; intracellular membrane-bounded organelle [GO:0043231]; microtubule [GO:0005874]; secondary cell wall [GO:0009531] | ATP binding [GO:0005524]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, KIN-13 subfamily | null | SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:20587735}. | null | null | null | null | null | null | Oryza sativa subsp. japonica (Rice) |
B9J3S4 | COLQ1_BACCQ | MNKKSKINKVMLSISTMALSLGALQAPASAEEKVPYNVLKTKPVGIEKPVDEIGHVSKAEETLSFQERLKVGDFSQRPASIPNKAAVKQVKESYSMADLNKMNDQELVETLGCIKWHQITDLFQFNEDAKAFYKDKGKMQVIIDELAHRGSTFTRDDSKGIQTFTEVLRSAFYLAFYNNELSELNERSFQDKCLPALKAIAKNPNFKLGTAEQDTVVSAYGKLISNASSDVETVQYASNILKQYNDNFNTYVNDRMKGQAIYDIMQGIDYDIQSYLIEARKEANETMWYGKVDGFINEINRIALLNEVTPENKWLVNNGI... | 3.4.24.3 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9X721}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9X721}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF18496;PF01752;PF08453;PF18911;PF04151; | 1.10.390.20;2.60.120.380;3.30.980.50;3.40.30.160;2.60.40.10; | Peptidase M9B family, Collagenase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33603127}. | CATALYTIC ACTIVITY: Reaction=Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.; EC=3.4.24.3; Evidence={ECO:0000269|PubMed:33603127}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.36 uM for gelatin {ECO:0000269|PubMed:33603127}; KM=1.72 uM for native collagen from rat tail {ECO:0000269|PubMed:33603127}; Note=kcat is 7.7 sec(-1) with gelatin as substrate (PubMed:33603127). kcat is 2.1 sec(-1) with native collagen from rat tail as substrate ... | null | null | null | FUNCTION: Acts as a true collagenase, which is highly active and cleaves natively folded collagen (PubMed:33603127). In vitro, can also cleave gelatin and the synthetic peptide FALGPA (furylacryloyl-Leu-Gly-Pro-Ala) (PubMed:33603127). Causes damage on dermal collagen (COL), resulting in gaps in the tissue, which might ... | Bacillus cereus (strain Q1) |
B9J8S0 | PDA_RHIR8 | MSYSFMSPPNAARFVLSNATVPAVTVVGFTGPSSEGLMKADIVVADGLIKDILPAGTAPAELAKADMRDGMVWPTFADMHTHLDKGHIWERRANPDGSFMGALDAVRSDREANWSAADVRKRMEFSLRAAYAHGTSLIRTHLDSLAPQHRISFEVFSEVREAWKDKIALQAVALFPLDFMVDDAFFADLTTVVREAGGLLGGVTQMNPDIDAQLDKLIRAAAANGLDIDLHVDETEDREVLTLKAIAAAVLRNGFTGKVTAGHCCSLARQDENVAAATIDLVAKAGISIVALPMCNMYLQDRHPGRTPRWRGVTLLHELA... | 3.5.4.11 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:P25524}; | cytosine catabolic process [GO:0006209] | null | cytosine deaminase activity [GO:0004131]; isoguanine deaminase activity [GO:0035888]; metal ion binding [GO:0046872]; pterin deaminase activity [GO:0050228]; sepiapterin deaminase activity [GO:0050279] | PF07969; | 3.20.20.140;2.30.40.10; | Metallo-dependent hydrolases superfamily, Pterin deaminase family | null | null | CATALYTIC ACTIVITY: Reaction=a 2-amino-4-hydroxypteridine + H(+) + H2O = a 2,4-dihydroxypteridine + NH4(+); Xref=Rhea:RHEA:36055, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:73184, ChEBI:CHEBI:73186; EC=3.5.4.11; Evidence={ECO:0000269|PubMed:23256477}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for formylpterin {ECO:0000269|PubMed:23256477}; KM=27 uM for pterin-6-carboxylate {ECO:0000269|PubMed:23256477}; KM=13 uM for pterin-7-carboxylate {ECO:0000269|PubMed:23256477}; KM=39 uM for pterin {ECO:0000269|PubMed:23256477}; KM=23 uM for hydroxymethylpter... | null | null | null | FUNCTION: Catalyzes the deamination of many pterin metabolites, such as formylpterin, pterin-6-carboxylate, pterin-7-carboxylate, pterin, hydroxymethylpterin, biopterin, D-(+)-neopterin, isoxanthopterin, sepiapterin, folate, xanthopterin, and 7,8-dihydrohydroxymethylpterin. May be involved in a degradative pathway for ... | Rhizobium rhizogenes (strain K84 / ATCC BAA-868) (Agrobacterium radiobacter) |
B9K712 | IYD_THENN | MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF | 1.21.1.1 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:34748729}; | thyroid hormone metabolic process [GO:0042403]; tyrosine metabolic process [GO:0006570] | null | FMN binding [GO:0010181]; iodotyrosine deiodinase activity [GO:0140616]; tyrosine binding [GO:0072545] | PF00881; | 3.40.109.10; | Nitroreductase family | null | null | CATALYTIC ACTIVITY: Reaction=2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH; Xref=Rhea:RHEA:32479, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.21.1.1; Evidence={ECO:0000269|PubMed:34748729}; PhysiologicalDirection=rig... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 uM for 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:34748729}; KM=3.5 uM for 3-iodo-L-tyrosine (at pH 7.4 and 60 degrees Celsius) {ECO:0000269|PubMed:34748729}; KM=4200 uM for 2-iodophenol (at pH 7.4 and 25 degrees Celsius) {ECO:000... | null | null | null | FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (PubMed:34748729). Activity towards 2-iodophenol is weak (PubMed:34748729). {ECO:0000269|PubMed:34748729}. | Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E) |
B9K7M5 | BGLA_THENN | MKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDVACDHYNRWKEDIEIIEKIGAKAYRFSISWPRILPEGTGKVNQKGLDFYNRIIDTLLEKNITPFITIYHWDLPFSLQLKGGWANRDIADWFAEYSRVLFENFGDRVKHWITLNEPWVVAIVGHLYGVHAPGMKDIYVAFHTVHNLLRAHAKSVKVFRETVKDGKIGIVFNNGYFEPASEREEDIRAARFMHQFNNYPLFLNPIYRGEYPDLVLEFAREYLPRNYEDDMEEIKQEIDFVGLNYYSGHMVKYDPNSPARVSFVERNLPKTAM... | 3.2.1.21; 3.2.1.74 | null | cellulose catabolic process [GO:0030245] | cytosol [GO:0005829] | glucan 1,4-beta-glucosidase activity [GO:0031217]; scopolin beta-glucosidase activity [GO:0102483] | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-linkages in (1->4)-beta-D-glucans, to remove successive glucose units.; EC=3.2.1.74; Evidence={ECO:0000269|PubMed:10960102}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28.6 mM for cellobiose {ECO:0000269|PubMed:10960102}; KM=4.55 mM for cellotriose {ECO:0000269|PubMed:10960102}; KM=2.15 mM for cellotetraose {ECO:0000269|PubMed:10960102}; Note=kcat is 285.0, 345.7 and 333.7 sec(-1) for the hydrolysis of cellobiose, cellotriose and... | PATHWAY: Glycan metabolism; cellulose degradation. {ECO:0000303|PubMed:10960102}.; PATHWAY: Glycan metabolism; beta-D-glucan degradation. {ECO:0000303|PubMed:10960102}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:10960102}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 95 degrees Celsius. Is highly thermostable, retaining 85% activity after incubation for 9 hours at 90 degrees Celsius and 88% activity after 1 hour at 95 degrees Celsius. {ECO:0000269|PubMed:10960102}; | FUNCTION: Broad substrate specificity glycosidase. Releases glucose from soluble glucooligomers, with a preference for longer oligomers; acts more readily on cellotetraose than on cellobiose. Displays similar activities towards the disaccharides lactose and cellobiose. Is also able to hydrolyze various aryl-beta-glycos... | Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E) |
B9KDD4 | PGLB_CAMLR | MKLQQNFTDNNSIKYTCILILIAFAFSVLCRLYWVAWASEFYEFFFNDQLMITTNDGYAFAEGARDMIAGFHQPNDLSYFGSSLSTLTYWLYSILPFSFESIILYMSAFFASLIVVPIILIAREYKLTTYGFIAALLGSIANSYYNRTMSGYYDTDMLVLVLPMLILLTFIRLTINKDIFTLLLSPVFIMIYLWWYPSSYSLNFAMIGLFGLYTLVFHRKEKIFYLTIALMIIALSMLAWQYKLALIVLLFAIFAFKEEKINFYMIWALIFISILILHLSGGLDPVLYQLKFYVFKASDVQNLKDAAFMYFNVNETIMEV... | 2.4.99.19 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21677752}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:21677752, ECO:0000269|PubMed:29058712}; | post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279] | plasma membrane [GO:0005886] | dolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]; glycosyltransferase activity [GO:0016757]; magnesium ion binding [GO:0000287] | PF02516;PF21436;PF18527; | 3.40.1380.40; | STT3 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000269|PubMed:21677752}. | CATALYTIC ACTIVITY: Reaction=tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine.; EC=2.4.99.19; Evidence={ECO:0000269|PubMed:21677752, ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for an Asp-Gln-Asn-Ala-Thr pentapeptide {ECO:0000269|PubMed:23382388}; Note=Glycosylates at a rate of 1.55 peptides per second per OST. {ECO:0000269|PubMed:23382388}; | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:23382388}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:24149797}; | null | FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (GalNAc(2)GlcGalNAc(3)Bac(NAc)(2) in eubacteria, where Bac(NAc)(2) is di-N-acetyl bacillosamine) from the lipid carrier undecaprenol-pyrophosphate to an asparagine residue within an Asp/Glu-Asn-X-Ser/Thr consensus motif i... | Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060) |
B9NAE4 | NRP31_POPTR | MPSPEEDPQPLLKDQEETAYDSDGKVLSFGIDYDTESGGSTVVPSFSWRKLWLFTGPGFLMCIAFLDPGNLEGDLQAGAIAGYSLLWLLLWATAMGLLVQLLSARLGVATGRHLAELCREEYPTWARMILWIMAELALIGADIQEVIGSAIAIQILSNGVLPLWAGVIITASDCFIFLFLENYGVRKLEAAFGILIGIMAVTFAWMFADAKPSAPELFLGILIPKLSSKTIKQAVGVVGCIIMPHNVFLHSALVQSREIDHNKKGQVQEALRYYSIESTAALAISFMINLFVTTIFAKGFHGTELANSIGLVNAGQYLQD... | null | null | defense response to bacterium [GO:0042742]; intracellular iron ion homeostasis [GO:0006879]; intracellular manganese ion homeostasis [GO:0030026]; iron ion transmembrane transport [GO:0034755]; iron ion transport [GO:0006826]; manganese ion transmembrane transport [GO:0071421]; manganese ion transport [GO:0006828]; pos... | trans-Golgi network membrane [GO:0032588]; vacuolar membrane [GO:0005774] | cadmium ion transmembrane transporter activity [GO:0015086]; manganese ion transmembrane transporter activity [GO:0005384]; metal ion transmembrane transporter activity [GO:0046873] | PF01566; | null | NRAMP (TC 2.A.55) family | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:35700212}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to intracellular punctuate structures. {ECO:0000269|PubMed:35700212}. | CATALYTIC ACTIVITY: Reaction=Mn(2+)(in) = Mn(2+)(out); Xref=Rhea:RHEA:28699, ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:35700212}; CATALYTIC ACTIVITY: Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486, ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:35700212}; | null | null | null | null | FUNCTION: Divalent metal transporter (PubMed:35700212). Can transport manganese (Mn) and iron (Fe) (PubMed:35700212). Involved in the control of cell-to-cell transport of manganese (Mn) between organs and tissues to monitor Mn homeostasis (PubMed:35700212). {ECO:0000269|PubMed:35700212}. | Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) |
B9TSP7 | FACR6_ARATH | MATTNVLATSHAFKLNGVSYFSSFPRKPNHYMPRRRLSHTTRRVQTSCFYGETSFEAVTSLVTPKTETSRNSDGIGIVRFLEGKSYLVTGATGFLAKVLIEKLLRESLEIGKIFLLMRSKDQESANKRLYDEIISSDLFKLLKQMHGSSYEAFMKRKLIPVIGDIEEDNLGIKSEIANMISEEIDVIISCGGRTTFDDRYDSALSVNALGPGRLLSFGKGCRKLKLFLHFSTAYVTGKREGTVLETPLCIGENITSDLNIKSELKLASEAVRKFRGREEIKKLKELGFERAQHYGWENSYTFTKAIGEAVIHSKRGNLPV... | 1.2.1.84 | null | long-chain fatty-acyl-CoA metabolic process [GO:0035336]; response to wounding [GO:0009611]; suberin biosynthetic process [GO:0010345] | chloroplast [GO:0009507] | alcohol-forming long-chain fatty acyl-CoA reductase activity [GO:0102965]; alcohol-forming very long-chain fatty acyl-CoA reductase activity [GO:0080019] | PF07993;PF03015; | 3.40.50.720; | Fatty acyl-CoA reductase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:22166367}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2 NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.84; Evidence={ECO:0000269|PubMed:22166367}; PhysiologicalDirection=left-to... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.48 uM for C16:0-ACP (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:22166367}; KM=3.36 uM for C16:0-CoA (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:22166367}; Vmax=293 pmol/min/mg enzyme with C16:0-ACP as substrate (at pH 7 and 30 degrees Celsius) {... | null | null | null | FUNCTION: Catalyzes the reduction of fatty acyl-CoA and -ACP (acyl carrier protein) substrates to fatty alcohols (PubMed:19062129, PubMed:22166367). Triggers the accumulation of C16 and, to a lower extent, of C18 fatty alcohols; converts palmitoyl-acyl carrier protein to the corresponding C16:0 alcohol with NAD(P)H as ... | Arabidopsis thaliana (Mouse-ear cress) |
B9U3F2 | DISP3_CHICK | MDTEDDPLLQDAWLDEEDEEVAFSSRKRREGALLCGKSSCRVRPLRVTLPVSGFWNIVGWIFTNPYCAGFILFLGCAIPAVLAVVMFLHYPALDIDISYNAFEIRNHESSQRFDALALALKSQFGSWGRNRRDLADFTSETLQRLIFEQLQQLHLNASHLQVSTRAKRSAPQGRTSSPEPRAHPHPGNETSRVTRGAPRWDYSNTYISANTQTHAHWRIELIFLARGDSENNIFTTERLVTIHEVERKIMDHPRFREFCWKPHEVLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIQGSLELAMTHPE... | null | null | cell differentiation [GO:0030154]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; negative regulation of neuron differentiation [GO:0045665]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of neural precursor cell proliferation [GO:2000179]; response ... | cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear membrane [GO:0031965] | null | PF02460; | 1.20.1640.10; | Patched family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}.... | null | null | null | null | null | FUNCTION: Plays a role in neuronal proliferation and differentiation (By similarity). Plays a role in the accumulation of cellular cholesterol (PubMed:19179482). Involved in intracellular lipid droplet formation (PubMed:19179482). May contribute to cholesterol homeostasis in neuronal cells (PubMed:19179482). {ECO:00002... | Gallus gallus (Chicken) |
B9V5F5 | CE63A_XENLA | MEALLQGLQRQDRMGALQDSCEAELQELMKQIDIMLDHKRSQWEAETETMKTRLELKEQELNCALDREERLNQEVRRLRQQLIQQEEETQNKTTQYEAQLSGFKEELNRLKKSYEKVQKKHLRSEMKAKAEEERSEVSRLTRRLEEFRQRSLDWEKQRLLYQQQLAGLEAQRKTLIEQTEMYQHQSHNRKQMLEQTSLVGRSELQNLSGQLHRANDSLCAKEEELETLKIQLRCAVEGQKRAEHETELSKQAVQALKEEKAELRATLQAHTEFLQGSRVQKHELLPEGYRGSEVLRENNSIRSVEERLQEMGQVGGETEV... | null | null | cell division [GO:0051301]; centriole replication [GO:0007099]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; DNA damage checkpoint signaling [GO:0000077]; signal transduction in response to DNA damage [GO:0042770]; spindle assembly [GO:0051225] | centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; spindle pole [GO:0000922] | null | PF17045; | null | CEP63 family | PTM: Phosphorylation at Ser-560 by atm and atr promotes its delocalization from the centrosome and impairs its ability to promote centrosome dependent spindle assembly. {ECO:0000269|PubMed:19182792}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q96MT8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0CB05}. | null | null | null | null | null | FUNCTION: Required for normal spindle assembly (PubMed:19182792). Plays a key role in mother-centriole-dependent centriole duplication (PubMed:19182792). Plays a role in DNA damage response (PubMed:19182792). Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inact... | Xenopus laevis (African clawed frog) |
B9VRJ2 | COR15_PAPSO | MESNGVPMITLSSGIRMPALGMGTVETMEKGTEREKLAFLKAIEVGYRHFDTAAAYQTEECLGEAIAEALQLGLIKSRDELFITSKLWCADAHADLVLPALQNSLRNLKLDYLDLYLIHHPVSLKPGKFVNEIPKDHILPMDYKSVWAAMEECQTLGFTRAIGVCNFSCKKLQELMATANSPPVVNQVEMSPTLHQKNLREYCKANNIMITAHSVLGAVGAAWGTKAVMHSKVLHQIAVARGKSVAQVSMRWVYQQGASLVVKSFNEARMKENLKIFDWELTAEDMEKISEIPQSRTSSAAFLLSPTGPFKTEEEFWDEK... | 1.1.1.247 | null | alkaloid metabolic process [GO:0009820] | cytosol [GO:0005829] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; codeinone reductase (NADPH) activity [GO:0047036] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11079569}. Note=Present in the cytosolic part of laticifer cells that secrete latex. {ECO:0000269|PubMed:11079569}. | CATALYTIC ACTIVITY: Reaction=codeine + NADP(+) = codeinone + H(+) + NADPH; Xref=Rhea:RHEA:19209, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57871, ChEBI:CHEBI:58349, ChEBI:CHEBI:58473; EC=1.1.1.247; Evidence={ECO:0000269|PubMed:22098111, ECO:0000269|PubMed:29779229}; PhysiologicalDirection=left-to-right; Xref=Rh... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.7 uM for codeinone {ECO:0000269|PubMed:29779229}; KM=32.1 uM for codeine {ECO:0000269|PubMed:29779229}; KM=36 uM for NADPH {ECO:0000269|PubMed:29779229}; KM=46.2 uM for NADP(+) {ECO:0000269|PubMed:29779229}; Vmax=38.2 nmol/min/mg enzyme with codeinone as substra... | PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000269|PubMed:29779229}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8 for reduction (forward reaction) of codeinone to codeine and 9.0-10.0 for the oxidation (reverse reaction) of codeine to codeinone. {ECO:0000269|PubMed:29779229}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-42 degrees Celsius. {ECO:0000269|PubMed:29779229}; | FUNCTION: NADPH-dependent codeinone reductase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products (PubMed:15543134, PubMed:29779229). Reduces codeinone to codeine in the penultimate step in morphine biosynthesis (PubMed:15543134, PubMed:22098111, PubMed:29779229). Can use... | Papaver somniferum (Opium poppy) |
B9VUU3 | POLG_HE71 | MGSQVSTQRSGSHENSNSATEGSTINYTTINYYKDSYAATAGKQSLKQDPDKFANPVKDIFTEMAAPLKSPSAEACGYSDRVAQLTIGNSTITTQEAANIIVGYGEWPSYCSDSDATAVDKPTRPDVSVNRFYTLDTKLWEKSSKGWYWKFPDVLTETGVFGQNAQFHYLYRSGFCIHVQCNASKFHQGALLVAVLPEYVIGTVAGGTGTEDSHPPYKQTQPGADGFELQHPYVLDAGIPISQLTVCPHQWINLRTNNCATIIVPYINALPFDSALNHCNFGLLVVPISPLDYDQGATPVIPITITLAPMCSEFAGLRQA... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Human enterovirus 71 (EV71) (EV-71) |
B9VVJ6 | CK12_TRYBB | MSVELRVGNRFRIGQKIGSGSFGEIFRGTNIQTGDPVAIKLEQVKTRHPQLAFEARFYRVLNAGGGVVGIPNVLYHGVEGEFNVMVIDLLGPSLEDLFSFCGRRLSLKTTLMLAEQMIARIEFVHSKSIIHRDIKPDNFLMGTGKKGHHVYIIDFGLAKKYRDARTHQHIPYKEGKSLTGTARYCSINTHIGIEQSRRDDLEGIGYILMYFLRGSLPWQGLKAHTKQEKYARISDRKQTTSVETLCRSFPAEFAAYLNYTRSLHFEDKPDYSYLKRLFRELFVREGYHVDYVFDWTLKRIHDTLQEGRADQQQQQQQQQQ... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830}; | endocytosis [GO:0006897]; non-motile cilium assembly [GO:1905515]; phosphorylation [GO:0016310]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; regulation of circadian rhythm [GO:0042752]; regulation of ... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle microtubule [GO:0005876] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:19450734, ECO:000026... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 27 degrees Celsius. Loses activity at 41 degrees Celsius. {ECO:0000269|PubMed:27002830}; | FUNCTION: Serine/threonine protein kinase (PubMed:19450734, PubMed:27002830). May phosphorylate ZC3H11 during unstressed conditions, leading to proteasome-dependent degradation of ZC3H11 (PubMed:27002830). {ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830}. | Trypanosoma brucei brucei |
B9W4V6 | APO1_CYCAE | MKYFPLFPTLVFAARVVAFPAYASLAGLSQQELDAIIPTLEAREPGLPPGPLENSSAKLVNDEAHPWKPLRPGDIRGPCPGLNTLASHGYLPRNGVATPVQIINAVQEGLNFDNQAAVFATYAAHLVDGNLITDLLSIGRKTRLTGPDPPPPASVGGLNEHGTFEGDASMTRGDAFFGNNHDFNETLFEQLVDYSNRFGGGKYNLTVAGELRFKRIQDSIATNPNFSFVDFRFFTAYGETTFPANLFVDGRRDDGQLDMDAARSFFQFSRMPDDFFRAPSPRSGTGVEVVIQAHPMQPGRNVGKINSYTVDPTSSDFSTP... | 1.11.2.1 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:15294788}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000269|PubMed:15294788}; | hydrogen peroxide catabolic process [GO:0042744] | null | heme binding [GO:0020037]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF01328; | 1.10.489.10; | Chloroperoxidase family | PTM: N-glycosylated. {ECO:0000269|PubMed:19434406}. | null | CATALYTIC ACTIVITY: Reaction=RH + H2O2 = ROH + H2O.; EC=1.11.2.1; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37 uM for ABTS (at pH 4.5) {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; KM=1001 uM for benzyl alcohol (at pH 7) {ECO:0000269|PubMed:15294788, ECO:0000269|PubMed:17410351, ECO:0000269|PubMed:19022254}; KM=298 uM for dimeth... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.7 with ABTS as substrate. Optimum pH is 7.2 with benzyl alcohol as substrate, and there is another optimum at pH 6.2. Optimum pH is 7.2 with dimethoxyphenol as substrate. Optimum pH is 6.0 with naphthalene as substrate. Optimum pH is 7.0 with pyridine as su... | null | FUNCTION: Aromatic peroxidase that oxidizes aryl alcohols into the corresponding aldehydes and then into the corresponding benzoic acids. Oxidizes toluene and naphthalene. Catalyzes the regioselective peroxide-dependent hydroxylation of propranolol and diclofenac to 5-hydroxypropranolol and 4'-hydroxydiclofenac. Cataly... | Cyclocybe aegerita (Black poplar mushroom) (Agrocybe aegerita) |
B9W5G6 | ACTPC_ACTFR | SADVAGAVIDGAGLGFDVLKTVLEALGNVKRKIAVGIDNESGKTWTAMNTYFRSGTSDIVLPHKVAHGKALLYNGQKNRGPVATGVVGVIAYSMSDGNTLAVLFSVPYDYNWYSNWWNVRVYKGQKRADQRMYEELYYHRSPFRGDNGWHSRGLGYGLKSRGFMNSSGHAILEIHVTKA | 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]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; toxin activity [GO:0090729] | PF06369; | 2.60.270.20; | Actinoporin family, Sea anemone subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19563820}. Nematocyst {ECO:0000250|UniProtKB:P07845}. Target cell membrane {ECO:0000269|PubMed:19563820, ECO:0000269|PubMed:21300287, ECO:0000269|PubMed:25716479}. Note=Forms an alpha-helical membrane channel in the prey. {ECO:0000269|PubMed:19563820, ECO:0000269|PubMe... | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable up to about 53 degrees Celsius. {ECO:0000269|PubMed:31295915}; | FUNCTION: Pore-forming toxin (PFT) that consists of a crown-shaped octamer or nonamer that forms cation-selective hydrophilic pores of about 1.5 nm (inside) and 13 nm (outside) (PubMed:21300287, PubMed:25716479). It causes cardiac stimulation and cytolysis (EC(50)=1.6 nM on erythrocytes) (PubMed:19563820, PubMed:257593... | Actinia fragacea (Strawberry anemone) |
B9WFG1 | ARO1_CANDC | MSIERVPILGKETIHVGYGIADHIVNEVIANLASSTYVIVTDTNMARTPQYSKLTDDFKTNLSKKRPESRLLTYCVSPGENNKNRVTKAAVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSVGGKTAIDTPLGKNFIGAFHQPEYVFCDVSFLETLPARQFINGMAEVVKTAAIWNEEEFTRLENFSKKFLSVVTSKKPDLQSIKAELVKTVLESVRVKAGVVSSDEKEAGLRNLLNFGHTIGHAIEAVLTPEALHGECVSIGMIKEAELSRYLGILPPVAVARLSKCLVAYGLPV... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast) |
B9X187 | NMP1A_XENLA | MAGDVEGGGCRVSWGALLTLLLLPLPSLCTLASGKEPHVIKLYEGKVVRYNESKNFCYQRTYEPKWSDVWTKIQIRVNSTKMIRVTQVENEEKLKEMETFNMFDLFSSFLKEKLNDTFIYVDLYSNKTCIKVHVIDTDTYYSVALSRGFDPRLCFLFLCGLLLFFYGDALSRSQLFFYSTGITIGMLASMLILVFMLSKLMPKKSPFVALLLGGWSVSIYIIQLVFKNLQAICSEYWQYLLGYLGIVGFVSFAFCYKYGPLENDRSINILTWTLQLIGLLLMYISVQIQHIAVTMVVIAFCTKQIEYPVQWIYILYRKIK... | null | null | erythrocyte enucleation [GO:0043131]; erythrocyte maturation [GO:0043249]; eye development [GO:0001654] | nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637] | protein self-association [GO:0043621] | PF10225; | null | NEMP family | PTM: Phosphorylated. {ECO:0000269|PubMed:25946333}. | SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}; Multi-pass membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Note=Localization in the nuclear membrane is essential for its function. Colocalizes wit... | null | null | null | null | null | FUNCTION: In concert with ran, required for proper eye development (PubMed:25946333). May be involved in the expression of early eye marker genes (PubMed:19167377). Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity). Essential for normal erythropoiesis (By si... | Xenopus laevis (African clawed frog) |
B9XZG7 | RNJ_HELP8 | MTDNNHYENNESNENSSENSKVDEARAGAFERFTNRKKRFRENAQKNGESSHHEAPSHHKKEHRPNKKPNNHHKQKHAKTRNYAKEELDSNKVEGVTEILHVNERGTLGFHKELKKGVETNNKIQVEHLNPHYKMNLNSKASVKITPLGGLGEIGGNMMVIETPKSAIVIDAGMSFPKEGLFGVDILIPDFSYLHQIKDKIAGIIITHAHEDHIGATPYLFKELQFPLYGTPLSLGLIGSKFDEHGLKKYRSYFKIVEKRCPISVGEFIIEWIHITHSIIDSSALAIQTKAGTIIHTGDFKIDHTPVDNLPTDLYRLAHY... | 3.1.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01491}; Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important. {ECO:0000255|HAMAP-Rule:MF_01491}; | mRNA processing [GO:0006397]; rRNA processing [GO:0006364] | cytoplasm [GO:0005737] | 5'-3' RNA exonuclease activity [GO:0004534]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; zinc ion binding [GO:0008270] | PF00753;PF07521;PF17770; | 3.10.20.580;3.40.50.10710;3.60.15.10; | Metallo-beta-lactamase superfamily, RNA-metabolizing metallo-beta-lactamase-like family, Bacterial RNase J subfamily | PTM: Acetylated on nine lysine residues. Some of the residues are acetylated by multiple different mechanisms. RimL is partially responsible for the acetylation of Lys-323, Lys-397 and Lys-649. HPB8_1270 homolog is partially responsible for the acetylation of Lys-323, Lys-397, Lys-511 and Lys-649. Acetyl-phosphate-medi... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491, ECO:0000269|PubMed:23093592}. Note=The RNaseJ-RhpA complex co-localizes with 70S ribosomes and polysomes; remains associated with ribosomes in the absence of RhpA. {ECO:0000269|PubMed:23093592}. | null | null | null | null | null | FUNCTION: An RNase that has 5'-3' exoribonuclease and endoribonuclease activity (PubMed:23093592, PubMed:38057323). Degrades 5'-monophosphorylated ssRNA and dsRNA, considerably more active on ssRNA (PubMed:23093592). Association with RhpA significantly increases the dsRNase activity (PubMed:23093592). Degrades RNA subs... | Helicobacter pylori (strain B128) |
C0H5F4 | RH2B_PLAF7 | MKTTLFCSISFCNIIFFFLELSHEHFVGQSSNTHGASSVTDFNFSEEKNLKSFEGKNNNNDNYASINRLYRKKPYMKRSLINLENDLFRLEPISYIQRYYKKNINRSDIFHNKKERGSKVYSNVSSFHSFIQEGKEEVEVFSIWGSNSVLDHIDVLRDNGTVVFSVQPYYLDIYTCKEAILFTTSFYKDLDKSSITKINEDIEKFNEEIIKNEEQCLVGGKTDFDNLLIVLENAEKANVRKTLFDNTFNDYKNKKSSFYNCLKNKKNDYDKKIKNIKNEITKLLKNIESTGNMCKTESYVMNNNLYLLRVNEVKSTPIDL... | null | null | adhesion of symbiont to host cell [GO:0044650]; cell-cell adhesion [GO:0098609]; symbiont entry into host [GO:0044409] | apical plasma membrane [GO:0016324]; cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; host-symbiont bicellular tight junction [GO:0044647]; membrane [GO:0016020]; plasma membrane [GO:0005886]; rhoptry [GO:0020008]; rhoptry neck [GO:1990225]; tight junction [GO:0070160] | heparin binding [GO:0008201]; host cell surface receptor binding [GO:0046789] | null | null | null | PTM: Proteolytically processed into multiple fragments following schizont rupture (PubMed:12228308, PubMed:21698217, PubMed:27438226). In the mature schizont stage prior to merozoite release, full length RH2b is processed post-Golgi into C-terminal 297 kDa and N-terminal 85 kDa forms (PubMed:21698217, PubMed:27438226).... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27438226}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:27438226}. Cell junction, tight junction {ECO:0000269|PubMed:27438226}. Secreted {ECO:0000269|PubMed:2743... | null | null | null | null | null | FUNCTION: [Reticulocyte-binding protein homolog 2b]: During the asexual blood stage, binds to a chymotrypsin sensitive, neuraminidase and trypsin resistant receptor on the surface of the host erythrocyte and thus is involved in merozoite invasion (PubMed:12606570, PubMed:27438226). The various processed forms have diff... | Plasmodium falciparum (isolate 3D7) |
C0H9B6 | ZPLD1_SALSA | MEQICLIILLISKALSVGAQFNGYNCDANFHSRFPAERDISVYCGVQTITLKINFCPVLFSGYTDTDLALNGRHGDAHCRGFINNNTFPTVVLFSISLATLETCGNALVVSTAQGPNAYGNLSLVQIGNISGYIDTPDPPTIISYLPGLLYKFSCSYPLEYLVNNTQLASSAAAISVKDSNGTFVSTLSLLLYNDSSYVQQLSIPMAGLTLKTRVFAAVKATNLDRRWNVLMDYCYTTASGNPNDELRYDLFFSCDKDPQTTVFENGKSQMGRFAFEVFRFVKHKNQKMSTVFLHCVTKLCRADDCPMLMPICGSRKKRD... | null | null | null | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasmic vesicle membrane [GO:0030659]; extracellular space [GO:0005615] | null | PF00100; | 2.60.40.4100; | null | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted form found in the extracellular matrix of the cupula. {ECO:0000305|PubMed:25369234}.; PTM: N-glycosylated. {ECO:0000269|PubMed:25369234}. | SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein 1]: Cytoplasmic vesicle membrane {ECO:0000305|PubMed:25369234}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein 1, secreted form]: Secreted, extracellular space, extracellular ma... | null | null | null | null | null | FUNCTION: Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ. {ECO:0000269|PubMed:25369234}. | Salmo salar (Atlantic salmon) |
C0HJB3 | MANA_CANEN | MKYNTGAGTVPEQLNVHLVPHSHDDVGWLKTVDQYYVGSENYIQEACVENVLDSVVMSLQRDPNRKFVFGEMAFFHRWWLEQTPETKELXXKLVKAGQLEFVNGGWCMHDEATTHYIDMIDHTTLGHRFLQEQFNKIPRAGWQIDPFGHSAVQGYLLGAELGFDSVHFARIDYQDREKRKGEKSLEVVWRGSKTFGSSAQIFANAFPGHYGPPNGFNFEVRNNFVPLQDDPRLFDTNVEERVQNFLDAALTQAKLTRTNHLMWTMGDDFQYQYAESWFKQMDKLLHHVNKDGRVNALYSTPSLYTEAKNAANQTWPLKID... | 3.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1156387, ECO:0000269|PubMed:21924285, ECO:0000269|PubMed:4973951}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q29451}; | mannose metabolic process [GO:0006013] | protein storage vacuole [GO:0000326] | alpha-mannosidase activity [GO:0004559]; carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872] | PF09261;PF07748;PF01074; | 2.60.40.1360;3.20.110.10;1.20.1270.50;2.60.40.1180; | Glycosyl hydrolase 38 family | PTM: Produced as a precursor which is then proteolytically cleaved into a 66kD heavy subunit and a 44kD light subunit. Cleavage probably occurs in protein bodies/protein storage vacuoles. {ECO:0000269|PubMed:24221485, ECO:0000269|PubMed:24295789, ECO:0000269|PubMed:9442045, ECO:0000303|PubMed:24221485}. | SUBCELLULAR LOCATION: Protein storage vacuole {ECO:0000269|PubMed:24221485}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.; EC=3.2.1.24; Evidence={ECO:0000269|PubMed:1156387, ECO:0000269|PubMed:12325362, ECO:0000269|PubMed:4973951, ECO:0000269|PubMed:5145}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.5 mM for p-nitrophenyl-alpha-D-mannoside {ECO:0000269|PubMed:12325362}; KM=31 mM for benzyl-alpha-D-mannoside {ECO:0000269|PubMed:12325362}; KM=0.12 M for methyl-alpha-D-mannoside {ECO:0000269|PubMed:12325362}; KM=10.52 uM for 4-methylumbellideryl-alpha-mannoside... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5 (PubMed:12325362, PubMed:21924285, PubMed:5145). Activity is stable between pH 4.0 and pH 7.0 in the presence of Zn(2+) (PubMed:4973951). Activity is stable between pH 6.0 and pH 8.5, decreases below pH 5.5 at 25 degrees Celsius (PubMed:12325362). Activit... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Retains 50% activity after 5 min at 70 degrees Celsius (PubMed:12325362). Retains full activity after 5 min at 70 degrees Celsius but is completely inactive after 5 min at 80 degrees Celsius (PubMed:5145). Retains 100%, 50% and <10% activity after 2 hours at 40, 5... | FUNCTION: Liberates mannose from p-nitrophenyl-alpha-D-mannoside (PubMed:1156387, PubMed:12325362, PubMed:4973951). Liberates mannose from further alpha-D-mannosides including methyl-, benzyl-alpha-D-mannoside, 1-6-linked di-, tri- and tetrasaccharides of alpha-D-mannose and mannosyl-rhamnose (PubMed:12325362). Liberat... | Canavalia ensiformis (Jack bean) (Dolichos ensiformis) |
C0HJD3 | 3NB_OXYFU | QAIGPPFGLCFQCNQKTSSDCFNAKRCPPFHRTCYTLYKPDGGEEWAVKGCAKGCPTAGPDERVKCCHTPRCNN | null | null | null | extracellular region [GO:0005576] | toxin activity [GO:0090729] | PF00087; | 2.10.60.10; | Snake three-finger toxin family, Ancestral subfamily, Boigatoxin sub-subfamily | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:23851011}.; PTM: Contains 5 disulfide bonds. {ECO:0000269|PubMed:23851011}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23851011}. | null | null | null | null | null | FUNCTION: Reptile-specific three-finger toxin that is lethal at low doses for lizards, but not for mice. Probably acts as a neurotoxin. {ECO:0000269|PubMed:23851011}. | Oxybelis fulgidus (Green vine snake) (Coluber fulgidus) |
C0HJD9 | K6TX1_ACTBE | RCKTCSKGRCRPKPNCG | null | null | null | extracellular region [GO:0005576]; nematocyst [GO:0042151] | potassium channel regulator activity [GO:0015459]; toxin activity [GO:0090729] | null | null | Sea anemone type 6 potassium channel toxin family | null | SUBCELLULAR LOCATION: Secreted. Nematocyst {ECO:0000269|PubMed:30275388}. | null | null | null | null | null | FUNCTION: Potassium channel inhibitor that is the most potent on Kv1.1/KCNA1 (IC(50)=671.95 nM), Kv1.2/KCNA2 (IC(50)=167.36 nM), and Kv1.6/KCNA6 (IC(50)=115.68 nM), and less potent on Kv1.3/KCNA3 (20% inhibition at 3 uM) and on shaker IR (15% inhibition at 3 uM). It inhibits potassium currents, not only by blocking the... | Actinia bermudensis (Maroon anemone) |
C0HJE7 | OXLA_CRODU | MNVFFMFSLLFLAALGSCAHDRNPLEECFRETDYEEFLEIARNGLTVTSNPKHVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIRKFGLQLNEFFQENENAWYFIKNIRKRVREVKNNPGILEYPVKPSEEGKSAAQLYVESLRKVVKELKRTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDRETKVTYQTSANEMSSVTADYVIVCTTSRAARRI... | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P0C2D2}; | 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-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated (PubMed:26273287, PubMed:31078582). N-glycan probably consists of the disaccharide N-acetylglucosamine-fucose (HexNAc-Fuc) (PubMed:31078582). {ECO:0000269|PubMed:26273287, ECO:0000269|PubMed:31078582}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26273287}. | 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:26273287, ECO:0000269|PubMed:31078582}; CAT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 mM for L-Phe {ECO:0000269|PubMed:31078582}; KM=0.48 mM for L-Trp {ECO:0000269|PubMed:31078582}; KM=0.58 mM for L-Leu {ECO:0000269|PubMed:31078582}; KM=0.97 mM for L-Met {ECO:0000269|PubMed:31078582}; KM=3.9 mM for L-Ile {ECO:0000269|PubMed:31078582}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Activity is reduced to about 70% and 60% after incubation at pH 5.0 and pH 9.0, respectively, for 1 hour. {ECO:0000269|PubMed:26273287}; | 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:26273287, PubMed:31078582). Is highly active on L-Met, L-Leu, L-Trp, and L-Phe, moderately active on L-Ile, L-His... | Crotalus durissus terrificus (South American rattlesnake) |
C0HJG9 | ANXA2_MESAU | STVHEILCKLSLEGDHSTPPSAYGSVKDALNIETAVKGVDEVTIVNILTNRQDIAFAYQRKELPSALKTPAQYDASELKGLGTDEDSLIEIICSRTNQELQEINRTDLEKDIISDTSGDFRKLMVALAKRAEDGSVIDYELIDQDARDLYDAGVKRWISIMTERSVCHLQKDKVLIRIMVSRSEVDMLSLYYYIQQDTK | null | null | null | basement membrane [GO:0005604]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; cytoskeletal protein binding [GO:0008092]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [G... | PF00191; | 1.10.220.10; | Annexin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:P07355}. | null | null | null | null | null | FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity (By similarity). {ECO:0000250|UniProtKB:P07355}. | Mesocricetus auratus (Golden hamster) |
C0HJL8 | PA2B_BOTNI | NLLQFNRMIKLETKKNAVPFYAFYGCYCGWGGQGQPKDATDRCCFEHDCCYGKLTKCNTKSDLYSYSSKYGFLLCGKGTWCEEQICECDRIAATCLRRSLDTYKLKYMFYLDSYCKGPSEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P24027}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P24027}; | 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:20590130, ECO:0000269|PubMed:25434534}. | 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:0000255|PROSITE-ProRule:PRU10035}; | null | null | null | null | FUNCTION: Heterodimer A-B: Nigroviriditoxin possesses phospholipase A2 (PLA2) activity. It consists of a non-covalent association of a basic PLA2 subunit B with a non-enzymatic subunit A. {ECO:0000269|PubMed:25434534}.; FUNCTION: Subunit B: Snake venom phospholipase A2 (PLA2) that induces myonecrosis in mice. PLA2 cata... | Bothriechis nigroviridis (Black-speckled palm pit viper) |
C0HJM9 | SCX2_TITFA | MKRFLLFISILMMIGTIVVGKEGYAMDHEGCKFSCFIRPSGFCDGYCKTHLKASSGYCAWPACYCYGVPSNIKVWDYATNKCGK | null | null | defense response [GO:0006952]; envenomation resulting in negative regulation of voltage-gated sodium channel activity in another organism [GO:0044493] | extracellular region [GO:0005576] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF00537; | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily | PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:26083731}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26083731}. | null | null | null | null | null | FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active against hNav1.3/SCN3A. {ECO:0000269|PubMed:26083731}. | Tityus fasciolatus (Central Brazilian scorpion) |
C0HJQ2 | KA192_BUTOC | AACYSSDCRVKCRAMGFSSGKCIDSKCKCYK | null | null | negative regulation of voltage-gated potassium channel activity in another organism [GO:0044361] | extracellular region [GO:0005576] | potassium channel inhibitor activity [GO:0019870]; toxin activity [GO:0090729] | PF00451; | 3.30.30.10; | Short scorpion toxin superfamily, Potassium channel inhibitor family, Alpha-KTx 19 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26398235}. | null | null | null | null | null | FUNCTION: Blocks voltage-gated potassium channels rKv1.1/KCNA1, rKv1.2/KCNA2, hKv1.3/KCNA3, rKv1.6/KCNA6 (IC(50)=75.9 nM) and, to a lesser extent, Shaker IR (with the inactivation domain removed). {ECO:0000269|PubMed:26398235}. | Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus) |
C0HJQ3 | H2A_ACIGU | MSGRGKTGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAQRVGAGAPVYLILELAGNAARDNKKTRIIPRHLQL | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; immune system process [GO:0002376]; killing of cells of another organism [GO:0031640] | nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | null | 1.10.20.10; | Histone H2A family | PTM: Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription. {ECO:0000250|UniProtKB:P0C0S8}. | SUBCELLULAR LOCATION: [Histone H2A]: Nucleus {ECO:0000250|UniProtKB:P02264}. Chromosome {ECO:0000250|UniProtKB:P02264}. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Acipenser gueldenstaedtii (Russian sturgeon) (Danube sturgeon) |
C0HJQ9 | MYG_HYSCR | MGLSDGEWQLVLNVWGKVEGDIGGHGQEVLIRLFKGHPETLEKFDKFKHLKAEDEMRASEDLKKHGTTVLTALGGILKKKGQHAAELAPLAQSHATKHKIPVKYLEFISEAIIQVLQSKHPADFGADTQGAMSKALELFRNDIAAKYKELGFQG | 1.11.1.-; 1.7.-.- | null | removal of superoxide radicals [GO:0019430] | extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 6.10.140.2100;6.10.140.2110; | Globin family | null | SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:00002... | null | null | null | null | FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of... | Hystrix cristata (North African crested porcupine) |
C0HJR0 | MYG_RANTA | MGLSDGEWQLVLNAWGKVEADVAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGNTVLTALGGILKKKGHHEAEVKHLAESHANKHKIPVKYLEFISDAIIHVLHAKHPSDFGADAQGAMSKALELFRNDMAAQYKVLGFQG | 1.11.1.-; 1.7.-.- | null | removal of superoxide radicals [GO:0019430] | extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 6.10.140.2100;6.10.140.2110; | Globin family | null | SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:00002... | null | null | null | null | FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of... | Rangifer tarandus (Reindeer) (Cervus tarandus) |
C0HJU3 | PA2A1_BOTPA | NLVQFKTLIMKIAGRSVVYKYFYYGCYCGWGGIGQPRDATDRCCFVHD | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:17451767}; 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:17451767}. | 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:17451767}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.5. Activity decreases rapidly at basic or acidic pH and is virtually absent at pH 12 and pH 3.5, respectively. {ECO:0000269|PubMed:17451767}; | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows myotoxicity and induces paw edema in mice (PubMed:17451767). Exhibits indirect hemolytic activity (PubMed:17451767). Inhibits platelet aggregation induced by ADP and collagen (PubMed:17451767). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups ... | Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis) |
C0HJY1 | CONV_CANCT | ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFVFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN | null | null | vasodilation [GO:0042311] | null | calcium ion binding [GO:0005509]; glucose binding [GO:0005536]; manganese ion binding [GO:0030145]; mannose binding [GO:0005537] | PF00139; | 2.60.120.200; | Leguminous lectin family | PTM: Concanavalin A-like lectins of the Diocleinae subtribe undergo proteolytic processing referred to as circular permutation. The propeptide is split into an N-terminal and a C-terminal part, the gamma and beta chain, respectively. These are then religated in beta-gamma order to form the mature alpha chain. The beta ... | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-9 with activity decreasing quickly at higher or lower pH. {ECO:0000269|PubMed:24519628}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Hemagglutinating activity stable up to incubation at 80 degrees Celsius for 1 hour but diminishes with higher temperatures and is absent at 100 degrees Celsius. {ECO:0000269|PubMed:24519628}; | FUNCTION: D-mannose/D-glucose-binding lectin which binds alpha-methyl-D-mannoside, D-mannose and D-glucose in that order (PubMed:24519628, PubMed:27737777). Also binds to serum fetuin and ovalbumin (PubMed:24519628). Has hemagglutinating activity towards rabbit erythrocytes (PubMed:24519628). Is not toxic towards larva... | Canavalia cathartica (Jackbean) (Canavalia virosa) |
C0HJY4 | PON1A_ANOEM | WCASGCRKKRHGGCSC | null | null | null | extracellular region [GO:0005576] | calcium channel regulator activity [GO:0005246]; toxin activity [GO:0090729] | null | null | Poneritoxin-Ae1 family | PTM: C-terminal amidation is necessary for channel blocking activity. {ECO:0000269|PubMed:27474999}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27474999}. | null | null | null | null | null | FUNCTION: Weakly inhibits human L-type voltage-gated calcium channel Cav1 (CACNA1S, CACNA1C, CACNA1D, CACNA1F) (IC(50)=4.6 uM). In vivo, it induces reversible paralysis in blowfly L.cuprina. {ECO:0000269|PubMed:27474999}. | Anochetus emarginatus (Ant) (Stenomyrmex emarginatus) |
C0HK05 | PA2BC_CROOL | HLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVH | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:26996495}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14421}; | 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:26996495}. | 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:26996495}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.09 mM for 4-nitro-3-octanoyl benzioc acid (NOBA) {ECO:0000269|PubMed:26996495}; Vmax=15.97 nmol/min/mg enzyme with NOBA as substrate {ECO:0000269|PubMed:26996495}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:26996495}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:26996495}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows edema-inducing activity and local and systemic myotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:26996495}. | Crotalus oreganus lutosus (Great basin rattlesnake) (Crotalus viridis lutosus) |
C0HK25 | ADEL_APLDA | DPDKCKTIRVESWSYKYAEKVVEDASYVLNMTVVDRQSAAACTLGESFGYQKATLWVDHGCRADFKVCYLPVMPTECQTLRVESWNYKYAEKVVEGAALFINMTVEDRQSEASCDLDKSFGFYNQNSTVWVNHGCRADFNICYLKGAVTTSTINVSSWNYQYATKVLPAASCIYSMRVVNQQSAAPCTLGTTYGFVANTMWVDDGCRADFKPSYYSP | null | null | positive regulation of erythrocyte aggregation [GO:0034120] | null | galactose binding [GO:0005534]; galactoside binding [GO:0016936]; galacturonate binding [GO:0048032]; lactose binding [GO:0030395]; melibiose binding [GO:1903777] | PF11218; | null | null | PTM: Contains disulfide bonds. {ECO:0000269|PubMed:28150103}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7. {ECO:0000269|PubMed:28150103}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity is stable up to 60 degrees Celsius, then decreases and is lost at 80 degrees Celsius. {ECO:0000269|PubMed:28150103}; | FUNCTION: Binds in decreasing order of affinity: galacturonic acid, D-galactosamine, methyl-alpha-D-galactopyranoside and further galactose-containing carbohydrates. Has hemagglutinating activity against human and rabbit erythrocytes. {ECO:0000269|PubMed:28150103}. | Aplysia dactylomela (Spotted sea hare) |
C0HK27 | LECA_DIOLA | MGISKKSQLVPLLAFITMFLMVVSRVSSSIADANSLHFSFSQFSQNPKDLILQGDATTDSDGNLQLTRVSSDGSPQGSSVGRALFYAPVHIWEKSAVVASFDATFTFLIKSPDRDPADGITFFIANTDTSIPSGSGGRLLGLFPDANIIKNSTNLDFNAAYNADTIVAVELDSYPNTDIGDPSYPHIGIDIKSIRSKSTARWNMQTGKVGTAHISYNSVAKRLSAVVSYSGTSSTTVSYDVDLNNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKTNQLQDLRIASVV | null | null | null | null | mannose binding [GO:0005537]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF00139; | 2.60.120.200; | Leguminous lectin family | PTM: The mature chain consists of residues 163-280 followed by residues 29-147. Concanavalin A-like lectins of the Diocleinae subtribe undergo proteolytic processing referred to as circular permutation. The propeptide is split into an N-terminal and a C-terminal part, the gamma and beta chain, respectively. These are t... | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for hemagglutinating activity is 8. Activity drops with more acidic and basic pH and is lost at pH 5 and pH 8, respectively. {ECO:0000269|PubMed:24008245}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Hemagglutinating activity is stable after incubation at 70 degrees Celsius for 1 hour but lost at higher temperatures. {ECO:0000269|PubMed:24008245}; | FUNCTION: D-mannose-binding lectin that also binds alpha-methyl-D-mannoside with even higher affinity (PubMed:24008245). Has hemagglutinating activity against rabbit erythrocytes (PubMed:24008245). Shows toxicity against the brine shrimp A.nauplii (PubMed:24008245). Induces reversible paw edema and hypernociceptivity i... | Dioclea lasiophylla |
C0HK44 | LL3_LASLA | VNWKKILGKIIKVVK | null | null | defense response to bacterium [GO:0042742] | extracellular region [GO:0005576] | DNA binding [GO:0003677] | null | null | Lasioglossin-like family | PTM: The C-terminal amidation is required for full activity. {ECO:0000269|PubMed:19591185}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19591185}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide which assumes an amphiphilic alpha-helix conformation upon contact with membranes (PubMed:19591185). Insertion into membranes involves Trp-3 (By similarity). Penetrates into cells once membrane has been permeated (PubMed:22100226). Active against Gram-negative bacteria E.coli (MIC=1.4 uM... | Lasioglossum laticeps (Bee) |
C0HK49 | DEF_NICSU | KDCKRESNTFPGICITKPPCRKACIREKFTDGHCSKILRRCLCTKPC | null | null | defense response [GO:0006952]; killing of cells of another organism [GO:0031640] | vacuole [GO:0005773] | phosphatidic acid binding [GO:0070300] | PF00304; | 3.30.30.10; | DEFL family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:Q8GTM0}. | null | null | null | null | null | FUNCTION: Plant defense peptide (Probable). Disrupts membranes containing phosphatidic acid (PA) via a PA-dependent oligomerization process. {ECO:0000269|PubMed:27647905, ECO:0000303|PubMed:27647905}. | Nicotiana suaveolens (Australian tobacco) |
C0HK69 | SCXD_CENLI | KEGYLVDYHTGCKYTCAKLGDNDYCVRECRLRYYQSAHGYCYAFACWCTHLYEQAVVWPLPNKRCKGK | null | null | defense response [GO:0006952] | extracellular region [GO:0005576] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF00537; | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27871874}. | null | null | null | null | null | FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). Inhibits sodium channels Nav1.4/SCN4A, Nav1.5/SCN5A and Nav... | Centruroides limpidus (Mexican scorpion) |
C0HK98 | SC1A_DROME | MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG | 3.5.1.28 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8INK6}; | defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; negative regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria [GO:0002814]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; peptidoglycan ... | extracellular region [GO:0005576] | N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; peptidoglycan binding [GO:0042834]; zinc ion binding [GO:0008270] | PF01510; | 3.40.80.10; | N-acetylmuramoyl-L-alanine amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; Evidence={ECO:0000250|UniProtKB:C0HK99}; | null | null | null | null | FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity. {ECO:0000250|UniProtKB:C0HK99}. | Drosophila melanogaster (Fruit fly) |
C0HK99 | SC1B_DROME | MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG | 3.5.1.28 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:12496260}; | innate immune response [GO:0045087]; negative regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria [GO:0002814]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; peptidoglycan catabolic process [GO:0009253]; Toll receptor ligand prote... | extracellular region [GO:0005576] | N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; peptidoglycan binding [GO:0042834]; zinc ion binding [GO:0008270] | PF01510; | 3.40.80.10; | N-acetylmuramoyl-L-alanine amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; Evidence={ECO:0000269|PubMed:12496260}; | null | null | null | null | FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN) (PubMed:11106397, PubMed:12496260). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments (PubMed:12496260). Has no direct bacteriolytic activity (PubMed:1249626... | Drosophila melanogaster (Fruit fly) |
C0HKB8 | PA2A1_MICDM | NLIDFKNMIKCTTKRSVLDFADYGCYCGSGGSGTPVDDLDRCCKVHDDCYGEAEKVHGCWPKWTLYSYDCSNGQLTCKDNNTKCKDFVCNCDRTAAICFAKAPYDDNNFMINNPRCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P15445}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15445}; | arachidonic acid secretion [GO:0050482]; phosphatidylcholine catabolic process [GO:0034638] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28315380}. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows strong myotoxicity and induces edema in mice. Shows no cytotoxicity in vitro. Has a strong anticoagulant effect in vitro. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:28315380}. | Micrurus dumerilii (Coral snake) |
C0HKB9 | PA2B1_MICMP | NLIHFSSMIKCTIPGSKPVPDYSDYGCYCGKGGSGTPVDALDRCCQVHDKCYGDAESIYGCTPFLTYYSYECSERQDLCRGNGTKCKAFVCNCDRLAALCFAKAPYNKKNYNINLNRCK | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P15445}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15445}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; 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] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21963438, ECO:0000269|PubMed:28315380}. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows weak myotoxicity and induces edema in mice (PubMed:28315380). Shows no cytotoxicity in vitro (PubMed:28315380). Has an anticoagulant effect in vitro (PubMed:21963438, PubMed:28315380). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-p... | Micrurus mipartitus (Red-tailed coral snake) |
C0HKC3 | PA2B9_AGKPL | MRTLWIMAVLLLGVEGNLFQFEKLIKKMTGKSGMLWYSAYGCYCGWGGQGRPKDATDRCCFVHDCCYGKVTGCNPKMDIYTYSVENGNIVCGGTNPCKKQICECDRAAAICFRDNLKTYDSKTYWKYPKKNCKEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P14418}; Note=Binds 1 Ca(2+) ion per subunit. {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] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | PTM: Acylation causes dimerization. {ECO:0000250|UniProtKB:P51972}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28633930}. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that does not show antibacterial activity (PubMed:29928892). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:28633930). {ECO:0000269|PubMed:28633930, ECO:0000269|PubMed:29928892}. | Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias leucostoma) |
C0HKC4 | PA2B1_AGKCN | NLFQFEKLIKKMTGKSGMLWYSAYGCYCGWGGQGRPKDATDRCCFVHDCCYGKVTGCNPKMDIYTYSVDNGNIVCGGTNPCKKQICECDRAAAICFRDNLKTYDSKTYWKYPKKNCKEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P14418}; Note=Binds 1 Ca(2+) ion per subunit. {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] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28633930}. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:28633930}. | Agkistrodon conanti (Florida cottonmouth) (Agkistrodon piscivorus conanti) |
C0HKE1 | H2A1B_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | chromatin organization [GO:0006325]; heterochromatin organization [GO:0070828]; protein localization to CENP-A containing chromatin [GO:0061644] | CENP-A containing nucleosome [GO:0043505]; nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
C0HKE2 | H2A1C_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
C0HKE3 | H2A1D_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
C0HKE4 | H2A1E_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
C0HKE5 | H2A1G_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
C0HKE6 | H2A1I_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
C0HKE7 | H2A1N_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
C0HKE8 | H2A1O_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
C0HKE9 | H2A1P_MOUSE | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
C0HKG7 | TX1A_CHEPU | MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKNGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDDCCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR | null | null | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF10530; | null | Neurotoxin 19 (CSTX) family, Double-CSTX subfamily | PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:20657014, ECO:0000303|PubMed:24717175}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20657014}. Target cell membrane {ECO:0000269|PubMed:20657014}. Note=Probably forms a transmembrane alpha-helix in the target cell membrane. | null | null | null | null | null | FUNCTION: Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane (PubMed:20657014). Lethal to insect larvae (PubMed:20657014, PubMed:24717175). Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g cau... | Cheiracanthium punctorium (Yellow sac spider) (Aranea punctoria) |
C0HKG8 | TX1B_CHEPU | MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKNGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDECCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR | null | null | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF10530; | null | Neurotoxin 19 (CSTX) family, Double-CSTX subfamily | PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:20657014, ECO:0000303|PubMed:24717175}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20657014}. Target cell membrane {ECO:0000269|PubMed:20657014}. Note=Probably forms a transmembrane alpha-helix in the target cell membrane. | null | null | null | null | null | FUNCTION: Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane (PubMed:20657014). Lethal to insect larvae (PubMed:20657014, PubMed:24717175). Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g cau... | Cheiracanthium punctorium (Yellow sac spider) (Aranea punctoria) |
C0HKG9 | TX1C_CHEPU | MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKSGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDDCCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR | null | null | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF10530; | null | Neurotoxin 19 (CSTX) family, Double-CSTX subfamily | PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:20657014, ECO:0000303|PubMed:24717175}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20657014}. Target cell membrane {ECO:0000269|PubMed:20657014}. Note=Probably forms a transmembrane alpha-helix in the target cell membrane. | null | null | null | null | null | FUNCTION: Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane (PubMed:20657014). Lethal to insect larvae (PubMed:20657014, PubMed:24717175). Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g cau... | Cheiracanthium punctorium (Yellow sac spider) (Aranea punctoria) |
C0HKM3 | HYAL_CONPU | MRVVVVVTGLVVVVVATALSLPDHDVKSASSPLSSSSVYQGSSGDDCDEGLPPPDRPFYVVWNHPDTCKRNRIPLHLDHYGFIFNKNRLFLGEEIQTLYNTGLWPNISETGEFFNGGLPQLFTHHDYSETVEILGRYRTENFTGLGILDFEEWRAIYDTNFGIMRKYQDESIKLAKQRYPSYNKKELTMVAEQEWDQAAREIMSTKLAIGQALMPGGHWGYYGYPRTWGSKRNTQLRNNRIDWLWRQSTGLYPSIYIKDPNMTESAIAEFVSGNVEEAVRVQDEFSPPNTPIYPYAMLQSGDHIFFQVDHLKISLGLPAK... | 3.2.1.35 | null | carbohydrate metabolic process [GO:0005975]; hyaluronan catabolic process [GO:0030214] | cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576] | hyalurononglucosaminidase activity [GO:0004415] | PF01630; | 3.20.20.70; | Glycosyl hydrolase 56 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28479398}. | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35; Evidence={ECO:0000269|PubMed:28479398}; | null | null | null | null | FUNCTION: Hyaluronidase catalyzes the hydrolysis of hyaluronic acid (HA), an anionic, nonsulfated glycosaminoglycan distributed widely throughout connective, epithelial, and neural tissues (PubMed:28479398). In venom, they are known to enhance diffusion of the venom by degrading the extracellular matrix (Probable). {EC... | Conus purpurascens (Purple cone) |
C0HKQ7 | CECA1_DROME | MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATARG | null | null | antibacterial humoral response [GO:0019731]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to insect [GO:0002213]; humoral immune response [GO:0006959]; innate immune response [GO:0045087]; response to bacterium [GO:0009617] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | null | PF00272; | null | Cecropin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16510152}. | null | null | null | null | null | FUNCTION: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria (PubMed:11266367, PubMed:2390977). Functions in the imd/NF-kappa-B (Imd) epithelial and humoral immune response to Gram-negative bacteria (PubMed:11266367). {ECO:0000269|PubMed:11266367, ECO:0000269|PubMed... | Drosophila melanogaster (Fruit fly) |
C0HKQ8 | CECA2_DROME | MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATARG | null | null | antibacterial humoral response [GO:0019731]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to insect [GO:0002213]; humoral immune response [GO:0006959]; innate immune response [GO:0045087] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | null | PF00272; | null | Cecropin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. {ECO:0000269|PubMed:2390977}. | Drosophila melanogaster (Fruit fly) |
C0HL12 | AGRB1_RAT | MRGQAAAPGPIWILAPLLLLLLLLGRWARAASGADIGPGTEQCTTLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPAPCSGPGRVRTYQFDSFLESTRTYLGVESFDEVLRLCDPSAPLAFLQASKQFLQMQRQQPPQDGDLGPQGSGDDFSVEYLVVGNRNPSHAACQMLCRWLDACLAGSRSSHPCGIMQTPCACLGGEAGDTASSPLVPRGDVCLRDGVAGGPENCLTSLTQDRGGHGSAGGWKLWSLWGECTRDCGGGLQTRTRTCSPTLGVEGRGCEGVLEEGRLCNRKACGPTGRTSSRS... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic cell clearance [GO:0043277]; cell surface receptor signaling pathway [GO:0007166]; defense response to Gram-negative bacterium [GO:0050829]; engulfment of apoptotic cell [GO:0043652]; innate immune response [GO:0045087]; m... | dendrite [GO:0030425]; dendritic spine [GO:0043197]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:00... | G protein-coupled receptor activity [GO:0004930]; lipopolysaccharide binding [GO:0001530]; PDZ domain binding [GO:0030165]; phosphatidylserine binding [GO:0001786]; transmembrane signaling receptor activity [GO:0004888] | PF00002;PF19188;PF16489;PF01825;PF02793;PF00090; | 1.25.40.610;2.60.220.50;4.10.1240.10;1.20.1070.10;2.20.100.10; | G-protein coupled receptor 2 family, LN-TM7 subfamily | PTM: Proteolytically cleaved to produce vasculostatin-40 and vasculostatin-120. Vasculostatin-40 is the major form and is produced through proteolytic cleavage by MMP14 between residues 317 and 325 with cleavage likely to be between Ser-322 and Leu-323. {ECO:0000250|UniProtKB:O14514}.; PTM: Ubiquitinated. {ECO:0000250|... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14514}; Multi-pass membrane protein {ECO:0000255}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q3UHD1}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q3UHD1}. Cell projection, dendritic spine {ECO:0000269|PubMed:23595754}. Postsynaptic densit... | null | null | null | null | null | FUNCTION: Phosphatidylserine receptor which enhances the engulfment of apoptotic cells (By similarity). Also mediates the binding and engulfment of Gram-negative bacteria (By similarity). Stimulates production of reactive oxygen species by macrophages in response to Gram-negative bacteria, resulting in enhanced microbi... | Rattus norvegicus (Rat) |
C0HL13 | LRP2_PIG | MERWAAAAACTLLLAFAACLAPASGRECLGNEFRCSNGHCITESWRCDGTRDCLDGSDEIGCPPSTCGSTQFHCENEDVCIPLYWVCDGEEDCSNGADEHQRCPPGRTCSSHHFTCTNGECIPVEYRCDHSTDCLDGTDEINCRYPVCQQQTCHNGACYNTSQRCDGEIDCRDASDELNCTQRCLRNEFQCGSGECIPRDYVCDHDPDCSDSSDEHSCSVYQPCKGNEFACSNGFCINQNWVCDGMADCLDNSDEDGCESSIIRTHECYPNEWACPEDGKCIPLSRVCDGIADCPRGGDENKQGRVCDVNMCPSLGCEYQ... | null | null | coronary artery morphogenesis [GO:0060982]; folate import across plasma membrane [GO:1904447]; male gonad development [GO:0008584]; metal ion transport [GO:0030001]; negative regulation of BMP signaling pathway [GO:0030514]; neural tube closure [GO:0001843]; neuron projection arborization [GO:0140058]; outflow tract se... | apical plasma membrane [GO:0016324]; axon [GO:0030424]; brush border membrane [GO:0031526]; clathrin-coated pit [GO:0005905]; dendrite [GO:0030425]; endosome lumen [GO:0031904]; external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235] | calcium ion binding [GO:0005509]; hormone binding [GO:0042562]; protein-folding chaperone binding [GO:0051087]; SH3 domain binding [GO:0017124] | PF12662;PF07645;PF14670;PF00057;PF00058; | 4.10.1220.10;2.10.25.10;4.10.400.10;2.120.10.30; | LDLR family | PTM: A fraction undergoes proteolytic cleavage of the extracellular domain at the cell membrane to generate a cytoplasmic tail fragment. This is internalized into the early endosome from where it trafficks in an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment (ERC). In the ERC, it is further cleaved... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P98158}; Single-pass type I membrane protein {ECO:0000255}. Endosome lumen {ECO:0000250|UniProtKB:P98158}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, dendrite {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, axon {ECO:... | null | null | null | null | null | FUNCTION: Multiligand endocytic receptor (By similarity). Acts together with CUBN to mediate endocytosis of high-density lipoproteins (By similarity). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and c... | Sus scrofa (Pig) |
C0HL58 | NDB4B_ISOMC | FLGSLFSIGSKLLPGVIKLFQRKKQ | null | null | cytolysis in another organism [GO:0051715]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF08024; | null | Non-disulfide-bridged peptide (NDBP) superfamily, Medium-length antimicrobial peptide (group 3) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28941793}. Target cell membrane {ECO:0000305|PubMed:28941793}. | null | null | null | null | null | FUNCTION: May act by disrupting the integrity of the bacterial cell membrane. Has antibacterial activity against Gram-negative bacterium E.coli NBRC 3972 (MIC=10 uM) and against Gram-positive bacteria S.aureus NBRC 13276 (MIC=2.5-5 uM) and B.subtilis NBRC 3009 (MIC=0.5-1 uM). Toxic to cricket A.domestica. Has hemolytic... | Isometrus maculatus (Lesser brown scorpion) (Scorpio maculatus) |
C0HL66 | H33A_DROME | MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | null | null | nucleosome assembly [GO:0006334] | nucleosome [GO:0000786]; nucleus [GO:0005634]; polytene chromosome [GO:0005700] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Phosphorylation at Ser-11 by aurB/ial during mitosis and meiosis is crucial for chromosome condensation and cell-cycle progression. Phosphorylation at Ser-11 by JIL-1 during interphase is linked to gene activation and restricts the formation of heterochromatin at inappropriate sites. Phosphorylation at Ser-11 is e... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesi... | Drosophila melanogaster (Fruit fly) |
C0HL67 | H33B_DROME | MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | null | null | nucleosome assembly [GO:0006334] | nucleosome [GO:0000786]; nucleus [GO:0005634]; polytene chromosome [GO:0005700] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Phosphorylation at Ser-11 by aurB/ial during mitosis and meiosis is crucial for chromosome condensation and cell-cycle progression. Phosphorylation at Ser-11 by JIL-1 during interphase is linked to gene activation and restricts the formation of heterochromatin at inappropriate sites. Phosphorylation at Ser-11 is e... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesi... | Drosophila melanogaster (Fruit fly) |
C0HL84 | PNG1_PANCL | LNWGAILKHIIK | null | null | cytolysis in another organism [GO:0051715]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; disruption of plasma membrane integrity in another organism [GO:0051673]; killing of cells of another organism [GO:0031... | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | null | null | null | null | SUBCELLULAR LOCATION: Target cell membrane {ECO:0000305|PubMed:23483218}. Secreted {ECO:0000269|PubMed:23483218}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide active against Gram-positive bacteria M.luteus (MIC=1.5 uM), B.subtilis (MIC=1.3 uM) and S.aureus (MIC=10.6 uM), against Gram-negative bacteria E.coli (MIC=3.7 uM) and P.aeruginosa (MIC=51.7 uM) as well as against yeast C.albicans (MIC=7.3 uM). Has weak hemolytic activity against human e... | Panurgus calcaratus (Solitary bee) |
C0HL98 | MAC1_MACFV | GFGMALKLLKKVL | null | null | defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; disruption of plasma membrane integrity in another organism [GO:0051673]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | null | null | Lasioglossin-like family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24616110}. Target cell membrane {ECO:0000269|PubMed:24616110, ECO:0000269|PubMed:29185466}. Note=Adopts an alpha-helical structure in a membrane mimic environment. {ECO:0000269|PubMed:24616110, ECO:0000269|PubMed:29185466}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide with activity against Gram-positive bacteria (B.subtilis, S.aureus and L.monocytogenes) and Gram-negative bacteria (E.coli and P.aeruginosa) (MIC=1.3-35 uM) (PubMed:24616110, PubMed:29185466). Also active against fungus C.albicans (MIC=6.3 uM) (PubMed:24616110). Has little hemolytic acti... | Macropis fulvipes (Solitary bee) (Megilla fulvipes) |
C0HLF0 | PA2_POROP | NLFQFRKMIKKMTKKEPVVYYAFYGCYCGKGGRGKPKDATDRCCFVHDCCYEKVTGCNPKWGYYTYSMNKQIVCGGDDPCKKQVCECDKAAAICFRDNLKTYKKKYMSFPNFFCTDPSEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29886171}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; 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 I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29886171}. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that displays moderate myotoxic activity in vivo, and cytotoxic activity in vitro. In vitro, shows anticoagulant activity on human plasma and in mice causes inflammatory cell infiltration and myonecrosis in the gastrocnemius muscles of CD-1 mice 3 hours after injection (100... | Porthidium ophryomegas (Slender hognose viper) |
C0HLF7 | PA2B_OPHSH | HLLQFNKMIKEETGKNAIPFYAFYGCYCGWGGSGKPKDATDRCCFEHDCCYGKLTNCNTKWDIYSYSLKDGYITCGKGTWCEKEVCECDKCLRRNLRTYKYGYMFYL | 3.1.1.4 | null | 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:30205237}. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Heterodimer A-B: Sphenotoxin is a potent neurotoxin that possesses phospholipase A2 (PLA2) activity. It consists of a non-covalent association of a basic PLA2 subunit B with a non-enzymatic subunit A. {ECO:0000269|PubMed:30205237}.; FUNCTION: Monomer B: Not found in vivo. In vitro, potent neurotoxin that poss... | Ophryacus sphenophrys (Broad-horned pitviper) (Bothrops sphenophrys) |
C0HLG3 | RNAG_CYCAE | MSESSTFTTAVVPEGEGVAPMAETVQYYNSYSDASIASCAFVDSGKDKIDKTKLVTYTSRLAASPAYQKVVGVGLKTAAGSIVPYVRLDMDNTGKGIHFNATKLSDSSAKLAAVLKTTVSMTEAQRTQLYMEYIKGIENRSAQFIWDWWRTGKAPA | 4.6.1.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30262416}; | killing of cells of another organism [GO:0031640] | vacuolar lumen [GO:0005775] | lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; RNA endonuclease activity [GO:0004521]; rRNA endonuclease activity [GO:0033902] | null | null | Ribotoxin-like family | null | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:32998313}. Note=Possibly sequestered into the vacuole to avoid its toxic activity on ribosomes. {ECO:0000305|PubMed:32998313}. | CATALYTIC ACTIVITY: Reaction=a 28S rRNA containing guanosine-adenosine pair + H2O = an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment].; EC=4.6.1.23; Evidence={ECO:0000269|PubMed:28232091, ECO:0000269|PubMed:30262416, ECO:0000269|PubMed:31444206}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Has a melting temperature of 78 degrees Celsius at pH 7.4. {ECO:0000269|PubMed:30262416}; | FUNCTION: Fungal ribonuclease involved in fungal defense. Highly specific and highly toxic fungal endonuclease that cleaves a single phosphodiester bond in the 28S RNA of eukaryotic ribosomes at a universally conserved GAGA tetraloop of the sarcin-ricin loop (SRL). The damage of the SRL inhibits the binding of translat... | Cyclocybe aegerita (Black poplar mushroom) (Agrocybe aegerita) |
C0HLG4 | KKX1U_UROMN | MKYFTLALTLLFLLLINPCKDMNFAWAESSEKVERASPQQAKYCYEQCNVNKVPFDQCYQMCSPLERS | null | null | null | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430] | ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | null | Short scorpion toxin superfamily, Potassium channel inhibitor kappa-KTx family, Kappa-KTx 1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31447178}. Host cytoplasm {ECO:0000269|PubMed:31447178}. Note=Penetrates into cell via passive diffusion and binds to the cytoplasmic side of TRPA1 (PubMed:31447178). {ECO:0000269|PubMed:31447178}. | null | null | null | null | null | FUNCTION: Cell-penetrating peptide (CPP) with defensive purpose that induces pain by specifically activating mammalian sensory neuron TRPA1 channels. It non-covalently binds to the same region than other TRPA1 agonists (irritants), but acts via a distinct biochemical mechanism. Its binding stabilizes the TRPA1 open sta... | Urodacus manicatus (Black rock scorpion) |
C0HLL2 | PA2_PITAZ | MAFLVFAFLTLMAVETYGSLFQFRLMINYLTGKLPILSHSFYGCYCGAGGSGWPKDAIDWCCQVHDCCYGRMSASGCDPYFQPYNFSYINKNLQCVETDTSGCPRRICECDRLASICFQQHDATYNSSNIDPKRKGCGTKSPPCPN | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:31173792}; | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; glycerophospholipid catabolic process [GO:0046475]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family | PTM: N-glycosylated. Glycosylated with mannose chains including Man2(GlcNAc), Man2(GlcNAc)2, Man2(GlcNAc)3, Man2(GlcNAc)4 and Man2(GlcNAc)5. {ECO:0000269|PubMed:31173792}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31173792}. | 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:31173792}; | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:31173792}. | Pithecopus azureus (Orange-legged monkey tree frog) (Phyllomedusa azurea) |
C0HLR3 | SCX1_CENBA | KEGYIVNHSTGCKYECYKLGDNDYCLRECKAQYGKGAGGYCYAFGCWCTHLYEQAVVWPLPKKTCN | null | null | defense response [GO:0006952]; envenomation resulting in negative regulation of voltage-gated sodium channel activity in another organism [GO:0044493] | extracellular space [GO:0005615] | calcium channel regulator activity [GO:0005246]; sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | null | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32479835}. | null | null | null | null | null | FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and reduces peak current and shifts the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (PubMed:32479835). Has an inhibitory effect on vol... | Centruroides baergi (Scorpion) (Centruroides nigrovariatus baergi) |
C0HLV2 | NEPRN_NEPVE | MQAKFFTFVILSSVFYFNYPLAEARSIQARLANKPKGTIKTIKGDDGEVVDCVDIYKQPAFDHPLLKNHTLQMQPSSYASKVGEYNKLEQPWHKNGECPKGSIPIRRQVITGLPVVKKQFPNLKFAPPSANTNHQYAVIAYFYGNASLQGANATINIWEPNLKNPNGDFSLTQIWISAGSGSSLNTIEAGWQVYPGRTGDSQPRFFIYWTADGYTSTGCYDLTCPGFVQTNNYYAIGMALQPSVYGGQQYELNESIQRDPATGNWWLYLWGTVVGYWPASIYNSITNGADTVEWGGEIYDSSGTGGFHTTTQMGSGHFPT... | 3.4.21.26 | null | proteolysis [GO:0006508] | extracellular region [GO:0005576] | endopeptidase activity [GO:0004175]; oligopeptidase activity [GO:0070012] | PF03080;PF14365; | 3.90.1320.10; | Peptidase G3 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27481162}. Note=Secreted into the viscoelastic fluid of the pitcher. {ECO:0000269|PubMed:27481162}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000269|PubMed:27481162, ECO:0000269|PubMed:28404794, ECO:0000269|PubMed:35915115}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.36 M for fluorogenic FS6 peptide {ECO:0000269|PubMed:35915115}; KM=2.74 M for fluorogenic FS6-QPQL peptide {ECO:0000269|PubMed:35915115}; Note=kcat is 1.81 sec(-1) for the cleavage of the fluorogenic FS6 peptide (PubMed:35915115). kcat is 6.55 sec(-1) for the cle... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 2.5 (PubMed:28404794). At pH 4.5, the enzyme retains approximately 50% of its activity but it is almost completely inactivated at pH 8 (PubMed:28404794). Optimum pH is 3 with fluorescent bovine serum albumin (BSA) as substrate (PubMed:35915115). {ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 37-50 degrees Celsius. {ECO:0000269|PubMed:28404794}; | FUNCTION: Glutamic endopeptidase that preferentially cleaves peptide bonds on the C-terminal side of proline residues (PubMed:27481162, PubMed:28404794, PubMed:35915115). Also cleaves peptide bonds on the C-terminal side of alanine residues but with less efficiency (PubMed:28404794). In contrast to most proline-cleavin... | Nepenthes x ventrata (Red tropical pitcher plant) (Nepenthes ventricosa x Nepenthes alata) |
C0HLV6 | LACS_TRAHI | FQLNVIANMNNHTMLKQTSIHWHCHFQKGTNWADGHAFVNACPIASGHSFLYDFTAPDQHGTFWYHSHLSTQYCDGLRGHFVVYDPADPHHDLYDVDDEHTIITLADWYHVAAKLGHHFQLGADSTLINGSGRFAGDPTAHLTVIYVTQGKRYRFHLVSLSCDPNHVFSIDSNHMTVIEADAVSHEHCTVDSIQIYAGQRYSFHLTVDQDVDNYWIRAHPSFGTYSFHDGINSAIARY | 1.10.3.2 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:34093489}; Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:D0VWU3}; | lignin catabolic process [GO:0046274] | extracellular region [GO:0005576] | copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716] | PF00394;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34093489}. | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:34093489}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=87.47 uM for ABTS (at pH 6.0 and 50 degrees Celsius); Note=kcat is 129.37 sec(-1) for ABTS oxidation (at pH 6.0 and 50 degrees Celsius). {ECO:0000269|PubMed:34093489}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 at 25 degrees Celsius (PubMed:34093489). Retains over 60 percent activity in the pH range from 4 to 10 (PubMed:34093489). Retains activity above 50% after incubation at pH 5-10 for 72 hours (PubMed:34093489). {ECO:0000269|PubMed:34093489}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius (PubMed:34093489). Retains over 57 percent activity when incubated for 2 hours at temperatures between 30-65 degrees Celsius (PubMed:34093489). {ECO:0000269|PubMed:34093489}; | FUNCTION: Lignin degradation and detoxification of lignin-derived products (By similarity). Has activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) (PubMed:34093489). {ECO:0000250|UniProtKB:D0VWU3, ECO:0000269|PubMed:34093489}. | Trametes hirsuta (White-rot fungus) (Coriolus hirsutus) |
C0HLV7 | LACF_GANAU | FQLNVIANNNNHTMLTQTTIHCHGFFQGTNSADGHAFVNCCPIASGHSFLYDFSHPDQHGTFCYHSHLSTQYCCGLRGHFVVYDPSDPHCGLYDVDHDSTVITLSDWYHVAAKLGHSFCLGADSTLINGSGRSTGDCAASLTVISVTQGKRYRFHLVSLSCDPNHTFSIDGHDMSVIEVDSIASQHVTVDSIQIFAGQRYSFVLTANQSINNYWIRANPSFGNIGFHDGINSAILRY | 1.10.3.2 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:34467865}; Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:D0VWU3}; | cellular response to iron ion starvation [GO:0010106]; lignin catabolic process [GO:0046274]; reductive iron assimilation [GO:0033215] | extracellular region [GO:0005576]; high-affinity iron permease complex [GO:0033573] | copper ion binding [GO:0005507]; ferroxidase activity [GO:0004322]; hydroquinone:oxygen oxidoreductase activity [GO:0052716] | PF00394;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34467865}. | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:34467865}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=164.14 uM for ABTS (at pH 6.0 and 55 degrees Celsius) {ECO:0000269|PubMed:34467865}; KM=156.55 uM for ABTS (at 55 degrees Celsius in the presence of 5 mM NaCl) {ECO:0000269|PubMed:34467865}; KM=147.48 uM for ABTS (at 55 degrees Celsius in the presence of 10 mM NaCl... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 (PubMed:34467865). Retains over 72 percent activity in the pH range 5 to 8 (PubMed:34467865). Retains activity above 89% after incubation at pH 6 for 72 hours (PubMed:34467865). Retains activity above 61% after incubation at pH 5-8 for 72 hours (PubMed:3446... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius (PubMed:34467865). Thermostable (PubMed:34467865). Retains over 84 percent activity when incubated for 3 hours at temperatures between 10-60 degrees Celsius (PubMed:34467865). {ECO:0000269|PubMed:34467865}; | FUNCTION: Lignin degradation and detoxification of lignin-derived products (By similarity). Multicopper oxidase that catalyzes the oxidation of a variety of substrates, including phenolic and non-phenolic compounds (PubMed:34467865). Has highest activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (A... | Ganoderma australe (Bracket fungus) (Polyporus australis) |
C0HLX7 | GLEC_CHOCI | TYAEVESFGVGQSATAVYTAPGDGRDLNITIDADGGYVIHMDYRFDWGGNPSTGKPWEDILILNSKPAQTWGPQQHVNNFYFTPGTHVTLGDKSNDGHFAIIADGIQVATYDHRLPVNSVKEVKFSTTAGSGTDIWDLLLLP | null | null | aggregation of unicellular organisms [GO:0098630]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832] | null | galactose binding [GO:0005534]; protein homodimerization activity [GO:0042803] | PF00337; | 2.60.120.200; | null | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for hemagglutination activity is 9. {ECO:0000269|PubMed:29175164}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable at high temperatures. {ECO:0000269|PubMed:29175164}; | FUNCTION: Galactose-binding lectin (PubMed:29175164, PubMed:34508835). Displays antibacterial and hemagglutinin activity (PubMed:29175164, PubMed:34508835). Inhibits the growth of L.infantum promastigotes by damaging their membrane integrity and inducing cell apoptosis via the production of reactive oxygen species (ROS... | Chondrilla caribensis (Chicken liver sponge) |
C0HLZ9 | BARA1_DROME | MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY | null | null | antifungal innate immune response [GO:0061760]; killing of cells of another organism [GO:0031640]; response to Gram-positive bacterium [GO:0140459]; response to toxic substance [GO:0009636] | extracellular space [GO:0005615] | null | null | null | null | PTM: Proteolytically cleaved. {ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}. | SUBCELLULAR LOCATION: [Immune-induced peptide 24]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 6]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 12]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCA... | null | null | null | null | null | FUNCTION: Secreted immune-induced peptides induced by Toll signaling (PubMed:34432851, PubMed:9736738). Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705 (PubMed:34432851). In adult males, activity appears to be importa... | Drosophila melanogaster (Fruit fly) |
C0HM00 | BARA2_DROME | MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY | null | null | antifungal innate immune response [GO:0061760]; defense response [GO:0006952]; humoral immune response [GO:0006959]; killing of cells of another organism [GO:0031640]; response to bacterium [GO:0009617] | extracellular space [GO:0005615] | null | null | null | null | PTM: Proteolytically cleaved. {ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}. | SUBCELLULAR LOCATION: [Immune-induced peptide 24]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 6]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 12]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCA... | null | null | null | null | null | FUNCTION: Secreted immune-induced peptides induced by Toll signaling (PubMed:34432851, PubMed:9736738). Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705 (PubMed:34432851). In adult males, activity appears to be importa... | Drosophila melanogaster (Fruit fly) |
C0HM14 | PA2BD_CRODU | HLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTKWDIYRYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P62022}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P62022}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; ion channel regulator activity [GO:0099106]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3753003, ECO:0000269|PubMed:8033889}. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (monomer CBd) {ECO:0000269|PubMed:8513799}; KM=0.35 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 1 heterodimer CA2-CBd) {ECO:00002... | null | null | null | FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (PubMed:8513799). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a... | Crotalus durissus terrificus (South American rattlesnake) |
C0HM45 | LEC_NARPS | DNILYSGETLSPGEFLNNGRYVFIMQEDCNLVLYDVDKPIWATNTGGLDRRCHLSMQSDGNLVVYSPRNNPIWASNTGGENGNYVCVLQKDRNVVIYGTARWATGTNIH | null | null | defense response to virus [GO:0051607]; regulation of defense response to virus [GO:0050688]; response to virus [GO:0009615] | extracellular space [GO:0005615] | mannose binding [GO:0005537]; protein homodimerization activity [GO:0042803] | null | 2.90.10.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10388566}. | null | null | null | null | null | FUNCTION: D-mannose-binding lectin which binds alpha-D-linked mannose (PubMed:10388566, PubMed:14505313, PubMed:1645507, PubMed:1874921, PubMed:2350177). Displays a high affinity for alpha-(1-6)-mannose oligomers (PubMed:1645507, PubMed:2350177). Able to interact with both terminal and internal alpha-D-mannosyl residue... | Narcissus pseudonarcissus (Daffodil) |
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