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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P0DP30 | CALM2_RAT | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | null | null | autophagosome membrane docking [GO:0016240]; cellular response to interferon-beta [GO:0035458]; cellular response to type II interferon [GO:0071346]; detection of calcium ion [GO:0005513]; establishment of protein localization to membrane [GO:0090150]; establishment of protein localization to mitochondrial membrane [GO... | calcium channel complex [GO:0034704]; catalytic complex [GO:1902494]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; membrane [GO:0016020]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; protein-containing complex [GO:0032991]; sarcomere [GO:0030017]; spindle microtubule [GO:0005876... | adenylate cyclase activator activity [GO:0010856]; adenylate cyclase binding [GO:0008179]; calcium channel inhibitor activity [GO:0019855]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; nitric-oxide synthase binding [GO:0050998]; nitric-oxide synthase regulator activity [GO:0030235];... | PF13499; | 1.10.238.10; | Calmodulin family | PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000269|PubMed:12392717}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calciu... | Rattus norvegicus (Rat) |
P0DP31 | CALM3_RAT | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | null | null | autophagosome membrane docking [GO:0016240]; cellular response to interferon-beta [GO:0035458]; cellular response to type II interferon [GO:0071346]; detection of calcium ion [GO:0005513]; establishment of protein localization to membrane [GO:0090150]; establishment of protein localization to mitochondrial membrane [GO... | calcium channel complex [GO:0034704]; catalytic complex [GO:1902494]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; protein-containing complex [GO:0032991]; sarcomere [GO:0030017]; spindle microtubule [GO:0005876]; spindle pole [GO:000... | adenylate cyclase activator activity [GO:0010856]; adenylate cyclase binding [GO:0008179]; calcium channel inhibitor activity [GO:0019855]; calcium ion binding [GO:0005509]; nitric-oxide synthase binding [GO:0050998]; nitric-oxide synthase regulator activity [GO:0030235]; protein kinase binding [GO:0019901]; protein ph... | PF13499; | 1.10.238.10; | Calmodulin family | PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000269|PubMed:12392717}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calciu... | Rattus norvegicus (Rat) |
P0DP43 | CTSRE_MOUSE | MPSAGQRKPGSLLALQALQKWLLRGGVGAMLARQVVAALLLWLSCCVSALWRYYINSQDYSIFSTRSSIKLEYEGNSFVSWKIPESCKVENTTSPKTTLHCKRAGIHTIKPIAGNQEVERHLTVDNSYICYLWYFTVVDVYYNLSQIVTIWVYDPESASTEELIWTAKKPSLSSRVLTKQMNTLGQRPFIFTVEKRLTYHPGPLTSEGTWVIHLPMSSDDIAKVIRGNKVAFQDCFIANLYFMLTYPMTIISEPPGYEPLTVPPGSPLMLSWDTCISTFALLATDQETFQTNDSFQTWTRVRAPPGILSDAQRHSLRDVI... | null | null | flagellated sperm motility [GO:0030317]; sperm capacitation [GO:0048240] | CatSper complex [GO:0036128]; sperm principal piece [GO:0097228] | null | PF15020; | null | CATSPERD family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:28226241}; Single-pass type I membrane protein {ECO:0000255}. Note=Specifically located in the principal piece of sperm tail. {ECO:0000269|PubMed:28226241}. | null | null | null | null | null | FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation (PubMed:28226241, PubMed:34225353). Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (PubMed:28226241). {ECO:0000269|PubMed:28226241, ECO:00... | Mus musculus (Mouse) |
P0DP57 | SLUR2_HUMAN | MQLGTGLLLAAVLSLQLAAAEAIWCHQCTGFGGCSHGSRCLRDSTHCVTTATRVLSNTEDLPLVTKMCHIGCPDIPSLGLGPYVSIACCQTSLCNHD | null | null | acetylcholine receptor signaling pathway [GO:0095500]; regulation of neurotransmitter receptor activity [GO:0099601] | extracellular space [GO:0005615]; plasma membrane [GO:0005886]; synapse [GO:0045202] | acetylcholine receptor binding [GO:0033130]; acetylcholine receptor inhibitor activity [GO:0030550]; acetylcholine receptor regulator activity [GO:0030548] | PF00021; | 2.10.60.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16575903}. | null | null | null | null | null | FUNCTION: Binds and may modulate the functional properties of nicotinic and muscarinic acetylcholine receptors. May regulate keratinocytes proliferation, differentiation and apoptosis. In vitro moderately inhibits ACh-evoked currents of alpha-3:beta-2-containing nAChRs and strongly these of alpha-4:beta-2-containing nA... | Homo sapiens (Human) |
P0DP58 | LYNX1_HUMAN | MTPLLTLILVVLMGLPLAQALDCHVCAYNGDNCFNPMRCPAMVAYCMTTRTYYTPTRMKVSKSCVPRCFETVYDGYSKHASTTSCCQYDLCNGTGLATPATLALAPILLATLWGLL | null | null | regulation of neurotransmitter receptor activity [GO:0099601]; synaptic transmission, cholinergic [GO:0007271] | dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202] | acetylcholine receptor binding [GO:0033130]; acetylcholine receptor inhibitor activity [GO:0030550]; acetylcholine receptor regulator activity [GO:0030548]; ion channel inhibitor activity [GO:0008200] | PF00087; | 2.10.60.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0DP60}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P0DP60}. Note=Detected in Purkinje cells soma and proximal dendrites. {ECO:0000250|UniProtKB:P0DP60}. | null | null | null | null | null | FUNCTION: Acts in different tissues through interaction to nicotinic acetylcholine receptors (nAChRs) (PubMed:21252236). The proposed role as modulator of nAChR activity seems to be dependent on the nAChR subtype and stoichiometry, and to involve an effect on nAChR trafficking and its cell surface expression, and on si... | Homo sapiens (Human) |
P0DP60 | LYNX1_MOUSE | MTHLLTVFLVALMGLPVAQALECHVCAYNGDNCFKPMRCPAMATYCMTTRTYFTPYRMKVRKSCVPSCFETVYDGYSKHASATSCCQYYLCNGAGFATPVTLALVPALLATFWSLL | null | null | regulation of neurotransmitter receptor activity [GO:0099601]; synaptic transmission, cholinergic [GO:0007271] | dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202] | acetylcholine receptor binding [GO:0033130]; acetylcholine receptor inhibitor activity [GO:0030550]; acetylcholine receptor regulator activity [GO:0030548]; ion channel inhibitor activity [GO:0008200] | PF00087; | 2.10.60.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:10402197}. Endoplasmic reticulum {ECO:0000269|PubMed:25193667}. Note=Detected in Purkinje cells soma and proximal dendrites. {ECO:0000269|PubMed:10402197}. | null | null | null | null | null | FUNCTION: Acts in different tissues through interaction to nicotinic acetylcholine receptors (nAChRs) (PubMed:10402197). The proposed role as modulator of nAChR activity seems to be dependent on the nAChR subtype and stoichiometry, and to involve an effect on nAChR trafficking and its cell surface expression, and on si... | Mus musculus (Mouse) |
P0DP76 | ELA_RAT | MRFQPLFWVFFIFAMSLLFITEEKSVNFPRRRKLYRHNCFRRRCISLHSRVPFP | null | null | adult heart development [GO:0007512]; angiogenesis [GO:0001525]; apelin receptor signaling pathway [GO:0060183]; coronary vasculature development [GO:0060976]; embryonic heart tube development [GO:0035050]; mesoderm migration involved in gastrulation [GO:0007509]; placenta blood vessel development [GO:0060674]; positiv... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | apelin receptor binding [GO:0031704]; hormone activity [GO:0005179] | null | null | Elabela/Toddler family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DMC4}. Secreted, extracellular space {ECO:0000250|UniProtKB:P0DMC4}. Note=Found in blood plasma. Found in serum of pregnant mice, peaking at midgestation; indicating a maternal and zygotic origin of circulating APELA during pregnancy. {ECO:0000250|UniProtKB:P0DMC3... | null | null | null | null | null | FUNCTION: Endogenous ligand for the apelin receptor (APLNR) (PubMed:28137936). Hormone required for mesendodermal differentiation, blood vessels formation and heart morphogenesis during early development and for adult cardiovascular homeostasis (PubMed:26611206, PubMed:28137936). Drives internalization of APLNR. Acts a... | Rattus norvegicus (Rat) |
P0DP90 | ILVG_ECOLI | MNGAQWVVHALRAQGVNTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALLDSIPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLEELPRIMAEAFDVACSGRPGPVLVDIPKDIQLASGDLEPWFTTVENEVTFPHAEVEQARQMLAKAQKPMLYVGGGVGMAQAVPALREFLAATKMPATCTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPHASVIHMDIDPAEMNKLRQAHVALQGDLNALLPA... | 2.2.1.6 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:9581571}; Note=Binds 1 FAD per subunit. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry. However, after removal of the FAD no AHAS activity can be detected (PubMed:9581571), indicating that the... | amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | acetolactate synthase complex [GO:0005948] | acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6; Evidence={ECO:0000269|PubMed:9581571}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 mM for pyruvate {ECO:0000269|PubMed:9581571}; | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. | null | null | FUNCTION: Catalyzes the first step in the biosynthesis of branched-chain amino acids. {ECO:0000269|PubMed:9581571}. | Escherichia coli (strain K12) |
P0DP91 | ERPG3_HUMAN | MPNEGIPHSSQTQEQDCLQSQPVSNNEEMAIKQESGGDGEVEEYLSFRSVGDGLSTSAVGCASAAPRRGPALLHIDRHQIQAVEPSAQALELQGLGVDVYDQDVLEQGVLQQVDNAIHEASRASQLVDVEKEYRSVLDDLTSCTTSLRQINKIIEQLSPQAATSRDINRKLDSVKRQKYNKEQQLKKITAKQKHLQAILGGAEVKIELDHASLEEDAEPGPSSLGSMLMPVQETAWEELIRTGQMTPFGTQIPQKQEKKPRKIMLNEASGFEKYLADQAKLSFERKKQGCNKRAARKAPAPVTPPAPVQNKNKPNKKARV... | null | null | positive regulation of defense response to virus by host [GO:0002230]; positive regulation of DNA repair [GO:0045739]; positive regulation of gene expression [GO:0010628]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141] | nuclear body [GO:0016604]; nucleoplasm [GO:0005654] | sequence-specific DNA binding [GO:0043565] | PF13843; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26218421}. | null | null | null | null | null | FUNCTION: Involved in repair of DNA damage following UV irradiation, acting either in the absence of ERCC6 or synergistically with ERCC6. Involved in the regulation of gene expression. In the absence of ERCC6, induces the expression of genes characteristic of interferon-like antiviral responses. This response is almost... | Homo sapiens (Human) |
P0DP99 | STMP1_MOUSE | MLQFLLGFTLGNVVGMYLAQNYEMPNLAKKLEEIKKDLEAKKKPPSS | null | null | innate immune response [GO:0045087]; mitochondrial cytochrome c oxidase assembly [GO:0033617]; mitochondrial respirasome assembly [GO:0097250]; mitochondrial respiratory chain complex III assembly [GO:0034551]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of NLRP3 inflammasome ... | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; mitochondrial respirasome [GO:0005746] | null | PF15054; | null | STMP1 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:35101990}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:31836654}; Single-pass membrane protein {ECO:0000255}. Mitochondrion intermembrane space {ECO:0000269|PubMed:31836654}. | null | null | null | null | null | FUNCTION: Microprotein involved in mitochondrial respiratory chain complex III (ubiquinol-cytochrome c oxidoreductase) and complex IV (mitochondrial cytochrome c oxidase complex) assembly (PubMed:35101990). Required for the formation of mitochondrial supercomplexes (SCs) (PubMed:35101990). Also required for the activat... | Mus musculus (Mouse) |
P0DPA8 | PSIK_PSICU | MAFDLKTEDGLITYLTKHLSLDVDTSGVKRLSGGFVNVTWRIKLNAPYQGHTSIILKHAQPHMSTDEDFKIGVERSVYEYQAIKLMMANREVLGGVDGIVSVPEGLNYDLENNALIMQDVGKMKTLLDYVTAKPPLATDIARLVGTEIGGFVARLHNIGRERRDDPEFKFFSGNIVGRTTSDQLYQTIIPNAAKYGVDDPLLPTVVKDLVDDVMHSEETLVMADLWSGNILLQLEEGNPSKLQKIYILDWELCKYGPASLDLGYFLGDCYLISRFQDEQVGTTMRQAYLQSYARTSKHSINYAKVTAGIAAHIVMWTDFM... | 2.7.1.-; 2.7.1.222 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32101345}; | phosphorylation [GO:0016310]; psilocybin biosynthetic process [GO:0140380] | null | 4-hydroxytryptamine kinase activity [GO:0140383]; ATP binding [GO:0005524] | PF01636; | 3.90.1200.10; | Methylthioribose kinase family | null | null | CATALYTIC ACTIVITY: Reaction=4-hydroxytryptamine + ATP = 4-hydoxytryptamine 4-phosphate + ADP + H(+); Xref=Rhea:RHEA:55564, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:139069, ChEBI:CHEBI:139070, ChEBI:CHEBI:456216; EC=2.7.1.222; Evidence={ECO:0000269|PubMed:28763571, ECO:0000269|PubMed:31150155, ECO:0000269|PubM... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=72 uM for psilocin {ECO:0000269|PubMed:32101345}; KM=67 uM for 4-hydroxytryptamine {ECO:0000269|PubMed:32101345}; KM=89 uM for ATP {ECO:0000269|PubMed:32101345}; | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:28763571}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:32101345}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:32101345}; | FUNCTION: 4-hydroxytryptamine kinase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product (PubMed:28763571, PubMed:31150155, PubMed:32101345). The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD... | Psilocybe cubensis (Psychedelic mushroom) (Stropharia cubensis) |
P0DPA9 | PSIM_PSICU | MHIRNPYRTPIDYQALSEAFPPLKPFVSVNADGTSSVDLTIPEAQRAFTAALLHRDFGLTMTIPEDRLCPTVPNRLNYVLWIEDIFNYTNKTLGLSDDRPIKGVDIGTGASAIYPMLACARFKAWSMVGTEVERKCIDTARLNVVANNLQDRLSILETSIDGPILVPIFEATEEYEYEFTMCNPPFYDGAADMQTSDAAKGFGFGVGAPHSGTVIEMSTEGGESAFVAQMVRESLKLRTRCRWYTSNLGKLKSLKEIVGLLKELEISNYAINEYVQGSTRRYAVAWSFTDIQLPEELSRPSNPELSSLF | 2.1.1.- | null | psilocybin biosynthetic process [GO:0140380]; rRNA base methylation [GO:0070475] | nucleus [GO:0005634] | 23S rRNA (adenine(1618)-N(6))-methyltransferase activity [GO:0052907]; 4-hydroxytryptamine 4-phosphate methyltransferase activity [GO:0140381] | PF05971; | 3.40.50.150; | Methyltransferase superfamily, METTL16/RlmF family | null | null | CATALYTIC ACTIVITY: Reaction=4-hydoxytryptamine 4-phosphate + S-adenosyl-L-methionine = 4-hydroxy-N-methyltryptamine 4-phosphate + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55572, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:139070, ChEBI:CHEBI:139071; Evidence={ECO:0000269|PubMed:2876357... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:28763571}. | null | null | FUNCTION: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product (PubMed:28763571, PubMed:31150155). The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD (PubMed:28763571, PubMe... | Psilocybe cubensis (Psychedelic mushroom) (Stropharia cubensis) |
P0DPB3 | SCHI1_HUMAN | MERSGQRVTTWDCDQGKHSDSDYREDGMDLGSDAGSSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDERDQRGYRDDRSPAREPGDVSARTRSGGGGGRSATTAMPPPVPNGNLHQHDPQDLRHNGNVVVAGRPSCSRGPRRAIQKPQPAGGRRSGRGPAAGGLCLQPPDGGTCVPEEPPVPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSSRLQSGMNLQICFVNDSGSDKDSDADDSK... | null | null | positive regulation of hippo signaling [GO:0035332] | cell junction [GO:0030054]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802] | PF10148; | null | SCHIP1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10669747}. | null | null | null | null | null | null | Homo sapiens (Human) |
P0DPB4 | SCHI1_MOUSE | MERSEQRVRAAWDCDPGKQADRDYREDGMDLGSDAGSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDDRGYRDDGCPAREPGDVSARIGSSGSGSRSAATTMPSPMPNGNLHPHDPQDLRHNGNVVVAGRPNASRVPRRPIQKTQPPGSRRGGRNRASGGLCLQPPDGGTRVPEEPPAPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSARLQSGMNLQICFVNDSGSDKDSDADDSKTET... | null | null | estrogen metabolic process [GO:0008210]; face morphogenesis [GO:0060325]; female gonad development [GO:0008585]; fibroblast migration [GO:0010761]; kidney development [GO:0001822]; luteinization [GO:0001553]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of hippo signaling ... | cell junction [GO:0030054]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | protein homodimerization activity [GO:0042803] | PF10148; | null | SCHIP1 family | null | null | null | null | null | null | null | null | Mus musculus (Mouse) |
P0DPB6 | RPAC2_HUMAN | MEEDQELERKISGLKTSMAEGERKTALEMVQAAGTDRHCVTFVLHEEDHTLGNSLRYMIMKNPEVEFCGYTTTHPSESKINLRIQTRGTLPAVEPFQRGLNELMNVCQHVLDKFEASIKDYKDQKASRNESTF | null | null | transcription by RNA polymerase III [GO:0006383]; transcription elongation by RNA polymerase I [GO:0006362] | RNA polymerase I complex [GO:0005736]; RNA polymerase III complex [GO:0005666] | DNA binding [GO:0003677]; protein dimerization activity [GO:0046983]; RNA polymerase I activity [GO:0001054]; RNA polymerase III activity [GO:0001056] | PF13656; | 3.30.1360.10; | Archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33335104}. Nucleus, nucleolus {ECO:0000305|PubMed:34887565}. | null | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and short non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs, respectively. {ECO:... | Homo sapiens (Human) |
P0DPC1 | PHZD2_PSEAE | MSGIPEITAYPLPTAQQLPANLARWSLEPRRAVLLVHDMQRYFLRPLPESLRAGLVANAARLRRWCVEQGVQIAYTAQPGSMTEEQRGLLKDFWGPGMRASPADREVVEELAPGPDDWLLTKWRYSAFFHSDLLQRMRAAGRDQLVLCGVYAHVGVLISTVDAYSNDIQPFLVADAIADFSEAHHRMALEYAASRCAMVVTTDEVLE | 3.3.2.15 | null | phenazine biosynthetic process [GO:0002047] | null | isochorismatase activity [GO:0008908] | PF00857; | 3.40.50.850; | Isochorismatase family | null | null | CATALYTIC ACTIVITY: Reaction=(2S)-2-amino-4-deoxychorismate + H2O = (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxyate + pyruvate; Xref=Rhea:RHEA:49456, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:58792, ChEBI:CHEBI:60849; EC=3.3.2.15; Evidence={ECO:0000269|PubMed:12741825}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4 uM for isochorismate {ECO:0000269|PubMed:12741825}; KM=68 uM for 2-amino-2-deoxyisochorismate {ECO:0000269|PubMed:12741825}; KM=590 uM for 4-amino-4-deoxychorismate {ECO:0000269|PubMed:12741825}; KM=983 uM for chorismate {ECO:0000269|PubMed:12741825}; Note=kcat i... | PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis. {ECO:0000305|PubMed:11591691}. | null | null | FUNCTION: Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control. PhzD2 (operon phzA2B2C2E2F2G2) has a role in the biosynthesis of the phenazine during both planktonic growth and biofilm development, a... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P0DPC3 | CSRA1_PSEPH | MLILTRKVGESINIGDDITITILGVSGQQVRIGINAPKDVAVHREEIYQRIQAGLTAPDKRETP | null | null | mRNA catabolic process [GO:0006402]; negative regulation of translational initiation [GO:0045947]; positive regulation of translational initiation [GO:0045948]; regulation of carbohydrate metabolic process [GO:0006109] | cytosol [GO:0005829] | mRNA 5'-UTR binding [GO:0048027] | PF02599; | 2.60.40.4380; | CsrA/RsmA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}. | null | null | null | null | null | FUNCTION: A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability (PubMed:17704818, PubMed:23635605). Post-transcriptionally represses the expression of genes controlled by GacA/GacS (PubMed:15601712, PubMed:23635605). Binds the 5' UTR of mRNA; the mRNA binds to the outside ed... | Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0) |
P0DPD6 | ECE2_HUMAN | MNVALQELGAGSNMVEYKRATLRDEDAPETPVEGGASPDAMEVGKGASPFSPGPSPGMTPGTPRSSGLFWRVTCPHLRSISGLCSRTMVGFQKGTRQLLGSRTQLELVLAGASLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAEQKTQRFYLSCLQVERIEELGAQPLRDLIEKIGGWNITGPWDQDNFMEVLKAVAGTYRATPFFTVYISADSKSSNSNVIQVDQSGLFLPSRDYYLNRTANEKVL... | 3.4.24.71 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P42892}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P42892}; | cell-cell signaling [GO:0007267]; G protein-coupled receptor signaling pathway [GO:0007186]; methylation [GO:0032259]; peptide hormone processing [GO:0016486]; protein processing [GO:0016485] | cytoplasmic vesicle membrane [GO:0030659]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; transport vesicle membrane [GO:0030658] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; methyltransferase activity [GO:0008168] | PF01431;PF05649; | 3.40.390.10;1.10.1380.10; | Peptidase M13 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:F1N476}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:F1N476}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.; EC=3.4.24.71; Evidence={ECO:0000269|PubMed:12560336}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 uM for big ET-1 {ECO:0000269|PubMed:12560336}; KM=1.4 uM for peptide E {ECO:0000269|PubMed:12560336}; KM=27.4 uM for bradykinin {ECO:0000269|PubMed:12560336}; KM=48.4 uM for dynorphin B {ECO:0000269|PubMed:12560336}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-5.5. Inactive at neutral pH. {ECO:0000269|PubMed:12560336}; | null | FUNCTION: Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides. May play a role in amyloid-beta processing (By similarity). {ECO:0000250|UniProtK... | Homo sapiens (Human) |
P0DPD7 | EFMT4_HUMAN | MASPGAGRAPPELPERNCGYREVEYWDQRYQGAADSAPYDWFGDFSSFRALLEPELRPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSSVVVAAMQARHAHVPQLRWETMDVRKLDFPSASFDVVLEKGTLDALLAGERDPWTVSSEGVHTVDQVLSEVSRVLVPGGRFISMTSAAPHFRTRHYAQAYYGWSLRHATYGSGFHFHLYLMHKGGKLSVAQLALGAQILSPPRPPTSPCFLQDSDHEDFLSAIQL | 2.1.1.- | null | methylation [GO:0032259] | null | methyltransferase activity [GO:0008168]; protein-lysine N-methyltransferase activity [GO:0016279] | PF08241; | 3.40.50.150; | Methyltransferase superfamily | null | null | CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:00002... | null | null | null | null | FUNCTION: Protein-lysine methyltransferase that efficiently catalyzes three successive methylations on 'Lys-36' in eukaryotic translation elongation factor 1 alpha (EEF1A1 or EEF1A2). {ECO:0000269|PubMed:28520920}. | Homo sapiens (Human) |
P0DPD8 | EFCE2_HUMAN | MASPGAGRAPPELPERNCGYREVEYWDQRYQGAADSAPYDWFGDFSSFRALLEPELRPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSSVVVAAMQARHAHVPQLRWETMDVRKLDFPSASFDVVLEKGTLDALLAGERDPWTVSSEGVHTVDQVLSEVGFQKGTRQLLGSRTQLELVLAGASLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAEQKTQRFYLSCLQVERIEELGAQPLRDLIEKI... | 2.1.1.-; 3.4.24.71 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P42892}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P42892}; | brain development [GO:0007420]; cardioblast differentiation [GO:0010002]; heart development [GO:0007507]; methylation [GO:0032259]; protein processing [GO:0016485] | Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; transport vesicle membrane [GO:0030658] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; methyltransferase activity [GO:0008168] | PF13649;PF01431;PF05649; | 3.40.390.10;1.10.1380.10;3.40.50.150; | Methyltransferase superfamily; Peptidase M13 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P0DPE2}; Single-pass membrane protein {ECO:0000250|UniProtKB:P0DPE2}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P0DPE2}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.; EC=3.4.24.71; Evidence={ECO:0000250|UniProtKB:P0DPE2}; | null | null | null | null | FUNCTION: Converts big endothelin-1 to endothelin-1. May also have methyltransferase activity (By similarity). May play a role in amyloid-beta processing (By similarity). {ECO:0000250|UniProtKB:P0DPD9, ECO:0000250|UniProtKB:P0DPE2}. | Homo sapiens (Human) |
P0DPD9 | EFCE2_MOUSE | MASPRTPVSPPELPEKNFQYRQVQYWDQRYKDAADSGPYEWFGDFASFRALLEPELCPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSPVVVAAMQVRYAHVPSLRWETMDVRALDFPSGSFDVVLEKGTLDAMLAGEPDPWNVSSEGVHTVDQVLSEVGFQKRTRQLFGSHTQLELVLAGLILVLAALLLGCLVALWVHRDPAHSTCVTEACIRVAGKILESLDRGVSPCQDFYQFSCGGWIRRNPLPNGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTRSFYLSCLQSERIEKLGAKPLRDLIDKIGG... | 2.1.1.-; 3.4.24.71 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P42892}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P42892}; | brain development [GO:0007420]; cardioblast differentiation [GO:0010002]; heart development [GO:0007507]; methylation [GO:0032259]; peptide hormone processing [GO:0016486]; protein processing [GO:0016485] | cytoplasmic vesicle membrane [GO:0030659]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]; transport vesicle membrane [GO:0030658] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; methyltransferase activity [GO:0008168] | PF13649;PF01431;PF05649; | 3.40.390.10;1.10.1380.10;3.40.50.150; | Methyltransferase superfamily; Peptidase M13 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P0DPE2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P0DPE2}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P0DPE2}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.; EC=3.4.24.71; Evidence={ECO:0000250|UniProtKB:P0DPE2}; | null | null | null | null | FUNCTION: Converts big endothelin-1 to endothelin-1. May also have methyltransferase activity (By similarity). May play a role in amyloid-beta processing (PubMed:12464614). {ECO:0000250|UniProtKB:P0DPE2, ECO:0000269|PubMed:12464614}. | Mus musculus (Mouse) |
P0DPE2 | EFCE2_BOVIN | MACLGPSAQVPELPEKNCGYREVQYWDQRYQGAADSAPYEWFGDFSCFRDLLEPELRPLDRILVLGCGNSALSYEIFLGGFPDVTSVDYSSVVVAAMRARYAHVPTLRWETMDVRALGFPSGSFDVVLEKGTLDALLTGEQDPWTVSSEGVHTVDQVLNEAGFRKRTSRLLGLHTQLELVLAGVSLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTQRFYLSCLQVERIEELGAQPLRDLIDKI... | 2.1.1.-; 3.4.24.71 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P42892}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P42892}; | brain development [GO:0007420]; cardioblast differentiation [GO:0010002]; heart development [GO:0007507]; methylation [GO:0032259]; peptide hormone processing [GO:0016486]; protein processing [GO:0016485] | Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; transport vesicle membrane [GO:0030658] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; methyltransferase activity [GO:0008168] | PF13649;PF01431;PF05649; | 3.40.390.10;1.10.1380.10;3.40.50.150; | Methyltransferase superfamily; Peptidase M13 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12054617}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:12054617}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.; EC=3.4.24.71; Evidence={ECO:0000269|PubMed:7797512}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. Inactive at neutral pH. {ECO:0000269|PubMed:7797512}; | null | FUNCTION: Converts big endothelin-1 to endothelin-1 (PubMed:7797512). May also have methyltransferase activity (Probable). {ECO:0000269|PubMed:7797512, ECO:0000305}. | Bos taurus (Bovine) |
P0DPH7 | TBA3C_HUMAN | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR... | 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]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634] | 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: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate... | 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... | Homo sapiens (Human) |
P0DPH8 | TBA3D_HUMAN | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR... | 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]; microtubule cytoskeleton [GO:0015630] | 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: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate... | 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... | Homo sapiens (Human) |
P0DPI0 | BXA1_CLOBO | MPFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEK... | 3.4.24.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11565902, ECO:0000269|PubMed:11700044, ECO:0000269|PubMed:1429690, ECO:0000269|PubMed:15592454, ECO:0000269|PubMed:19351593, ECO:0000269|PubMed:22363010, ECO:0000269|PubMed:7578132}; Note=Binds 1 zinc ion per subunit (PubMed:11700044, PubMed:14... | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020] | ganglioside GT1b binding [GO:1905576]; metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07951;PF07953;PF07952; | 1.20.58.540;2.60.120.200;2.80.10.50;1.20.1120.10;4.10.1280.10;3.90.1240.10; | Peptidase M27 family | PTM: In a bacterial culture the precursor chain is initally cleaved on the amino side of Gly-445 and is processed more slowly between Lys-448 and Ala-449 to give the final mature heavy chain sequence. {ECO:0000269|PubMed:2126206}.; PTM: [Botulinum neurotoxin A light chain]: Has slow autocatalytic activity, cleaves 250-... | SUBCELLULAR LOCATION: [Botulinum neurotoxin type A]: Secreted {ECO:0000269|PubMed:7592120}. Secreted, cell wall {ECO:0000269|PubMed:7592120}. Host synapse, host presynaptic cell membrane {ECO:0000269|PubMed:6694738}. Note=Whole toxin may be released from the bacteria during cell wall exfoliation (PubMed:7592120). There... | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000269|PubMed:10694409, ECO:0000269|PubMed:7578132, ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:9886085}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=41 uM for purified SNAP25 with isolated botulinum neurotoxin A light chain {ECO:0000269|PubMed:10694409}; KM=9.8 uM for purified SNAP25 with isolated botulinum neurotoxin A light chain {ECO:0000269|PubMed:11827515}; Note=kcat is 140 min(-1) (PubMed:10694409). kcat ... | null | null | null | FUNCTION: [Botulinum neurotoxin type A]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure (PubMed:15394302, PubMed:757... | Clostridium botulinum |
P0DPI1 | BXA1_CLOBH | MPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEK... | 3.4.24.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17173035, ECO:0000269|PubMed:21434688, ECO:0000269|PubMed:9783750}; Note=Binds 1 zinc ion per subunit (PubMed:17173035, PubMed:21434688, PubMed:9783750). {ECO:0000269|PubMed:17173035, ECO:0000269|PubMed:21434688, ECO:0000269|PubMed:9783750}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020] | metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07951;PF07953;PF07952; | 1.20.58.540;2.60.120.200;2.80.10.50;1.20.1120.10;4.10.1280.10;3.90.1240.10; | Peptidase M27 family | PTM: In a bacterial culture the precursor chain is initally cleaved on the amino side of Gly-445 and is processed more slowly between Lys-448 and Ala-449 to give the final mature heavy chain sequence. {ECO:0000250|UniProtKB:P0DPI0}. | SUBCELLULAR LOCATION: [Botulinum neurotoxin A light chain]: Secreted {ECO:0000305|PubMed:9783750}. Host cytoplasm, host cytosol {ECO:0000305|PubMed:8103915, ECO:0000305|PubMed:8294407}.; SUBCELLULAR LOCATION: [Botulinum neurotoxin A heavy chain]: Secreted {ECO:0000305|PubMed:9783750}. Host synapse, host presynaptic cel... | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000269|PubMed:8103915, ECO:0000269|PubMed:8294407}; | null | null | null | null | FUNCTION: [Botulinum neurotoxin type A]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure (PubMed:8103915). Precursor ... | Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) |
P0DPK1 | BXX_CLOBO | MKLEINKFNYNDPIDGINVITMRPPRHSDKINKGKGPFKAFQVIKNIWIVPERYNFTNNTNDLNIPSEPIMEADAIYNPNYLNTPSEKDEFLQGVIKVLERIKSKPEGEKLLELISSSIPLPLVSNGALTLSDNETIAYQENNNIVSNLQANLVIYGPGPDIANNATYGLYSTPISNGEGTLSEVSFSPFYLKPFDESYGNYRSLVNIVNKFVKREFAPDPASTLMHELVHVTHNLYGISNRNFYYNFDTGKIETSRQQNSLIFEELLTFGGIDSKAISSLIIKKIIETAKNNYTTLISERLNTVTVENDLLKYIKNKIP... | 3.4.24.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:29540745}; Note=Binds 1 zinc ion per subunit (PubMed:29540745). {ECO:0000269|PubMed:29540745}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020] | metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07951;PF07953;PF07952; | 2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10; | Peptidase M27 family | PTM: An interchain disulfide bond is required for toxin stability in an artificial construct with the light chain and translocation domain; which of Cys-461 or Cys-467 forms the disulfide bond with Cys-423 in vivo is unknown. {ECO:0000305|PubMed:28770820}. | SUBCELLULAR LOCATION: [Botulinum neurotoxin type X]: Secreted {ECO:0000250|UniProtKB:P0DPI0}.; SUBCELLULAR LOCATION: [Botulinum neurotoxin X light chain]: Secreted {ECO:0000250|UniProtKB:P0DPI0}. Host cytoplasm, host cytosol {ECO:0000250|UniProtKB:P0DPI0}.; SUBCELLULAR LOCATION: [Botulinum neurotoxin X heavy chain]: Se... | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000269|PubMed:28770820}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 uM for a human VAMP1 fragment (residues 34-87) construct {ECO:0000269|PubMed:29540745}; Note=Apparent rate is 271 min(-1). {ECO:0000269|PubMed:29540745}; | null | null | null | FUNCTION: [Botulinum neurotoxin type X]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotox... | Clostridium botulinum |
P0DPK2 | H3Y1_HUMAN | MARTKQTARKATAWQAPRKPLATKAAGKRAPPTGGIKKPHRYKPGTLALREIRKYQKSTQLLLRKLPFQRLVREIAQAISPDLRFQSAAIGALQEASEAYLVQLFEDTNLCAIHARRVTIMPRDMQLARRLRREGP | null | null | null | nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). {ECO:0000250|UniProtKB:P84243}.; PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) imp... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20819935}. Chromosome {ECO:0000269|PubMed:27016736, ECO:0000269|PubMed:28334823, ECO:0000305|PubMed:20819935}. Note=Histone H3.Y-containing nucleosomes are depleted from repressive post-translational histone modifications (PubMed:28334823). Histone H3.Y-containing nucle... | null | null | null | null | null | FUNCTION: Primate-specific variant histone H3, which constitutes a core component of nucleosomes (PubMed:20819935, PubMed:27016736). Histone H3.Y-containing nucleosomes accumulate around transcription start sites and have flexible DNA ends, suggesting that they form relaxed chromatin that allows transcription factor ac... | Homo sapiens (Human) |
P0DPK3 | NT2NB_HUMAN | MPALRPALLWALLALWLCCATPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGICLNLPGSYQCQCLQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDREVWNGKEHDEN | null | null | axon guidance [GO:0007411]; cerebral cortex development [GO:0021987]; negative chemotaxis [GO:0050919]; Notch signaling pathway [GO:0007219]; positive regulation of Notch signaling pathway [GO:0045747] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; heparin binding [GO:0008201]; Notch binding [GO:0005112]; Roundabout binding [GO:0048495] | PF00008;PF07645; | 2.10.25.10; | NOTCH family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29856954, ECO:0000269|PubMed:29856955}. | null | null | null | null | null | FUNCTION: Human-specific protein that promotes neural progenitor proliferation and evolutionary expansion of the brain neocortex by regulating the Notch signaling pathway (PubMed:29561261, PubMed:29856954, PubMed:29856955). Able to promote neural progenitor self-renewal, possibly by down-regulating neuronal differentia... | Homo sapiens (Human) |
P0DPK4 | NT2NC_HUMAN | MWICPGGGGGGGGGGGGGDREDARPAPLCCGRCWRSGCAARPPRMCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGTCLNLPGSYQCQCLQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDREVWNGKEHDEN | null | null | axon guidance [GO:0007411]; cerebral cortex development [GO:0021987]; negative chemotaxis [GO:0050919]; Notch signaling pathway [GO:0007219]; positive regulation of Notch signaling pathway [GO:0045747] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; heparin binding [GO:0008201]; Roundabout binding [GO:0048495] | PF00008;PF07645; | 2.10.25.10; | NOTCH family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29856954, ECO:0000269|PubMed:33693509}. | null | null | null | null | null | FUNCTION: Human-specific protein that promotes neural progenitor proliferation and evolutionary expansion of the brain neocortex by regulating the Notch signaling pathway (PubMed:29561261, PubMed:29856954, PubMed:29856955). Able to promote neural progenitor self-renewal, possibly by down-regulating neuronal differentia... | Homo sapiens (Human) |
P0DPK5 | H3Y2_HUMAN | MARTKQTARKATAWQAPRKPLATKAARKRASPTGGIKKPHRYKPGTLALREIRKYQKSTQLLLRKLPFQRLVREIAQAISPDLRFQSAAIGALQEASEAYLVQLFEDTNLCAIHARRVTIMPRDMQLARRLRGEGAGEPTLLGNLAL | null | null | null | nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). {ECO:0000250|UniProtKB:P84243}.; PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) imp... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20819935}. Chromosome {ECO:0000305|PubMed:20819935}. | null | null | null | null | null | FUNCTION: Primate-specific variant histone H3, which constitutes a core component of nucleosomes (PubMed:20819935). 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, D... | Homo sapiens (Human) |
P0DPQ7 | GCOA_AMYS7 | MTTTERPDLAWLDEVTMTQLERNPYEVYERLRAEAPLAFVPVLGSYVASTAEVCREVATSPDFEAVITPAGGRTFGHPAIIGVNGDIHADLRSMVEPALQPAEVDRWIDDLVRPIARRYLERFENDGHAELVAQYCEPVSVRSLGDLLGLQEVDSDKLREWFAKLNRSFTNAAVDENGEFANPEGFAEGDQAKAEIRAVVDPLIDKWIEHPDDSAISHWLHDGMPPGQTRDREYIYPTIYVYLLGAMQEPGHGMASTLVGLFSRPEQLEEVVDDPTLIPRAIAEGLRWTSPIWSATARISTKPVTIAGVDLPAGTPVMLS... | 1.14.14.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:29950589}; | aromatic compound catabolic process [GO:0019439]; cholesterol catabolic process [GO:0006707] | null | cholest-4-en-3-one 26-monooxygenase activity [GO:0036199]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=guaiacol + O2 + reduced [NADH--hemoprotein reductase] = catechol + formaldehyde + H(+) + H2O + oxidized [NADH--hemoprotein reductase]; Xref=Rhea:RHEA:57424, Rhea:RHEA-COMP:14893, Rhea:RHEA-COMP:14894, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:18... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for guaiacol {ECO:0000269|PubMed:29950589}; KM=30 uM for 3-methoxycatechol {ECO:0000269|PubMed:29950589}; KM=43 uM for anisole {ECO:0000269|PubMed:29950589}; KM=15 uM for guaethol {ECO:0000269|PubMed:29950589}; KM=27 uM for 2-methylanisole {ECO:0000269|PubMed... | PATHWAY: Aromatic compound metabolism. {ECO:0000305|PubMed:29950589}. | null | null | FUNCTION: Part of a two-component P450 system that efficiently O-demethylates diverse aromatic substrates such as guaiacol and a wide variety of lignin-derived monomers. Is likely involved in lignin degradation, allowing Amycolatopsis sp. ATCC 39116 to catabolize plant biomass. GcoA binds and processes the substrate wi... | Amycolatopsis sp. (strain ATCC 39116 / 75iv2) |
P0DPQ9 | BNCR_DANRE | MGCVLLFLLLVCVPVVLPQGLRCLFCPVTSLNSSCAPVVTECPVQELCYTADGRFGRSSVLFRKGCMLRADCSRSRHQMIRGNNISFSFSCCGGHYCNSQPRAEPGGRLLLLLLPAAALTAAGAL | null | null | fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; single fertilization [GO:0007338]; sperm-egg recognition [GO:0035036] | membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | null | PF00021; | 2.10.60.10; | SPACA4/bouncer family | PTM: N-glycosylated. {ECO:0000269|PubMed:30190407}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30190407}; Lipid-anchor, GPI-anchor {ECO:0000255}. | null | null | null | null | null | FUNCTION: Oocyte-expressed fertilization factor that mediates sperm-egg binding and is essential for sperm entry into the egg (PubMed:30190407). Necessary and sufficient to mediate species-specific gamete recognition and fertilization, which is essential for vertebrate species performing external fertilization (PubMed:... | Danio rerio (Zebrafish) (Brachydanio rerio) |
P0DPR0 | HA33C_CBCP | MSQTNANDLRNNEVFFISPSNNTNKVLDKISQSEVKLWNKLSGANQKWRLIYDTNKQAYKIKVMDNTSLILTWNAPLSSVSVKTDTNGDNQYWYLLQNYISRNVIIRNYMNPNLVLQYNIDDTLMVSTQTSSSNQFFKFSNCIYEALNNRNCKLQTQLNSDRFLSKNLNSQIIVLWQWFDSSRQKWIIEYNETKSAYTLKCQENNRYLTWIQNSNNYVETYQSTDSLIQYWNINYLDNDASKYILYNLQDTNRVLDVYNSQIANGTHVIVDSYHGNTNQQWIINLI | null | null | null | extracellular region [GO:0005576] | carbohydrate binding [GO:0030246] | PF14200; | 2.80.10.50; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2205574, ECO:0000269|PubMed:7802661}. | null | null | null | null | null | FUNCTION: Agglutinates human erythrocytes (PubMed:2205574). The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host (PubMed:9421908). The hemagglutinin (HA) component is involved i... | Clostridium botulinum C phage (Clostridium botulinum C bacteriophage) |
P0DPR1 | HA33D_CBDP | MSQTNANDLRNNEVFFISPSNNTNKVLDKISQSEVKLWNKLSGANQKWRLIYDTNKQAYKIKVMDNTSLILTWNAPLSSVSVKTDTNGDNQYWYLLQNYISRNVIIRNYMNPNLVLQYNIDDTLMVSTQTSSSNQFFKFSNCIYEALNNRNCKLQTQLNSDRFLSKNLNSQIIVLWQWFDSSRQKWIIEYNETKSAYTLKCQENNRYLTWIQNSNNYVETYQSTDSLIQYWNINYLDNDASKYILYNLQDTNRVLDVYNSQIANGTHVIVDSYHGNTNQQWIINLI | null | null | null | extracellular region [GO:0005576] | carbohydrate binding [GO:0030246] | PF14200; | 2.80.10.50; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11713244, ECO:0000269|PubMed:17581814, ECO:0000269|PubMed:8569530, ECO:0000269|PubMed:9802560}. | null | null | null | null | null | FUNCTION: The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host. Involved in binding to the small intestine through interactions with glycolipids and glycoproteins containing sialic ac... | Clostridium botulinum D phage (Clostridium botulinum D bacteriophage) |
P0DPR2 | RNF43_XENTR | MNRARLQLASLWLLLTVTLQAVASAMGTTEREMDVKALIRVTPLQAEESGGVGQGNLTLEGLFARVAEISPAEGRLLQFHPLSLCNTSEDDQTKPGFISIVKLETPDRDTQPCLSLANKARLAGERGAHAVLFDITNDRGALQQLQQPAGINQPVVLIWGPDAEKLMDVVNKNKEALVKIEVQEQPKWLHHDIWILLTVAGTVMFFVLYAVARLLCRQPPPQDSIQQQTLLAISRLGTRRYQQRMLKDQRASGGWVETASTSSSVPVCAICLEEFTDGQELRILPCCHEYHLGCVDPWLRQNHTCPLCMYDILDSGTPPR... | 2.3.2.27 | null | protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]; Wnt receptor catabolic process [GO:0038018]; Wnt signaling pathway [GO:0016055] | endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886] | frizzled binding [GO:0005109]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF13639;PF18212; | 3.50.30.30;3.30.40.10; | ZNRF3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q68DV7}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q68DV7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q68DV7}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q68DV7}. Nucleus envelope {ECO:0000250|UniProtKB:Q68DV7}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q68DV7}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q68DV7}. | null | null | FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway (By similarity). Along with RSPO2 and Z... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
P0DPS3 | VASP1_VIPAA | VIGGDECNINEHPFLVALHTARXXRFYCAGTLINQEWVLTAARCDRXXXXXILGVHSKXXXXXXXXXXXXXXXXXXXXXXTYTRWDKDIMLIRLKRXXXXXXXXXXXXXXXXXXXXXXXXXIMGWGTITTTKVTYPDVPHCADINMFDYSVCQKXXXKLPEKSRTLCAGILQGGIDSCKGISGGPLICNGEIQGIVSYGK | null | null | regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | extracellular region [GO:0005576]; secretory granule [GO:0030141] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: N-glycosylated. The protein exist in multiple isoforms. {ECO:0000269|PubMed:24269689}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24269689}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48.2 uM for N-benzoyl-Phe-Val-Arg-p-nitroanilide {ECO:0000269|PubMed:24269689}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:24269689}; | null | FUNCTION: Snake venom serine protease active on several blood coagulation enzymes. It completely cleaves fibrinogen Aalpha chain (FGA) after 120 minutes, partially cleaves Bbeta chain (FGB) (overnight) and has no activity on gamma chain. It does not release fibrinopeptides A and/or B exclusively, since the enzyme does ... | Vipera ammodytes ammodytes (Western sand viper) |
P0DPS4 | PA2B_CERCE | NLYQFGKMINHMVGKSPIFSYGDYGCYCGWGGKGTPVDATDRCCFVHDCCYGRANGCDPKLSTYSYNFQNGNIVCGNKYGCLRHICECDRVAAICFGENVNTYDKKFLSSSRCRQTSEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P14418}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418}; | arachidonic acid secretion [GO:0050482]; killing of cells of another organism [GO:0031640]; 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:24384926}. | 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: Basic phospholipase A2 that inhibits ADP-, thrombin- and arachidonic acid-induced platelet aggregation (PubMed:24384926, PubMed:30239061). It also exhibits anticoagulant effects upon human plasma in vitro (PubMed:30239061). It induces a high hemolytic activity reaching its maximum after 24 hours (PubMed:24384... | Cerastes cerastes (Horned desert viper) |
P0DQD1 | PLA2_WALAE | NLYQFKNMVQCVGTQLCVAYVKYGCYCGPG | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29885399}; | arachidonic acid secretion [GO:0050482]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; phospholipase A2 activity [GO:0004623] | null | 1.20.90.10; | Phospholipase A2 family, Group I subfamily | PTM: Glycosylated. {ECO:0000269|PubMed:29885399}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29885399}. | 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:0000305}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=2100 umol/min/mg enzyme {ECO:0000269|PubMed:29885399}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:29885399}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:29885399}; | FUNCTION: Relatively highly potent phospholipase A2 that displays potent antimicrobial and hemolytic activities. It does not show cytotoxic effects on the three human cell lines tested. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. It shows similar potencies on both Gra... | Walterinnesia aegyptia (Desert black snake) |
P0DQD2 | INLB_LISMO | MKEKHNPRRKYCLISGLAIIFSLWIIIGNGAKVQAETITVPTPIKQIFSDDAFAETIKDNLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVTKLFLNGNKLTDIKPLANLKNLGWLFLDENKVKDLSSLKDLKKLKSLSLEHNGISDINGLVHLPQLESLYLGNNKITDITVLSRLTKLDTLSLEDNQISDIVPLAGLTKLQNLYLSKNHISDLRALAGLKNLDVLELFSQECLNKPINHQSNLVVPNTVKNTDGSLVTPEIISDDGDYEKPNVKWHLPEFTNEVSFIFYQPVTIGKAKARFHGRVTQPLK... | null | null | null | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | heparin binding [GO:0008201]; lipid binding [GO:0008289] | PF09479;PF13457;PF12354;PF12799;PF08191; | 2.30.30.170;2.60.40.1220;2.60.40.4270;3.80.10.10; | Internalin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DQD3}. Cytoplasm {ECO:0000269|PubMed:11929538}. Cell membrane {ECO:0000269|PubMed:11929538}. Note=Approximately half the protein is secreted. Cell surface association is mediated by the GW domains and can occur when protein is added externally; externally added pr... | null | null | null | null | null | FUNCTION: Mediates the entry of L.monocytogenes into normally non-phagocytic mammalian host cells (PubMed:19900460). Its host receptor is hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-phosphorylated in response to InlB. Downstream targets MAPK1/MAPK3 (Erk1/2) and AKT are pho... | Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
P0DQD3 | INLB_LISMG | MKEKHNPRRKYCLISGLAIIFSLWIIIGNGAKVQAETITVSTPIKQIFPDDAFAETIKDNLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVTKLFLNGNKLTDIKPLTNLKNLGWLFLDENKIKDLSSLKDLKKLKSLSLEHNGISDINGLVHLPQLESLYLGNNKITDITVLSRLTKLDTLSLEDNQISDIVPLAGLTKLQNLYLSKNHISDLRALAGLKNLDVLELFSQECLNKPINHQSNLVVPNTVKNTDGSLVTPEIISDDGDYEKPNVKWHLPEFTNEVSFIFYQPVTIGKAKARFHGRVTQPLK... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10635330, ECO:0000269|PubMed:15020228}; Note=Binds 2 Ca(2+) ions; binding site 1 has a 10-fold higher affinity binding site 2 (PubMed:10635330, PubMed:15020228). Loss of Ca(2+)-binding has no measurable effect on host receptor activation or inv... | entry of bacterium into host cell [GO:0035635] | cell surface [GO:0009986]; extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | heparin binding [GO:0008201]; lipid binding [GO:0008289]; metal ion binding [GO:0046872] | PF09479;PF13457;PF12354;PF12799;PF08191; | 2.30.30.170;2.60.40.1220;2.60.40.4270;3.80.10.10; | Internalin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10594817, ECO:0000269|PubMed:9282740}. Cell surface {ECO:0000269|PubMed:9282740}. Cell membrane {ECO:0000269|PubMed:10594817}. Note=Approximately half the protein is secreted (PubMed:10594817, PubMed:9282740). Cell surface association is mediated by the GW domains and ... | null | null | null | null | null | FUNCTION: Mediates the entry of L.monocytogenes into normally non-phagocytic mammalian host cells (Probable) (PubMed:11081636, PubMed:9282740). Its host receptor is hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-phosphorylated in response to InlB in human, green monkey, mouse... | Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness) |
P0DQH9 | OXLAB_CERCE | ADDKNPLEECFREADYEEFLEIAKVTVLEASERNDKEDWYANLGPMRLPEKLNEFVQETENGWYFIKYPVKPSEEGKSAGQLYEESLRKSAGQLYQESLGKAHDDIFAYEKRFDEIVDGMDKLPTSMYQAIQERINFKPPLPPKKYAMGAITTFTPYQFQHFSEALTAPVGR | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | 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] | null | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30647580}. | 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:30647580}; CATALYTIC ACTIVITY: Reaction=H2O... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.67 mM for L-Leu (Cc-LAAOI isoform) {ECO:0000269|PubMed:30647580}; KM=0.82 mM for L-Leu (Cc-LAAOII isoform) {ECO:0000269|PubMed:30647580}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 (Cc-LAAOI) and 7 (Cc-LAAOII). {ECO:0000269|PubMed:30647580}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 (Cc-LAAOI) and 60 (Cc-LAAOII) degrees Celsius. {ECO:0000269|PubMed:30647580}; | 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:30647580). Shows high specificity for L-Arg, L-Met, L-Phe, L-Leu, L-Tyr, L-Ile and L-Trp, low specificity for L-V... | Cerastes cerastes (Horned desert viper) |
P0DQM9 | CX07_CONZO | GFRSPCPPFC | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; toxin activity [GO:0090729] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32234761}. | null | null | null | null | null | FUNCTION: Inhibits the human alpha-3-beta-4/CHRNA3-CHRNB4 (IC(50)=15.7 uM) and alpha-7/CHRNA7 (IC(50)=77.2 uM) nicotinic acetylcholine receptor (nAChR) (PubMed:32234761). Incomplete inhibition of responses is observed for both subtypes, indicating a potential non-competitive mode of action (PubMed:32234761). {ECO:00002... | Conus zonatus (Zoned cone) |
P0DQN3 | TXPR1_BUMPU | ECRYWLGGCSAGQTCCKHLVCSRRHGWCVWDGTFS | null | null | null | extracellular region [GO:0005576] | calcium channel regulator activity [GO:0005246]; ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 54 (ProTx-1) subfamily | PTM: An unnatural amidation at Ser-35 provokes a 14-fold increased toxin ability to inhibit Nav1.2/SCN2A and a ~2-fold decreased toxin ability to inhibit both Nav1.5/SCN5A and Nav1.7/SCN9A. {ECO:0000269|PubMed:32511987}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32511987}. | null | null | null | null | null | FUNCTION: Ion channel impairing toxin that inhibits voltage-gated calcium channel Cav3.1/CACNA1G (IC(50)=53 nM), voltage-gated potassium channels Kv2.1/KCNB1 (IC(50)=411 nM), all sodium channels tested (Nav1.2/SCN2A (IC(50)=60-104 nM), Nav1.5/SCN5A (IC(50)=76-358 nM), Nav1.6/SCN8A (IC(50)=21-133 nM), Nav1.7/SCN9A (IC(5... | Bumba pulcherrimaklaasi (Tarantula spider) (Euathlus pulcherrimaklaasi) |
P0DQP0 | PV22_POMMA | MVKKIHFVMERHASIVAFLLAVLALTESQAFTSVKLPRDEHWPYNYVSVGPAGVWAVNRQNKLFYRTGTYGDNANMGSGWQFKQDGVGQVDVGKDKVGYINLSGGSLFRIEGISQANPVGGTPKSWEWWTKYIGMSLREDTRFSSRIENQNKVLTFTFRTCFWASRITNWCFADSSYTETVTAGGSGTWITKSQLKYKSGTFGNPDTEGGDWILVDSGSFQHVSSGSGVVLAVRSNGELVQRTGITCSLPQGTGWTSMLNSMSRVDTYGTVAWAVDTAGDLYFINL | null | null | autophagosome maturation [GO:0097352] | autophagosome membrane [GO:0000421]; extracellular region [GO:0005576]; lysosomal membrane [GO:0005765]; other organism cell membrane [GO:0044218] | carbohydrate binding [GO:0030246]; nutrient reservoir activity [GO:0045735]; phosphatidylinositol-3-phosphate binding [GO:0032266]; toxin activity [GO:0090729] | PF19193; | null | Tectonin family | PTM: PV2 is a very high density lipoprotein (VHDL). It contains 3.75% of lipids. The major lipid classes are free sterols and phospholipids and also have significant quantities of energy-providing triacylglycerides and free fatty acids. {ECO:0000250|UniProtKB:P0C8G7}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane {ECO:0000269|PubMed:32231667, ECO:0000269|PubMed:32446810}. | null | null | null | null | null | FUNCTION: The egg defensive protein perivitellin-2 is a pore-forming two-subunit glycoprotein that affects both the nervous and digestive systems of mammals (PubMed:32231667, PubMed:32446810). In addition, it is a source of both structural and energetic molecules during embryonic development (By similarity). The tachyl... | Pomacea maculata (Giant applesnail) |
P0DQP9 | PA2B1_BOTBZ | SLWEFGQMILKETGKLPFPYYGAYGCYCGWGGRRGPKDATDRCCYVHDCKQICECDKAAAVCFRERKYMAYLRVLCKK | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:18602430}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; defense response to bacterium [GO:0042742]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; 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]; 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:18602430}. | 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:18602430}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits myotoxin and anticoagulant activity (PubMed:18602430). Displays edema-inducing activities in mouse paw (PubMed:18602430). Also displays cytotoxic activity against some cell lines and myotubes, and antimicrobial activities against E.coli, C.albicans and Leishma... | Bothrops brazili (Brazil's lancehead) |
P0DQQ0 | PA2B3_BOTBZ | SLWEWGQMILKETGKNPFPYYGAYGCYCGWGGRRKPKDATDRCCFVHDCCRYKKLTGCPKTNDRYSYSRLDYTIVCGEDDPCKEICECDKAAAVCFRENLRTYNKKYMAHLRVLCKKDKPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:19539640}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; defense response to bacterium [GO:0042742]; 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:19539640}. | 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:19539640}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:19539640}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35-45 degrees Celsius. {ECO:0000269|PubMed:19539640}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits myotoxin and anticoagulant activity (PubMed:19539640). Displays edema-inducing activities in mouse paw (PubMed:19539640). Also displays cytotoxic activity against some cell lines and myotubes, and antimicrobial activities against E.coli, C.albicans and Leishma... | Bothrops brazili (Brazil's lancehead) |
P0DQQ4 | PDE_CRODO | GLKEPVQPQVSCRYRCNETFSRMASGCSCDDKCTERQACCSDYEDTCVLPTQSWSCSKLRCGEKRIANVLCSCSEDCLEKKDCCTDYKTICKGETSWLKDKCASSGATQCPAGFEQSPLILFSMDGFRAGYLENWDSLMPNINKLKTCGTHAKYMRAVYPTKTFVNHYTIATGLYPESHGIIDNNIYDVNLNLNFSLSSSTARNPAWWGGQPIWHTATYQGLKAATYFWPGSEVKINGSYPTIFKNYDKSIPFEARVTEVLKWLDLPKAKRPDFFTLYIEEPDTTGHKYGPVSGEIIKALQMADRTLGMLMEGLKQRNLH... | 3.6.1.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:W8E7D1}; Note=Binds 2 divalent metal cations per subunit. {ECO:0000250|UniProtKB:W8E7D1}; | nucleoside triphosphate catabolic process [GO:0009143] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; nucleoside triphosphate diphosphatase activity [GO:0047429]; toxin activity [GO:0090729] | PF01223;PF01663;PF01033; | 4.10.410.20;3.40.720.10;3.40.570.10; | Nucleotide pyrophosphatase/phosphodiesterase family | PTM: N-glycosylated. Glycosylation counts for an increased mass of ~9%. {ECO:0000269|PubMed:33636276}.; PTM: Contains 16 disulfide bonds. {ECO:0000305|PubMed:33636276}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33636276}. | CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:W8E7D1}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.38 mM for bis(p-nitrophenyl) phosphate {ECO:0000269|PubMed:33636276}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:33636276}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:33636276}; | FUNCTION: Hydrolyzes ADP with high activity. Shows weak or no activity on 5'-AMP, 5'-GMP, 3'-AMP, ATP, cAMP, and cGMP (By similarity). Is devoid of monophosphatase and proteinase activities (By similarity). Inhibits ADP-induced platelet aggregation and is cytotoxic to human keratinocytes (PubMed:33636276). Kinetic para... | Crotalus durissus collilineatus (Brazilian rattlesnake) |
P0DRC8 | VM1_MACLN | QFSDCSKDEYQRYLT | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:20398688}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P85420}; | envenomation resulting in damage of muscle extracellular matrix in another organism [GO:0044523]; proteolysis [GO:0006508] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | null | null | Venom metalloproteinase (M12B) family, P-I subfamily | PTM: Glycosylated. {ECO:0000250|UniProtKB:P83255}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20398688}. | null | null | null | null | null | FUNCTION: Snake venom metalloproteinase that disrupts the muscle fibers interaction with extracellular matrix proteins. In vitro, is able to proteolyse extracellular matrix proteins surrounding muscle fibers such as laminin and fibronectin, but does not show any direct cytolytic activity towards the myogenic cell line ... | Macrovipera lebetina transmediterranea (Blunt-nosed viper) (Vipera lebetina transmediterranea) |
P0DSE0 | APOE_ACIJB | MKVLWAALLVALLAGCWADVEPEPQLERELEPEAPWQASQPWEQALGRFRDYLRWVQTLSDQVQEEVLNTQVTQELTVLMEETMKEVKAYREELEEQLGPMASETQARVAKELQAAQARLGSDMEDVRNRLAQYRSEVQAMLGQSAEELRARLASHLRKLRKRLLRDAEDLHKRLAVYRAGVREGAERSVSSIRERFWPLVEQARARNANVAAVAAQPLRERAEALGQQLRGRLDEVREQVEEMRVKMEEQADQMRQQAEAFQARLKSWFEPLVQDMQRQWAGLVEKLQAAVGTSPTTAPVEKQ | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of amyloid-beta clea... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Acinonyx jubatus (Cheetah) |
P0DSE1 | TRAR1_HUMAN | MVLKFSVSILWIQLAWVSTQLLEQSPQFLSIQEGENLTVYCNSSSVFSSLQWYRQEPGEGPVLLVTVVTGGEVKKLKRLTFQFGDARKDSSLHITAAQPGDTGLYLCAGGGSQGNLIFGKGTKLSVKPIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESSCDVKLVEKSFETDTNLNFQNLSVIGFRILLLKVAGFNLLMTLRLWSS | null | null | adaptive immune response [GO:0002250]; response to bacterium [GO:0009617]; T cell activation involved in immune response [GO:0002286] | cell surface [GO:0009986]; T cell receptor complex [GO:0042101] | null | PF09291;PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29997621}. | null | null | null | null | null | FUNCTION: The alpha chain of TRAV27*01J42*01C*01/TRBV19*01J2S7*01C*02 alpha-beta T cell receptor (TR) clonotype that is specific for HLA-A*02:01-restricted M/matrix protein 1 immunodominant epitope GILGFVFTL of influenza A virus (IAV). Classified as a public TR clonotype, it is preferentially selected in effector memor... | Homo sapiens (Human) |
P0DSE2 | TRBR1_HUMAN | MSNQVLCCVVLCLLGANTVDGGITQSPKYLFRKEGQNVTLSCEQNLNHDAMYWYRQDPGQGLRLIYYSQIVNDFQKGDIAEGYSVSREKKESFPLTVTSAQKNPTAFYLCASSIRSSYEQYFGPGTRLTVTEDLKNVFPPKVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSESYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDSRG | null | null | adaptive immune response [GO:0002250]; cell surface receptor signaling pathway [GO:0007166]; T cell activation involved in immune response [GO:0002286] | cell surface [GO:0009986]; T cell receptor complex [GO:0042101] | null | PF07654;PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29997621}. | null | null | null | null | null | FUNCTION: The beta chain of TRAV27*01J42*01C*01/TRBV19*01J2S7*01C*02 alpha-beta T cell receptor (TR) clonotype that is specific for HLA-A*02:01-restricted M/matrix protein 1 immunodominant epitope GILGFVFTL of influenza A virus (IAV). Classified as a public TCR clonotype, it is preferentially selected in effector memor... | Homo sapiens (Human) |
P0DSI1 | CDIA_ECONC | MHQPPVRFTYRLLSYLISTIIAGQPLLPAVGAVITPQNGAGMDKAANGVPVVNIATPDGAGISHNRFTDYNVGKEGLILNNATGKLNPTQLGGLIQNNPNLKAGGEAKGIINEVTGGNRSLLQGYTEVAGKAANVMVANPYGITCDGCGFINTPHATLTTGRPVMNADGSLQALEVTEGSITINGAGLDGTRSDAVSIIARATEVNAALHAKDLTVTAGANRITADGRVSALKGEGDVPKVAVDTGALGGMYARRIHLTSTESGVGVNLGNLYARDGDITLDASGRLTVNNSLATGAVTAKGQGVTLTGDHKAGGNLSVS... | 3.1.-.- | null | null | extracellular region [GO:0005576] | endonuclease activity [GO:0004519]; toxin activity [GO:0090729] | PF21726;PF13332;PF04829;PF05860; | 2.160.20.10; | CdiA toxin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell, target cell cytoplasm {ECO:0000269|PubMed:28973472}. Note=Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner. {ECO:0000305}. | null | null | null | null | null | FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (target cell counts decrease about 10... | Escherichia coli (strain NC101) |
P0DSO6 | MAMKL_PARM1 | MIVNDNQNILYVGIDFGYSKTVIMTSRGKSLSLKSLVGYPKDFVGLARLGRPYLVGDEAFEMRSYLHLRNPLLDGLLNPISEQDIDVTRHFISHIIKCAEPAAGEKVFAVIGVTPRFTAANKKLLLKLAQEYCQNVLLMSAPFLAGNSIGKASGSIIIDIGAWTTDICAMKGRIPRPEDQSSIAKAGSYIDERLKNSILERYPALQINANIARMVKEQFAFVGRPQLVAACEFRSAGKAVRCDVTEQVRAACESPFAEIAERIGAVLCVVPPEDQALVLKNIVITGAGAQIRGLPEYVKSMLAPYGDARVSIANEPLMEA... | 3.6.1.- | null | magnetosome assembly [GO:0140923] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF06723; | 3.30.420.40; | FtsA/MreB family, MamK subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:20161777, ECO:0000305|PubMed:24957623}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20161777, ECO:0000269|PubMed:24957623}. Note=Protein forms filaments extending along most of the cell associated with its inner curvature, in the correct position to be filaments that ... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24957623}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=127 uM for ATP {ECO:0000269|PubMed:24957623}; | null | null | null | FUNCTION: Protein with ATPase activity which forms pole-to-pole filaments in vivo, probably with MamK. Efficient filament formation requires MamK. Probably promotes turnover of MamK filaments, by providing a monomer pool (PubMed:24957623). In vivo, in the absence of its paralog MamK, forms thin filaments from pole to p... | Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum) |
P0DSP1 | SORL_RAT | MATRSSRRESRLPFLFTLVALLPPGALGGGWTQRLHGGGAPLPQDRGFFVVQGDPHELRLGTHGDAWGASPAARKPLRTRRSAALQPQPIQVYGQVSLNDSHNQMVVHWAGEKSNVIVALARDSLALTRPKSSDVYVSYDYGKSFNKISEKLNFGVGNSSEAVISQFYHSPADNKRYIFVDAYARYLWITFDFGSTIHGFSIPFRAADLLLHSKASNLLLGFDSSHPNKQLWKSDDFGQTWIMIQEHVKSFSWGIDPYDQPNTIYIERHEPFGFSTVFRSTDFFQSRENQEVILEEVRDFQLRDKYLFATKVVHLPGSQQ... | null | null | adaptive thermogenesis [GO:1990845]; cell migration [GO:0016477]; diet induced thermogenesis [GO:0002024]; endosome to plasma membrane protein transport [GO:0099638]; insulin receptor recycling [GO:0038020]; negative regulation of amyloid precursor protein catabolic process [GO:1902992]; negative regulation of amyloid-... | cell surface [GO:0009986]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi cisterna [GO:0031985]; Golgi membrane [GO:0000139]; ... | amyloid-beta binding [GO:0001540]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; low-density lipoprotein particle binding [GO:0030169]; neuropeptide binding [GO:0042923]; small GTPase binding [GO:0031267]; transmembrane signaling receptor activity [GO:0004888] | PF00041;PF00057;PF00058;PF15902;PF15901; | 2.10.70.80;3.30.60.270;2.60.40.10;4.10.400.10;2.120.10.30;2.130.10.10; | VPS10-related sortilin family, SORL1 subfamily | PTM: Within the Golgi apparatus, the propeptide may be cleaved off by FURIN or a furin-like protease. After cleavage, the propeptide interacts with the mature protein N-terminus, preventing the association with other ligands. At the cell surface, partially subjected to proteolytic shedding that releases the ectodomain ... | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92673}. Endosome membrane {ECO:0000... | null | null | null | null | null | FUNCTION: Sorting receptor that directs several proteins to their correct location within the cell. Along with AP-1 complex, involved Golgi apparatus - endosome sorting. Sorting receptor for APP, regulating its intracellular trafficking and processing into amyloidogenic-beta peptides. Retains APP in the trans-Golgi net... | Rattus norvegicus (Rat) |
P0DSP2 | CDNE_ELIME | MNFSEQQLINWSRPVSTTEDLKCQNAITQITAALRAKFGNRVTIFLQGSYRNNTNVRQNSDVDIVMRYDDAFYPDLQRLSESDKAIYNAQRTYSGYNFDELKADTEEALRNVFTTSVERKNKCIQVNGNSNRITADVIPCFVLKRFSTLQSVEAEGIKFYSDDNKEIISFPEQHYSNGTEKTNQTYRLYKRMVRILKVVNYRLIDDGEIADNLVSSFFIECLVYNVPNNQFISGNYTQTLRNVIVKIYEDMKNNADYTEVNRLFWLFSNRSPRTRQDALGFMQKCWNYLGYQ | 2.7.7.-; 2.7.7.65; 2.7.7.85 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30787435}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:30787435}; | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | null | 3',3'-cyclic GMP-AMP synthase activity [GO:0140701]; ATP binding [GO:0005524]; diadenylate cyclase activity [GO:0106408]; diguanylate cyclase activity [GO:0052621]; GTP binding [GO:0005525]; metal ion binding [GO:0046872] | PF18144; | 3.30.460.10; | CD-NTase family, E01 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85; Evidence={ECO:0000269|PubMed:30787435}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35656; Evidence={ECO:0000305|PubMed:30787435}; CATALYTIC ACTIVITY:... | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:30787435). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific s... | Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) |
P0DSP3 | CDNE2_LEGPN | MSIDWEQTFRKWSKPSSETESTKAENAERMIKAAINSSQILSTKDISVFPQGSYRNNTNVREDSDVDICVCLNTLVLSDYSLVPGMNDKLAELRTASYTYKQFKSDLETALKNKFGTLGVSRGDKAFDVHANSYRVDADVVPAIQGRLYYDKNHNAFIRGTCIKPDSGGTIYNWPEQNYSNGVNKNKSTGNRFKLIVRAIKRLRNHLAEKGYNTAKPIPSYLMECLVYIVPDQYFTGDSYKTNVENCINYLYNQIDSSDWTEINEIKYLFGSHQMWNKTQVKEFLLTAWSYIQKN | 2.7.7.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:37604815}; Note=Binds 2-3 Mg(2+) ions per subunit; the third Mg(2+), liganded by Asp-65, Asp-128 and Asp-139, is only seen in complex with a substrate analog (PubMed:37604815). It is unclear if it is physiological (PubMed:37604815). {ECO:000026... | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | null | metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; nucleotidyltransferase activity [GO:0016779] | PF01909; | 3.30.460.10; | CD-NTase family, E02 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2 UTP = c-di-UMP + 2 diphosphate; Xref=Rhea:RHEA:60480, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:143807; Evidence={ECO:0000269|PubMed:30787435}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60481; Evidence={ECO:0000305|PubMed:30787435}; CATALYTIC ACTIVITY: Reaction=CTP + UT... | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:30787435). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific s... | Legionella pneumophila |
P0DSP4 | CDND2_ENTH5 | MELQPQFNEFLANIRPTDTQKEDWKSGARTLRERLKNFEPLKEIVVSTFLQGSIRRSTAIRPLGDKRPDVDIVVVTNLDHTRMSPTDAMDLFIPFLEKYYPGKWETQGRSFGITLSYVELDLVITAIPESGAEKSHLEQLYKSESVLTVNSLEEQTDWRLNKSWTPNTGWLSESNSAQVEDAPASEWKAHPLVLPDREKNEWGRTHPLAQIRWTAEKNRLCNGHYINLVRAVKWWRQQNSEDLPKYPKGYPLEHLIGNALDNGTTSMAQGLVQLMDTFLSRWAAIYNQKSKPWLSDHGVAEHDVMARLTAEDFCSFYEGI... | 2.7.7.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:33836064, ECO:0000312|PDB:7D4J, ECO:0000312|PDB:7D4O}; Note=Binds 3 Mg(2+) ions per subunit; 1 is probably structural, the other 2 are probably catalytic. {ECO:0000269|PubMed:33836064}; | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | null | ATP binding [GO:0005524]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779] | PF18144; | null | CD-NTase family, D02 subfamily | PTM: In bacteria expressing cap4-dncV-cap2-cap3, this protein is conjugated to a number of other proteins by Cap2, probably via this protein's C-terminal Ala residue (PubMed:36755092, PubMed:36848932). More conjugated DncV is found in the absence of Cap3 (PubMed:36848932). {ECO:0000269|PubMed:36755092, ECO:0000269|PubM... | null | CATALYTIC ACTIVITY: Reaction=2 ATP + GTP = 3',3',3'-cAAG + 3 diphosphate; Xref=Rhea:RHEA:60476, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:143810; Evidence={ECO:0000269|PubMed:30787435, ECO:0000269|PubMed:34077735, ECO:0000269|PubMed:36755092}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:30787435, PubMed:34077735, PubMed:36755092). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages (PubMed:32544385, PubMed:36755092, PubMed:36796558). The CD-NTase pro... | Enterobacter hormaechei subsp. hoffmannii (strain UCI 50) |
P0DSX5 | MCEL_VAR67 | MDANVVSSSTIATYIDALAKNASELEQGSTAYEINNELELVFIKPPLITLTNVVNISTIQESFIRFTVTNKEGVKIRTKIPLSKVHGLDVKNVQLVDAIDNIVWEKKSLVTENRLHKACLLRLSTEERHIFLDYKKYGSSIRLELVNLIQAKTKNFTIDFKLKYFLGSGAQSKSSLLHAINHPKSRPNTSLEIEFTPRDNETVPYDELIKELTTFSRHIFMASPENVILSPPINAPIKTFMLPKQDIVGMDLENLYAVTKTDGIPITIRVTSKGLYCYFTHLGYIIRYPVKRIIDSEVVVFGEAVKDKNWTVYLIKLIEP... | 2.1.1.56; 2.7.7.50; 3.6.1.74 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04298}; | null | virion component [GO:0044423] | inorganic triphosphate phosphatase activity [GO:0050355]; metal ion binding [GO:0046872]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA guanylyltransferase activity [GO:0004484]; polynucleotide 5'-phosphatase activity [GO:0004651]; RNA binding [GO:000... | PF21004;PF21005;PF10640;PF03291; | 2.40.50.830;3.20.100.20;3.30.470.140;3.40.50.150; | DsDNA virus mRNA guanylyltransferase family; Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0 methyltransferase family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. | CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Ev... | null | null | null | null | FUNCTION: Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) met... | Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus) |
P0DSX6 | MCEL_VARV | MDANVVSSSTIATYIDALAKNASELEQGSTAYEINNELELVFIKPPLITLTNVVNISTIQESFIRFTVTNKEGVKIRTKIPLSKVHGLDVKNVQLVDAIDNIVWEKKSLVTENRLHKECLLRLSTEERHIFLDYKKYGSSIRLELVNLIQAKTKNFTIDFKLKYFLGSGAQSKSSLLHAINHPKSRPNTSLEIEFTPRDNETVPYDELIKELTTFSRHIFMASPENVILSPPINAPIKTFMLPKQDIVGMDLENLYAVTKTDGIPITIRVTSKGLYCYFTHLGYIIRYPVKRIIDSEVVVFGEAVKDKNWTVYLIKLIEP... | 2.1.1.56; 2.7.7.50; 3.6.1.74 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04298}; | null | virion component [GO:0044423] | inorganic triphosphate phosphatase activity [GO:0050355]; metal ion binding [GO:0046872]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA guanylyltransferase activity [GO:0004484]; polynucleotide 5'-phosphatase activity [GO:0004651]; RNA binding [GO:000... | PF21004;PF21005;PF10640;PF03291; | 2.40.50.830;3.20.100.20;3.30.470.140;3.40.50.150; | DsDNA virus mRNA guanylyltransferase family; Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0 methyltransferase family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. | CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Ev... | null | null | null | null | FUNCTION: Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) met... | Variola virus |
P0DTA4 | PCCA_PIG | MAGLWVGGSVLVAAGRRGSRSPRPLMRSVALWTLKHVPQYSRQRLLVSRSLCLAGYDSNEKTFDKILIANRGEIACRVIKTCKKMGIKTVAVHSDVDASSVHVTMADEAVCVGPAPTSKSYLNMDAIMEAVRTTRAQAVHPGYGFLSENKEFAKCLAAEGVIFIGPDTHAIQAMGDKIESKLLAKKAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDSETRRAMGEQA... | 6.4.1.3 | 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 2 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:5758... | short-chain fatty acid catabolic process [GO:0019626] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; methylcrotonoyl-CoA carboxylase activity [GO:0004485]; propionyl-CoA carboxylase activity [GO:0004658]; urea carboxylase activity [GO:0004847] | PF02785;PF00289;PF00364;PF02786;PF18140; | 2.40.50.100;3.30.700.30;3.40.50.20;3.30.1490.20;3.30.470.20; | null | PTM: Acetylated. {ECO:0000250|UniProtKB:Q91ZA3}.; PTM: The biotin cofactor is covalently attached to the C-terminal biotinyl-binding domain and is required for the catalytic activity (By similarity). Biotinylation is catalyzed by HLCS (By similarity). {ECO:0000250|UniProtKB:P05165}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:13752080}. | CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392, ChEBI:CHEBI:456216; EC=6.4.1.3; Evidence={ECO:0000269|PubMed:1375... | null | PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3. {ECO:0000269|PubMed:13752080}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.2 for the propionyl-CoA carboxylase activity. {ECO:0000269|PubMed:13752080}; | null | FUNCTION: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites (PubMed:13752080). Propionyl-CoA carboxylase catalyz... | Sus scrofa (Pig) |
P0DTC1 | R1A_SARS2 | MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAPHGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQENWNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAWYTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTL... | 2.7.7.50; 3.4.19.12; 3.4.22.-; 3.4.22.69 | null | induction by virus of host autophagy [GO:0039520]; methylation [GO:0032259]; proteolysis [GO:0006508]; symbiont-mediated degradation of host mRNA [GO:0039595]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signa... | double membrane vesicle viral factory outer membrane [GO:0062243]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell endosome [GO:0044174]; host cell Golgi apparatus [GO:0044177]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; G-quadruplex RNA binding [GO:0002151]; ISG15-specific peptidase activity [GO:0019785]; lipid binding [GO:0008289]; methyltransferase activity [GO:0008168]; omega peptidase activity ... | PF16251;PF11501;PF12379;PF12124;PF11633;PF09401;PF19212;PF19211;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF01661;PF05409; | 1.10.8.1190;2.60.120.1680;3.10.20.350;3.10.20.540;6.10.140.2090;1.10.150.420;3.40.30.150;3.40.220.10;1.10.1840.10;3.40.220.20;3.40.220.30;1.10.8.370;3.30.70.3540;2.40.10.250;3.40.50.11020;2.40.10.10; | Coronaviruses polyprotein 1ab family | PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed. {ECO:0000250|UniProtKB:P0C6X7}. | SUBCELLULAR LOCATION: [Host translation inhibitor nsp1]: Host cytoplasm {ECO:0000269|PubMed:33060197}.; SUBCELLULAR LOCATION: [Non-structural protein 2]: Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endosome {ECO:0000269|PubMed:33060197}.; SUBCELLULAR LOCATION: [Papain-like protease nsp3]: Host endoplasmic reticu... | CATALYTIC ACTIVITY: [Papain-like protease nsp3]: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:32726803};... | null | null | null | null | FUNCTION: [Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Host translation inhibitor nsp1]: Inhibits host translation by associating wit... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTC2 | SPIKE_SARS2 | MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFDNPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRV... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; membrane fusion [GO:0061025]; positive regulation of viral entry into host cell [GO:0046598]; receptor-mediated endocyt... | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; host cell plasma membrane [GO:0020002]; host cell surface [GO:0044228]; host extracellular space [GO:0043655]; membrane [GO:0016020]; plasma membrane [GO:0005886]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789]; identical protein binding [GO:0042802]; receptor ligand activity [GO:0048018]; structural constituent of virion [GO:0039660] | PF16451;PF09408;PF19209;PF01601; | 1.20.5.300;3.30.70.1840;1.20.5.790;2.60.120.960; | Betacoronaviruses spike protein family | PTM: The cytoplasmic Cys-rich domain is palmitoylated. Palmitoylated spike proteins drive the formation of localized ordered cholesterol and sphingo-lipid-rich lipid nanodomains in the early Golgi, where viral budding occurs. {ECO:0000269|PubMed:34599882}.; PTM: Specific enzymatic cleavages in vivo yield mature protein... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32979942}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:34504087}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMe... | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. The major receptor is host ACE2 (PubMed:32142651, PubMed:32155444, PubMed:33607086). When S2/S2' has been cleaved, binding to the receptor triggers direct fusion at the cell membrane (PubM... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTC3 | AP3A_SARS2 | MDLFMRIFTIGTVTLKQGEIKDATPSDFVRATATIPIQASLPFGWLIVGVALLAVFQSASKIITLKKRWQLALSKGVHFVCNLLLLFVTVYSHLLLVAAGLEAPFLYLYALVYFLQSINFVRIIMRLWLCWKCRSKNPLLYDANYFLCWHTNCYDYCIPYNSVTSSIVITSGDGTTSPISEHDYQIGGYTEKWESGVKDCVVLHSYFTSDYYQLYSTQLSTDTGVEHVTFFIYNKIVDEPEEHVQIHTIDGSSGVVNPVMEPIYDEPTTTTSVPL | null | null | induction by virus of host reticulophagy [GO:0140883]; inorganic cation transmembrane transport [GO:0098662]; protein complex oligomerization [GO:0051259] | cytoplasmic side of plasma membrane [GO:0009898]; extracellular region [GO:0005576]; host cell endoplasmic reticulum [GO:0044165]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell endosome [GO:0044174]; host cell lysosome [GO:0044187]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]... | identical protein binding [GO:0042802]; molecular function activator activity [GO:0140677]; monoatomic ion channel activity [GO:0005216] | PF11289; | null | null | PTM: Exists in both O-glycosylated and non-glycosylated forms. The glycosylated form is associated with the virion. {ECO:0000250|UniProtKB:P59632}. | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P59632}. Host cell membrane {ECO:0000250|UniProtKB:P59632, ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:34158638}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P59632, ECO:0000269|PubMed:34158638}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:35239... | null | null | null | null | null | FUNCTION: Plays a role in viral egress via lysosomal trafficking (PubMed:33157038, PubMed:33422265). Forms homotetrameric ion channels (viroporins) localized at endosomes and lysosomes, that may induce deacidification of lysosomes, allowing safe egress of virions via lysosomal trafficking (PubMed:33157038, PubMed:33422... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTC4 | VEMP_SARS2 | MYSFVSEETGTLIVNSVLLFLAFVVFLLVTLAILTALRLCAYCCNIVNVSLVKPSFYVYSRVKNLNSSRVPDLLV | null | null | cytoplasmic capsid assembly [GO:0039709]; disruption of cellular anatomical structure in another organism [GO:0140975]; viral budding from Golgi membrane [GO:0046760] | endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; virion membrane [GO:0055036] | identical protein binding [GO:0042802]; monoatomic ion channel activity [GO:0005216]; structural constituent of virion [GO:0039660] | PF02723; | 6.10.250.1810; | Betacoronaviruses E protein family | null | SUBCELLULAR LOCATION: Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04204}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04204, ECO:0000269|PubMed:32898469, ECO:0000269|PubMed:33177698}. Note=The cytoplasmic tail functions as a Golgi complex-targeting signal. {ECO:0000255|HAMAP-Rule:MF_04... | null | null | null | null | null | FUNCTION: Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis (By similarity). Regulates the localization of S protein at cis-Golgi, the place o... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTC5 | VME1_SARS2 | MADSNGTITVEELKKLLEQWNLVIGFLFLTWICLLQFAYANRNRFLYIIKLIFLWLLWPVTLACFVLAAVYRINWITGGIAIAMACLVGLMWLSYFIASFRLFARTRSMWSFNPETNILLNVPLHGTILTRPLLESELVIGAVILRGHLRIAGHHLGRCDIKDLPKEITVATSRTLSYYKLGASQRVAGDSGFAAYSRYRIGNYKLNTDHSSSSDNIALLVQ | null | null | cytoplasmic capsid assembly [GO:0039709]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; virus-mediated perturbation of host defense response [GO:0019049] | endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; host cell Golgi membrane [GO:0044178]; plasma membrane [GO:0005886]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | identical protein binding [GO:0042802]; protein sequestering activity [GO:0140311]; structural constituent of virion [GO:0039660] | PF01635; | null | Betacoronaviruses M protein family | PTM: Glycosylated at N-terminus. {ECO:0000250|UniProtKB:P59596}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04202}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000269|PubMed:33060197}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04202}. Host membrane {ECO:0000269|... | null | null | null | null | null | FUNCTION: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins (By similarity). Regulates the localization of S protein at cis-Golgi, the place of virus budding (PubMed:33229438). May act by binding cytoplasmic c-terminus of S (PubM... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTC6 | NS6_SARS2 | MFHLVDFQVTIAEILLIIMRTFKVSIWNLDYIINLIIKNLSKSLTENKYSQLDEEQPMEID | null | null | symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity [GO:0039548]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of ST... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; nuclear pore [GO:0005643] | protein sequestering activity [GO:0140311] | PF12133; | null | Coronaviruses accessory protein 6 family | null | SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:35187564}; Peripheral membrane protein {ECO:0000269|PubMed:35187564}. Host Golgi apparatus membrane {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:35187564}; Peripheral membrane protein {ECO:0000269|PubMed:35187... | null | null | null | null | null | FUNCTION: Disrupts bidirectional nucleocytoplasmic transport by interacting with the host RAE1-NUP98 complex (PubMed:33360543, PubMed:33849972). Disrupts cell nuclear import complex formation by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane (PubMed:32979938). Retention of import factors at the ER... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTC7 | NS7A_SARS2 | MKIILFLALITLATCELYHYQECVRGTTVLLKEPCSSGTYEGNSPFHPLADNKFALTCFSTQFAFACPDGVKHVYQLRARSVSPKLFIRQEEVQELYSPIFLIVAAIVFITLCFTLKRKTE | null | null | suppression by virus of host tetherin activity [GO:0039587]; symbiont-mediated perturbation of host cell cycle G0/G1 transition checkpoint [GO:0039646]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; host cell Golgi membrane [GO:0044178]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; virion membrane [GO:0055036] | null | PF08779; | 2.60.40.1550; | null | PTM: Poly-ubiquitinated by host with K63-linked polyubiquitin chains. {ECO:0000269|PubMed:33473190}. | SUBCELLULAR LOCATION: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:33930332}. Virion {ECO:0000250|UniProtKB:P59635}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:36574644}; Single-pass membrane protein {ECO:0000269|PubMed:36574644}. Host endoplasmic reticulum-Golgi intermediate compartment mem... | null | null | null | null | null | FUNCTION: Plays a role as antagonist of host tetherin (BST2), disrupting its antiviral effect (PubMed:33930332). Acts by binding to BST2 and sequestering it to perinuclear region, thereby preventing its antiviral function at cell membrane (PubMed:33930332). May specifically downregulate MHC-I allele HLA-A*02:01 (HLA-A2... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTC8 | NS8_SARS2 | MKFLVFLGIITTVAAFHQECSLQSCTQHQPYVVDDPCPIHFYSKWYIRVGARKSAPLIELCVDEAGSKSPIQYIDIGNYTVSCLPFTINCQEPKLGSLVVRCSFYEDFLEYHDVRVVLDFI | null | null | negative regulation of interferon-beta production [GO:0032688]; positive regulation of immunoglobulin mediated immune response [GO:0002891]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; virus-mediated perturbation of host defense response [GO... | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764] | cytokine activity [GO:0005125]; identical protein binding [GO:0042802] | PF12093; | null | null | PTM: Glycosylated by the host when secreted via the conventional pathway. The glycosylated form cannot bind IL17A and would not participate in the cytokine storm. {ECO:0000269|PubMed:36689483}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:35157849, ECO:0000269|PubMed:35343786}. Note=Is secreted during a normal viral infection by unconventional pathway (PubMed:35157849, PubMed:36689483). Its mRNA is expressed in cytoplasm and not spliced during a viral infection, but is spliced when expressed from cDNA i... | null | null | null | null | null | FUNCTION: Plays a role in modulating the host immune response (PubMed:31986261, PubMed:35343786, PubMed:36689483). May act as a secreted virokine by mimicking interleukin-17A (IL17A), and thereby binding to the IL17RA receptor, leading to activation of the IL17 pathway and increased secretion of pro-inflammatory factor... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTC9 | NCAP_SARS2 | MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRNSSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRI... | null | null | cytoplasmic capsid assembly [GO:0039709]; negative regulation of interferon-beta production [GO:0032688]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; response to host immune response [GO:0052572]; viral RNA genome packaging [GO:0019074] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; host cell perinuclear region of cytoplasm [GO:0044220]; host extracellular space [GO:0043655]; intracellular non-membrane-bounded organelle [GO:... | identical protein binding [GO:0042802]; MHC class I protein binding [GO:0042288]; molecular condensate scaffold activity [GO:0140693]; protein homodimerization activity [GO:0042803]; protein sequestering activity [GO:0140311]; RNA binding [GO:0003723]; RNA stem-loop binding [GO:0035613] | PF00937; | null | Betacoronavirus nucleocapsid protein family | PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection. {ECO:0000255|HAMAP-Rule:MF_04096}.; PTM: Phosphorylated on serine residues by host GSK3A and GSK3B (PubMed:34593624, PubMed:35728038). This promotes the solubility of homodimers that would otherwise aggregate (PubMed:32974389). Host ... | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:34341353}. Secreted {ECO:0000269|PubMed:35921414}. Host extracellular space {ECO:0000269|PubMed:35921414}. Note=Probably associates with ER-derived membranes where it participates in viral RNA... | null | null | null | null | null | FUNCTION: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M (PubMed:33264373). Plays an important role in enhancing the efficiency of subgenomic viral RNA transcrip... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTD1 | R1AB_SARS2 | MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAPHGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQENWNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAWYTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTL... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 2.7.7.50; 3.1.13.-; 3.4.19.12; 3.4.22.-; 3.4.22.69; 3.6.4.12; 3.6.4.13; 4.6.1.- | COFACTOR: [Uridylate-specific endoribonuclease nsp15]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:33564093}; Note=Likely affects Nsp15 binding to RNA. {ECO:0000250|UniProtKB:P0C6X7}; COFACTOR: [RNA-directed RNA polymerase nsp12]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:3... | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated degradation of host mRNA [GO:0039595]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host cytoplasmic pattern recognitio... | double membrane vesicle viral factory outer membrane [GO:0062243]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell endosome [GO:0044174]; host cell Golgi apparatus [GO:0044177]; host cell nucleus [GO:0042025]; host cell perinu... | 3'-5'-RNA exonuclease activity [GO:0000175]; 5'-3' DNA helicase activity [GO:0043139]; 5'-3' RNA helicase activity [GO:0032574]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; copper ion binding [GO:0005507]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0... | PF13087;PF16251;PF11501;PF12379;PF12124;PF11633;PF06471;PF06460;PF09401;PF20631;PF20633;PF20632;PF19215;PF19216;PF19219;PF19212;PF19211;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF06478;PF01661;PF05409;PF00680; | 1.10.8.1190;2.60.120.1680;3.10.20.350;3.10.20.540;3.40.50.11580;6.10.140.2090;1.10.150.420;3.40.30.150;3.40.220.10;1.10.1840.10;3.30.160.820;3.40.220.20;3.40.220.30;1.10.8.370;3.30.70.3540;3.40.50.300;2.40.10.250;3.40.50.11020;2.40.10.10;3.40.50.150; | Coronaviruses polyprotein 1ab family | PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed. {ECO:0000250|UniProtKB:P0C6X7}. | SUBCELLULAR LOCATION: [Host translation inhibitor nsp1]: Host cytoplasm {ECO:0000269|PubMed:33060197}.; SUBCELLULAR LOCATION: [Non-structural protein 2]: Host cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:35878012}. Host endosome {ECO:0000269|PubMed:33060197}.; SUBCELLULAR LOCATION: [Papain-like protease n... | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000269|PubMed:32358203, ECO:000026... | null | null | null | null | FUNCTION: [Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Host translation inhibitor nsp1]: Inhibits host translation by associating wi... | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTD2 | ORF9B_SARS2 | MDPKISEMHPALRLVDPQIQLAVTRMENAVGRDQNNVGPKVYPIILRLGSPLSLNMARKTLNSLEDKAFQLTPIAVQMTKLATTEELPDEFVVVTVK | null | null | negative regulation of defense response to virus [GO:0050687]; negative regulation of mitochondrial fission [GO:0090258]; positive regulation of autophagosome assembly [GO:2000786]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:00395... | host cell mitochondrion [GO:0033650]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; outer mitochondrial membrane protein complex [GO:0098799] | identical protein binding [GO:0042802]; protein sequestering activity [GO:0140311] | PF09399; | null | Coronavirus group 2 protein 9b family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:32728199, ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:34502139}. Host mitochondrion {ECO:0000269|PubMed:32728199, ECO:0000269|PubMed:33060197}. | null | null | null | null | null | FUNCTION: Plays a role in inhibiting the host innate immune response by targeting the mitochondrial-associated innate immune response. Acts by binding to host TOMM70, inhibiting its binding to HSP90AB1 thereby disrupting the interferon activation pathway. {ECO:0000269|PubMed:32728199, ECO:0000269|PubMed:34502139}. | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
P0DTE4 | UD2A1_HUMAN | MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALFITPTSNPSLTFEIYKVPFGKERIEGVIKDFVLTWLENRPSPSTIWRFYQEMAKVIKDFHMVSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVEKHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGGLLLCCPGWSAVADLGSLQPLLPGFKRFSRLSLHCSWDYRLPAGRPTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVG... | 2.4.1.17 | null | bile acid metabolic process [GO:0008206]; cellular glucuronidation [GO:0052695]; response to stimulus [GO:0050896]; sensory perception of chemical stimulus [GO:0007606]; sensory perception of smell [GO:0007608] | endoplasmic reticulum membrane [GO:0005789] | glucuronosyltransferase activity [GO:0015020] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:10359671}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:19858781}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; Evidence={ECO:0000269|PubMed:10359671, ECO:0000269|PubMed:18719240... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=99 uM for 17alpha-estradiol/epiestradiol (when assaying glucuronidation at position 3) {ECO:0000269|PubMed:18719240}; KM=174 uM for 17beta-estradiol/estradiol (when assaying glucuronidation at position 3) {ECO:0000269|PubMed:18719240}; KM=36 uM for 17alpha-estradio... | null | null | null | FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:10359671, PubMed:18719240, PubMed:1902293... | Homo sapiens (Human) |
P0DTE5 | UD2A2_HUMAN | MVSIRDFTMPKKFVQMLVFNLTLTEVVLSGNVLIWPTDGSHWLNIKIILEELIQRNHNVTVLASSATLFINSNPDSPVNFEVIPVSYKKSNIDSLIEHMIMLWIDHRPTPLTIWAFYKELGKLLDTFFQINIQLCDGVLKNPKLMARLQKGGFDVLVADPVTICGDLVALKLGIPFMYTLRFSPASTVERHCGKIPAPVSYVPAALSELTDQMTFGERIKNTISYSLQDYIFQSYWGEWNSYYSKILGRPTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKNGVVVFSLGSMV... | 2.4.1.17 | null | bile acid metabolic process [GO:0008206]; cellular glucuronidation [GO:0052695] | endoplasmic reticulum membrane [GO:0005789] | glucuronosyltransferase activity [GO:0015020] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:19858781}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; Evidence={ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:19858781... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=45.4 uM for 17beta-estradiol/estradiol (when assaying glucuronidation at position 3) {ECO:0000269|PubMed:18719240}; KM=55.1 uM for UDP-glucuronate (with 4-methyl-umbelliferone as substrate) {ECO:0000269|PubMed:19858781}; KM=4469 uM for 4-nitrophenol {ECO:0000269|Pu... | null | null | null | FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:18719240, PubMed:19858781, PubMed:2328886... | Homo sapiens (Human) |
P0DTE7 | AMY1B_HUMAN | MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGH... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:... | carbohydrate metabolic process [GO:0005975]; oligosaccharide metabolic process [GO:0009311] | extracellular exosome [GO:0070062]; extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]; chloride ion binding [GO:0031404] | PF00128;PF02806; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:12527308}; | null | null | null | null | FUNCTION: Calcium-binding enzyme that initiates starch digestion in the oral cavity (PubMed:12527308). Catalyzes the hydrolysis of internal (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose, isomaltose, small amounts of glucose as well as small linear and branched oligosaccharides called dextrins (PubMed:1... | Homo sapiens (Human) |
P0DTE8 | AMY1C_HUMAN | MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGH... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:... | carbohydrate metabolic process [GO:0005975]; oligosaccharide metabolic process [GO:0009311] | extracellular exosome [GO:0070062]; extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]; chloride ion binding [GO:0031404] | PF00128;PF02806; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:12527308}; | null | null | null | null | FUNCTION: Calcium-binding enzyme that initiates starch digestion in the oral cavity (PubMed:12527308). Catalyzes the hydrolysis of internal (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose, isomaltose, small amounts of glucose as well as small linear and branched oligosaccharides called dextrins (PubMed:1... | Homo sapiens (Human) |
P0DTE9 | CAPV_ECOTW | MSDVSAVDKPRVRVLSLNGGGARGMFTISILAEIERILARKHPHQDIKIGDYFDLITGTSIGGILALGLATGKSARELESVFFDKAKDIFPTRWSLVNLCKALCAPIYNSSPLRETIEMMIGAETTFNDLTRRVMIPAVNLSTGKPLFFKTPHNPDFTRDGPLKLIDAALATSAAPTYFAPHYCKDLRSYFADGGLVANNPSYIGLLEVFRDMKSDFDVSHKDVYILNIGTVGEDYSLSPSLLSKKRWTGYCHLWGMGKRLVLTTMTANQHLHKNMLLRELALHDALDNYLYLDEVIPNEAASDITLDNASDSSLQNLSA... | 3.1.1.32 | null | D-xylose catabolic process [GO:0042843]; defense response to virus [GO:0051607]; lipid catabolic process [GO:0016042] | null | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; acylglycerol lipase activity [GO:0047372]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]; xylose isomerase activity [GO:0009045] | PF01734; | 3.40.1090.10; | Patatin family | null | null | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:Q9KVG8}; Physiologic... | null | null | null | null | FUNCTION: Effector phospholipase of a CBASS antiviral system (PubMed:31533127). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (DncV) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals.... | Escherichia coli (strain TW11681) |
P0DTF0 | DNCV2_ECOTW | MHWDLNNYYSNNMDGLISKLKLSKTESTKLKELRQIVRERTRDVFKEARAVAADVKKHTLTLEGVRLKLGQTNVRYLSTADQAEVARLIFEMDDDARNDFINLQPRFWTQGSFQYDTLNKPFQPGQEMDIDDGTYMPMTVFESEPRIGHTLLLLLVDTSLKSLEAENDGWRFEEKNTCGRIKIPHEKTHIDVPMYAIPKNQFQTKQTAADSAHILKSESIFESVALNRDSREAYLVESDKVNLALREGAKRWSISDPKIVEDWFNDSCKRIGGHVRSICRFMKAWRDAQWDVGGPSSISLMTAVVNILNREEHNDSDLAG... | 2.7.7.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9KVG7}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9KVG7}; | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | null | 3',3'-cyclic GMP-AMP synthase activity [GO:0140701]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; metal ion binding [GO:0046872] | PF21654;PF21713; | null | CD-NTase family, A02 subfamily | PTM: In bacteria expressing capV-dncV-cap2-cap3, this protein is conjugated to about 130 cellular proteins by Cap2, most of which are involved in metabolism; more conjugated protein is found in the absence of Cap3 (PubMed:36848932). Most conjugation occurs via an isopeptide bond with the epsilon-amine of Lys on the tar... | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:35647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71501; Evidence={ECO:0000269|PubMed:36848932}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35648; Evidence={ECO:0000269|PubMed:36848932}; | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:36848932). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (DncV, this protein) synthesizes cyclic nucleotides in response to infection; the... | Escherichia coli (strain TW11681) |
P0DTF7 | CDND_PSEAI | MLSIDEAFRKFKSRLELNEREQKNASQRQNEVRDYLQTKFGIARSFLTGSYARYTKTKPLKDIDIFFVLKDSEKHYHGKAASVVLDDFHSALVEKYGSAAVRKQARSINVDFGVHIDAEDNTDYRVVSVDAVPAFDTGDQYEIPDTASGKWIKTDPEIHKDKATAAHQAYANEWKGLVRMVKYWNNNPKHGDLKPVKPSFLIEVMALECLYGGWGGSFDREIQSFFATLADRVHDEWPDPAGLGPAISNDMDAARKQRAQQLLFQASQDASIAIDHARRGRNIEALRAWRALFGPKFPLS | 2.7.7.-; 2.7.7.85 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:31932165}; Note=Crystallized with and without Mg-ATP. {ECO:0000269|PubMed:31932165}; | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | null | ATP binding [GO:0005524]; diadenylate cyclase activity [GO:0106408]; metal ion binding [GO:0046872] | PF18144; | 3.30.460.10; | CD-NTase family, D05 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=3 ATP = 3',3',3'-c-tri-AMP + 3 diphosphate; Xref=Rhea:RHEA:72755, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:192523; Evidence={ECO:0000269|PubMed:31932165}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72756; Evidence={ECO:0000305|PubMed:31932165}; CATALYTIC ACTIVITY: Reactio... | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:31932165). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific s... | Pseudomonas aeruginosa |
P0DTJ0 | GP_BCCV | MGRLYLIVLGVLITATAGFPRSVHELKIECPHTVVLGQGYVTGSVELGFIALDQVTDLKIESSCSFDHHAAPTTTQNFTQLKWAKTASTTDTTNAAETTFESKSTEVHLKGVCTIPSNVLDGPSRPVTGRKTVVCYDLACNQTHCQPTVHLLAPIQTCMSVRSCMISLLASRIQVVYEKTYCVTGQLIEGLCFNPVPNLALTQPGHTYDTFTLPITCFLVAKKGANLKIAVELEKLTTKTGCAENALQAYYICFIGQHSEPLTVPMLEDYRSAEIFTRIMMNPKGEDHDMEQSSQGALRIVGPIKGKVPPTETSDTVQGI... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; signal transduction [GO:0007165]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via in... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; host cell surface [GO:0044228]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF20682;PF01561;PF20679;PF01567;PF10538; | 1.10.8.1320; | Hantavirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Envelope polyprotein precursor is quickly cleaved in vivo just after synthesis, presumably by host signal peptidase. {ECO:0000250|UniProtKB:P08668}. | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein {ECO:0000305}. Host cell surface {ECO:0000269|PubMed:8995636}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic re... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at the surface of the virion (By similarity). Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (By similarity). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity)... | Black Creek Canal orthohantavirus (BCCV) (Black Creek Canal virus) |
P0DTJ1 | GP_TULV | MFCLCLSLLGLLLCWPAATRNLLELKVECPHTIGLGQGIVIGSAELPPVPLAKVESLKLESSCNFDLHTSTAAQQAFTKWSWEKKADTAENAKAASTTFQSSSKEVQLRGLCVIPTLVLETASRTRKTVTCFDLSCNQTVCQPTVYLMAPIQTCVTTKSCLLGLGDQRIQVVYEKTYCVSGQLIEGNCFNPLHTIAISQPTHTYDIMTLAVHCFFISKKGGTDDTLKIEKQFETLVEKTGCTENALKGYYACILGTSSEVVYVPAMDDYRSSEILSRMTTAPHGEDHDIDPNAISSLRIVGQLTGKAPSTESSDTVQGIA... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; signal transduction [GO:0007165]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via in... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; host cell surface [GO:0044228]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF20682;PF01561;PF20679;PF01567;PF10538; | 1.10.8.1320; | Hantavirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Envelope polyprotein precursor is quickly cleaved in vivo just after synthesis, presumably by host signal peptidase. {ECO:0000250|UniProtKB:P08668}. | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000269|PubMed:20219926}; Multi-pass membrane protein {ECO:0000305}. Host cell surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic r... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at the surface of the virion (By similarity). Attaches the virion to host cell receptors including integrin alpha5/ITGB1 (Probable). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity). Me... | Tula orthohantavirus (TULV) (Tula virus) |
P0DTM4 | ENV_ALVA | MEAVIKAFLTGYPGKTSKKDSKEKPLATSKKDPEKTPLLPTRVNYILIIGVLVLCEVTGVRADVHLLEQPGNLWITWANRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVSDNCTTLGTDRLVSSADFTGGPDNSTTLTYRKVSCLLLKLNVSMWDEPHELQLLGSQSLPNITNIAQISGITGGCVGFRPQGVPWYLGWSRQEATRFLLRHPSFSKSTEPFTVVTADRHNLFMGSEYCGAYGYRFWNMYNCSQVGRQYRCGNARSPRPGLPEIQCTRRGGKWVNQSQEINESEPFSFTVNCTASSLGNASGCC... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF03708;PF00429; | 1.10.287.210; | Alpharetroviruses envelope glycoprotein family | PTM: [Envelope glycoprotein gp95]: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000303|PubMed:31151254}. Host cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000303|PubMed:31151254}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000305}; P... | null | null | null | null | null | FUNCTION: [Surface protein]: The surface protein (SU) attaches the virus to the host cell entry receptor TVA (PubMed:15731243, PubMed:22099981). This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate on Cys-100 to activate ... | Avian leukosis virus subgroup A (isolate RSA) (ALV-A RSA) |
P0DTM5 | ENV_RSVSA | IPSRPVGGPCYLGKLTMLAPKHTDILKVLVNSSRTGIRRKRSTSHLDDTCSDEVQLWGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCEDVAGMCCFNLSDQSESIQKKFQLMKEHVNKIGVDSDLIGSWLRGLFGGIGEWAVHLLKGLLLGLVVILLLVVCLPCLLQMLCGNRRKMINNSISYHTEYKKLQKACGQPESRIV | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF03708;PF00429; | 1.10.287.210; | Alpharetroviruses envelope glycoprotein family | PTM: [Envelope glycoprotein gp95]: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000303|PubMed:31151254}. Host cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000303|PubMed:31151254}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000305}; P... | null | null | null | null | null | FUNCTION: [Surface protein]: The surface protein (SU) attaches the virus to the host cell entry receptor TVA (PubMed:15731243, PubMed:22099981). This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate to activate its fusogen... | Rous sarcoma virus subgroup A (strain Schmidt-Ruppin) (RSV-SR-A) |
P0DTQ0 | DRDA_BACT7 | MLLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVIEGERKPSSELDMHLIYYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIAFAGPNVRCAPYETFGTKQLADAAFEGMIDRRAVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYYQTKSIGEPKLLPEDEMENLAKKFEGYGQQ | 4.1.2.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:30082730}; Note=Binds 1 Mn(2+) ion per subunit. To a much lesser extent, can also use Co(2+) and Mg(2+) as cofactor, but not Zn(2+). {ECO:0000269|PubMed:30082730}; | carbohydrate metabolic process [GO:0005975]; pentose catabolic process [GO:0019323]; toxic metabolite repair [GO:0110052] | cytosol [GO:0005829] | aldehyde-lyase activity [GO:0016832]; manganese ion binding [GO:0030145] | PF00596; | 3.40.225.10; | Aldolase class II family | null | null | CATALYTIC ACTIVITY: Reaction=5-deoxy-D-ribulose 1-phosphate = acetaldehyde + dihydroxyacetone phosphate; Xref=Rhea:RHEA:61300, ChEBI:CHEBI:15343, ChEBI:CHEBI:57642, ChEBI:CHEBI:144504; Evidence={ECO:0000269|PubMed:30082730}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61301; Evidence={ECO:0000269|PubMed:300827... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 uM for 5-deoxy-D-ribulose 1-phosphate {ECO:0000269|PubMed:30082730}; Note=kcat is 6.3 sec(-1) for the cleavage of 5-deoxy-D-ribulose 1-phosphate. {ECO:0000269|PubMed:30082730}; | PATHWAY: Carbohydrate degradation. {ECO:0000305|PubMed:30082730}. | null | null | FUNCTION: Catalyzes the cleavage of 5-deoxy-D-ribulose 1-phosphate to yield dihydroxyacetone phosphate (DHAP) and acetaldehyde, as part of a 5-deoxyribose salvage pathway that recycles this toxic radical SAM enzyme by-product to mainstream metabolites. Is also able to catalyze the reverse reaction, using several aldehy... | Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73) |
P0DTQ1 | DRDI_BACT7 | MMEEQLIPIQWKDDALVLLDQTLLPNEIVYESFKTAESVWDAIQVMKVRGAPVIGVSAAYGVYLGVKEFAESTEEGFMDEVRKVCTYLATSRPTAVNLFWALERMESVAADNIHLSISQLKDRLLEEAKEIHREDEEINRQIGEHALTLFHDGMGVLTHCNAGALATTKYGTATAPMYLAKEKGWDLKIFSDETRPRLQGSTLTALELQRAGIDVTVITDNMAAMVMSQGKIDAVIVGCDRVAANGDIANKIGTLGVSILAKYYNIPFYVAAPTPTIDLKTPTGKEIPIEERDASEVINRFGQYSAPKESKVYNPAFDVT... | 5.3.1.-; 5.3.1.23 | null | carbohydrate metabolic process [GO:0005975]; L-methionine salvage from methylthioadenosine [GO:0019509]; pentose catabolic process [GO:0019323]; toxic metabolite repair [GO:0110052] | null | intramolecular oxidoreductase activity, interconverting aldoses and ketoses [GO:0016861]; S-methyl-5-thioribose-1-phosphate isomerase activity [GO:0046523] | PF01008; | 1.20.120.420; | EIF-2B alpha/beta/delta subunits family, DrdI subfamily | null | null | CATALYTIC ACTIVITY: Reaction=5-deoxy-alpha-D-ribose 1-phosphate = 5-deoxy-D-ribulose 1-phosphate; Xref=Rhea:RHEA:61296, ChEBI:CHEBI:58749, ChEBI:CHEBI:144504; Evidence={ECO:0000255|HAMAP-Rule:MF_02229, ECO:0000269|PubMed:30082730}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61297; Evidence={ECO:0000255|HAMAP-... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22 mM for 5-deoxy-alpha-D-ribose 1-phosphate {ECO:0000269|PubMed:30082730}; Note=kcat is 3.5 sec(-1) with 5-deoxy-alpha-D-ribose 1-phosphate as substrate. {ECO:0000269|PubMed:30082730}; | PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02229, ECO:0000305|PubMed:30082730}. | null | null | FUNCTION: Catalyzes the isomerization of 5-deoxy-alpha-D-ribose 1-phosphate to 5-deoxy-D-ribulose 1-phosphate, as part of a 5-deoxyribose salvage pathway that recycles this toxic radical SAM enzyme by-product to mainstream metabolites. Also seems to be able to catalyze the conversion of methylthioribose-1-phosphate (MT... | Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73) |
P0DTQ4 | TYRDC_ENTF3 | MKNEKLAKGEMNLNALFIGDKAENGQLYKDLLIDLVDEHLGWRQNYMPQDMPVISSQERTSESYEKTVNHMKDVLNEISSRMRTHSVPWHTAGRYWGHMNSETLMPSLLAYNFAMLWNGNNVAYESSPATSQMEEEVGHEFAHLMSYKNGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVKPELVAGKSDWELLNMPTKEIMDLLESAEDEIDEIKAHSARSGKHLQAIGKWLVPQTKHYSWLKAADIIGIGLDQVIPVPVDHNYRMDINELEKIVRGLAEEQIPVLGVVGVVGSTEEGAVDSIDKIIALRDELMKDG... | 4.1.1.-; 4.1.1.25 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305|PubMed:31196984}; | L-dopa metabolic process [GO:1903184] | null | L-dopa decarboxylase activity [GO:0036468]; pyridoxal phosphate binding [GO:0030170]; tyrosine decarboxylase activity [GO:0004837] | PF00282;PF21391; | 3.40.640.10; | Group II decarboxylase family, Tyrosine decarboxylase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315, ChEBI:CHEBI:327995; EC=4.1.1.25; Evidence={ECO:0000269|PubMed:31196984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346; Evidence={ECO:0000305|PubMed:31196984}; CAT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=315 uM for L-tyrosine (at pH 5.5); KM=1475 uM for L-dopa (at pH 5.5); Note=kcat is 63.6 sec(-1) for the decarboxylation of L-tyrosine. kcat is 55.5 sec(-1) for the decarboxylation of L-dopa (at pH 5.5). {ECO:0000269|PubMed:31196984}; | PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:31196984}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: L-dopa decarboxylation occurs more rapidly at lower pH, suggesting that this metabolism is likely accelerated at the lower pH of the upper small intestine. {ECO:0000269|PubMed:31196984}; | null | FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:31196984). Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastroint... | Enterococcus faecalis (strain EnGen0310 / MMH594) |
P0DTR4 | ADAC_FLAPL | MRNRRKAVSLLTGLLVTAQLFPTAALAADSSESALNKAPGYQDFPAYYSDSAHADDQVTHPDVVVLEEPWNGYRYWAVYTPNVMRISIYENPSIVASSDGVHWVEPEGLSNPIEPQPPSTRYHNCDADMVYNAEYDAMMAYWNWADDQGGGVGAEVRLRISYDGVHWGVPVTYDEMTRVWSKPTSDAERQVADGEDDFITAIASPDRYDMLSPTIVYDDFRDVFILWANNTGDVGYQNGQANFVEMRYSDDGITWGEPVRVNGFLGLDENGQQLAPWHQDVQYVPDLKEFVCISQCFAGRNPDGSVLHLTTSKDGVNWEQ... | 3.5.1.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:31182795}; | metabolic process [GO:0008152] | null | hydrolase activity, acting on glycosyl bonds [GO:0016798]; metal ion binding [GO:0046872] | PF02368;PF00754; | 2.60.40.1080;2.60.120.260; | null | null | null | CATALYTIC ACTIVITY: Reaction=an N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative + H2O = acetate + an alpha-D-galactosaminyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative; Xref=Rhea:RHEA:14869, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:140559, ChEBI:CHE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=340 uM for A antigen type 1 penta-MU {ECO:0000269|PubMed:31182795}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:31182795}; | null | FUNCTION: One of an enzyme pair that work together to convert the A antigen to the H antigen of the O blood type, which together release galactosamine. Catalyzes the first step in the conversion, generating the substrate for the subsequent enzyme (FpGalNase, AC P0DTR5). Works on many different A antigen subtypes. Glu-9... | Flavonifractor plautii (Fusobacterium plautii) |
P0DTR8 | APOE_THEGE | MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSELQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Theropithecus gelada (Gelada baboon) |
P0DTT0 | BIPA_ECOLI | MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCG... | 3.6.5.- | null | ribosome biogenesis [GO:0042254] | cytosol [GO:0005829]; ribonucleoprotein complex [GO:1990904] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; ribosome binding [GO:0043022]; rRNA binding [GO:0019843]; tRNA binding [GO:0000049] | PF21018;PF00679;PF00009;PF03144; | 3.30.70.240;2.40.50.250;3.30.70.870;3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, BipA subfamily | PTM: Very poorly to not phosphorylated on tyrosine (PubMed:30305394, PubMed:9622352, PubMed:9642082). Phosphorylation in vitro is strongly activated by proteins present in pathogenic strain E2348/69 / EPEC / MAR001 but not non-pathogenic strain K12 / DH5 alpha. Phosphorylation in vitro increases GTPase activity (PubMed... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:30305394, ECO:0000269|Ref.12}. Note=Associates with 70S ribosomes and 30S and 50S subunits in the presence of GMPPNP (a nonhydrolyzable GTP analog) at both 20 and 37 degrees Celsius; no change in ribosome association is seen in the pre... | 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:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:30305394}; | null | null | null | null | FUNCTION: A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity, required for 50S subunit assembly at low temperatures, may also play a role in translation (PubMed:30305394). Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it... | Escherichia coli (strain K12) |
P0DTT1 | APOE_ARCGZ | MKVLWAALVVALLAGCWADVEPESPLEENLEPELEPKRELEQEVEPEAGWQAGQPWELALARFWDYLRWVQTLSDQVQEEVLSNQVTQELTTLMEETMKEIKAYRAELEEQLGPMASETQARVAKELQAAQARLRSDMEDVRTRLSQYRGEVQAMLGQSTEELRARFASHMRKLRKRVLRDAEDLQKRLAVYRAGVREGAERSVSTIRERLWPLLEQARTRHAKVDALATQPLRERVNALGQQLRGRLEEMGSRARSHLDEVREQMEEVQAKMEEQANQMRQQAEPFQARLKGWFEPLVEDMQRQWAVLVEKVQAAVGTS... | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Arctocephalus gazella (Antarctic fur seal) |
P0DTT2 | APOE_EUMJU | MKVLWAALVVALLAGCWADVEPESPLEENLEPELEPKRELEQEVEPEAGWQAGQPWELALARFWDYLRWVQTLSDQVQEEVLSNQVTQELTTLMEETMKEIKAYRAELEEQLGPMASETQARVAKELQAAQARLRSDMEDVRTRLSQYRGEVQAMLGQSTEELRARFASHMRKLRKRVLRDAEDLQKRLAVYRAGVREGAERSVSTIRERLWPLLEQARTRHAKVDALATQPLRERVNALGQQLRGRLEEVGSRARSHLDEVREQMEEVQAKMEEQANQMRQQAEAFQARLKGWFEPLVEDMQRQWAVLVEKVQAAVGTS... | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Eumetopias jubatus (Steller sea lion) (Phoca jubata) |
P0DTU3 | TRAR2_HUMAN | MACPGFLWALVISTCLEFSMAQTVTQSQPEMSVQEAETVTLSCTYDTSESDYYLFWYKQPPSRQMILVIRQEAYKQQNATENRFSVNFQKAAKSFSLKISDSQLGDAAMYFCAYRSAVNARLMFGDGTQLVVKPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESSCDVKLVEKSFETDTNLNFQNLSVIGFRILLLKVAGFNLLMTLRLWSS | null | null | detection of tumor cell [GO:0002355]; response to bacterium [GO:0009617]; T cell mediated cytotoxicity directed against tumor cell target [GO:0002419] | alpha-beta T cell receptor complex [GO:0042105] | signaling receptor activity [GO:0038023] | PF09291;PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31959982}. | null | null | null | null | null | FUNCTION: The alpha chain of TRAV38-2DV8*01J31*01C*01/TRBV25-1*01J2S3*01C2*01 alpha-beta T cell receptor (TR) clonotype that displays pan-cancer cell recognition via the invariant MR1 molecule. On CD8-positive T cell clone MC.7.G5, likely recognizes tumor-specific or -associated metabolite(s) essential for cancer cell ... | Homo sapiens (Human) |
P0DTU4 | TRBR2_HUMAN | MTIRLLCYMGFYFLGAGLMEADIYQTPRYLVIGTGKKITLECSQTMGHDKMYWYQQDPGMELHLIHYSYGVNSTEKGDLSSESTVSRIRTEHFPLTLESARPSHTSQYLCASSEARGLAEFTDTQYFGPGTRLTVLEDLKNVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSESYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDSRG | null | null | cell surface receptor signaling pathway [GO:0007166]; detection of tumor cell [GO:0002355]; T cell mediated cytotoxicity directed against tumor cell target [GO:0002419] | alpha-beta T cell receptor complex [GO:0042105]; plasma membrane [GO:0005886] | signaling receptor activity [GO:0038023] | PF07654;PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31959982}. | null | null | null | null | null | FUNCTION: The beta chain of TRAV38-2DV8*01J31*01C*01/TRBV25-1*01J2S3*01C2*01 alpha-beta T cell receptor (TR) clonotype that displays pan-cancer cell recognition via the invariant MR1 molecule. On CD8-positive T cell clone MC.7.G5, likely recognizes tumor-specific or -associated metabolite(s) essential for cancer cell s... | Homo sapiens (Human) |
P0DTV7 | SPEFL_ECOLI | MENNSRTMPHIRRTTHIMKFAHRNSFDFHFFNAR | null | null | regulation of translational elongation [GO:0006448]; transcriptional attenuation by ribosome [GO:0031556] | null | rRNA binding [GO:0019843] | null | null | SpeF operon leader peptide family | null | null | null | null | null | null | null | FUNCTION: A small protein (arrest peptide) encoded upstream of inducible ornithine carboxylase gene (speF) that controls expression of downstream genes (speF and patE) by nascent chain-translational arrest and transcriptional attenuation. In the presence of ornithine a toeprint due to ribosomal arrest can be seen on th... | Escherichia coli (strain K12) |
P0DUB4 | TCSL2_PAESO | MSLVNKAQLQKMAYVKFRIQEDEYVAILNALEEYHNMSESSVVEKYLKLKDINNLTDNYLNTYKKSGRNKALKKFKEYLTMEVLELKNNSLTPVEKNLHFIWIGGQINDTAINYINQWKDVNSDYTVKVFYDSNAFLINTLKKTIVESATNNTLESFRENLNDPEFDYNKFYRKRMEIIYDKQKHFIDYYKSQIEENPEFIIDNIIKTYLSNEYSKDLEALNKYIEESLNKITANNGNDIRNLEKFADEDLVRLYNQELVERWNLAAASDILRISMLKEDGGVYLDVDMLPGIQPDLFKSINKPDSITDTSWEMIKLEAI... | 2.4.1.-; 3.4.22.- | COFACTOR: [Cytotoxin-L]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P18177}; Note=Binds 1 Zn(2+) ion per subunit. Zn(2+) is required for autocatalytic cleavage. {ECO:0000250|UniProtKB:P18177}; COFACTOR: [Glucosyltransferase TcsL]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniP... | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytosol [GO:0044164]; host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | cysteine-type peptidase activity [GO:0008234]; glycosyltransferase activity [GO:0016757]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF01473;PF19127;PF11647;PF11713;PF12919;PF12920;PF12918; | 1.10.10.1780;1.10.274.80;1.10.3730.30;1.20.58.1190;3.40.50.11050;2.10.270.10; | Clostridial glucosylating toxin (LCGT) family | PTM: [Cytotoxin-L]: Undergoes autocatalytic cleavage to release the N-terminal part (Glucosyltransferase TcsL), which constitutes the active part of the toxin, in the host cytosol. 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C80 domain and promotes autoprocessing. {ECO:0000250|UniProtKB:Q46... | SUBCELLULAR LOCATION: [Cytotoxin-L]: Secreted {ECO:0000250|UniProtKB:P18177}. Host endosome membrane {ECO:0000250|UniProtKB:P18177}. Note=Secreted from P.sordellii cell into the extracellular environment via help of holin-like protein TcdE/UtxA. Binds to the cell surface receptors via the receptor-binding region and en... | CATALYTIC ACTIVITY: [Glucosyltransferase TcsL]: Reaction=L-threonyl-[protein] + UDP-alpha-D-glucose = 3-O-(alpha-D-glucosyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:64684, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:16656, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:156085... | null | null | null | null | FUNCTION: [Cytotoxin-L]: Precursor of a cytotoxin that targets the vascular endothelium, inducing an anti-inflammatory effect and resulting in lethal toxic shock syndrome (By similarity). TcsL constitutes the main toxin that mediates the pathology of P.sordellii infection, an anaerobic Gram-positive bacterium found in ... | Paeniclostridium sordellii (Clostridium sordellii) |
P0DUB6 | AMY1A_HUMAN | MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGH... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:... | carbohydrate metabolic process [GO:0005975]; oligosaccharide metabolic process [GO:0009311] | extracellular exosome [GO:0070062]; extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]; chloride ion binding [GO:0031404] | PF00128;PF02806; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:12527308}; | null | null | null | null | FUNCTION: Calcium-binding enzyme that initiates starch digestion in the oral cavity (PubMed:12527308). Catalyzes the hydrolysis of internal (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose, isomaltose, small amounts of glucose as well as small linear and branched oligosaccharides called dextrins (PubMed:1... | Homo sapiens (Human) |
P0DUB8 | LIP_BURPL | MVRSMRSRVAARAVAWALAVMPLAGAAGLTMAASPAAVAADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSY... | 3.1.1.3 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16518399, ECO:0000269|PubMed:8405390}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:16518399, ECO:0000269|PubMed:8405390}; | lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; triglyceride lipase activity [GO:0004806] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily, Pseudomonas lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:1476423, ECO:0000305|PubMed:8412704}. Note=Correct periplasmic folding, necessary for secretion, requires the lipase-specific foldase LifO (also called lipB). Secretion probably occurs via a type II secretion system. {ECO:0000269|PubMed:8412705, ECO:0000305|PubMed:8412... | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000305|PubMed:1476423}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for oil emulsion {ECO:0000269|PubMed:1476423}; Vmax=4 umol/min/mg enzyme {ECO:0000269|PubMed:1476423}; | null | null | null | FUNCTION: Catalyzes the hydrolysis of triacylglycerol. {ECO:0000269|PubMed:1476423, ECO:0000269|PubMed:7786905}. | Burkholderia plantarii |
P0DUB9 | LIP_PSEPS | ADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDPVAVIRTHVNRLKLQGV | 3.1.1.3 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:8683577, ECO:0000305|Ref.3}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:8683577, ECO:0000305|Ref.3}; | lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; triglyceride lipase activity [GO:0004806] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily, Pseudomonas lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DUB8}. Note=Correct periplasmic folding, necessary for secretion, requires the lipase-specific foldase LifO. Secretion probably occurs via a type II secretion system. {ECO:0000250|UniProtKB:P0DUB8}. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000305|PubMed:7786905}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of triacylglycerol. {ECO:0000269|PubMed:7786905}. | Pseudarthrobacter phenanthrenivorans (Arthrobacter phenanthrenivorans) |
P0DUD0 | YOPJ_YERPY | MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV | 2.3.1.- | COFACTOR: Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130; Evidence={ECO:0000250|UniProtKB:O68718}; | peptidyl-serine O-acetylation [GO:0030919]; peptidyl-threonine O-acetylation [GO:0120258]; regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070432]; symbiont-mediated activation of host programmed cell death [GO:0052042] | extracellular region [GO:0005576] | O-acetyltransferase activity [GO:0016413]; toxin activity [GO:0090729] | PF03421; | null | Acetyltransferase YopJ family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8045884, ECO:0000269|PubMed:9535085}. Note=Secreted via type III secretion system (T3SS). {ECO:0000269|PubMed:9535085}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141025; Evidence={ECO:0000269|PubMed:22520462}; PhysiologicalDirection=left-to-righ... | null | null | null | null | FUNCTION: Serine/threonine-protein acetyltransferase translocated into infected cells, which inhibits the host immune response and induces cell death by mediating acetylation of target proteins (PubMed:22520462, PubMed:9535085). Inhibits the MAPK and NF-kappa-B signaling pathways by acetylating protein-kinases such as ... | Yersinia pseudotuberculosis serotype O:3 (strain YPIII) |
P0DUD5 | CAP4_ENTH5 | MATSVLANWHGHDYQARYFWIEASRLKNPQQDFVVEVSYEADGPKAFDDVITRYNPPRRSTGPDRIQADYYQIKFHVTQAASFGFEDLIDPAFIGAETFSILERLKQAKGTEPANSAFHLVTTDRIIDEDPLGEIISNVDGSIRLDKLFDGTTDRSRKGKVRKLWRQHLKLSTDQELEQVLSGFHIQQSQPTLEAMREKVNTCFQIIGLITCETSSDFRFDGAARALRSQERYRFTREQFTALCEEENWIRSEAPESFRNVALRSFSDGPLDIMDALPEHTLSLLSLFEGRFPSPGIEWNDVIKPQVETFLTGIRQTERK... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:36796558, ECO:0000305|PubMed:32544385}; Note=Probably binds 2 Mg(2+), only 1 is seen in the crystal structure (PubMed:36796558). {ECO:0000269|PubMed:36796558}; | defense response to virus [GO:0051607] | null | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF18145; | null | Cap4 nuclease family | null | null | null | null | null | null | null | FUNCTION: Effector DNase of a CBASS antivirus system (PubMed:32544385, PubMed:36796558). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages (PubMed:32544385, PubMed:36755092, PubMed:36796558). The CD-NTase protein (CdnD) synthesizes cyclic nucleotides in response to... | Enterobacter hormaechei subsp. hoffmannii (strain UCI 50) |
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