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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P00504 | AATC_CHICK | MAASIFAAVPRAPPVAVFKLTADFREDGDSRKVNLGVGAYRTDEGQPWVLPVVRKVEQLIAGDGSLNHEYLPILGLPEFRANASRIALGDDSPAIAQKRVGSVQGLGGTGALRIGAEFLRRWYNGNNNTATPVYVSSPTWENHNSVFMDAGFKDIRTYRYWDAAKRGLDLQGLLDDMEKAPEFSIFILHACAHNPTGTDPTPDEWKQIAAVMKRRCLFPFFDSAYQGFASGSLDKDAWAVRYFVSEGFELFCAQSFSKNFGLYNERVGNLSVVGKDEDNVQRVLSQMEKIVRTTWSNPPSQGARIVATTLTSPQLFAEWK... | 2.6.1.1; 2.6.1.3 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:7897655}; | 2-oxoglutarate metabolic process [GO:0006103]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; cellular response to insulin stimulus [GO:0032869]; fatty acid homeostasis [GO:0055089]; gluconeogenesis [GO:0006094]; glutamate catabolic proce... | cytosol [GO:0005829] | L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-cysteine transaminase activity [GO:0047801]; phosphatidylserine decarboxylase activity [GO:0004609]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P13221}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825; Evidence={ECO:0000250... | null | null | null | null | FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic gluc... | Gallus gallus (Chicken) |
P00505 | AATM_HUMAN | MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPP... | 2.6.1.1; 2.6.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | 2-oxoglutarate metabolic process [GO:0006103]; 4-hydroxyproline catabolic process [GO:0019470]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; fatty acid transport [GO:0015908]; glutamate catabolic process to 2-oxoglutarate [GO:0019551]; ... | extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; pyridoxal phosphate binding [GO:0030170]; RNA binding [GO:0003723] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:9537447}. Cell membrane {ECO:0000269|PubMed:9537447}. Note=Exposure to alcohol promotes translocation to the cell membrane. {ECO:0000269|PubMed:9537447}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:26902786, ECO:0000269|PubMed:31422819}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynur... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:26902786}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 47.5 degrees Celsius. {ECO:0000269|PubMed:26902786}; | FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid... | Homo sapiens (Human) |
P00506 | AATM_PIG | MALLHSGRVLSGVASAFHPGLAAAASARASSWWAHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRYVTVQTISGTGALRIGANFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLHSYRYYDPKTCGFDFTGALEDISKIPAQSVILLHACAHNPTGVDPRPEQWKEMATLVKKNNLFAFFDMAYQGFASGDGNKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPMYSNPP... | 2.6.1.1; 2.6.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | 2-oxoglutarate metabolic process [GO:0006103]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; glutamate metabolic process [GO:0006536]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]; lipid transport [GO:0006869] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P00507}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L... | null | null | null | null | FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid... | Sus scrofa (Pig) |
P00507 | AATM_RAT | MALLHSGRVLSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAGKNLDKEYLPIGGLADFCKASAELALGENSEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEMAAVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPP... | 2.6.1.1; 2.6.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | 2-oxoglutarate metabolic process [GO:0006103]; amino acid metabolic process [GO:0006520]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; dicarboxylic acid metabolic process [GO:0043648]; fatty acid transport [GO:0015908]; female pregnancy... | cell surface [GO:0009986]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; T-tubule [GO:0030315] | amino acid binding [GO:0016597]; carboxylic acid binding [GO:0031406]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [... | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11962739}. Cell membrane {ECO:0000269|PubMed:11962739}. Note=Located in the mitochondria of liver, pancreas, spleen, heart, pituitary gland and submandibular gland cells. In kidney, located in the mitochondria, on the cell surface of regions with protrusion... | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:17442055}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-... | null | null | null | null | FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid... | Rattus norvegicus (Rat) |
P00508 | AATM_CHICK | MALLQSRLLLSAPRRAAATARASSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKSYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGIDVVLSQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIA... | 2.6.1.1; 2.6.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:1593633, ECO:0000269|PubMed:7903048, ECO:0000269|PubMed:8665890, ECO:0000269|PubMed:8952476}; | 2-oxoglutarate metabolic process [GO:0006103]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; glutamate metabolic process [GO:0006536]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:8665890}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P00507}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L... | null | null | null | null | FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid... | Gallus gallus (Chicken) |
P00509 | AAT_ECOLI | MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR... | 2.6.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11148029}; | aspartate catabolic process [GO:0006533]; L-phenylalanine biosynthetic process [GO:0009094]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | identical protein binding [GO:0042802]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:10556573}; | null | null | null | null | null | Escherichia coli (strain K12) |
P00511 | PFKAM_RABIT | MTHEEHHAARTLGVGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITAEEATRSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRITEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDNWEDHLCRRLSETRTRGSRLNIIIVAEGAIDRNGKPITSEGVKDLVVRRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEA... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002] | 6-phosphofructokinase complex [GO:0005945]; membrane [GO:0016020] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}. | Oryctolagus cuniculus (Rabbit) |
P00512 | PFKA_GEOSE | MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDIIHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCVGVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWSGLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGFETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEALANKHTIDQRMYALSKELSI | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6115424}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002] | 6-phosphofructokinase complex [GO:0005945]; membrane [GO:0016020] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Prokaryotic clade 'B1' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:8136379}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for ATP {ECO:0000269|PubMed:8136379}; KM=0.033 mM for fructose 6-phosphate {ECO:0000269|PubMed:8136379}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00339}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:8136379}. | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
P00514 | KAP0_BOVIN | MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPS... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cardiac muscle cell proliferation [GO:0060038]; cellular response to glucagon stimulus [GO:0071377]; mesoderm formation [GO:0001707]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of gene ex... | axoneme [GO:0005930]; cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; immunological synapse [GO:0001772]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; nucleotide-activated protein kin... | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subunit binding [GO:0034236]; ubiquitin protein ligase binding [GO:0031625] | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. The physiological significance of the in vitro phosphorylation of a proximal serine is unclear. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. | Bos taurus (Bovine) |
P00515 | KAP2_BOVIN | MSHIQIPPGLTELLQGYTVEVLRQRPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQDFDPGAGLVADAVADSESEDEEDLDVPIPGRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDPEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKVYKDGERIITQGEKADSFYIIESGEVSILIKSKTKVNKDGENQ... | null | null | regulation of protein phosphorylation [GO:0001932] | axoneme [GO:0005930]; cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; cytosol [GO:0005829]; nucleotide-activated protein kinase complex [GO:0031588]; plasma membrane raft [GO:0044853] | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subunit binding [GO:0034236]; ubiquitin protein ligase binding [GO:0031625] | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: A second phosphorylation site has not been located. {ECO:0000269|PubMed:1654846}.; PTM: Phosphorylation of Thr-212 by PDPK1 seems to attenuate the activity of PKA, perhaps by strengthening interaction between the regulatory and the catalytic subunits. {ECO:0000269|PubMed:1654846}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
P00516 | KGP1_BOVIN | MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGKVNVTREDSPNEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDS... | 2.7.11.12 | null | cGMP-mediated signaling [GO:0019934]; collateral sprouting [GO:0048668]; dendrite development [GO:0016358]; forebrain development [GO:0030900]; negative regulation of platelet aggregation [GO:0090331]; negative regulation of vascular associated smooth muscle cell migration [GO:1904753]; negative regulation of vascular ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; cGMP binding [GO:0030553]; cGMP-dependent protein kinase activity [GO:0004692]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310] | PF00027;PF16808;PF00069; | 2.60.120.10;1.20.5.490;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cGMP subfamily | PTM: Autophosphorylation increases kinase activity. {ECO:0000250}.; PTM: 65 kDa monomer is produced by proteolytic cleavage. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized with TRPC7 in the plasma membrane. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.12; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Serine/threonine protein kinase that acts as a key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but... | Bos taurus (Bovine) |
P00517 | KAPCA_BOVIN | MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFK... | 2.7.11.11 | null | cellular response to heat [GO:0034605]; mesoderm formation [GO:0001707]; negative regulation of TORC1 signaling [GO:1904262]; peptidyl-serine phosphorylation [GO:0018105]; protein kinase A signaling [GO:0010737]; protein phosphorylation [GO:0006468] | acrosomal vesicle [GO:0001669]; cAMP-dependent protein kinase complex [GO:0005952]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; neuromuscular junction [GO:0031594]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126... | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein domain specific binding [GO:0019904]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; pr... | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin K(2). Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity (By similarity). Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficiency (By simila... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10684253}. Cell membrane {ECO:0000250|UniProtKB:P17612}. Membrane {ECO:0000250|UniProtKB:P17612}; Lipid-anchor {ECO:0000250|UniProtKB:P17612}. Nucleus {ECO:0000269|PubMed:10684253}. Mitochondrion {ECO:0000250|UniProtKB:P05132}. Note=Translocates into the nucleus (mono... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus (By similarity). Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (By similarity). Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 wh... | Bos taurus (Bovine) |
P00518 | PHKG1_RABIT | MTRDAALPGSHSTHGFYENYEPKEILGRGVSSVVRRCIHKPTCKEYAVKIIDVTGGGSFSAEEVQELREATLKEVDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKLREVCGTPSYLAPEIIECSMNDNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDYSDTVKDLVSRFLVVQPQKRYTAEEALAHPFFQQYVVEEVRHFSPRGKFKVICLTVLASVRIYY... | 2.7.11.1; 2.7.11.19; 2.7.11.26 | null | glycogen biosynthetic process [GO:0005978]; phosphorylation [GO:0016310] | phosphorylase kinase complex [GO:0005964]; skeletal muscle myofibril [GO:0098723] | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; phosphorylase kinase activity [GO:0004689]; protein serine kinase activity [GO:0106310]; tau-protein kinase activity [GO:0050321] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP + phosphorylase b = 2 ADP + phosphorylase a.; EC=2.7.11.19; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:3061... | null | null | null | null | FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3. {ECO:0000269|PubMed:8454596, ECO... | Oryctolagus cuniculus (Rabbit) |
P00519 | ABL1_HUMAN | MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTY... | 2.7.10.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00520}; | actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; activated T cell proliferation [GO:0050798]; activation of protein kinase C activity [GO:1990051]; alpha-beta T cell differentiation [GO:0046632]; associative learning [GO:0008306]; autophagy [GO:0006914]; B cell proliferation inv... | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; growth cone [GO:0030426]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nuclear body [GO:0016604]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; p... | actin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; ATP binding [GO:0005524]; bubble DNA binding [GO:0000405]; delta-catenin binding [GO:0070097]; DNA binding [GO:0003677]; ephrin receptor binding [GO:0046875]; four-way junction DNA binding [GO:0000400]; kinase activity [GO:0016301]; magnesium ion ... | PF08919;PF07714;PF00017;PF00018; | 1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, ABL subfamily | PTM: Acetylated at Lys-711 by EP300 which promotes the cytoplasmic translocation. {ECO:0000269|PubMed:16648821}.; PTM: Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm depending on environmental signals. Sequestered into the cytoplasm through interaction with 14-3-3 proteins. Localizes to mitochondria in response to oxidative stress (By similarity). {EC... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling thr... | Homo sapiens (Human) |
P00520 | ABL1_MOUSE | MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTIYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTY... | 2.7.10.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12748290}; Note=Mg(2+) and Mn(2+) were both present in the kinase buffer but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305}; | actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; activated T cell proliferation [GO:0050798]; alpha-beta T cell differentiation [GO:0046632]; associative learning [GO:0008306]; autophagy [GO:0006914]; B cell proliferation [GO:0042100]; B cell proliferation involved in immune res... | actin cytoskeleton [GO:0015629]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; growth cone [GO:0030426]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleus [GO:0005... | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; bubble DNA binding [GO:0000405]; delta-catenin binding [GO:0070097]; ephrin receptor binding [GO:0046875]; four-way junction DNA binding [GO:0000400]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; mito... | PF08919;PF07714;PF00017;PF00018; | 1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, ABL subfamily | PTM: Acetylated at Lys-710 by EP300 which promotes the cytoplasmic translocation. {ECO:0000250}.; PTM: Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity (By si... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion. Note=The myristoylated c-ABL protein is reported to be nuclear. Sequestered into the cytoplasm through interaction with 14-3-3 proteins (By similarity). Localizes to mitochondria in response to oxidative stress. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling thr... | Mus musculus (Mouse) |
P00522 | ABL_DROME | MGAQQGKDRGAHSGGGGSGAPVSCIGLSSSPVASVSPHCISSSSGVSSAPLGGGSTLRGSRIKSSSSGVASGSGSGGGGGGSGSGLSQRSGGHKDARCNPTVGLNIFTEHNEALLQSRPLPHIPAGSTAASLLADAAELQQHQQDSGGLGLQGSSLGGGHSSTTSVFESAHRWTSKENLLAPGPEEDDPQLFVALYDFQAGGENQLSLKKGEQVRILSYNKSGEWCEAHSDSGNVGWVPSNYVTPLNSLEKHSWYHGPISRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRISEDPDGKVFVTQEAKFN... | 2.7.10.2 | null | axis elongation [GO:0003401]; axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; axonogenesis [GO:0007409]; branchiomotor neuron axon guidance [GO:0021785]; central nervous system development [GO:0007417]; chemical synaptic transmission [GO:0007268]; compound eye development [GO:0048749]; d... | apical cortex [GO:0045179]; axon [GO:0030424]; cell cortex [GO:0005938]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; synapse [GO:0045202] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713] | PF08919;PF07714;PF00017;PF00018; | 1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, ABL subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis; critical for embryonic epithelial morphogenesis regulating cell shape changes and cell migration (PubMed:11756472, PubMed:12973825, PubMed:9635189). Plays a critical role in transducing embryonic midline repulsive... | Drosophila melanogaster (Fruit fly) |
P00523 | SRC_CHICK | MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE... | 2.7.10.2 | null | bone resorption [GO:0045453]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of in... | cell junction [GO:0030054]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; nucleus [GO:0005634]; perinuclear region of... | ATP binding [GO:0005524]; connexin binding [GO:0071253]; heme binding [GO:0020037]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Myristoylated at Gly-2, and this is essential for targeting to membranes. {ECO:0000250}.; PTM: Dephosphorylated at Tyr-527 by PTPRJ. Phosphorylated on Tyr-527 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-416. Normally maintained in an inactive conformation wi... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1378446, ECO:0000269|PubMed:8325872}; Lipid-anchor {ECO:0000250|UniProtKB:P05480}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05480}. Endosome membrane {ECO:0000269|PubMed:1378446}; Peripheral membrane protein {ECO:0000269|PubMed:1378446}. Nucleus {ECO:0... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates i... | Gallus gallus (Chicken) |
P00524 | SRC_RSVSA | MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESWIETDLSFKKGERLQIVNNTEGNWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE... | 2.7.10.2 | null | bone resorption [GO:0045453]; cell adhesion [GO:0007155]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast... | extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: The phosphorylated form is termed pp60v-src. {ECO:0000269|PubMed:6264320}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. Causes mitotic slippage in addition to cytokinesis failure in the host cell (PubMed:30135207). Phosphorylates and attenu... | Rous sarcoma virus subgroup A (strain Schmidt-Ruppin) (RSV-SR-A) |
P00525 | SRC_AVISR | MGSSKSKPKDPSQRRCSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE... | 2.7.10.2 | null | bone resorption [GO:0045453]; cell adhesion [GO:0007155]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast... | extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: The phosphorylated form is termed pp60v-src. {ECO:0000250|UniProtKB:P00524}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. | Avian sarcoma virus (strain rASV1441) |
P00526 | SRC_RSVP | MGSSKSKPKDPSQRRHSLEPPDSTHHGGFPASQTPDETAAPDAHRNPSRSFGTVATEPKLFWGFNTSDTVTSPQRAGALAGGVTTFVALYDYESWTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRKSETAKGAYCLSVSDFDNAKGPNVKHYKIYKLYSGGFYITSRTQFGSLQQLVAYYSKHADGLCHRLANVCPTSKPQTQGLAKDAWEIPRESLRLEAKLGQGCFGEVWMGTWNDTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE... | 2.7.10.2 | null | bone resorption [GO:0045453]; cell adhesion [GO:0007155]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast... | extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: The phosphorylated form is termed pp60v-src. {ECO:0000269|PubMed:6264320}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. | Rous sarcoma virus subgroup C (strain Prague) (RSV-Pr-C) |
P00528 | SRC64_DROME | MGNKCCSKRQDQELALAYPTGGYKKSDYTFGQTHINSSGGGNMGGVLGQKHNNGGSLDSRYTPDPNHRGPLKIGGKGGVDIIRPRTTPTGVPGVVLKRVVVALYDYKSRDESDLSFMKGDRMEVIDDTESDWWRVVNLTTRQEGLIPLNFVAEERSVNSEDWFFENVLRKEADKLLLAEENPRGTFLVRPSEHNPNGYSLSVKDWEDGRGYHVKHYRIKPLDNGGYYIATNQTFPSLQALVMAYSKNALGLCHILSRPCPKPQPQMWDLGPELRDKYEIPRSEIQLLRKLGRGNFGEVFYGKWRNSIDVAVKTLREGTMS... | 2.7.10.2 | null | actin cytoskeleton organization [GO:0030036]; adherens junction organization [GO:0034332]; axon guidance [GO:0007411]; cell differentiation [GO:0030154]; cellularization [GO:0007349]; epithelial cell-cell adhesion [GO:0090136]; female germline ring canal formation [GO:0007301]; female germline ring canal formation, act... | cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; germline ring canal [GO:0045172]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Phosphorylated. {ECO:0000269|PubMed:31491385}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that may play a role in the development of neural tissue and smooth muscle (PubMed:2996778). May contribute to tyrosine phosphorylation of Dscam1, a cell surface receptor involved in targeting of growing axons during eye morphogenesis (PubMed:12014990). {ECO:0000269|PubMed:12014990, EC... | Drosophila melanogaster (Fruit fly) |
P00533 | EGFR_HUMAN | MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEE... | 2.7.10.1 | null | activation of phospholipase C activity [GO:0007202]; astrocyte activation [GO:0048143]; cell surface receptor signaling pathway [GO:0007166]; cell-cell adhesion [GO:0098609]; cellular response to amino acid stimulus [GO:0071230]; cellular response to cadmium ion [GO:0071276]; cellular response to dexamethasone stimulus... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cell junction [GO:0030054]; cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane ... | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATPase binding [GO:0051117]; cadherin binding [GO:0045296]; calmodulin binding [GO:0005516]; chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899]; epidermal growth factor binding [GO:0048408]; epidermal growt... | PF00757;PF14843;PF07714;PF01030;PF21314; | 1.20.5.420;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily | PTM: Phosphorylated on Tyr residues in response to EGF (PubMed:20462955, PubMed:27153536). Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and s... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:23589287, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960, ECO:0000269|PubMed:35538033}; Single-pass type I membrane protein {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane {ECO:000026... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10805725, PubMed:27153536, PubMed:2790960, PubMed:35538033). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacell... | Homo sapiens (Human) |
P00536 | MOS_MOUSE | MPSPLSLCRYLPRELSPSVDSRSCSIPLVAPRKAGKLFLGTTPPRAPGLPRRLAWFSIDWEQVCLMHRLGSGGFGSVYKATYHGVPVAIKQVNKCTKDLRASQRSFWAELNIARLRHDNIVRVVAASTRTPEDSNSLGTIIMEFGGNVTLHQVIYGATRSPEPLSCREQLSLGKCLKYSLDVVNGLLFLHSQSILHLDLKPANILISEQDVCKISDFGCSQKLQDLRCRQASPHHIGGTYTHQAPEILKGEIATPKADIYSFGITLWQMTTREVPYSGEPQYVQYAVVAYNLRPSLAGAVFTASLTGKTLQNIIQSCWEA... | 2.7.11.1 | null | chromatin organization [GO:0006325]; establishment of meiotic spindle orientation [GO:0051296]; MAPK cascade [GO:0000165]; meiotic spindle organization [GO:0000212]; negative regulation of metaphase/anaphase transition of meiotic cell cycle [GO:1902103]; oocyte maturation [GO:0001556]; positive regulation of ERK1 and E... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00540}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine kinase involved in the regulation of MAPK signaling. Is an activator of the ERK1/2 signaling cascade playing an essential role in the stimulation of oocyte maturation. {ECO:0000250|UniProtKB:P00540}. | Mus musculus (Mouse) |
P00539 | MOS_RAT | MPSPLILCRYLPRELSPTVDSRSCSSPLVASRAGKFLGATPPRAPRLSRRLAWCFIDWGQVCLLHRLGSGGFGSVYKATYHGVPVAIKQVNKCTRTLRASQRNFWAELNIARLHHDNIIRVVAASTRTPEGSNSLGTIIMEFGGNVTLHQVIYGATRSPEPLSCREQLSLGKCLKYSLDIVNGLLFLHSQSILHLDLKPANILISEKDVCKISDFGCSQKLQDLRCRPSLHHIGGTYTHQAPELLKGEIATPKADIYSFGITLWQMTTREVPYSGEPQYVQYAVVAYNLRPHWQAVFTASLTGKTLQNNVQSCWEARALQ... | 2.7.11.1 | null | chromatin organization [GO:0006325]; establishment of meiotic spindle orientation [GO:0051296]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; meiotic spindle organization [GO:0000212]; negative regulation of metaphase/anaphase transition of meiotic cell cycle [GO:1902103]; oocyte maturation... | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00540}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine kinase involved in the regulation of MAPK signaling. Is an activator of the ERK1/2 signaling cascade playing an essential role in the stimulation of oocyte maturation. {ECO:0000250|UniProtKB:P00540}. | Rattus norvegicus (Rat) |
P00540 | MOS_HUMAN | MPSPLALRPYLRSEFSPSVDARPCSSPSELPAKLLLGATLPRAPRLPRRLAWCSIDWEQVCLLQRLGAGGFGSVYKATYRGVPVAIKQVNKCTKNRLASRRSFWAELNVARLRHDNIVRVVAASTRTPAGSNSLGTIIMEFGGNVTLHQVIYGAAGHPEGDAGEPHCRTGGQLSLGKCLKYSLDVVNGLLFLHSQSIVHLDLKPANILISEQDVCKISDFGCSEKLEDLLCFQTPSYPLGGTYTHRAPELLKGEGVTPKADIYSFAITLWQMTTKQAPYSGERQHILYAVVAYDLRPSLSAAVFEDSLPGQRLGDVIQRC... | 2.7.11.1 | null | chromatin organization [GO:0006325]; establishment of meiotic spindle orientation [GO:0051296]; MAPK cascade [GO:0000165]; meiotic spindle organization [GO:0000212]; negative regulation of metaphase/anaphase transition of meiotic cell cycle [GO:1902103]; oocyte maturation [GO:0001556]; positive regulation of ERK1 and E... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35670744}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine kinase involved in the regulation of MAPK signaling. Is an activator of the ERK1/2 signaling cascade playing an essential role in the stimulation of oocyte maturation. {ECO:0000269|PubMed:34779126, ECO:0000269|PubMed:34997960, ECO:0000269|PubMed:35670744}. | Homo sapiens (Human) |
P00545 | KFMS_FSVMD | RMPSGPGHYGASAETPGPRPPLCPASSCCLPTEAMGPRALLVLLMATAWHAQGVPVIQPSGPELVVEPGTTVTLRCVGNGSVEWDGPISPHWNLDLDPPSSILTTNNATFQNTGTYHCTEPGNPRGGNATIHLYVKDPARPWKVLAQEVTVLEGQDALLPCLLTDPALEAGVSLVRVRGRPVLRQTNYSFSPWHGFTIHKAKFIENHVYQCSARVDGRTVTSMGIWLKVQKDISGPATLTLEPAELVRIQGEAAQIVCSASNIDVNFDVSLRHGDTKLTISQQSDFHDNRYQKVLTLNLDHVSFQDAGNYSCTATNAWGN... | 2.7.10.1 | null | osteoclast differentiation [GO:0030316]; phosphorylation [GO:0016310]; positive regulation of cell migration [GO:0030335]; regulation of MAPK cascade [GO:0043408]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | CSF1-CSF1R complex [GO:1990682]; membrane [GO:0016020]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; macrophage colony-stimulating factor receptor activity [GO:0005011] | PF00047;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Truncated version of the receptor for colony-stimulating factor 1 (CSF-1). | Feline sarcoma virus (strain McDonough) |
P00546 | CDK1_YEAST | MSGELANYKRLEKVGEGTYGVVYKALDLRPGQGQRVVALKKIRLESEDEGVPSTAIREISLLKELKDDNIVRLYDIVHSDAHKLYLVFEFLDLDLKRYMEGIPKDQPLGADIVKKFMMQLCKGIAYCHSHRILHRDLKPQNLLINKDGNLKLGDFGLARAFGVPLRAYTHEIVTLWYRAPEVLLGGKQYSTGVDTWSIGCIFAEMCNRKPIFSGDSEIDQIFKIFRVLGTPNEAIWPDIVYLPDFKPSFPQWRRKDLSQVVPSLDPRGIDLLDKLLAYDPINRISARRAAIHPYFQES | 2.7.11.22 | null | 7-methylguanosine mRNA capping [GO:0006370]; cell division [GO:0051301]; DNA damage response [GO:0006974]; DNA double-strand break processing [GO:0000729]; double-strand break repair via nonhomologous end joining [GO:0006303]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO... | cellular bud neck [GO:0005935]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; histone binding [GO:0042393]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II complex... | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P24941}; CATALYT... | null | null | null | null | FUNCTION: Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles (By similarity). Required to drive the G1-S transition (PubMed:2664468). More than 200 substrates have been identified (PubMed:14574415). Substrate specificity is in part regulated by the bound cyclin protein (By si... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P00549 | KPYK1_YEAST | MSRLERLTSLNVVAGSDLRRTSIIGTIGPKTNNPETLVALRKAGLNIVRMNFSHGSYEYHKSVIDNARKSEELYPGRPLAIALDTKGPEIRTGTTTNDVDYPIPPNHEMIFTTDDKYAKACDDKIMYVDYKNITKVISAGRIIYVDDGVLSFQVLEVVDDKTLKVKALNAGKICSHKGVNLPGTDVDLPALSEKDKEDLRFGVKNGVHMVFASFIRTANDVLTIREVLGEQGKDVKIIVKIENQQGVNNFDEILKVTDGVMVARGDLGIEIPAPEVLAVQKKLIAKSNLAGKPVICATQMLESMTYNPRPTRAEVSDVGN... | 2.7.1.40 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10413488}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000305|PubMed:9519410}; | cellular response to insulin stimulus [GO:0032869]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]; pyruvate metabolic process [GO:0006090] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; potassium ion binding [GO:0030955]; pyruvate kinase activity [GO:0004743] | PF00224;PF02887; | 3.20.20.60;2.40.33.10;3.40.1380.20; | Pyruvate kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; Evidence={ECO:0000269|PubMed:10413488}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for phosphoenolpyruvate (with magnesium as divalent cation) {ECO:0000269|PubMed:10413488}; KM=0.021 mM for phosphoenolpyruvate (with manganese as divalent cation) {ECO:0000269|PubMed:10413488}; KM=1.1 mM for ADP (with magnesium as divalent cation) {ECO:0000... | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:10413488}; | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P00550 | PTM3C_ECOLI | MSSDIKIKVQSFGRFLSNMVMPNIGAFIAWGIITALFIPTGWLPNETLAKLVGPMITYLLPLLIGYTGGKLVGGERGGVVGAITTMGVIVGADMPMFLGSMIAGPLGGWCIKHFDRWVDGKIKSGFEMLVNNFSAGIIGMILAILAFLGIGPIVEALSKMLAAGVNFMVVHDMLPLASIFVEPAKILFLNNAINHGIFSPLGIQQSHELGKSIFFLIEANPGPGMGVLLAYMFFGRGSAKQSAGGAAIIHFLGGIHEIYFPYVLMNPRLILAVILGGMTGVFTLTILGGGLVSPASPGSILAVLAMTPKGAYFANIAGVC... | 2.7.1.197 | null | mannitol transmembrane transport [GO:0015797]; phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]; phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | kinase activity [GO:0016301]; protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity [GO:0022872]; protein-phosphocysteine-mannitol phosphotransferase system transporter activity [GO:0090565]; protein-phosphocysteine-sugar phosphotransferase activity [GO:0090563] | PF00359;PF02378;PF02302; | 3.40.50.2300; | null | PTM: An intramolecular phosphotransfer takes places between His-554 and Cys-384. {ECO:0000305|PubMed:16443929}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:6309813}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:368051}. | CATALYTIC ACTIVITY: Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannitol 1-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381, ChEBI:CHEBI:64837; EC=2.7.1.197; Evidence={ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=66 uM for mannitol phosphorylation {ECO:0000269|PubMed:2123863}; Vmax=21.7 nmol/min/mg enzyme toward mannitol {ECO:0000269|PubMed:2123863}; | null | null | null | FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in D-mannitol transport (PubMed:21238... | Escherichia coli (strain K12) |
P00558 | PGK1_HUMAN | MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPES... | 2.7.2.3 | null | canonical glycolysis [GO:0061621]; cellular response to hypoxia [GO:0071456]; epithelial cell differentiation [GO:0030855]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; negative regulation of angiogenesis [GO:0016525]; phosphorylation [GO:0016310]; plasminogen activation [GO:0031639] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; membrane raft [GO:0045121] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; phosphoglycerate kinase activity [GO:0004618]; protein-disulfide reductase (NAD(P)) activity [GO:0047134] | PF00162; | 3.40.50.1260; | Phosphoglycerate kinase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; Evidence={ECO:0000269|PubMed:30323285, ECO:0000269|PubMed:7391028}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. {ECO:0000269|PubMed:30323285, ECO:0000269|PubMed:7391028}. | null | null | FUNCTION: Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate (PubMed:30323285, PubMed:7391028). In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer re... | Homo sapiens (Human) |
P00560 | PGK_YEAST | MSLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFTFKKVLENTEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVTDKEGIPAGWQGLDNGPESRK... | 2.7.2.3 | null | gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; phosphoglycerate kinase activity [GO:0004618] | PF00162; | 3.40.50.1260; | Phosphoglycerate kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}. Mitochondrion {ECO:0000269|PubMed:16823961}. | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P00561 | AK1H_ECOLI | MRVLKFGGTSVANAERFLRVADILESNARQGQVATVLSAPAKITNHLVAMIEKTISGQDALPNISDAERIFAELLTGLAAAQPGFPLAQLKTFVDQEFAQIKHVLHGISLLGQCPDSINAALICRGEKMSIAIMAGVLEARGHNVTVIDPVEKLLAVGHYLESTVDIAESTRRIAASRIPADHMVLMAGFTAGNEKGELVVLGRNGSDYSAAVLAACLRADCCEIWTDVDGVYTCDPRQVPDARLLKSMSYQEAMELSYFGAKVLHPRTITPIAQFQIPCLIKNTGNPQAPGTLIGASRDEDELPVKGISNLNNMAMFSV... | 1.1.1.3; 2.7.2.4 | null | homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; phosphorylation [GO:0016310]; protein homotetramerization [GO:0051289]; threonine biosynthetic process [GO:0009088] | null | aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524]; homoserine dehydrogenase activity [GO:0004412]; identical protein binding [GO:0042802]; NADP binding [GO:0050661] | PF00696;PF13840;PF00742;PF03447; | 3.40.1160.10;3.40.50.720;3.30.2130.10; | Aspartokinase family; Homoserine dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3; CATALYTIC ACTIVITY: Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH... | null | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de n... | null | null | null | Escherichia coli (strain K12) |
P00562 | AK2H_ECOLI | MSVIAQAGAKGRQLHKFGGSSLADVKCYLRVAGIMAEYSQPDDMMVVSAAGSTTNQLINWLKLSQTDRLSAHQVQQTLRRYQCDLISGLLPAEEADSLISAFVSDLERLAALLDSGINDAVYAEVVGHGEVWSARLMSAVLNQQGLPAAWLDAREFLRAERAAQPQVDEGLSYPLLQQLLVQHPGKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSEIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHDDVCLI... | 1.1.1.3; 2.7.2.4 | null | homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; methionine biosynthetic process [GO:0009086]; phosphorylation [GO:0016310]; threonine biosynthetic process [GO:0009088] | cytosol [GO:0005829] | aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524]; homoserine dehydrogenase activity [GO:0004412]; NADP binding [GO:0050661] | PF00696;PF00742;PF03447; | 3.40.1160.10;1.20.120.1320;3.40.50.720; | Aspartokinase family; Homoserine dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3; CATALYTIC ACTIVITY: Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH... | null | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de n... | null | null | null | Escherichia coli (strain K12) |
P00568 | KAD1_HUMAN | MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDAGPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDSVFSQVCTHLDALK | 2.7.4.10; 2.7.4.3; 2.7.4.6 | null | ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; outer dense fiber [GO:0001520] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899] | PF00406; | 3.40.50.300; | Adenylate kinase family, AK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05081}. | CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:2542324}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-tr... | null | null | null | null | FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (PubMed:2542324). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate ... | Homo sapiens (Human) |
P00569 | KAD1_RABIT | MEEKLKKAKIIFVVGGPGSGKGTQCEKIVHKYGYTHLSTGDLLRAEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKADTSKGFLIDGYPRQVQQGEEFERRIAQPTLLLYVDAGPETMQKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDNVFSQVCTHLDALK | 2.7.4.10; 2.7.4.3; 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P05081}; | ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899] | PF00406; | 3.40.50.300; | Adenylate kinase family, AK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05081}. | CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:... | null | null | null | null | FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (By similarity). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate d... | Oryctolagus cuniculus (Rabbit) |
P00570 | KAD1_BOVIN | MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSARGKMLSEIMEKGQLVPLETVLDMLRDAMVAKVDTSKGFLIDGYPREVQQGEEFERRIAQPTLLLYVDAGPETMTKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDNVFSQVCTHLDALK | 2.7.4.10; 2.7.4.3; 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P05081}; | ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; outer dense fiber [GO:0001520] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899] | PF00406; | 3.40.50.300; | Adenylate kinase family, AK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05081}. | CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:... | null | null | null | null | FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (By similarity). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate d... | Bos taurus (Bovine) |
P00571 | KAD1_PIG | MEEKLKKSKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSARGKMLSEIMEKGQLVPLETVLDMLRDAMVAKVDTSKGFLIDGYPREVKQGEEFERKIGQPTLLLYVDAGPETMTKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDDVFSQVCTHLDTLK | 2.7.4.10; 2.7.4.3; 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:2551297, ECO:0000305|PubMed:2551298}; | ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899] | PF00406; | 3.40.50.300; | Adenylate kinase family, AK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03171}. | CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:2551297}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-tr... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.83 mM for ThDP {ECO:0000269|PubMed:2551298}; KM=43 mM for ADP {ECO:0000269|PubMed:2551298}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.0 for ThTP synthesis. {ECO:0000269|PubMed:2551298}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius for ThTP synthesis. {ECO:0000269|PubMed:2551298}; | FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (PubMed:2551297). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate ... | Sus scrofa (Pig) |
P00572 | KTHY_YEAST | MMGRGKLILIEGLDRTGKTTQCNILYKKLQPNCKLLKFPERSTRIGGLINEYLTDDSFQLSDQAIHLLFSANRWEIVDKIKKDLLEGKNIVMDRYVYSGVAYSAAKGTNGMDLDWCLQPDVGLLKPDLTLFLSTQDVDNNAEKSGFGDERYETVKFQEKVKQTFMKLLDKEIRKGDESITIVDVTNKGIQEVEALIWQIVEPVLSTHIDHDKFSFF | 2.7.4.9 | null | dTDP biosynthetic process [GO:0006233]; dTTP biosynthetic process [GO:0006235]; dUDP biosynthetic process [GO:0006227]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP binding [GO:0005524]; nucleoside diphosphate kinase activity [GO:0004550]; thymidylate kinase activity [GO:0004798]; UMP/dUMP kinase activity [GO:0009041] | PF02223; | 3.40.50.300; | Thymidylate kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000269|PubMed:6088527}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13518; Evidence={ECO:0000269|PubMed:6088527}; | null | PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000305|PubMed:6088527}. | null | null | FUNCTION: Catalyzes the conversion of dTMP to dTDP. {ECO:0000269|PubMed:6088527}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P00573 | RPOL_BPT7 | MNTINIAKNDFSDIELAAIPFNTLADHYGERLAREQLALEHESYEMGEARFRKMFERQLKAGEVADNAAAKPLITTLLPKMIARINDWFEEVKAKRGKRPTAFQFLQEIKPEAVAYITIKTTLACLTSADNTTVQAVASAIGRAIEDEARFGRIRDLEAKHFKKNVEEQLNKRVGHVYKKAFMQVVEADMLSKGLLGGEAWSSWHKEDSIHVGVRCIEMLIESTGMVSLHRQNAGVVGQDSETIELAPEYAEAIATRAGALAGISPMFQPCVVPPKPWTGITGGGYWANGRRPLALVRTHSKKALMRYEDVYMPEVYKAI... | 2.7.7.6 | null | DNA-templated transcription [GO:0006351]; DNA-templated viral transcription [GO:0039695] | DNA-directed RNA polymerase complex [GO:0000428] | DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; mitochondrial promoter sequence-specific DNA binding [GO:0001018] | PF00940;PF14700; | 1.10.287.260;1.10.287.280;1.10.150.20;1.10.1320.10; | Phage and mitochondrial RNA polymerase family | null | null | CATALYTIC ACTIVITY: 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=2.7.7.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031, ECO:0000255|PROSITE-ProRule:PRU10032, E... | null | null | null | null | FUNCTION: Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an 'abortive phase' where very short transcripts are synthesized and released before proceeding to the processive transcription o... | Escherichia phage T7 (Bacteriophage T7) |
P00579 | RPOD_ECOLI | MEQNPQSQLKLLVTRGKEQGYLTYAEVNDHLPEDIVDSDQIEDIIQMINDMGIQVMEEAPDADDLMLAENTADEDAAEAAAQVLSSVESEIGRTTDPVRMYMREMGTVELLTREGEIDIAKRIEDGINQVQCSVAEYPEAITYLLEQYDRVEAEEARLSDLITGFVDPNAEEDLAPTATHVGSELSQEDLDDDEDEDEEDGDDDSADDDNSIDPELAREKFAELRAQYVVTRDTIKAKGRSHATAQEEILKLSEVFKQFRLVPKQFDYLVNSMRVMMDRVRTQERLIMKLCVEQCKMPKKNFITLFTGNETSDTWFNAAI... | null | null | DNA-templated transcription initiation [GO:0006352]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription initiation [GO:2000142]; response to heat [GO:0009408] | cytosol [GO:0005829]; cytosolic DNA-directed RNA polymerase complex [GO:0000345]; sigma factor antagonist complex [GO:1903865] | DNA binding [GO:0003677]; sigma factor activity [GO:0016987] | PF04546;PF03979;PF00140;PF04542;PF04539;PF04545; | 1.10.601.10;1.10.220.120;1.10.10.10; | Sigma-70 factor family, RpoD/SigA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}. | null | null | null | null | null | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. Preferentially transcribes genes associated with fast growth, such as ribosomal operons, other protein... | Escherichia coli (strain K12) |
P00581 | DPOL_BPT7 | MIVSDIEANALLESVTKFHCGVIYDYSTAEYVSYRPSDFGAYLDALEAEVARGGLIVFHNGHKYDVPALTKLAKLQLNREFHLPRENCIDTLVLSRLIHSNLKDTDMGLLRSGKLPGKRFGSHALEAWGYRLGEMKGEYKDDFKRMLEEQGEEYVDGMEWWNFNEEMMDYNVQDVVVTKALLEKLLSDKHYFPPEIDFTDVGYTTFWSESLEAVDIEHRAAWLLAKQERNGFPFDTKAIEELYVELAARRSELLRKLTETFGSWYQPKGGTEMFCHPRTGKPLPKYPRIKTPKVGGIFKKPKNKAQREGREPCELDTREY... | 2.7.7.7; 3.1.11.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04101, ECO:0000305|PubMed:9440688}; | DNA synthesis involved in DNA replication [GO:0090592]; DNA-templated DNA replication [GO:0006261]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]; viral DNA genome replication [GO:0039693] | null | 3'-5' exonuclease activity [GO:0008408]; DNA binding [GO:0003677]; DNA exonuclease activity [GO:0004529]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF00476; | 3.30.70.370;3.30.420.10; | DNA polymerase type-A family | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|HAMAP-Rule:MF_04101, ECO:0000269|PubMed:24591606}; | null | null | null | null | FUNCTION: Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction (By similarity). Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). ... | Escherichia phage T7 (Bacteriophage T7) |
P00582 | DPO1_ECOLI | MVQIPQNPLILVDGSSYLYRAYHAFPPLTNSAGEPTGAMYGVLNMLRSLIMQYKPTHAAVVFDAKGKTFRDELFEHYKSHRPPMPDDLRAQIEPLHAMVKAMGLPLLAVSGVEADDVIGTLAREAEKAGRPVLISTGDKDMAQLVTPNITLINTMTNTILGPEEVVNKYGVPPELIIDFLALMGDSSDNIPGVPGVGEKTAQALLQGLGGLDTLYAEPEKIAGLSFRGAKTMAAKLEQNKEVAYLSYQLATIKTDVELELTCEQLEVQQPAAEELLGLFKKYEFKRWTADVEAGKWLQAKGAKPAAKPQETSVADEAPEV... | 2.7.7.7 | null | base-excision repair [GO:0006284]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA-templated DNA replication [GO:0006261]; double-strand break repair [GO:0006302]; double-strand break repair via alternative nonhomologous end joining [GO:0097681] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | 3'-5' exonuclease activity [GO:0008408]; 5'-3' exonuclease activity [GO:0008409]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887] | PF01367;PF02739;PF00476;PF01612; | 3.30.70.370;1.10.150.20;3.40.50.1010;3.30.420.10; | DNA polymerase type-A family | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; | null | null | null | null | FUNCTION: In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template. | Escherichia coli (strain K12) |
P00586 | THTR_BOVIN | MVHQVLYRALVSTKWLAESVRAGKVGPGLRVLDASWYSPGTREARKEYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGSLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQGRYLGTQPEPDAVGLDSGHIRGSVNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIATCRKGVTACHIALAAYLCGKPDVAIYDGSWFEWFHRAPPETWVSQGKGGKA | 2.8.1.1 | null | rRNA import into mitochondrion [GO:0035928]; rRNA transport [GO:0051029] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | 3-mercaptopyruvate sulfurtransferase activity [GO:0016784]; 5S rRNA binding [GO:0008097]; thiosulfate sulfurtransferase activity [GO:0004792] | PF00581; | 3.40.250.10; | null | null | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407, ChEBI:CHEBI:33542; EC=2.8.1.1; Evidence={ECO:0000269|PubMed:711738}; | null | null | null | null | FUNCTION: Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA (By similarity). Formation of iron-sulfur complexes and cyanide detoxification. Binds molecular oxygen and sulfur. {ECO:0000250}. | Bos taurus (Bovine) |
P00588 | DTX_CORBE | MLVRGYVVSRKLFASILIGALLGIGAPPSAHAGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYEYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQV... | 2.4.2.36 | null | null | extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; NAD+-diphthamide ADP-ribosyltransferase activity [GO:0047286]; nucleotidyltransferase activity [GO:0016779]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729] | PF02763;PF01324;PF02764; | 3.90.175.10;2.60.40.700;1.10.490.40; | null | PTM: Proteolytic activation by host furin cleaves the protein in two parts, Diphtheria toxin fragment A and Diphtheria toxin fragment B; which remain associated via a disulfide bond. {ECO:0000269|PubMed:8253774}. | null | CATALYTIC ACTIVITY: Reaction=diphthamide-[translation elongation factor 2] + NAD(+) = H(+) + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] + nicotinamide; Xref=Rhea:RHEA:11820, Rhea:RHEA-COMP:10174, Rhea:RHEA-COMP:10175, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:... | null | null | null | null | FUNCTION: Diphtheria toxin, produced by a phage infecting Corynebacterium diphtheriae, is a proenzyme that, after activation, catalyzes the covalent attachment of the ADP ribose moiety of NAD to eukaryotic elongation factor 2 (eEF-2). Fragment A is the catalytic portion responsible for enzymatic ADP-ribosylation of elo... | Corynephage beta |
P00590 | CUTI1_FUSVN | MKFFALTTLLAATASALPTSNPAQELEARQLGRTTRDDLINGNSASCRDVIFIYARGSTETGNLGTLGPSIASNLESAFGKDGVWIQGVGGAYRATLGDNALPRGTSSAAIREMLGLFQQANTKCPDATLIAGGYSQGAALAAASIEDLDSAIRDKIAGTVLFGYTKNLQNRGRIPNYPADRTKVFCNTGDLVCTGSLIVAAPHLAYGPDARGPAPEFLIEKVRAVRGSA | 3.1.1.74 | null | null | extracellular region [GO:0005576] | cutinase activity [GO:0050525] | PF01083; | 3.40.50.1820; | Cutinase family | PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}.; PTM: O-glycosylated; contains one mole each of mannose, arabinose, N-acetylglucosamine, and glucuro... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}. | CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109, ECO:0000269|PubMed:18658138, ECO:0000305|PubMed:19810726, ECO:0000305|PubMed:8286366, ECO:0000305|PubMed:8555209}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.67 uM for p-nitrophenyl acetate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=1.26 uM for p-nitrophenyl butyrate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=0.68 mM for p-nitrophenyl butyrate (at pH 9 and 30 degrees Celsius) {ECO:0000269|PubMed:8555209}; KM=1.4... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:18658138}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is below 30 degrees Celsius (PubMed:19810726). Optimum temperature is 30-40 degrees Celsius (PubMed:18658138). {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:19810726}; | FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18658138, PubMed:19810726, PubMed:8286366, PubMed:8555209). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18658138, PubMed:19810726, PubMed:8286366, PubMed:8555209). Allow... | Fusarium vanettenii (Neocosmospora pisi) |
P00591 | LIPP_PIG | SEVCFPRLGCFSDDAPWAGIVQRPLKILPWSPKDVDTRFLLYTNQNQNNYQELVADPSTITNSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEVLKSSLGYSPSNVHVIGHSLGSHAAGEAGRRTNGTIERITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDAAPIIPNLGFGMSQTVGHLDFFPNGGKQMPGCQKNILSQIVDIDGIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPCPSEGCPQMGHYADRFPGKTN... | 3.1.1.3 | null | lipid catabolic process [GO:0016042] | extracellular space [GO:0005615] | all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity [GO:0047376]; metal ion binding [GO:0046872]; triglyceride lipase activity [GO:0004806] | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16233}. | 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:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12... | null | null | null | null | FUNCTION: Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones. {ECO:0000250|UniPro... | Sus scrofa (Pig) |
P00592 | PA21B_PIG | MKFLVLAVLLTVGAAQEGISSRALWQFRSMIKCAIPGSHPLMDFNNYGCYCGLGGSGTPVDELDRCCETHDNCYRDAKNLDSCKFLVDNPYTESYSYSCSNTEITCNSKNNACEAFICNCDRNAAICFSKAPYNKEHKNLDTKKYC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593}; | cellular response to insulin stimulus [GO:0032869]; fatty acid biosynthetic process [GO:0006633]; intracellular signal transduction [GO:0035556]; leukotriene biosynthetic process [GO:0019370]; lipid catabolic process [GO:0016042]; neutrophil chemotaxis [GO:0030593]; neutrophil mediated immunity [GO:0002446]; phosphatid... | cell surface [GO:0009986]; extracellular region [GO:0005576] | bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family | PTM: Acylation causes dimerization. {ECO:0000269|PubMed:2498336}.; PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}. | 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: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (PubMed:17603006). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosph... | Sus scrofa (Pig) |
P00593 | PA21B_BOVIN | MRLLVLAALLTVGAGQAGLNSRALWQFNGMIKCKIPSSEPLLDFNNYGCYCGLGGSGTPVDDLDRCCQTHDNCYKQAKKLDSCKVLVDNPYTNNYSYSCSNNEITCSSENNACEAFICNCDRNAAICFSKVPYNKEHKNLDKKNC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:10089353, ECO:0000305|PubMed:7265241, ECO:0000305|PubMed:9115986}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305|PubMed:10089353, ECO:0000305|PubMed:7265241, ECO:0000305|PubMed:9115986}; | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; arachidonic acid secretion [GO:0050482]; defense response to Gram-positive bacterium [GO:0050830]; fatty acid biosynthetic process [GO:0006633]; innate immune response in mucosa [GO:0002227... | cell surface [GO:0009986]; extracellular space [GO:0005615] | bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family | PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P04054, ECO:0000250|U... | null | null | null | null | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols ov... | Bos taurus (Bovine) |
P00594 | PA21B_HORSE | ENGISPRAVWQFRSMIQCTIPNSKPYLEFNDYGCYCGLGGSGTPVDELDACCQVHDNCYTQAKELSSCRFLVDNPYTESYKFSCSGTEVTCSDKNNACEAFICNCDRNAAICFSKAPYNPENKNLDSKRKCA | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593}; | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phosphatidylglycerol metabolic process [GO:0046471]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of podocyte apo... | extracellular region [GO:0005576] | bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family | PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P04054, ECO:0000250|U... | null | null | null | null | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols ov... | Equus caballus (Horse) |
P00596 | PA2A1_NAJKA | MNPAHLLILAAVCVSPLGAFSNRPMPLNLYQFKNMIQCTVPNRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISRCWPYFKTYSYECSQGTLTCKGDNDACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7460933}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=165 umol/min/mg enzyme {ECO:0000269|PubMed:19622365}; | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable). Is able to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7 (CHRNA7)-similar nAChRs in L.stagnalis neurons (IC(50)=37 nM) and to compete with alpha-bungarotoxin for binding to muscle- ... | Naja kaouthia (Monocled cobra) (Naja siamensis) |
P00597 | PA2A2_NAJKA | MNPAHLLILAAVCVSSLGASSNRPMPLNLYQFKNMIQCTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Naja kaouthia (Monocled cobra) (Naja siamensis) |
P00598 | PA2A1_NAJAT | MTPAHLLILAAVCVSPLGASSNRPMPLNLYQFKNMIQCTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:2274785, ECO:0000305|PubMed:2274787}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305|PubMed:2274785, ECO:0000305|PubMed:2274787}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of ... | Naja atra (Chinese cobra) |
P00608 | PA2B_NOTSC | NLVQFSYLIQCANHGKRPTWHYMDYGCYCGAGGSGTPVDELDRCCKIHDDCYDEAGKKGCFPKMSAYDYYCGENGPYCRNIKKKCLRFVCDCDVEAAFCFAKAPYNNANWNIDTKKRCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P60043}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P60043}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Is directly toxic to skeletal muscle upon local application in vivo (dystrophic effect). Also has direct nephrotoxicity in experimental mice; a single subcutaneous dose (1.38 ... | Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake) |
P00611 | PA2A1_LATSE | MYPAHLLVLLAVCVSLLGATAIPPLPLNLVQFSNLIQCVNKGSRASYHYADYGCYCGAGGSGTPVDELDRCCKIHDDCYGEAEKMGCYPKWTLYTYDCSTEEPNCSTKTGCQGFVCACDLEAAKCFARSPYNNKNYNIDTSKRCK | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000250}. | Laticauda semifasciata (Black-banded sea krait) (Pseudolaticauda semifasciata) |
P00614 | PA2TA_OXYSC | NLLQFGFMIRCANRRSRPVWHYMDYGCYCGKGGSGTPVDDLDRCCQVHDECYGEAVRRFGCAPYWTLYSWKCYGKAPTCNTKTRCQRFVCRCDAKAAECFARSPYQNSNWNINTKARCR | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | 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: Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuro... | Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan) |
P00615 | PA2HB_OXYSC | MHPAHLLVLLAVCVSLLGASDIPPLPLNLVQFGKMIECAIRNRRPALDFMNYGCYCGKGGSGTPVDDLDRCCQVHDECYAEAEKHGCYPSLTTYTWECRQVGPYCNSKTQCEVFVCACDFAAAKCFAQEDYNPAHSNINTGERCK | null | null | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuro... | Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan) |
P00616 | PA2HG_OXYSC | MHPAHLLVLLAVCVSLLGSSEIPQPSLDFEQFSNMIQCTIPCGESCLAYMDYGCYCGPGGSGTPIDDLDRCCKTHDECYAEAGKLSACKSVLSEPNNDTYSYECNEGQLTCNDDNDECKAFICNCDRTAVTCFAGAPYNDLNYNIGMIEHCK | null | null | arachidonic acid secretion [GO:0050482]; 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] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | PTM: Contains 0.9% fucose, 2.2% mannose, 4.2% N-acetyl-D-glucosamine, 3.5% galactose, and 3.8% N-acetyl-neuraminic acid (sialic acid). {ECO:0000269|PubMed:976268}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuro... | Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan) |
P00617 | PA2B1_BUNMU | MNPAHLLVLSAVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYADYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCGRIVCDCDRTAALCFGNSEYIEGHKNIDTARFCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:8590005}; Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:8590005}; | arachidonic acid secretion [GO:0050482]; 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 I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:624701, ECO:0000269|PubMed:7096304}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Bungarus multicinctus (Many-banded krait) |
P00618 | PA2B2_BUNMU | MLIFLWCGAVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYADYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCARIVCDCDRTAALCFGNSEYIERHKNIDTKRHCR | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; 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 I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Bungarus multicinctus (Many-banded krait) |
P00619 | PA2A3_BUNMU | MYPAHLLVLSAVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYTNYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAANIRDCNPKTQSYSYKLTKRTIICYGAAGTCARVVCDCDRTAALCFGDSEYIEGHKNIDTARFCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; 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 I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Bungarus multicinctus (Many-banded krait) |
P00623 | PA2A_CROAD | MRTLWIVAVLLLGVEGSLVQFETLIMKVAKRSGLLWYSAYGCYCGWGGHGRPQDATDRCCFVHDCCYGKATDCNPKTVSYTYSEENGEIVCGGDDPCGTQICECDKAAAICFRDNIPSYDNKYWLFPPKNCREEPEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Crotalus adamanteus (Eastern diamondback rattlesnake) |
P00624 | PA2A_CROAT | MRTLWIVAVLLLGVEGSLVQFETLIMKIAGRSGLLWYSAYGCYCGWGGHGLPQDATDRCCFVHDCCYGKATDCNPKTVSYTYSEENGEIICGGDDPCGTQICECDKAAAICFRDNIPSYDNKYWLFPPKNCREEPEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q8AXY1}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8AXY1}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Crotalus atrox (Western diamondback rattlesnake) |
P00625 | PA2A1_OVOOK | MRTLWIMAVLLLGVEGHLMQFETLIMKIAGRSGVWWYGSYGCYCGAGGQGRPQDPSDRCCFVHDCCYGKVTGCNTKDEFYTYSEENGAITCGGENPCLKEVCECDLAAAICFRDNLDTYNSKKYWMFPAKNCLEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; 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. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits the ADP- and collagen-induced human platelet aggregation (By similarity). Exhibits high hydrolytic activities and preferred the anionic micelles to the zwitterionic micelles. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphog... | Ovophis okinavensis (Ryukyu Island pit viper) (Trimeresurus okinavensis) |
P00626 | PA2BA_VIPAA | MRTLWIVAVCLIGVEGSLLEFGMMILGETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCSPKTDRYKYHRENGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNYIYRNYPDFLCKKESEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16156665}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:16156665}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18261469}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:18261469}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that acts as a presynaptic neurotoxin, an inhibitor of blood coagulation, and has been found to bind with high affinity to intracellular proteins. The response of indirectly stimulated neuromuscular preparations to ammodytoxin (Atx) is triphasic. The first phase, the transi... | Vipera ammodytes ammodytes (Western sand viper) |
P00627 | PA2B6_BUNFA | AVCVSLLGAANIPPQSLNLYQFKNMIECAGTRTWLAYVKYGCYCGPGGTGTPLDELDRCCQTHDHCYDNAKKFGNCIPYLKTYVYTCNKPDITCTGAKGSCGRNVCDCDRAAAICFAAAPYNLANFGIDKEKHCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; 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 I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17166178, ECO:0000269|PubMed:700923}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Very weakly suppress the acetylcholine (ACh)-evoked current mediated by alpha-7... | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
P00628 | PA2BV_BUNFA | AVCVSLLGAANIPPQPLNLLQFKNMIQCAGSRLWVAYVKYGCYCGPGGTGTPLDQLDRCCQTHDHCYDNAKKFGNCIPYFKSYEYTCNKPDLTCTDAKGSCARNVCDCDRAAAICFAAAPYNLANFGINKETHCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
P00629 | PA2B3_BUNFA | AVCVSLLGAANIPPQPLNLLQFKNMIQCAGSRLWVAYVKYGCYCGPGGTGTPLDQLDRCCQTHDHCYDNAKKFGNCIPYFKTYEYTCNKPDITCTDAKGSCGRTVCDCDRAAAICFAAAPYNLANFGIDKEKHCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; 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 I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that has only a weak enzymatic activity. Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
P00630 | PA2_APIME | MQVVLGSLFLLLLSTSHGWQIRDRIGDNELEERIIYPGTLWCGHGNKSSGPNELGRFKHTDACCRTHDMCPDVMSAGESKHGLTNTASHTRLSCDCDDKFYDCLKNSADTISSYFVGKMYFNLIDTKCYKLEHPVTGCGERTEGRCLHYTVDKSKPKVYQWFDLRKY | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:2274788}; Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:2274788}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498] | PF05826; | 1.20.90.10; | Phospholipase A2 family, Group III subfamily | PTM: N-glycosylated; contains mannose, N-acetylglucosamine and fucose alphal-6 and/or alphal-3 linked to the innermost N-acetylglucosamine. {ECO:0000269|PubMed:8504812}. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035}; | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Apis mellifera (Honeybee) |
P00634 | PPB_ECOLI | MKQSTIALALLPLLFTPVTKARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPT... | 3.1.3.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions.; | dephosphorylation [GO:0016311]; protein dephosphorylation [GO:0006470] | outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597] | alkaline phosphatase activity [GO:0004035]; hydrogenase (acceptor) activity [GO:0033748]; magnesium ion binding [GO:0000287]; oxidoreductase activity, acting on phosphorus or arsenic in donors [GO:0030613]; phosphoprotein phosphatase activity [GO:0004721]; zinc ion binding [GO:0008270] | PF00245; | 3.40.720.10; | Alkaline phosphatase family | null | SUBCELLULAR LOCATION: Periplasm. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042}; | null | null | null | null | null | Escherichia coli (strain K12) |
P00635 | PPA5_YEAST | MFKSVVYSILAASLANAGTIPLGKLADVDKIGTQKDIFPFLGGAGPYYSFPGDYGISRDLPEGCEMKQLQMVGRHGERYPTVSLAKTIKSTWYKLSNYTRQFNGSLSFLNDDYEFFIRDDDDLEMETTFANSDDVLNPYTGEMNAKRHARDFLAQYGYMVENQTSFAVFTSNSKRCHDTAQYFIDGLGDQFNITLQTVSEAESAGANTLSACNSCPAWDYDANDDIVNEYDTTYLDDIAKRLNKENKGLNLTSTDASTLFSWCAFEVNAKGYSDVCDIFTKDELVHYSYYQDLHTYYHEGPGYDIIKSVGSNLFNASVKL... | 3.1.3.2 | null | cellular response to phosphate starvation [GO:0016036]; phosphate-containing compound metabolic process [GO:0006796]; regulation of cell size [GO:0008361] | cell periphery [GO:0071944]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277] | acid phosphatase activity [GO:0003993]; nucleoside triphosphate diphosphatase activity [GO:0047429]; ribonucleoside triphosphate phosphatase activity [GO:0017111] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | PTM: Glycosylated during secretion across the membrane. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000269|PubMed:3537710, ECO:0000269|PubMed:6300772}; | null | null | null | null | FUNCTION: Partially mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and NPP2. {ECO:0000269|PubMed:16278456}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P00636 | F16P1_PIG | MTDQAAFDTNIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKGSIYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPIILG... | 3.1.3.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:9708979}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:97... | cellular response to magnesium ion [GO:0071286]; cellular response to xenobiotic stimulus [GO:0071466]; dephosphorylation [GO:0016311]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; ne... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | AMP binding [GO:0016208]; fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00316;PF18913; | 3.40.190.80;3.30.540.10; | FBPase class 1 family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:15767255, ECO:0000305|PubMed:1313579}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for fructose-1,6-diphosphate {ECO:0000269|PubMed:15767255}; | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. | null | null | FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liv... | Sus scrofa (Pig) |
P00637 | F16P1_RABIT | MADKAPFDTDISTMTRFVMEEGRKAGGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSTKDALQPGRNLVAAGYALYGSATMLVLAGGSGVNSFMLDPAIGEFILVDKNVKIKKKGNIYSLNEGYAKDFDPAVTEYIQKKKFPPDNSSPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPDGKLRLLYECNPMAFIMEKAGGMATTGKEAILDIVPTDIHQRAPVILG... | 3.1.3.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00636}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P00636}; | cellular response to magnesium ion [GO:0071286]; cellular response to xenobiotic stimulus [GO:0071466]; dephosphorylation [GO:0016311]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; ne... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | AMP binding [GO:0016208]; fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00316;PF18913; | 3.40.190.80;3.30.540.10; | FBPase class 1 family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:202200}; | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. | null | null | FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liv... | Oryctolagus cuniculus (Rabbit) |
P00639 | DNAS1_BOVIN | MRGTRLMGLLLALAGLLQLGLSLKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTLT | 3.1.21.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:3352748, ECO:0000269|PubMed:4976790, ECO:0000269|PubMed:5166750}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:3352748, ECO:0000269|PubMed:4976790, ECO:0000269|PubMed:5166750}; Note=Divalent metal cations. Prefers Ca(2+) or... | apoptotic process [GO:0006915]; DNA catabolic process [GO:0006308]; neutrophil activation involved in immune response [GO:0002283]; regulation of acute inflammatory response [GO:0002673]; regulation of neutrophil mediated cytotoxicity [GO:0070948] | extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; zymogen granule [GO:0042588] | actin binding [GO:0003779]; deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677] | PF03372; | 3.60.10.10; | DNase I family | PTM: The only differences between the A and B forms and the C and D forms are in the compositions of the carbohydrate bound to Asn-40. {ECO:0000269|PubMed:1748997}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4734471}. Zymogen granule {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.21.1; Evidence={ECO:0000269|PubMed:3352748, ECO:0000269|PubMed:4976790, ECO:0000269|PubMed:5166750}; | null | null | null | null | FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:2395459, PubMed:3352748, PubMed:4976790, PubMed:5166750). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in c... | Bos taurus (Bovine) |
P00642 | T2E1_ECOLX | MSNKKQSNRLTEQHKLSQGVIGIFGDYAKAHDLAVGEVSKLVKKALSNEYPQLSFRYRDSIKKTEINEALKKIDPDLGGTLFVSNSSIKPDGGIVEVKDDYGEWRVVLVAEAKHQGKDIINIRNGLLVGKRGDQDLMAAGNAIERSHKNISEIANFMLSESHFPYVLFLEGSNFLTENISITRPDGRVVNLEYNSGILNRLDRLTAANYGMPINSNLCINKFVNHKDKSIMLQAASIYTQGDGREWDSKIMFEIMFDISTTSLRVLGRDLFEQLTSK | 3.1.21.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per subunit.; | DNA restriction-modification system [GO:0009307] | null | DNA binding [GO:0003677]; magnesium ion binding [GO:0000287]; type II site-specific deoxyribonuclease activity [GO:0009036] | PF02963; | 3.40.580.10; | EcoRI type II restriction endonuclease family | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; Evidence={ECO:0000269|PubMed:3024321}; | null | null | null | null | FUNCTION: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GAATTC-3' and cleaves after G-1. {ECO:0000269|PubMed:3024321, ECO:0000303|PubMed:12654995}. | Escherichia coli |
P00644 | NUC_STAAU | MLVMTEYLLSAGICMAIVSILLIGMAISNVSKGQYAKRFFFFATSCLVLTLVVVSSLSSSANASQTDNGVNRSGSEDPTVYSATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ | 3.1.31.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.; | null | extracellular region [GO:0005576]; membrane [GO:0016020] | endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters [GO:0016894]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676] | PF00565; | 2.40.50.90; | Thermonuclease family | null | SUBCELLULAR LOCATION: [Nuclease A]: Secreted {ECO:0000269|PubMed:893427, ECO:0000305|PubMed:4324890}.; SUBCELLULAR LOCATION: [Nuclease B]: Membrane. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.; EC=3.1.31.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10048, ECO:0000255|PROSITE-ProRule:PRU10049}; | null | null | null | null | FUNCTION: Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond. | Staphylococcus aureus |
P00646 | CEA3_ECOLX | MSGGDGRGHNTGAHSTSGNINGGPTGLGVGGGASDGSGWSSENNPWGGGSGSGIHWGGGSGHGNGGGNGNSGGGSGTGGNLSAVAAPVAFGFPALSTPGAGGLAVSISAGALSAAIADIMAALKGPFKFGLWGVALYGVLPSQIAKDDPNMMSKIVTSLPADDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSGVPMSVPVVDAKPTERPGVFTASIPGAPVLNISVNNSTPAVQTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHNAVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAE... | 4.6.1.- | null | defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; negative regulation of ion transmembrane transporter activity [GO:0032413] | extracellular region [GO:0005576]; extrachromosomal circular DNA [GO:0005727] | endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; ribosome binding [GO:0043022]; rRNA binding [GO:0019843]; transmembrane transporter binding [GO:0044325]; tRNA binding [GO:0000049] | PF03515;PF09000;PF11570; | 3.10.380.10;1.10.287.620;1.20.5.740; | Cloacin colicin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4944624}. | null | null | null | null | null | FUNCTION: Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria (PubMed:3889348, PubMed:4930243, PubMed:4930244, PubMed:6295812). Cleaves 16S rRNA between adenosine-1492 and guanosine-1493 (E.coli 16S rRNA numbering), releasing a 49 nucleotide (nt) 'colicin' fragment (PubMed... | Escherichia coli |
P00655 | RNAS_ASPGI | MVAIKNLVLVALTAVTALAVPSPLEARAVTWTCLNDQKNPKTNKYETKRLLYNQNKAESNSHHAPLSDGKTGSSYPHWFTNGYDGDGKLPKGRTPIKFGKSDCDRPPKHSKDGNGKTDHYLLEFPTFPDGHDYKFDSKKPKENPGPARVIYTYPNKVFCGIIAHTKENQGELKLCSH | 4.6.1.23 | null | negative regulation of cytoplasmic translation [GO:2000766] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; rRNA endonuclease activity [GO:0033902] | null | 3.10.450.30; | Ribonuclease U2 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 28S rRNA containing guanosine-adenosine pair + H2O = an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment].; EC=4.6.1.23; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Alpha-sarcin is specific for purines in both single- and double-stranded RNA. Its toxic action on eukaryotic cells is the result of cleavage of a single phosphodiester bond in the 60S subunit of ribosomes (By similarity). Inhibits both the EFl (elongation factor 1)-dependent binding of aminoacyl-tRNA and the ... | Aspergillus giganteus |
P00657 | RNAS1_BUBBU | KETAAAKFQRQHMDSSTSSASSSNYCNQMMKSRNMTSDRCKPVNTFVHESLADVQAVCSQENVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHYDASV | 4.6.1.18 | null | defense response to Gram-positive bacterium [GO:0050830] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | PTM: Swamp breed ribonuclease do not bind carbohydrate, but there is evidence of a polymorphic form that does. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; | null | null | null | null | FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). {ECO:0000250}. | Bubalus bubalis (Domestic water buffalo) |
P00659 | RNAS1_DAMKO | KESAAAKFZRZHMBSSTSSASSSBYCBZMMKSRNLTQDRCKPVBTFVHZSLABVZAVCSZKBVACKBGZTBCYZSYSTMSITBCRZTGSSKYPBCAYKTTQAKKHIIVACZGBPYVPVHFBASV | 4.6.1.18 | null | defense response to Gram-positive bacterium [GO:0050830] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; | null | null | null | null | FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). {ECO:0000250}. | Damaliscus korrigum (Topi) (Damaliscus lunatus korrigum) |
P00660 | RNAS1_CONTA | KESAAAKFERQHMDSSTSSASSSNYCNQMMKSRNLTQDRCKPVNTFVHEPLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKATQAKKHIIVACEGNPYVPVHFDASV | 4.6.1.18 | null | defense response to Gram-positive bacterium [GO:0050830] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; | null | null | null | null | FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). {ECO:0000250}. | Connochaetes taurinus (Blue wildebeest) |
P00669 | RNS_BOVIN | MALKSLVVLPLLVLVLLLVRVQPSLGKESAAAKFERQHMDSGNSPSSSSNYCNLMMCCRKMTQGKCKPVNTFVHESLADVKAVCSQKKVTCKNGQTNCYQSKSTMRITDCRETGSSKYPNCAYKTTQVEKHIIVACGGKPSVPVHFDASV | 4.6.1.18 | null | defense response to Gram-positive bacterium [GO:0050830]; metabolic process [GO:0008152] | extracellular region [GO:0005576] | identical protein binding [GO:0042802]; lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000269|PubMed:4664228}; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide... | null | null | null | null | FUNCTION: This enzyme hydrolyzes both single- and double-stranded RNA. | Bos taurus (Bovine) |
P00684 | RNS1B_RAT | MGLEKSLFLFSLLVLVLGWVQPSLGGESRESSADKFKRQHMDTEGPSKSSPTYCNQMMKRQGMTKGSCKPVNTFVHEPLEDVQAICSQGQVTCKNGRNNCHKSSSTLRITDCRLKGSSKYPNCDYTTTDSQKHIIIACDGNPYVPVHFDASV | 4.6.1.18 | null | defense response to Gram-positive bacterium [GO:0050830]; response to bacterium [GO:0009617] | cytosol [GO:0005829]; extracellular region [GO:0005576]; lysosomal lumen [GO:0043202] | lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; | null | null | null | null | FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
P00687 | AMY1_MOUSE | MKFFLLLSLIGFCWAQYDPHTQYGRTAIVHLFEWRWVDIAKECERYLAPNGFAGVQVSPPNENIVVHSPSRPWWERYQPISYKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMCGVGAQAGQSSTCGSYFNPNNRDFPGVPYSGFDFNDGKCRTASGGIENYQDAAQVRDCRLSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAVSSNEYFGNGRVTEFKYGAKLGKVMRKWDGEKMSYLKNWGEGWGLMPSDRALVFVDNHDNQRGH... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746}; | carbohydrate metabolic process [GO:0005975]; response to bacterium [GO:0009617] | extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; amylase activity [GO:0016160]; metal ion binding [GO:0046872] | PF00128;PF02806; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted. | 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:0000250|UniProtKB:P04746}; | null | null | null | null | null | Mus musculus (Mouse) |
P00688 | AM2A5_MOUSE | MKFVLLLSLIGFCWAQYDPHTSDGRTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENVVVHNPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCGAGNPAGTSSTCGSYLNPNNREFPAVPYSAWDFNDNKCNGEIDNYNDAYQVRNCRLTGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAIKGSEYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGLVPSDRALVFVDNHDNQRGHGAG... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746}; | carbohydrate catabolic process [GO:0016052]; carbohydrate metabolic process [GO:0005975] | extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; amylase activity [GO:0016160]; 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, extracellular space. | 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:0000250|UniProtKB:P04746}; | null | null | null | null | null | Mus musculus (Mouse) |
P00690 | AMYP_PIG | MKLFLLLSAFGFCWAQYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGH... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631}; Note=Bin... | carbohydrate catabolic process [GO:0016052]; carbohydrate metabolic process [GO:0005975] | 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, extracellular space. | 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:0000250|UniProtKB:P04746}; | null | null | null | null | null | Sus scrofa (Pig) |
P00693 | AMY1_HORVU | MGKNGSLCCFSLLLLLLLAGLASGHQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDASKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDIDHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAASAGMVFDFTTKGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAATFVDNHDTGSTQ... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:1... | starch catabolic process [GO:0005983] | extracellular region [GO:0005576] | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509] | PF07821;PF00128; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. | 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:16030022, ECO:0000269|PubMed:18588886, ECO:0000269|PubMed:24089528, ECO:0000269|PubMed:7901200}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 with p-nitrophenyl maltoheptaoside or amylopectin as substrate. {ECO:0000269|PubMed:24089528}; | null | FUNCTION: Alpha-amylase displaying a robust amylolytic activity toward p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit dextrin (PubMed:24089528). {ECO:0000269|PubMed:24089528}. | Hordeum vulgare (Barley) |
P00697 | LYSC1_RAT | MKALLVLGFLLLSASVQAKIYERCQFARTLKRNGMSGYYGVSLADWVCLAQHESNYNTQARNYNPGDQSTDYGIFQINSRYWCNDGKTPRAKNACGIPCSALLQDDITQAIQCAKRVVRDPQGIRAWVAWQRHCKNRDLSGYIRNCGV | 3.2.1.17 | null | defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152] | endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; Golgi cis cisterna [GO:0000137]; Golgi stack [GO:0005795]; microvillus [GO:0005902]; rough endoplasmic reticulum lumen [GO:0048237]; secretory granule [GO:0030141]; trans-Golgi network transport vesicle [GO:0030140] | hydrolase activity, acting on glycosyl bonds [GO:0016798]; identical protein binding [GO:0042802]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; | null | null | null | null | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. In the intestine they may also have a digestive function. | Rattus norvegicus (Rat) |
P00698 | LYSC_CHICK | MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL | 3.2.1.17 | null | cell wall macromolecule catabolic process [GO:0016998]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615] | beta-N-acetylglucosaminidase activity [GO:0016231]; identical protein binding [GO:0042802]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; | null | null | null | null | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus. {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000269|PubMed:22044478}. | Gallus gallus (Chicken) |
P00701 | LYSC_COTJA | MRSLLVLVLCFLPLAALGKVYGRCELAAAMKRHGLDKYQGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDVHGMNAWVAWRNRCKGTDVNAWIRGCRL | 3.2.1.17 | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152] | extracellular region [GO:0005576] | lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000269|Ref.3}; | null | null | null | null | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. | Coturnix japonica (Japanese quail) (Coturnix coturnix japonica) |
P00702 | LYSC_PHACO | MRSLLILVLCFLPLAAPGKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCHIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRKHCKGTDVNVWIRGCRL | 3.2.1.17 | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152] | extracellular region [GO:0005576] | lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | PTM: By an evolutionary shift in the site of proteolytic cleavage of prelysozyme, Gly-18 became the N-terminal residue of the mature protein instead of being the C-terminal residue of the signal sequence as in other birds. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; | null | null | null | null | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. | Phasianus colchicus colchicus (Black-necked pheasant) |
P00703 | LYSC_MELGA | MRSLLILVLCFLPLAALGKVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL | 3.2.1.17 | null | cell wall macromolecule catabolic process [GO:0016998]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640] | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | glycosaminoglycan binding [GO:0005539]; identical protein binding [GO:0042802]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; | null | null | null | null | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. | Meleagris gallopavo (Wild turkey) |
P00709 | LALBA_HUMAN | MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL | null | null | apoptotic process [GO:0006915]; cell-cell signaling [GO:0007267]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989]; signal transduction [GO:0007165] | extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; protein-containing complex [GO:0032991] | calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers g... | Homo sapiens (Human) |
P00711 | LALBA_BOVIN | MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989]; response to 11-deoxycorticosterone [GO:1903496]; response to dehydroepiandrosterone [GO:1903494]; response to estradiol [GO:0032355]; response to progesterone [G... | extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers g... | Bos taurus (Bovine) |
P00712 | LALBA_CAPHI | MMSFVSLLLVGILFHATQAEQLTKCEVFQKLKDLKDYGGVSLPEWVCTAFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSRNICNISCDKFLDDDLTDDIVCAKKILDKVGINYWLAHKALCSEKLDQWLCEKL | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989] | extracellular region [GO:0005576]; protein-containing complex [GO:0032991] | calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers g... | Capra hircus (Goat) |
P00713 | LALBA_CAVPO | MMSFFPLLLVGILFPAVQAKQLTKCALSHELNDLAGYRDITLPEWLCIIFHISGYDTQAIVKNSDHKEYGLFQINDKDFCESSTTVQSRNICDISCDKLLDDDLTDDIMCVKKILDIKGIDYWLAHKPLCSDKLEQWYCEAQ | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989] | extracellular region [GO:0005576]; protein-containing complex [GO:0032991] | calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers g... | Cavia porcellus (Guinea pig) |
P00714 | LALBA_RAT | MMRFVPLFLACISLPAFQATEFTKCEVSHAIEDMDGYQGISLLEWTCVLFHTSGYDSQAIVKNNGSTEYGLFQISNRNWCKSSEFPESENICDISCDKFLDDELADDIVCAKKIVAIKGIDYWKAHKPMCSEKLEQWRCEKPGAPALVVPALNSETPVP | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989] | extracellular region [GO:0005576]; protein-containing complex [GO:0032991] | calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers g... | Rattus norvegicus (Rat) |
P00716 | LALBA_RABIT | MMPLVPLLLVSIVFPGIQATQLTRCELTEKLKELDGYRDISMSEWICTLFHTSGLDTKITVNNNGSTEYGIFQISDKLWCVSKQNPQSKNICDTPCENFLDDNLTDDVKCAMKILDKEGIDHWLAHKPLCSENLEQWVCKK | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers g... | Oryctolagus cuniculus (Rabbit) |
P00720 | ENLYS_BPT4 | MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDAYKNL | 3.2.1.17 | null | cell wall macromolecule catabolic process [GO:0016998]; defense response to bacterium [GO:0042742]; peptidoglycan catabolic process [GO:0009253]; viral release from host cell by cytolysis [GO:0044659] | host cell cytoplasm [GO:0030430] | lysozyme activity [GO:0003796] | PF00959; | 1.10.530.40; | Glycosyl hydrolase 24 family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04110}. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04110}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:4865643}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.3. {ECO:0000269|PubMed:4865643}; | null | FUNCTION: Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach th... | Enterobacteria phage T4 (Bacteriophage T4) |
P00722 | BGAL_ECOLI | MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTAD... | 3.2.1.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 magnesium ions per monomer. Can also use manganese.; COFACTOR: Name=Na(+); Xref=ChEBI:CHEBI:29101; Note=Binds 1 sodium ion per monomer.; | lactose catabolic process [GO:0005990] | beta-galactosidase complex [GO:0009341] | alkali metal ion binding [GO:0031420]; beta-galactosidase activity [GO:0004565]; carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287] | PF02929;PF00703;PF02836;PF02837;PF16353; | 2.70.98.10;2.60.120.260;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 2 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for p-nitrophenyl beta-D-galactoside {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=0.12 mM for o-nitrophenyl beta-D-galactoside ... | null | null | null | null | Escherichia coli (strain K12) |
P00724 | INV2_YEAST | MLLQAFLFLLAGFAAKISASMTNETSDRPLVHFTPNKGWMNDPNGLWYDEKDAKWHLYFQYNPNDTVWGTPLFWGHATSDDLTNWEDQPIAIAPKRNDSGAFSGSMVVDYNNTSGFFNDTIDPRQRCVAIWTYNTPESEEQYISYSLDGGYTFTEYQKNPVLAANSTQFRDPKVFWYEPSQKWIMTAAKSQDYKIEIYSSDDLKSWKLESAFANEGFLGYQYECPGLIEVPTEQDPSKSYWVMFISINPGAPAGGSFNQYFVGSFNGTHFEAFDNQSRVVDFGKDYYALQTFFNTDPTYGSALGIAWASNWEYSAFVPTN... | 3.2.1.26 | null | fructan catabolic process [GO:0010147]; inulin catabolic process [GO:1902927]; raffinose catabolic process [GO:0034484]; sucrose catabolic process [GO:0005987] | cell periphery [GO:0071944]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; fungal-type vacuole [GO:0000324]; mitochondrion [GO:0005739] | beta-fructofuranosidase activity [GO:0004564]; inulinase activity [GO:0051670]; sucrose alpha-glucosidase activity [GO:0004575] | PF08244;PF00251; | null | Glycosyl hydrolase 32 family | PTM: Isoform Secreted is glycosylated. Isoform Intracellular is not glycosylated. {ECO:0000269|PubMed:3284881}. | SUBCELLULAR LOCATION: [Isoform Intracellular]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Secreted]: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.; EC=3.2.1.26; Evidence={ECO:0000255|PROSITE-ProRule:PRU10067}; | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
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