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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D4A280 | PAK5_RAT | MFGKKKKKIEISGPSNFEHRVHTGFDPQEQKFTGLPQQWHSLLADTANRPKPMVDPSCITPIQLAPMKTIVRGNKSCKESSINGLLEDFDNISVTRSNSLRKESPPTPDQGAASRIQGHSEENGFITFSQYSSESDTTTDYTTEKYRDRSLYGDDLDLYYRGSHAAKQNGHAMKMKHGDAYYPEMKPLKSDLARFPVDYHTHLDSLSKASEYGDLKWDYQRASSSSPLDYSFQLTPSRTAGTSRCSKESLAYSESDWGPSFDDYDRRPKSSYLHQTSPQPAMRQRSKSGSGLQEPMMPFGASAFKTHPQGHSYNSYTYPR... | 2.7.11.1 | null | apoptotic process [GO:0006915]; cytoskeleton organization [GO:0007010]; intracellular signal transduction [GO:0035556]; learning [GO:0007612]; locomotory behavior [GO:0007626]; memory [GO:0007613]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; phosphorylation [GO:0016310]; regulation of MAP... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; synapse [GO:0045202] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00786;PF00069; | 3.90.810.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated when activated by CDC42/p21. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the mitochondria, and mitochondrial localization is essential for the role in cell survival. {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=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a ... | Rattus norvegicus (Rat) |
D4A2H2 | SPTC1_RAT | MATVAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSRNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKAAAFASLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPAYSKRGDIVFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVAEGLYMNTGTICPLPELVRLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCG... | 2.3.1.50 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; | ceramide biosynthetic process [GO:0046513]; positive regulation of lipophagy [GO:1904504]; regulation of fat cell apoptotic process [GO:1904649]; sphinganine biosynthetic process [GO:0046511]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; sphingomyelin biosynthetic process... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; serine C-palmitoyltransferase complex [GO:0017059]; SPOTS complex [GO:0035339] | pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | PTM: Phosphorylation at Tyr-164 inhibits activity and promotes cell survival. {ECO:0000250|UniProtKB:O15269}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O35704}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35704}. | CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-rig... | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:O15269}. | null | null | FUNCTION: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is also composed of SPTLC2 or SPTLC3 and S... | Rattus norvegicus (Rat) |
D4A2Z8 | DHX36_RAT | MSYDYHQSWSRDGGPRGSGQGSGGGGGGSRGSGGGGGGRGGRGRHPAHLKGREIGLWYAKKQTQKNKEAERQERAVVHMDERREEQIVQLLNSVQAKNDKDSEAQISWFAPEDHGYGTEVSSEKKINSEKKLDNQEKKLLNQEKKTYRITDKSYIDRDSEYLLQQNEPNLGLDQQLLEDLQKKKTDPRYIEMQRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSACRIVCTQPRRISAISVAERVAAERAESCGNGNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSV... | 3.6.4.12; 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q05B79}; | 3'-UTR-mediated mRNA destabilization [GO:0061158]; cell differentiation [GO:0030154]; cellular response to arsenite ion [GO:1903843]; cellular response to heat [GO:0034605]; cellular response to UV [GO:0034644]; defense response to virus [GO:0051607]; G-quadruplex DNA unwinding [GO:0044806]; innate immune response [GO:... | axon [GO:0030424]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; dendrite [GO:0030425]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; perikaryon [GO:0043204] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA helicase activity [GO:0003678]; double-stranded RNA binding [GO:0003725]; G-quadruplex DNA binding [GO:0051880]; G-quadruplex RNA binding [GO:0002151]; histone deacetylase binding [GO:0042826]; magnes... | PF00270;PF21010;PF04408;PF00271;PF07717; | 1.20.120.1080;3.40.50.300; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8VHK9}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9H2U1}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H2U1}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9H2U1}. Mitoch... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q9H2U1}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:130... | null | null | null | null | FUNCTION: Multifunctional ATP-dependent helicase that unwinds G-quadruplex (G4) structures (By similarity). Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses (PubMed:23651854). G4 structures correspond to helical structures c... | Rattus norvegicus (Rat) |
D4A3K5 | H11_RAT | MSETAPVPQPASVAPEKPAATKKTRKPAKAAVPRKKPAGPSVSELIVQAVSSSKERSGVSLAALKKSLAAAGYDVEKNNSRIKLGLKSLVNKGTLVQTKGTGAAGSFKLNKKAESKASTTKVTVKAKASGAAKKPKKTAGAAAKKTVKTPKKPKKPAVSKKTSSKSPKKPKVVKAKKVAKSPAKAKAVKPKAAKVKVTKPKTPAKPKKAAPKKK | null | null | chromosome condensation [GO:0030261]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334]; positive regulation of receptor-mediated endocytosis [GO:0048260]; spermatogenesis [GO:0007283] | cell surface [GO:0009986]; chromatin [GO:0000785]; euchromatin [GO:0000791]; nucleosome [GO:0000786]; nucleus [GO:0005634]; vesicle [GO:0031982] | chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; heparin binding [GO:0008201]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P43275}.; PTM: Citrullination at Arg-56 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}. Note=Mainly localizes in euchromatin. {ECO:0000250}. | null | null | null | null | null | FUNCTION: H1 histones bind to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. H1 histones are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling ... | Rattus norvegicus (Rat) |
D4A4D7 | E2F7_RAT | MEVNCLTLKDLISPRQTRLDFAVEDAETAQKENIFVDRSRMTPKTPMKNEPIDLSKQRIFTPERSPITPVKLVDRQPQVEPWTPTANLKMLISAASPDIRDREKKKELFRPIENKGDAFVNSLQLDVVGDSAVDDYEKRRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHGRHSLPKTLRTLQRLGEEQKYEEQMACLQQKELDLMEYRFGERRKDGSPDPRDQHLLDFSESDYPSSSANSRKDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIEES... | null | null | chorionic trophoblast cell differentiation [GO:0060718]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; hepatocyte differentiation [GO:0070365]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cytokinesis [GO:0032466]... | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; DNA-binding transcription repressor activity, RNA polym... | PF02319; | 1.10.10.10; | E2F/DP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-... | Rattus norvegicus (Rat) |
D4A4K3 | BAKOR_RAT | MASPSGKGSWTPEAPGFGPRALAPDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTSDLREHYDRLACLRRLHILELTSVIFPMDEVKTSGRDPADVSSETDSAMTSSMVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYNWVEEKKTTQGPDMEHNNPAYTISAALGYATQLVNIVSHI... | null | null | autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; autophagosome membrane docking [GO:0016240]; autophagy [GO:0006914]; cellular response to glucose starvation [GO:0042149]; cellular response to starvation [GO:0009267]; early endosome to late endosome transport [GO:0045022]; endosome to lysosom... | autophagosome [GO:0005776]; axoneme [GO:0005930]; endoplasmic reticulum membrane [GO:0005789]; extrinsic component of omegasome membrane [GO:0097629]; extrinsic component of phagophore assembly site membrane [GO:0097632]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; phagocytic vesicle [GO:004533... | GTPase binding [GO:0051020]; phosphatidylinositol 3-kinase inhibitor activity [GO:0141039]; protein-membrane adaptor activity [GO:0043495] | PF10186; | null | ATG14 family | PTM: Ubiquitinated via 'Lys-6', 'Lys-11' and 'Lys-63'-linked polyubiquitin chains on multiple lysines by MARCHF7, leading to ATG14 aggregation and loss of interaction with STX17. {ECO:0000250|UniProtKB:Q6ZNE5}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZNE5}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6ZNE5}; Peripheral membrane protein {ECO:0000305}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q6ZNE5}; Peripheral membrane protein {ECO:0000305}. Note=Cytosolic under nutrient-rich con... | null | null | null | null | null | FUNCTION: Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex. Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes. Enhances PIK3... | Rattus norvegicus (Rat) |
D4A523 | NLRP3_RAT | MKMMSVRCKLAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKKDQPEWNDACTSNLSMVCQEDSLEEEWIGLLGYLSRISICKKKKDYCKIYRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRTKMWDRPMSSLKLELLFEPEDEHLEPVHTVVFQGAAGIGKTILARKIMLDWALGKLFKDKFDYLFFIHCREVSLRAPKSLADLIISCWPDPNPPVCKILCKPSRILFLMDGFDELQGAFDEHIEEVCTDW... | 3.6.4.- | null | acute inflammatory response [GO:0002526]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to peptidoglycan [GO:0071224]; cellular response to virus [GO:0098586]; defense response to Gram-positive bacterium [GO:0050830]; defense response to virus [GO:0051607]; detection of biotic stimulus [GO:000... | canonical inflammasome complex [GO:0061702]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; interphase microtubule organizing center [GO:0031021]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; mitocho... | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; molecular condensate scaffold act... | PF14484;PF13516;PF05729;PF17776;PF17779;PF02758; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: Phosphorylation by MAPK8/JNK1 increases inflammasome activation by promoting deubiquitination by BRCC3 and NLRP3 homooligomerization. Phosphorylation at Ser-805 by CSNK1A1 prevents inflammasome activation by preventing NEK7 recruitment. Phosphorylation at Ser-5 in the pyrin domain inhibits homomultimerization of N... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R4B8}. Inflammasome {ECO:0000250|UniProtKB:Q8R4B8}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8R4B8}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8R4B8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8R4B8}. Mito... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q8R4B8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q8R4... | null | null | null | null | FUNCTION: Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, ini... | Rattus norvegicus (Rat) |
D4A612 | ELOV2_RAT | MFGPRDSRVRGWFLLDSYLPTFTLTIVYLLSIWLGNKYMKNRPALSLRGILTLYNLGITLLSAYMLVELVLSSWEGGYNLQCQNLDSAGEGDIRVAKVLWWYYFSKLVEFLDTIFFVLRKKTSQITFLHVYHHASMFNIWWCVLNWIPCGQSFFGPTLNSFIHILMYSYYGLSVFPSMHRYLWWKKYLTQAQLVQFVLTITHTLSAVVKPCGFPFGCLIFQSSYMMTLVILFLNFYIQTYRKKPMKKEMPEGAAGKEVKNGFPKAHSIAANGVTDKKVQ | 2.3.1.199 | null | fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid b... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; fatty acid elongase activity [GO:0009922] | PF01151; | null | ELO family, ELOVL2 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03202}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03202}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03202, ECO... | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268}. | null | null | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that... | Rattus norvegicus (Rat) |
D4A631 | BIG1_RAT | MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGSAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQHHLLQSPVSHHEPESPHLRYLPPQTVDHIAQEQEGDLDPQTHDVDKSLQDDIEPENGSDISSAENEQTEADQATAAETLSKDDVLCDGECEE... | null | null | endomembrane system organization [GO:0010256]; Golgi organization [GO:0007030]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of GTPase activity [GO:0034260]; neuron projection development [GO:0031175]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal... | cytosol [GO:0005829]; Golgi membrane [GO:0000139]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; small nuclear ribonucleoprotein complex [GO:0030532]; trans-Golgi network [GO:0005802] | guanyl-nucleotide exchange factor activity [GO:0005085]; myosin binding [GO:0017022]; protein kinase A regulatory subunit binding [GO:0034237] | PF20252;PF16213;PF01369;PF09324;PF12783; | 1.10.220.20;1.10.1000.11; | null | PTM: Phosphorylated. In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:11809827}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11809827}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. No... | null | null | null | null | null | FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-... | Rattus norvegicus (Rat) |
D4A693 | AZIN2_RAT | MAGYLSESDFVMVEEGFSTRDLLEELTLGASQATTGKVAAFFVADAVVRKHFCFLKYLPRVRPFYAVRCNSSLGVLKVLAELGLGFSCASKAEMELVQHIGVPASKIICANPCKQVAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKSWGEVLTLDALGLHHTHRRVGCSLMFQASVIASVAQGYLELVCQPFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGLEGAKVRFEEVTSVIGKNIPFYTPPPCHVPLRTHATKKMTSSDFCCRVHVTAKEKPLFSPFLTEQTGAAPKSIVYHLDEGV... | null | null | negative regulation of protein catabolic process [GO:0042177]; ornithine metabolic process [GO:0006591]; positive regulation of catalytic activity [GO:0043085]; positive regulation of polyamine transmembrane transport [GO:1902269]; putrescine biosynthetic process from ornithine [GO:0033387]; trans-Golgi network membran... | axon [GO:0030424]; cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; granular vesicle [GO:1990005]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinu... | catalytic activity [GO:0003824]; ornithine decarboxylase activator activity [GO:0042978] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family, ODC antizyme inhibitor subfamily | PTM: Ubiquitinated, leading to its proteasomal degradation; a process that is reduced in presence of antizymes. May also be degraded through the lysosomal degradative pathway in a proteasomal-independent manner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19718454}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Golgi appara... | null | null | null | null | null | FUNCTION: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhib... | Rattus norvegicus (Rat) |
D4A6D8 | LRRT1_RAT | MDFLLLGLCLHWLLRRPSGVVLCLLGACFQMLPAAPSGCPGQCRCEGRLLYCEALNLTEAPHNLSGLLGLSLRYNSLSELRAGQFTGLMQLTWLYLDHNHICSVQGDAFQKLRRVKELTLSSNQITELANTTFRPMPNLRSVDLSYNKLQALAPDLFHGLRKLTTLHMRANAIQFVPVRIFQDCRSLKFLDIGYNQLKSLARNSFAGLFKLTELHLEHNDLIKVNFAHFPRLISLNSLCLRRNKVAIVVSSLDWVWNLEKMDLSGNEIEYMEPHVFETVPYLQSLQLDSNRLTYIEPRILNSWKSLTSITLAGNLWDCGR... | null | null | establishment of localization in cell [GO:0051649]; exploration behavior [GO:0035640]; locomotory behavior [GO:0007626]; long-term synaptic potentiation [GO:0060291]; negative regulation of receptor internalization [GO:0002091]; positive regulation of synapse assembly [GO:0051965]; protein localization to synapse [GO:0... | axon [GO:0030424]; endoplasmic reticulum [GO:0005783]; excitatory synapse [GO:0060076]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; postsynaptic membrane [GO:0045211]; postsynaptic specialization memb... | null | PF13855; | 3.80.10.10; | LRRTM family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19285470}; Single-pass type I membrane protein {ECO:0000269|PubMed:19285470}. Postsynaptic cell membrane {ECO:0000269|PubMed:19285470}; Single-pass type I membrane protein {ECO:0000269|PubMed:19285470}. | null | null | null | null | null | FUNCTION: Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation, acting at both pre- and postsynaptic level. {ECO:0000269|PubMed:19285470}. | Rattus norvegicus (Rat) |
D4A6L0 | MGLYR_RAT | MGAMAYSLLLCLLLAHLGLGEVGASLDPSERPDSSRERTSRGKQHGQQLPRASAPDPSIPWSRSTDGTILAQKLAEEVPMDVASYLYTGDFHQLKRANCSGRYELAGLPGKSPSLASSHPSLHGALDTLTHATNFLNMMLQSNKSREQTVQDDLQWYQALVRSLLEGEPSISRAAITFSTESLSTPAPQVFLQATREESRILLQDLSSSAHHLANATLETEWFHGLRRKWRPHLHRRGSNQGPRGLGHSWRRRDGLGGDRSHVKWSPPFLECENGSYKPGWLVTLSAAFYGLQPNLVPEFRGVMKVDINLQKVDIDQCSS... | null | null | brain development [GO:0007420]; cognition [GO:0050890]; G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of neurotransmitter secretion [GO:0001956]; protein localization to plasma membrane [GO:0072659]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of ... | cell projection [GO:0042995]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734] | enzyme activator activity [GO:0008047]; G protein-coupled glycine receptor activity [GO:0160079]; transmembrane signaling receptor activity [GO:0004888] | PF00003; | 3.30.450.20; | G-protein coupled receptor 3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T848}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q8C419}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q8C419}; Multi-pass memb... | null | null | null | null | null | FUNCTION: Metabotropic receptor for glycine that controls synapse formation and function in the brain. Acts as an atypical G-protein coupled receptor that recruits and regulates the RGS7-GNB5 complex instead of activating G proteins. In absence of glycine ligand, promotes the GTPase activator activity of RGS7, increasi... | Rattus norvegicus (Rat) |
D4A702 | SYNP2_RAT | MGTGDFICISMTGGAPWGFRLQGGKEEKQPLQVAKIRSQSKASDSGLCVGDEVVSINGNPCADLTYPEVIKLMESITDSLHLLIKRPTSGTSEALDSETENTNHQHLPHGGPMESTTLQIQHAAKTQGKDFLLASVQTSAPRTEDQGNAWGYAECTTEDQVSQMPGSQEGHLVEEVILRKKPEAGQPGHVVELQLSLSKERQRCTSDPIVTLLGNEKFKSPDPDWGTQHGRTVHINSIPAPEKADTSLTSGTTVQTSSGRELTVIQGRDPGGTGLPQVEVILDCSDRLKAEECRLQAGRGCVASPVEGGRSEAPPSLVSF... | null | null | autophagosome assembly [GO:0000045]; chaperone-mediated autophagy [GO:0061684]; positive regulation of actin filament bundle assembly [GO:0032233]; positive regulation of cell migration [GO:0030335] | actin cytoskeleton [GO:0015629]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; stress fiber [GO:0001725]; Z disc [GO:0030018] | 14-3-3 protein binding [GO:0071889]; actin binding [GO:0003779]; alpha-actinin binding [GO:0051393]; filamin binding [GO:0031005]; muscle alpha-actinin binding [GO:0051371]; protein-macromolecule adaptor activity [GO:0030674] | PF00595; | 2.30.42.10; | Synaptopodin family | PTM: Phosphorylated by PKA, and by CaMK2 at multiple sites. Dephosphorylated by calcineurin at Ser-558 and Thr-605; abrogating interaction with YWHAB and impairing nuclear import. {ECO:0000250|UniProtKB:Q91YE8}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91YE8}. Cytoplasm {ECO:0000250|UniProtKB:Q91YE8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UMS6}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11673475}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9UMS6}. Note=Shuttles between the n... | null | null | null | null | null | FUNCTION: Has an actin-binding and actin-bundling activity. Can induce the formation of F-actin networks. At the sarcomeric Z lines is proposed to act as adapter protein that links nascent myofibers to the sarcolemma via ZYX and may play a role in early assembly and stabilization of the Z lines (By similarity). Involve... | Rattus norvegicus (Rat) |
D4A734 | MOT12_RAT | MTKITRVGSASPPDGGWGWMIVAGCFLVTICTRAVTRCISIFFVEFQTYFAQDYSQTAWIHSIVDCMTMLCAPLGSVVSNQLSCQAGIMLGGLLASTGLILGSFATSLKHLYLSLGVLTGLGFALCYSPAIAMVGKYFSRRKAFAYGIAMSGSGIGTFILAPVVQLLIEQFSWRGALLILGGFVLNLCVCGALMRPITLKEDPSGPEKSHDRDAQREDCKQASPYSPLTKEWTETRLCCSLQQGYGFLLMSDFVVLAVSVLFMAYGCSPLFVYLVPYALSVGVSHHQAAFLMSILGVIDIVGNITFGWLTDRRCLKNYRY... | null | null | creatine transmembrane transport [GO:0015881]; creatinine metabolic process [GO:0046449] | basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886] | creatine transmembrane transporter activity [GO:0005308]; monocarboxylic acid transmembrane transporter activity [GO:0008028]; uniporter activity [GO:0015292] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6ZSM3}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:34075817}; Multi-pass membrane protein {ECO:0000255}. Note=Localized on the sinusoidal membrane of the hepatocyte. Colocalized with SLC6A13 in hepatocytes around t... | CATALYTIC ACTIVITY: Reaction=creatine(in) = creatine(out); Xref=Rhea:RHEA:73043, ChEBI:CHEBI:57947; Evidence={ECO:0000269|PubMed:32781157, ECO:0000269|PubMed:34075817}; CATALYTIC ACTIVITY: Reaction=guanidinoacetate(in) = guanidinoacetate(out); Xref=Rhea:RHEA:73047, ChEBI:CHEBI:57742; Evidence={ECO:0000269|PubMed:327811... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.38 mM for guanidinoacetate {ECO:0000269|PubMed:32781157}; KM=240 uM for creatinine {ECO:0000269|PubMed:32781157}; | null | null | null | FUNCTION: Functions as a transporter for creatine and as well for its precursor guanidinoacetate. Transport of creatine and GAA is independent of resting membrane potential and extracellular Na(+), Cl(-), or pH. Contributes to the process of creatine biosynthesis and distribution. {ECO:0000269|PubMed:32781157, ECO:0000... | Rattus norvegicus (Rat) |
D4A7E1 | BATF_RAT | MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP | null | null | defense response to protozoan [GO:0042832]; DNA damage response [GO:0006974]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; hematopoietic stem cell differentiation [GO:0060218]; isotype switching [GO:0045190]; lymphoid progenitor cell differentiation [GO:0002320]; myeloid dendritic cell d... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-... | PF00170; | 1.20.5.170; | BZIP family | PTM: Phosphorylated on serine and threonine residues and at least one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Cytoplasm {ECO:0000250}. Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells. {ECO:0000250}. | null | null | null | null | null | FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the format... | Rattus norvegicus (Rat) |
D4A7H1 | SL9A9_RAT | MAGQLRLTSGKDEDHFQHQGAVELLAFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIDSGTVYNCGKLLFSPSTLLVNITDQVYEYKYQREINQHNISPHQGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCVVIGLIMYGFVKAMVHAGQLKSGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLNDAVAIVLTYSISIYSPKENPNAFDTAAFFQSVGNFLGIFAGSFAMGSAYAVVTALLTKFTKLREFPMLETGLFFLLS... | null | null | defense response to bacterium [GO:0042742]; phagosome maturation [GO:0090382]; potassium ion transmembrane transport [GO:0071805]; regulation of intracellular pH [GO:0051453]; sodium ion import across plasma membrane [GO:0098719]; sodium ion transmembrane transport [GO:0035725] | early endosome [GO:0005769]; early endosome membrane [GO:0031901]; early phagosome [GO:0032009]; late endosome membrane [GO:0031902]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038] | potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | null | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F7B113}. Early endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F7B113}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-p... | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q8BZ00}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence=... | null | null | null | null | FUNCTION: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH and consequently,... | Rattus norvegicus (Rat) |
D4A7K7 | GP183_RAT | MANNFTTPLAASHGNNCDLYAHHSTARILMPLHYSLVFIIGLVGNLLALVVIVQNRKKINSTTLYSMNLVISDILFTTALPTRIVYYALGFDWRIGDALCRITALLFYINTYAGVNFMTCLSIDRFFAVVHPLRYNKIKRIEYAKGICVFVWILVFAQTLPLLLKPMSKQEADKTTCMEYPNFEGTASLPWILLGACLLGYVLPLAIILLCYSQICCKLFRTAKQNPLTEKSGVNKKALNTIILIIGVFVLCFTPYHVAIMQHMVKTLYAPGALGCGVRHSFQISLHFTVCLMNFNCCMDPFIYFFACKGYKRKVMKMLK... | null | null | adaptive immune response [GO:0002250]; B cell activation involved in immune response [GO:0002312]; cell chemotaxis [GO:0060326]; dendritic cell chemotaxis [GO:0002407]; dendritic cell homeostasis [GO:0036145]; G protein-coupled receptor signaling pathway [GO:0007186]; humoral immune response [GO:0006959]; leukocyte che... | plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930]; oxysterol binding [GO:0008142] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32249}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: G-protein coupled receptor expressed in lymphocytes that acts as a chemotactic receptor for B-cells, T-cells, splenic dendritic cells, monocytes/macrophages and astrocytes (By similarity). Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols (By similarity). Med... | Rattus norvegicus (Rat) |
D4A7P2 | LRRT2_RAT | MGLHFKWPLGAPMLAAIYAMSVVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATDKGSLGLSLRHNHITALERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNKIFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDCRSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNKISNLTCGMEWTWSTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILSSLRSLTTVGLSGNLWECSPRVC... | null | null | long-term synaptic potentiation [GO:0060291]; negative regulation of receptor internalization [GO:0002091]; positive regulation of synapse assembly [GO:0051965]; regulation of postsynaptic density assembly [GO:0099151]; synapse organization [GO:0050808] | excitatory synapse [GO:0060076]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; postsynaptic density membrane [GO:0098839]; postsynaptic specialization membrane [GO:0099634]; S... | neurexin family protein binding [GO:0042043] | PF13855; | 3.80.10.10; | LRRTM family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Postsynaptic cell membrane; Single-pass type I membrane protein. Note=Localized to excitatory synapses. | null | null | null | null | null | FUNCTION: Involved in the development and maintenance of excitatory synapses in the nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B. {ECO:0000269|PubMed:19285470, ECO:00... | Rattus norvegicus (Rat) |
D4A7T3 | BRDT_RAT | MSLPSRQMAIVNPPPPEYINAKKTGRLTNQLQFLQRVVLKALWKHSFSWPFQQPVDAAKLKLPDYYTIIETPMDLSTIKKRLENRYYEKASECVGDFNTMFSNCYLYNKPGDDIVVMAQALEKLFMQKLSQMPQEEQIVGGKERMKKDIQQKTAVSSAKEQTPSKSAENVFKRQEIPAGFPDVCLSPLNMAQEAPPTCDSQTVVQITKGVKRRADTTTPTTSSAKASSESPPPLREAKPANAPVKENTVKSVLPDSQQQHRVLKTVKVTEQLKHCSEILKEMLAKKHLPYAWPFYNPVDVDALGLHNYYDIVKNPMDLGT... | null | null | chromatin remodeling [GO:0006338]; male meiosis I [GO:0007141]; male meiotic nuclear division [GO:0007140]; mRNA processing [GO:0006397]; positive regulation of gene expression [GO:0010628]; regulation of DNA-templated transcription [GO:0006355]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]; sperm... | chromatin [GO:0000785]; nucleus [GO:0005634] | histone binding [GO:0042393]; histone reader activity [GO:0140566]; lysine-acetylated histone binding [GO:0070577] | PF17035;PF17105;PF00439; | 1.20.1270.220;1.20.920.10; | BET family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22215678}. Note=Detected on chromatin. {ECO:0000250|UniProtKB:Q91Y44}. | null | null | null | null | null | FUNCTION: Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the pr... | Rattus norvegicus (Rat) |
D4A7V9 | E2AK4_RAT | MAGGRGAAGRGPAEPQESYSQRQDHELQALEAIYGSDFQDLRPDARGRVREPPEINLVLYPQGLAGEEVYVQVELRVKCPPTYPDVVPEIELKNTKGLSNESVNLLKSHLEELAKKQCGEVMIFELAHHVQSFLSEHNKPPPKSFHEEMLERQAQEKQQRLLEARQKEEQEQREILHEIQKRKEEIKEEKKRKEMAKQERLEITSLTNQDHASKRDPAGHRAAAFLHGGSPDFVGNGKARAHSSGRSRRERQYSVCSGEASPGSCDILYFCVGSADQLMVHKGKCVGSDEQLGKVVYNALETATGSFVLLYEWVLQWQKK... | 2.7.11.1 | null | cell cycle [GO:0007049]; cellular response to amino acid starvation [GO:0034198]; cellular response to cold [GO:0070417]; cellular response to starvation [GO:0009267]; cellular response to UV [GO:0034644]; DNA damage checkpoint signaling [GO:0000077]; endoplasmic reticulum unfolded protein response [GO:0030968]; GCN2-m... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tRNA binding [GO:0000049] | PF12745;PF00069;PF05773;PF13393; | 3.40.50.800;1.10.510.10;3.10.110.10; | Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily | PTM: Autophosphorylated; autophosphorylation on Thr-899 is increased upon amino acid starvation and in UV irradiation cells and inhibited in presence of IMPACT. {ECO:0000250|UniProtKB:Q9QZ05}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QZ05}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9QZ05}; CATALYTI... | null | null | null | null | FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability (By similarity). Plays a role as an activator of the integrated stress response (ISR) required for adaptation to amino aci... | Rattus norvegicus (Rat) |
D4AA47 | AT8B1_RAT | MNTERDSETTFDEDSQPNDEVVPYSDDETEDELEDQGPAVEPEQNRVNREVEKKKETFRKDCTWQVKANDRKFHEQPHFMNTKFFCIKESKYASNAIKTYKYNALTFLPMNLFEQFKRAANFYFLILLILQAIPQISTLAWYTTLVPLLLVLGITAIKDLVDDVARHKMDKEINNRTCEVIKDGRFKIIKWKDIQVGDVIRLKKNDFIPADILLLSSSEPNSLCYVETAELDGETNLKFKMALEITDQYLQIEDNLATFDGFIECEEPNNRLDKFTGTLFWRNQSFPLDADKILLRGCVIRNTDVCHGLVIFAGADTKIM... | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0}; | aminophospholipid transport [GO:0015917]; apical protein localization [GO:0045176]; bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; Golgi organization [GO:0007030]; inner ear receptor cell development [GO:0060119]; negative regulation of DNA-templated transcription [GO:0045892]... | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]; stereocilium [GO:0032420]; trans-Golgi network [GO:0005802] | aminophospholipid flippase activity [GO:0015247]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; cardiolipin binding [GO:1901612]; lipid transporter activity [GO:0005319]; magnesium ion binding [GO:0000287]; phosphatidylcholine flipp... | PF13246;PF00122;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43520}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O43520}. Apical cell membrane {ECO:0000250|UniProtKB:O43520}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q148W0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O43520}. Golgi apparatus {ECO:00... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:19027009}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rh... | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phospholipids, in particular phosphatidylcholines (PC), from the outer to the inner leaflet of the plasma membrane (By similarity) (PubMed:19027009). May participate in the establishment of th... | Rattus norvegicus (Rat) |
D4AB34 | ERFE_RAT | MASTRSPGGARTLLACASLLAAMGLGVPESAEPVGTQARPQPPGTELPAPPAHSPPEPTIAHAHSVDPRDAWMLFVKQSDKGINSKKRSRTKARRLKLGLPGPPGPPGPQGPPGPFIPSEVLLKEFQLLLKGAVRQRESTEHCTRDLTTPASGGPSRDPVTQELESQDQGAVLALLAATLAQSPRAPRVEAAFHCRLRRDVQVERRALHELGVYYLPEVEGAFRRGPGLNLTSGQYTAPVAGFYALAATLHVALTKQPRKGPPQPRDRLRLLICIQSLCQHNASLETVMGLENSSELFTISVNGVLYLQTGHYTSVFLDN... | null | null | establishment of localization in cell [GO:0051649]; fatty acid transport [GO:0015908]; intracellular iron ion homeostasis [GO:0006879]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagy [GO:0010507]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of osteob... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | hormone activity [GO:0005179]; identical protein binding [GO:0042802] | null | 2.60.120.40; | Adipolin/erythroferrone family | PTM: N-glycosylated; required for secretion of the mature protein. {ECO:0000250|UniProtKB:Q6PGN1}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6PGN1}. Note=Secreted when glycosylated at Asn-230 and Asn-282 (By similarity). Hydroxylation promotes secretion (By similarity). {ECO:0000250|UniProtKB:Q6PGN1}. | null | null | null | null | null | FUNCTION: Iron-regulatory hormone that acts as an erythroid regulator after hemorrhage: produced by erythroblasts following blood loss and mediates suppression of hepcidin (HAMP) expression in the liver, thereby promoting increased iron absorption and mobilization from stores (By similarity). Promotes lipid uptake into... | Rattus norvegicus (Rat) |
D4ABL6 | MCTP1_RAT | MEPRGAAAGEPEPAVSPSFQARLWKNLQLGVGKGKGGGGGRAGGPERRTAATPTPSLPPPKTTQDVGSTGSRWSGFKKRKQVLDRVFSSSQPNLCCSSPEPLEPGGAGRAEQGSTLRRRLREHLLPVAKGSSTAAGTVGVTPPGGRSPDSAPSSSASSSLSSSPQPPPRGDRIRDEGTRRGSPEAHLCHQKSSSLPGTACLEQLLEPAPPPAEPARRPAEPQSLQKGEELDCSQKINPVETSNADVPLADPGMYQLDITLRRGQSLAARDRGGTSDPYVKFKIGRKEVFRSKIIHKNLNPVWEEKACVLIDHLREPLYIK... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds Ca(2+) via the C2 domains in absence of phospholipids. {ECO:0000250|UniProtKB:Q6DN14}; | negative regulation of cell migration [GO:0030336]; negative regulation of endocytosis [GO:0045806]; negative regulation of response to oxidative stress [GO:1902883]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of neurotransmitter secretion [GO:0046928] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; recycling endosome [GO:0055037]; synaptic vesicle membrane [GO:0030672] | calcium ion binding [GO:0005509] | PF00168; | 2.60.40.150; | MCTP family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:26195140}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome {ECO:0000269|PubMed:26195140}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A1ZBD6}. | null | null | null | null | null | FUNCTION: Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity (By similarity). Overexpression in cultured neurons significantly inhibits neuronal transferrin endocytosis, secretory vesic... | Rattus norvegicus (Rat) |
D4ACE5 | INTU_RAT | MADPARRDPRGRAPELPGDLSSQEEEEEESDSDAGASSLGSCSSASSDTDLEPEWLDSVQRNGELFYLELSEDEEESLLPETQTVNHVNHVRFSEKEVIIEEDDSRERKKYEPKLRRFTKILKSKSLLPKRHHKKKSSNTGPVSILKHQSTQRTGVTVQQRYKDVTVYINPKKLTAIKAREQAKLLEVLVGVIHQTKWSWKRSGKQADGERLVVHGLVPGGSAMKSGQVLVGDVLVAVNDVDVTSENIERVLSCIPGPMQVKLTFENAYAVKKETAQPKKKKAQSSTNDLVKLLCGSEADATQHSTLSIPHITMYLTLQL... | null | null | cell division [GO:0051301]; cilium assembly [GO:0060271]; embryonic digit morphogenesis [GO:0042733]; establishment of planar polarity [GO:0001736]; hair follicle morphogenesis [GO:0031069]; keratinocyte differentiation [GO:0030216]; limb development [GO:0060173]; motile cilium assembly [GO:0044458]; negative regulatio... | cell surface [GO:0009986]; centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary transition zone [GO:0035869]; cilium [GO:0005929]; cytoplasm [GO:0005737]; motile cilium [GO:0031514] | null | PF19031;PF19032;PF19033; | 2.30.42.10; | Inturned family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q059U7}. Cell surface {ECO:0000250|UniProtKB:Q2I0E5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q2I0E5}. Note=Enriched at the apical surface in ciliated cells. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays a key role in ciliogenesis and embryonic development. Regulator of cilia formation by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules... | Rattus norvegicus (Rat) |
D4ACP5 | RECQ5_RAT | MSARPFSTPFDRERRVRSTLKKVFGFDSFKTPLQESAIMAVVKGDKDVFVCMPTGAGKSLCYQLPAVLAKGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKPRTKLLYITPEMAASASFQPTLNSLLSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVFAALHLKQPVASFKTPCFRANLFYDVQFKELIPDVYGNLRDFCLKALGQKADNGSSSGCGIVYCRTREACEQLAIELSSRGVNAKAYHAGLKASERTQVQNEWMEEKVPVIVATISF... | 5.6.2.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O94762}; Note=Binds a Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:O94762}; | cell division [GO:0051301]; cellular response to camptothecin [GO:0072757]; cellular response to xenobiotic stimulus [GO:0071466]; chromosome separation [GO:0051304]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous ... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657]; transcription preinitiation complex [GO:0097550] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; four-way junction helicase activity [GO:0009378]; helicase activity [GO:0004386]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872]; RNA p... | PF00270;PF00271;PF06959;PF16124; | 6.10.250.2460;6.10.250.3140;3.40.50.300; | Helicase family, RecQ subfamily | PTM: Phosphorylated by CDK1 at Ser-728; this phosphorylation is required for RECQL5-mediated disruption of RAD51 filaments on stalled replication forks. {ECO:0000250|UniProtKB:O94762}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O94762}. Note=Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks. {ECO:0000250|UniProtKB:O94762}. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000250|UniProtKB:O94762}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:306... | null | null | null | null | FUNCTION: DNA helicase that plays an important role in DNA replication, transcription and repair. Binds to the RNA polymerase II subunit POLR2A during transcription elongation and suppresses transcription-associated genomic instability. Associates also with POLR1A and enforces the stability of ribosomal DNA arrays. Pla... | Rattus norvegicus (Rat) |
D4ACX8 | PCD16_RAT | MQEELSVALSCPGMKSLGTLLPLLVLLGTTVPGIRGQAGSLDLQIDEEQPAGTLIGDISAGLPPGTAPPPMYFISAQEGSGVGTDLDIDEHSGVVCTARVLDRERRDRYRFTAVTPDGATVEVTVRVADINDHAPAFPQARAALQIPEHTALGTRYPLEPAHDADAGRLGTQGYALSGDGAGETFRLETRPGPGGAPVPELVIAGELDRENRSHYMLQLEAYDGGSPPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLAPGSPVLQVFASDADAGANGAVTYEINRRQSEGDGPFSIDAHTGFLKLERPLDFEQRR... | null | null | anatomical structure morphogenesis [GO:0009653]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell migration [GO:0016477]; cell migration involved in endocardial cushion formation [GO:0003273]; cell-cell adhesion [GO:0098609]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; coc... | apical part of cell [GO:0045177]; catenin complex [GO:0016342] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF00028; | 2.60.40.60; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=In the embryonic cortex, FAT4 and DCHS1 accumulated at the cell-cell boundaries located apical to the adherens junction. | null | null | null | null | null | FUNCTION: Calcium-dependent cell-adhesion protein. Mediates functions in neuroprogenitor cell proliferation and differentiation (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D4AD37 | IMPA3_RAT | MAPMGIRLSPLGVAVFFLLGLGVLYHLYSGFLAGRFSLFGLGGEPAGGAAEVAVDGGTVDLREMLAVAVLAAERGGDEVRRVRESNVLHEKSKGKTREGAEDKMTSGDVLSNRKMFYLLKTAFPNVQINTEEHVDASDKEVIVWNRKIPEDILKEIAAPKEVPAESVTVWIDPLDATQEYTEDLRKYVTTMVCVAVNGKPVLGVIHKPFSEYTAWAMVDSGSNVKARSSYNEKTPKIIVSRSHAGMVKQVALQTFGNQTLIIPAGGAGYKVLALLDVPDMTQEKADLYIHVTYIKKWDICAGNAILKALGGHMTTLSGEE... | 3.1.3.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | chondrocyte development [GO:0002063]; chondroitin sulfate metabolic process [GO:0030204]; embryonic digit morphogenesis [GO:0042733]; endochondral ossification [GO:0001958]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; post-embryonic development [GO:0009791]; skeletal system development [GO:0001501... | endomembrane system [GO:0012505]; trans-Golgi network membrane [GO:0032588] | 3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; 3',5'-nucleotide bisphosphate phosphatase activity [GO:0097657]; 3'-nucleotidase activity [GO:0008254]; metal ion binding [GO:0046872] | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | PTM: Contains N-linked glycan resistant to endoglycosydase H. {ECO:0000250|UniProtKB:Q9NX62}. | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NX62}. Note=The catalytic core is predicted to res... | CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000250|UniProtKB:Q80V26}; | null | PATHWAY: Sulfur metabolism. {ECO:0000250|UniProtKB:Q80V26}. | null | null | FUNCTION: Exhibits 3'-nucleotidase activity toward adenosine 3',5'-bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',... | Rattus norvegicus (Rat) |
D4AD53 | KCNG1_RAT | MTLLPGDNSDYDYSALSCASDTSFHPAFFPQRQAIKGVFYRRAQRLGPQDDLHQSISLGDRRRQIIINVGGIKYSLPWTTLDEFPLTRLGQLKACTNFDDILSVCDDYDVTCNEFFFDRNPGAFGTILTFLRAGKLRLLREMCALSFQEELLYWGIAEDHLDGCCKRRYLQKIEEFAEMMEREDEEEALDSEDQESEGPSTSEGRLSRCMRRLRDMVEKPHSGLPGKVFACLSVLFVTVTAVNLSVSTLPSLREEEEQGQCSQMCHNVFIVESVCVGWFSLEFLLRFIQAPSKFAFLRSPLTLIDLVAILPYYVTLLVDG... | null | null | potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; regulation of delayed rectifier potassium channel activity [GO:1902259] | plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, G (TC 1.A.1.2) subfamily, Kv6.1/KCNG1 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8980147}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 (PubMed:8980147). {ECO:0000269|PubMed:8980147}. | Rattus norvegicus (Rat) |
D4ADY9 | ELOV7_RAT | MAFSDLTSRTVRFYDNWIKDADPRVENWLLMSSPLPQTIILGLYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGTGYSFRCDIVDYSQSPRAMRMVHTCWLYYFSKFIELFDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYFYYGLCAMGPAYQKYLWWKKHLTSLQLVQFVLVTVHIGQIFFMEDCNYQYPVFLYIIMSYGCIFLLLFLHFWYRAYTKGQRLPKTMENGNCKSKHH | 2.3.1.199 | null | fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid bi... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | fatty acid elongase activity [GO:0009922] | PF01151; | null | ELO family, ELOVL7 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03207}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03207}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03207}; Ph... | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03207}. | null | null | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with... | Rattus norvegicus (Rat) |
D4AE59 | STK11_RAT | MDVADPQPLGLFPEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHRNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFRQLIDGLEYLHSQGIVHKDIKPGNLLLTTNGTLKISDLGVAEALHPFAVDDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGRGDFTIPCDCAPPLSDLLRGMLEYEPAKRFSIRQIRQHSWFRKKHPLAEALV... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | activation of protein kinase activity [GO:0032147]; anoikis [GO:0043276]; autophagy [GO:0006914]; axonogenesis [GO:0007409]; cellular response to UV-B [GO:0071493]; dendrite extension [GO:0097484]; DNA damage response [GO:0006974]; epithelial cell proliferation involved in prostate gland development [GO:0060767]; estab... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular protein-containing complex [GO:0140535]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; serine/threonine protein kinase complex [GO:1902554] | ATP binding [GO:0005524]; LRR domain binding [GO:0030275]; magnesium ion binding [GO:0000287]; p53 binding [GO:0002039]; protein kinase activator activity [GO:0030295]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, LKB1 subfamily | PTM: Phosphorylated by ATM at Thr-366 following ionizing radiation (IR). Phosphorylation at Ser-431 by RPS6KA1 and/or some PKA is required to inhibit cell growth. Phosphorylation at Ser-431 is also required during neuronal polarization to mediate phosphorylation of BRSK1 and BRSK2. Phosphorylation by PKC/PRKCZ at Ser-3... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18774945}. Cytoplasm {ECO:0000269|PubMed:18774945}. Membrane {ECO:0000269|PubMed:18774945}. Mitochondrion {ECO:0000250}. Note=A small fraction localizes at membranes. Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CA... | 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: Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, ... | Rattus norvegicus (Rat) |
D4AEC2 | CAMP2_RAT | MGDAADPREVRRTFIVPAIKPFDHYDFSRAKIACNLAWLVAKAFGTETVPEELREPFYTDQYDQEHIKPPVVNLLLSAELYCRAGSLILKSDAAKPLLGHDAVIQALAHKGLYVTDQEKLVTERDLHKKPIQMSAHLAMIDTLMMAYTVEMVSIEKVIACAQQYSAFFQATDLPYDIEDAVMYWINKVNEHLKDIMEQEQKSKEHHTAEAPGGQKSPSKWFWKLVPARYRKEQTLLKQLPCIPLVENLLKDGTDGCALAALIHFYCPAVVRLEDICLKETMSLADSLYNLQLIQEFCQEYLNHCCHFSLEDMLYAASSIK... | null | null | axon development [GO:0061564]; cytoplasmic microtubule organization [GO:0031122]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; regulation of dendrite development [GO:0050773]; regulation of Golgi organization [GO:1903358]; regulation of microtubul... | centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; microtubule cytoskeleton [GO:0015630]; microtubule minus-end [GO:0036449] | calmodulin binding [GO:0005516]; microtubule minus-end binding [GO:0051011]; spectrin binding [GO:0030507] | PF17095;PF11971;PF08683; | 3.10.20.360; | CAMSAP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q08AD1}. Golgi apparatus {ECO:0000250|UniProtKB:Q08AD1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8C1B1}. Cytoplasm {ECO:0000250|UniProtKB:Q8C1B1}. Note=Associated with the minus-end of microtubules and also detected at the c... | null | null | null | null | null | FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:24908486). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule m... | Rattus norvegicus (Rat) |
D4B387 | GGT1_ARTBC | MAPAAMNLLCTVLYLLSSFAQVSDAAPWLFSRSIPASYHDGRLGAVASENSMCSEYGADMLKIGGNAADAVCIYRLSLFFAFLPYPALQEDRAMYHSGIGGGGFMLIRAPNGTYEFIDFRETAPAAAFQDMFKNNTSGSTSGGLASGVPGEVRGLEYLHKNYGKLPWKTVMEPAIRTARDGFRVTEDLSRIMLHSTKNGNFLAENAAWALDFAPQGTLLKVGDIITRRRYGDTLDKIAKYGADAFYTGPMAQAMVNALRAANGTMTLEDLKNYTVVSRPTAQIEYRGMTVTSTTAPSSGVVLLSILKLLNGYKNFFRMDP... | 2.3.2.2; 3.4.19.13; 3.4.19.14 | null | glutathione biosynthetic process [GO:0006750]; glutathione catabolic process [GO:0006751]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | glutathione hydrolase activity [GO:0036374]; leukotriene C4 gamma-glutamyl transferase activity [GO:0103068]; leukotriene-C(4) hydrolase [GO:0002951] | PF01019; | 1.10.246.130;3.60.20.40; | Gamma-glutamyltransferase family | PTM: Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme. {ECO:0000250|UniProtKB:P19440}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}. | CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={... | null | PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000250|UniProtKB:P19440}. | null | null | FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence ... | Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
D4GP31 | XACC_HALVD | MTVTRVVDTSCRLGEGPVWHPDEKRLYWVDIESGRLHRYDPETGAHDCPVETSVIAGVTIQRDGSLLAFMDRGRVGRVVDGDRRESARIVDSPTRFNDVIADPAGRVFCGTMPSDTAGGRLFRLDTDGTVTTVETGVGIPNGMGFTRDRERFYFTETEARTVYRYAYDEETGAVSARERFVESPETPGLPDGMTVDSAGHIWSARWEGGCVVEYDADGTELGRFDVPTEKVTSVAFGGPDLDSLYVTTAGGDGDGSAGEGDESTGDAAGALFRLDVAATGRPEFRSDVRLG | 3.1.1.15; 3.1.1.68 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:28854683}; Note=Binds 1 divalent metal cation per subunit (By similarity). Most active with Co(2+), Mg(2+) or Mn(2+). Has weaker activity with Fe(2+), Ni(2+) or Zn(2+) (PubMed:28854683). {ECO:0000250|UniProtKB:Q15493, ECO:00002... | arabinose catabolic process [GO:0019568]; D-xylose metabolic process [GO:0042732]; L-ascorbic acid biosynthetic process [GO:0019853] | null | calcium ion binding [GO:0005509]; gluconolactonase activity [GO:0004341]; L-arabinonolactonase activity [GO:0050021]; xylono-1,4-lactonase activity [GO:0050402] | PF08450; | 2.120.10.30; | SMP-30/CGR1 family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + L-arabinono-1,4-lactone = H(+) + L-arabinonate; Xref=Rhea:RHEA:16217, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16501, ChEBI:CHEBI:17100; EC=3.1.1.15; Evidence={ECO:0000269|PubMed:28854683}; CATALYTIC ACTIVITY: Reaction=D-xylono-1,4-lactone + H2O = D-xylonate + H(+); Xref=Rhea... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37.1 mM for L-arabino-gamma-lactone {ECO:0000269|PubMed:28854683}; KM=10.9 mM for D-xylono-gamma-lactone {ECO:0000269|PubMed:28854683}; Vmax=761 umol/min/mg enzyme with L-arabino-gamma-lactone as substrate {ECO:0000269|PubMed:28854683}; Vmax=437 umol/min/mg enzyme ... | PATHWAY: Carbohydrate degradation. {ECO:0000269|PubMed:28854683}. | null | null | FUNCTION: Pentonolactonase involved in D-arabinose and D-xylose catabolism. Catalyzes the hydrolysis of both L-arabino-gamma-lactone and D-xylono-gamma-lactone to the corresponding acids. Can also hydrolyze D-galactono-gamma-lactone and D-glucono-delta-lactone. {ECO:0000269|PubMed:28854683}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GP33 | ARADH_HALVD | MARIAVTGAAGNVGRVTVEALASDHDVTPITHREREGLDSVILDVRDEDALTEAFEGHDIVVHLAANPNPDAAWDSVYEVNIGGTYNVYEAALAADIDRLVFASTNHVHQMYNIADATRPETLAADAEAVGVSDPPRPDSYYGVSKVFGEALGNYYADRHGLEVLNLRIGWLLTADEVREKMDEEESVARYVRAMWLSPGDCEQGMRRAVEASLPDSPLAVNLISANDDRYLSLTETMRAIGYRPRDNSATVVE | 1.1.1.376 | null | L-arabinose catabolic process [GO:0019572]; L-arabinose catabolic process to 2-oxoglutarate [GO:0019570] | null | L-arabinose 1-dehydrogenase (NAD+) activity [GO:0050022]; L-arabinose 1-dehydrogenase (NADP+) activity [GO:0044103]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF01370; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=alpha-L-arabinopyanose + NAD(+) = H(+) + L-arabinono-1,4-lactone + NADH; Xref=Rhea:RHEA:17925, ChEBI:CHEBI:15378, ChEBI:CHEBI:17100, ChEBI:CHEBI:46987, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.376; Evidence={ECO:0000269|PubMed:23949136}; CATALYTIC ACTIVITY: Reaction=alpha-L-arabinopya... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 mM for NADP(+) {ECO:0000269|PubMed:23949136}; KM=2 mM for NAD(+) {ECO:0000269|PubMed:23949136}; KM=2.1 mM for L-arabinose {ECO:0000269|PubMed:23949136}; | PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-arabinono-1,4-lactone pathway. {ECO:0000305|PubMed:23949136}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. It shows 50% activity at pH values of 6 and 10. {ECO:0000269|PubMed:23949136}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:23949136}; | FUNCTION: L-AraDH initiates the degradation of L-arabinose. Catalyzes the NAD(P)(+)-dependent conversion of L-arabinose to L-arabino-gamma-lactone. It is highly specific for L-arabinose as substrate and can use both NADP(+) and NAD(+) as electron acceptor, with a slight preference for NADP(+). {ECO:0000269|PubMed:23949... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GPK6 | LACC_HALVD | MTDWSRRRFLQTGAALGIAGTLPQTTTEVSAASPTLEKFVQPLPIPSVREPDGQRDGADAYEIAVTEFTQQLHPDLPETTVWGFDGSYPGPTIEADAGSPVHVRFDNSGLPSEHLFPVDDRLGGTTAENHPGYDGPVPEVRTVTHFHGLELDPANDGQSDMWTSPGGVEGPRFDSAWQELPMEQGRTTSTYHDHTLGITRLNAYAGLLGLYSITTDAERELGLPSGDYDIPLLLQDKEFNDDGSLHYPEEFVSAFLGDTAVVNGAVWPYVEVEPRRYRFRILNGANHRSFDLQLESESGSGVPTMYQFAPGHGFLESVVP... | 1.10.3.2 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000305}; Note=Binds 4 copper ions per subunit. {ECO:0000305}; | null | extracellular region [GO:0005576] | copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716] | PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | PTM: Exported by the Tat system.; PTM: Glycosylated. {ECO:0000269|PubMed:19966030}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19966030}. | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:19966030}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=671 uM for 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid {ECO:0000269|PubMed:19966030}; KM=35 uM for syringaldazine {ECO:0000269|PubMed:19966030}; Note=kcat is 9.9 sec(-1) with 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid as substrate. kcat is 21... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for the oxidation of 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid and 8.4 for the oxidation of syringaldazine. {ECO:0000269|PubMed:19966030}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-50 degrees Celsius. Highly thermostable. {ECO:0000269|PubMed:19966030}; | FUNCTION: Catalyzes the oxidation of a wide variety of organic substrates, including bilirubin, syringaldazine (SGZ), 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and dimethoxyphenol (DMP). No oxidation of Fe(2+) or guaiacol. {ECO:0000269|PubMed:19966030}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GSE6 | KDGK1_HALVD | MTALVTFGETMLRLSPPRGERLETARELEVQAGGAESNVAVAAARLGRDAAWFSKLPDSPLGRRIVSELRSHSVDTDGVVWTDDADARQGVYYLEHGASPRPTNVVYDRADAAVTTLETGEFDLDAVRDAEVCFTSGITPALSETLSETTADVLDEAQNAGTTTAFDLNYRTKLWSPDEAAEVYRDLLDSVDLLFAAERDAATVLGRDGDAESVARGLADDYDIETVVVTRGEEGSLAVSDGAVSEQGVYETETYDAIGTGDAFVGGFLAKHLDGGSVTESLEWASATASFKRTVEGDIAVVTPEDVERVVAEEGDGISR | 2.7.1.178 | null | D-galacturonate catabolic process [GO:0019698]; D-glucuronate catabolic process [GO:0042840]; DNA damage response [GO:0006974] | cytosol [GO:0005829] | 2-dehydro-3-deoxygalactonokinase activity [GO:0008671]; 2-dehydro-3-deoxygluconokinase activity [GO:0008673]; ATP binding [GO:0005524] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family | null | null | CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-D-gluconate + ATP = 2-dehydro-3-deoxy-6-phospho-D-gluconate + ADP + H(+); Xref=Rhea:RHEA:14797, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57569, ChEBI:CHEBI:57990, ChEBI:CHEBI:456216; EC=2.7.1.178; Evidence={ECO:0000269|PubMed:25287957}; PhysiologicalDirection=left... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.54 mM for KDG {ECO:0000269|PubMed:25287957}; KM=0.73 mM for KDGal {ECO:0000269|PubMed:25287957}; KM=0.36 mM for ATP {ECO:0000269|PubMed:25287957}; Vmax=78 umol/min/mg enzyme with KDG as substrate {ECO:0000269|PubMed:25287957}; Vmax=33 umol/min/mg enzyme with KDGa... | PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 1/2. {ECO:0000305}. | null | null | FUNCTION: Involved in the degradation of glucose via the semi-phosphorylative Entner-Doudoroff pathway. Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). Also catalyzes efficiently the phosphorylation of 2-keto-3-deoxygalactonate (KDGal) to 2-keto-3-deox... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GSF3 | UBAA_HALVD | MTLSLDATQLDRYSRHIIMDEVGPEGQGRLLSSRVVVVGAGGLGAPAIQYLAAVGVGELVVVDDDVVERSNLQRQVVHCDDDVGTPKAESAAAFVRGLNPDVSVEPVEARVDKSNVHEVVAGSDVVVDASDNFPTRYLLNDVCRFEGIPLVHGAIYKFEGQATTLVPDGPCYRCLFPEAPEPGTVPDCATTGVLGVLPGTVGCIQATEAMKLLLDEGEALDGRLLFYDAMDMTFETVPYRTNPDCPVCGEGGVDSIEDIDYVESCAISLD | 2.7.7.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | protein urmylation [GO:0032447]; tRNA wobble position uridine thiolation [GO:0002143] | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtransferase activity [GO:0004792]; ubiquitin-like modifier activating enzyme activity [GO:0008641]; URM1 activating enzyme activity [GO:0042292] | PF00899; | 3.40.50.720; | HesA/MoeB/ThiF family | PTM: Sampylated at Lys-113 with the archaeal ubiquitin-like protein SAMP2. Also sampylated with SAMP1. {ECO:0000269|PubMed:20054389}. | null | CATALYTIC ACTIVITY: Reaction=[small archaeal modifier protein]-C-terminal Gly-Gly + ATP + H(+) = [small archaeal modifier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:56100, Rhea:RHEA-COMP:14381, Rhea:RHEA-COMP:14383, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHE... | null | null | null | null | FUNCTION: Likely activates multiple ubiquitin-like SAMPs for protein conjugation as well as for sulfur transfer, via ATP-dependent adenylation at their C-terminus (PubMed:21368171, PubMed:24097257, PubMed:24906001). In fact, it is required for the formation of all three SAMP1-, SAMP2- and SAMP3-protein conjugates, and ... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GSH6 | NCSA_HALVD | MECDKCGRDAVMHAAYSGAHLCDDHFCASVEKRVRRRIREDNMLPRDASPENPQTWVIGLSGGKDSVVLTHILDDTFGRDPRIELVALTIHEGIEGYRDKSVDACVELAEDLDIHHELVTYEDEFGVQMDDVVEKDPENMAACAYCGVFRRDLLERFADELGADKLLTGHNLDDEAQTALMNFFEGDLKQVAKHFDASIGDFEKRRDAGEFIPRAKPLRDVPEKEVALYAHLKDLPAHITECPHSSEAYRGEIQQLLLKLEENHPGTRHSIMAGYEELAELTAREYRGEGRVDLNDCERCGSKTAGDVCRKCRLIESIEA... | 2.7.7.- | null | response to heat [GO:0009408]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble position uridine thiolation [GO:0002143] | cytosolic tRNA wobble base thiouridylase complex [GO:0002144] | CCA tRNA nucleotidyltransferase activity [GO:0004810]; enzyme binding [GO:0019899]; sulfurtransferase activity [GO:0016783]; tRNA binding [GO:0000049] | PF01171; | 3.40.50.620; | TtcA family, CTU1/NCS6/ATPBD3 subfamily | PTM: Sampylated at Lys-204 with the archaeal ubiquitin-like protein SAMP2. Polymeric chains of SAMP2 are also linked. {ECO:0000269|PubMed:24906001}. | null | null | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000269|PubMed:24906001}. | null | null | FUNCTION: Required for thiolation of mcm(5)S(2)U at the wobble uridine position of tRNA specific for lysine (tRNA(Lys)). Probably acts by catalyzing adenylation of tRNA, an intermediate required for 2-thiolation. May also act as a sulfurtransferase that transfers sulfur from thiocarboxylated SAMP2 onto the uridine of t... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GSH7 | FTSZ2_HALVD | MQDIVREAMERDEAERQTQSSLEDSDDQFGDPRIVIVGAGGAGNNTINRLYNIGVEGADTVAINTDKQHLKMIEADTKILVGKSLTQGLGAGGDPSMGERATEMAQGTIKDVLGDADLVFVTAGMGGGTGTGAAPVVAKIAKEQGAIVVGMVSTPFNVERARTVKAEEGLENLRNEADSIIVLDNNRLLDYVPNLPIGKAFSVMDQIIAETVKGISETITQPSLINLDYADMSTIMNQGGVAVMLVGETQDKNKTQEVVNDAMNHPLLDVDYRGASGGLVHITGGPDLTLKEAEGIASNITERLEAAANVIWGARIQDEY... | null | null | cell division [GO:0051301]; contractile ring contraction [GO:0036213]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]; protein polymerization [GO:0051258] | cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytoplasmic side of membrane [GO:0098562] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF12327;PF00091; | 3.30.1330.20;3.40.50.1440; | FtsZ family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:33903747, ECO:0000269|PubMed:34103513}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:33903747, ECO:0000269|PubMed:34103513}. | null | null | null | null | null | FUNCTION: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produc... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GT97 | IPYR_HALVD | MVNLWEDMETGPNAPDEIYAVVECLKGERNKYEYDKDIPGVVLDRVLHSNVHYPSDYGFIPQTYYDDEDPFDVLVLVEDQTFPGCVIEARPVALMKMDDDGEQDDKVIAVPVEDPRYDHIEDLDDIPQQTLDEIDEFFATYKNLEAGKEVETLGWEDKQAAKDAIEHAMDLYEENFA | 3.6.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00209, ECO:0000269|PubMed:26546423}; | phosphate-containing compound metabolic process [GO:0006796] | cytosol [GO:0005829] | inorganic diphosphate phosphatase activity [GO:0004427]; magnesium ion binding [GO:0000287] | PF00719; | 3.90.80.10; | PPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}. | CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209, ECO:0000269|PubMed:26546423}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.55 mM for diphosphate (at 42 degrees Celsius) {ECO:0000269|PubMed:26546423}; KM=0.26 mM for diphosphate (at 25 degrees Celsius) {ECO:0000269|PubMed:26546423}; Vmax=465 umol/min/mg enzyme (at 42 degrees Celsius) {ECO:0000269|PubMed:26546423}; Vmax=53 umol/min/mg e... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:26546423}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius. Is moderately thermostable, with a half-life of thermal inactivation of 2 hours at 65 degrees Celsius, and retains 82% activity after incubation for 2 hours at 42 degrees Celsius. {ECO:0000269|PubMed:26546423}; | FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions (By similarity) (PubMed:26546423). The hydrolysis of PPi by inorganic pyrophosphatase releases a considerable amount of energy that can drive unfavorable biochemical transformations to completion (Probable). Is not active on ... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GTL2 | ACEB_HALVD | MTERRHDREFVRTFFTSPTAVEGEDDSAKMLRRAAGLRGMQAPDVWVPDNEDATAPSMRDEGAENIVEVISEQGAEFPGEIHPRMVWHRDSPETRYQGFQHMLDITDPERGAVEHIHGFVIPEVGGIDDWKKADEFFTIVEHEHGLDEGSLAMSVIIESGEAELAMGDLRDEMGKPTNNLERLFLLVDGEVDYTKDMRAMTPTGELPAWPELRHNTSRGASAAGCVAVDGPYDDIRDVEGYRERMTDNQAKGMLGIWSLTPGQVVEANTSPLPPKTGSWLLDADGEEVELASEDGVEAYDGDRLSLEATDGGYELRVGGD... | 2.3.3.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21569248}; | glyoxylate cycle [GO:0006097]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737] | magnesium ion binding [GO:0000287]; malate synthase activity [GO:0004474]; metal ion binding [GO:0046872] | null | 1.20.58.1560;3.20.20.60; | HpcH/HpaI aldolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000269|PubMed:9738442}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.11 uM for glyoxylate (with 0.2 mM acetyl-CoA at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:9738442}; KM=0.119 uM for acetyl-CoA (with 0.5 mM glyoxylate at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:9738442}; Note=AceB requires a high salt concentratio... | PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8 and 9. {ECO:0000269|PubMed:9738442}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 45 and 65 degrees Celsius. The activity of the enzyme at 80 degrees Celsius is half of the maximum. {ECO:0000269|PubMed:9738442}; | FUNCTION: Involved in the glyoxylate cycle which synthesizes precursors for carbohydrates from C2 compounds such as acetate. Catalyzes the Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate that is subsequently hydrolyzed to produce malate and CoA. {ECO:0000269... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GTL3 | ACEA_HALVD | MNPTELDSDVFAQDVDNQKARELREMLNTQDFVFAPGMYHALDARLAEMTGHDAAYMSGYSTVLGQFGFPDLEMVTMTEMVENAKRMVEATNLPVIADCDTGYGGIHNVRRAVREYEKAGVAAVHIEDQTTPKRCGHIAGKQIVSREKAKARFEAAVDAKQSEDTVVIARTDAYGSSNGDWDEHVERGRIYADAGVDIVWPEMPNPSREDAVAYAEEIHETHPDLKLAFNYSSSFAWSEEEDPLTFQELGDLGYKYIFITLFGLHSGAHAVYEDFKKLAEQDEEGQFDLEQRYLDHPTESHHELSFVSRYQDIETEFDPE... | 4.1.3.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P0A9G6}; | glyoxylate cycle [GO:0006097]; propionate catabolic process, 2-methylcitrate cycle [GO:0019629] | null | isocitrate lyase activity [GO:0004451]; metal ion binding [GO:0046872]; methylisocitrate lyase activity [GO:0046421] | PF13714; | 3.20.20.60; | Isocitrate lyase/PEP mutase superfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate = glyoxylate + succinate; Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031, ChEBI:CHEBI:36655; EC=4.1.3.1; Evidence={ECO:0000269|PubMed:9738442}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.16 uM for isocitrate (at pH 7 and 40 degrees Celsius) {ECO:0000269|PubMed:9738442}; | PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2. {ECO:0000305|PubMed:9738442}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. Very little activity is detected at pH 6.1 or 8.0. {ECO:0000269|PubMed:9738442}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. Very little activity is found above 65 degrees Celsius, and the activity at 40 degrees Celsius is 50% of the maximum. {ECO:0000269|PubMed:9738442}; | FUNCTION: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substr... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GTS4 | JAMM1_HALVD | MTSSRLSLAADARDSILSHAREGAAGDPPAEVCGVLAGDSDARTVTAAHPVSNVAAEPRVAYELDPEETVSILEAIESAGDDAVGFYHSHPESDPVPSATDRERASWPGYVYLICSPDGRMTAHEWTGDEFRELSVAVE | 3.4.19.15 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22970855}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22970855}; | proteolysis [GO:0006508] | null | metalloexopeptidase activity [GO:0008235]; zinc ion binding [GO:0008270] | PF14464; | 3.40.140.10; | Peptidase M67B family | null | null | CATALYTIC ACTIVITY: Reaction=an N(6)-[small archaeal modifier protein]-[protein]-L-lysine + H2O = a [protein]-L-lysine + a [small archaeal modifier protein].; EC=3.4.19.15; Evidence={ECO:0000269|PubMed:22970855}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-10. Displays little to no activity at low pH (pH 6.5 and below). {ECO:0000269|PubMed:22970855}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. Is active over a wide range of temperature (20-60 degrees Celsius). However, the enzyme is not active at 70 degrees Celsius. {ECO:0000269|PubMed:22970855}; | FUNCTION: Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions a... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GUA0 | AGLD_HALVD | MGRPTERRPAAATAAGVEVSVVLPAYNEARTIENTVRVTVETLESFLPADAFEVIVAEDGCDDETPEIADRLAAEDDRIRHYHSDDRLGRGGALERAFEAARGDTLVYFDTDLATDMRHLEELVERVRSGEYDAATGSRWMPDRVADRPRKRGVPSRAYNGLVRLFLRSDLRDHQCGFKAFSREAFEALRDDVEDNHWFWDTEMLVRAQRAGFRVAEFPVDWEPKGDTKVDLVRDILGMGSQILRTWWQLTVRPRITRRVTIVAGLLLTVLALALMTLYIDPSEVISVLGDADPALVAAAAVIYVVSWPLRGIRYREILR... | 2.4.1.- | null | S-layer organization [GO:0045232] | plasma membrane [GO:0005886] | glycosyltransferase activity [GO:0016757] | PF00535;PF03706; | null | Glycosyltransferase 2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | PATHWAY: Cell surface structure biogenesis; S-layer biogenesis. {ECO:0000269|PubMed:17996897}. | null | null | FUNCTION: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition of the mannose found at position 5 of the pentasaccharide to its own distinct dolichol phosphate carrier. {ECO:0000269|PubMed:17996897, ECO:0000269|PubMed:21091511, ECO:0000269... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GUJ7 | PAN1_HALVD | MMTDTVDDVDLPYDKDSASQQEKITALQERLEVLETQNEEMRDKLLDTNAENNKYQQKLERLTHENKKLKQSPLFVATVQEITDEGVIIKQHGNNQEALTEVTDEMREELEPDARVAVNNSLSIVKRLDKETDVRARVMQVEHSPDVTYEDIGGLEEQMQEVRETVEMPLDRPEMFAEVGIDPPSGVLLYGPPGTGKTMLAKAVANQTNASFIKMAGSELVHKFIGEGAKLVRDLFEVARENEPAVIFIDEIDAIASKRTDSKTSGDAEVQRTMMQLLAEMDGFDERGNIRIIAATNRFDMLDPAILRPGRFDRLIEVPK... | null | null | proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein unfolding [GO:0043335] | cytoplasm [GO:0005737]; proteasome regulatory particle, base subcomplex [GO:0008540]; proteasome-activating nucleotidase complex [GO:0022623] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; proteasome-activating activity [GO:0036402] | PF00004;PF17862; | 1.10.8.60;2.40.50.140;3.40.50.300; | AAA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00553}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=438 uM for ATP (at 42 degrees Celsius, pH 8 and 2 M NaCl) {ECO:0000269|PubMed:24343376}; Vmax=471 nmol/h/mg enzyme for ATPase activity (at 42 degrees Celsius, pH 8 and 2 M NaCl) {ECO:0000269|PubMed:24343376}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius. ATPase activity is 1.5-fold decreased at 25 degrees Celsius and 37 degrees Celsius, 4.7-fold at 20 degrees Celsius. The protein is not active at 50 degrees Celsius. {ECO:0000269|PubMed:24343376}; | FUNCTION: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of pro... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GWB3 | Z2753_HALVD | MSESEQRHAHQCVSCGINIAGMSAATFKCPDCGQEISRCSKCRKQSNLYECPDCGFMGP | null | null | archaeal-type flagellum-dependent cell motility [GO:0097590]; single-species surface biofilm formation [GO:0090606] | null | zinc ion binding [GO:0008270] | PF07754; | null | null | null | null | null | null | null | null | null | FUNCTION: Zinc-binding protein that binds only one zinc ion. Is required for swarming and biofilm formation. {ECO:0000269|PubMed:32905660}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GY98 | DNLJ_HALVD | MSDADVDAESNPYLRDPPTEFEPAESLSREAAEGQAALLREAVREHDHRYYVAADPLVSDAAYDALFSRLVALEDAFDLDTTNSPTNRVGGEPIDALETVEHVAPMLSIDQSTDADDLREFDERVRREVGAVDYVCEPKFDGLSVEVVYEDGEFVRAATRGDGRRGDDVSAQVKTIPTVPLSLRGDHPDRLAVRGEIYMPKSDFSDLNARRVEAGEDAFANPRNAAAGTLRNLDPSVVADRPLAVFFYDILDASARPDSQWAALDRLREWGLRVTDRIERAEDVAEAIDYRDRMQAARDDLDYEIDGTVIKVDSRDARER... | 6.5.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:17132163}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:17132163}; | base-excision repair, DNA ligation [GO:0006288]; DNA replication [GO:0006260] | cytosol [GO:0005829] | DNA binding [GO:0003677]; DNA ligase (NAD+) activity [GO:0003911]; metal ion binding [GO:0046872] | PF00533;PF01653;PF03120;PF12826;PF14520; | 1.10.150.20;3.40.50.10190;3.30.470.30;1.10.287.610;2.40.50.140; | NAD-dependent DNA ligase family, LigA subfamily | null | null | CATALYTIC ACTIVITY: Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:17132163}; | null | null | null | null | FUNCTION: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. {ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYE0 | ALF_HALVD | MPFYGGEELATVYDEALDEGFGLIASNIAEPNIMMGLMEGADRMDSDLLLQMSGGACRFAGDGDAVAGLKAMGNYIETIAERYDIGVFLNMDHQTDLEFIEQQIELDIPSSIMIDASHEPFDENVATSREVVEMVEAAGSDVLIEAELGQIKGVEDEIEAEEAFYTDPEQAVEFVDKTGADLLAISVGTQHGVAKGKDLELRPDLANDIRQALRDHGLDTPLVLHGSSGVQPDQLQEMLKHGICKVNKDTRYQYEYTRTAYDRYNEEPNAIVPPEGVADARDTFFNETDWSPNKDVFDPRVAGRDIRERIADVHADLTEV... | 4.1.2.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. {ECO:0000250}; | glycolytic process [GO:0006096] | cytosol [GO:0005829] | fructose-bisphosphate aldolase activity [GO:0004332]; tagatose-bisphosphate aldolase activity [GO:0009025]; zinc ion binding [GO:0008270] | PF01116; | 3.20.20.70; | Class II fructose-bisphosphate aldolase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:22493022}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.24 mM for D-fructose 1,6-bisphosphate {ECO:0000269|PubMed:22493022}; Vmax=55 umol/min/mg enzyme {ECO:0000269|PubMed:22493022}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:22493022}; | null | FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. Is required for the utilization of fructose as a sole carbon and energy source. ... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYG6 | AGLQ_HALVD | MTSLSDILASSAEAGLSLQRSDGSMPAGHNGPYHDPETPVRNTSHWLVTFLKAHELTDENRFRQAASDAVSYLLSEEARPHGHTFEHRQNDTKDRCNGLMGQAWSLEALALAARALDNERAAAVAADVFLSHPFCDKLKLWQRVDTDGTILGFDRTFNHQLWFAASGGLVAHTAPQEVSQRVRDFLDSLPSTIDLYENGLIRHPLRPSMDLSELAESVTHDVHRSMVRNHLLHYLRPPRSKRRLRNKAEGYHSFNLYALAILAREFPSHSVWSTDLLSDILEYTLSEEFREATTDNKFSHPYNPPGFEVPAAMETFSVGS... | null | null | carbohydrate metabolic process [GO:0005975]; S-layer organization [GO:0045232] | cytoplasm [GO:0005737] | null | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24236216}. | null | null | PATHWAY: Cell surface structure biogenesis; S-layer biogenesis. {ECO:0000269|PubMed:24236216}. | null | null | FUNCTION: Putative isomerase involved in the N-glycosylation pathway. Required for the appearance of the methyl ester of hexuronic acid found at position four of the pentasaccharide N-linked to the S-layer glycoprotein. Either involved in preparing the third sugar for attachment of the fourth pentasaccharide subunit or... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYH4 | AGLB_HALVD | MSDEQTKYSPSIAELARDWYHIPVLSTIILVMLWIRLRSYDAFIREGTVFFSGNDAWYHLRQVEYTVRNWPATMPFDPWTEFPFGRTAGQFGTIYDQLVATAALVVGLGSPSSDLVAKSLLVAPAVFGALTVIPTYLIGKRLGGRLGGLFGAVILMLLPGTFLQRGLVGFADHNIVEPFFMGFAVLAIMIALTVADREKPVWELVAARDLDALREPLKWSVLAGVATAIYMWSWPPGILLVGIFGLFLVLKMASDYVRGRSPEHTAFVGAISMTVTGLLMFIPIEEPGFGVTDFGFLQPLFSLGVALGAVFLAALARWWE... | 2.4.99.21 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O29867}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O29867}; | post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; S-layer organization [GO:0045232] | plasma membrane [GO:0005886] | dolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872] | PF18079;PF02516; | 2.60.40.3390;3.40.50.12610; | STT3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.; EC=2.4.99.21; Evidence={ECO:0000269|PubMed:21091511}; | null | PATHWAY: Cell surface structure biogenesis; S-layer biogenesis. {ECO:0000269|PubMed:17996897}.; PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:17996897}. | null | null | FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a hexose-linked tetrasaccharide composed of a hexose, 2 hexuronic acids and a methyl ester of hexuronic acid in H.volcanii) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr c... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYI2 | GLPA1_HALVD | MKKSPSVLVIGGGSTGTGIARDLAMRGLDVTLVEKGNLTHGTTGRMHGLLHSGGRYAVSDQPSAKECIEENRVLRRIAGHCVEMTGGLFVQRPEDSDEYFEKKLEGCRECGIPAEVLSAEEAREIEPYLAKDIKRAIKVPDGAVDPFRLCVANAASAVEHGARIETHSEVTDVLVEGGEVVGVEVTHQTGTGPYVHGEPGEVEEIRADYVVNATGAWAGQIGDFAGVNVEVRPSKGVMTIMNTRQVDTVVNRCRPKGDADIIVPHETTCILGTTDEEVEDPEDYPEEGWEVDLMIETLSELVPMLADARTIRSFWGVRPL... | 1.1.5.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; | glycerol catabolic process [GO:0019563]; glycerol-3-phosphate metabolic process [GO:0006072] | glycerol-3-phosphate dehydrogenase complex [GO:0009331]; plasma membrane [GO:0005886] | flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; glycerol-3-phosphate dehydrogenase (quinone) activity [GO:0004368] | PF01266;PF04324; | 1.10.10.1100;3.30.9.10;3.50.50.60; | FAD-dependent glycerol-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3; Evidence={ECO:0000269|PubMed:21725010}; | null | PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1. | null | null | FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone phosphate. Required for growth on glycerol and for glycerol metabolism. {ECO:0000269|PubMed:21725010}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYV5 | SUFS_HALVD | MRVQESYPVDVDAIRADFPILERKVGGDISTPGEHDDDTTPLVYLDNAATSHTPEQVVDAIVDYYHGYNSNVHRGIHHLSQEASVAYEDAHDRVAEFIGASGGREEVVFTKNTTESMNLVAYAWGLDELGPGDSVVMTEMEHHASLVTWQQIAKKTGAEVRYIRVDDDGRLDMEHAKELIDDSTKMVSVVHVSNTLGTVNPVSELADMAHEVGSYIFVDGAQSVPTRPVDVEDIDADFFAFSGHKMCGPTGIGALYGKRDILDEMGPYLYGGEMIRSVTYEDSTWEDLPWKFEAGTPPIAQGVGFAAAVDYLDDIGMENV... | 2.8.1.7; 4.4.1.16 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20226884}; | cysteine metabolic process [GO:0006534] | null | cysteine desulfurase activity [GO:0031071]; pyridoxal phosphate binding [GO:0030170]; selenocysteine lyase activity [GO:0009000] | PF00266; | 3.90.1150.10;3.40.640.10; | Class-V pyridoxal-phosphate-dependent aminotransferase family, Csd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000269|PubMed:20226884}; CATALYTIC ACTIVITY: Reaction=A... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.032 mM for L-cysteine {ECO:0000269|PubMed:20226884}; KM=0.97 mM for L-selenocysteine {ECO:0000269|PubMed:20226884}; Vmax=0.051 umol/min/mg enzyme with L-cysteine as substrate {ECO:0000269|PubMed:20226884}; Vmax=11.8 umol/min/mg enzyme with L-selenocysteine as sub... | PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Remains partially active at pH 11. {ECO:0000269|PubMed:20226884}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55-60 degrees Celsius in the presence of 0-0.5 M KCl and 70-75 degrees Celsius in the presence of 2.5-3.0 M KCl. {ECO:0000269|PubMed:20226884}; | FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Able to reassemble a removed [2Fe-2S] cluster of an apo-ferredoxin. Shows a selenocysteine lyase activity approximately 280-fold higher than its cysteine desulfurase activity. {ECO:0000269|PubMed:20226884}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYZ1 | PSB_HALVD | MRTPTHDEFSGRLDSLNGDRSNVFGPELGEFSNADRRADELGDKETKTGTTTVGIKTEEGVVLATDMRASMGYMVSSKDVQKVEEIHPTGALTIAGSVSAAQSLISSLRAEVRLYEARRGEDMSMQALSTLVGNFLRSGGFYVVQPILGGVDETGPHIYSIDPAGSILEEEYTVTGSGSQYALGVLEQEFEDGLSIEEAKGVATKAIRSAVERDLASGNGINIAVVTEDGVDIQRHQNFEGLE | 3.4.25.1 | null | proteasomal protein catabolic process [GO:0010498] | cytoplasm [GO:0005737]; proteasome core complex, beta-subunit complex [GO:0019774] | endopeptidase activity [GO:0004175]; threonine-type endopeptidase activity [GO:0004298] | PF00227; | 3.60.20.10; | Peptidase T1B family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}. | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; Evidence={ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:10482525}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-9.3 for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype). {ECO:0000269|PubMed:10482525}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype). {ECO:0000269|PubMed:10482525}; | FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activ... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GZE7 | SAMP2_HALVD | MNVTVEVVGEETSEVAVDDDGTYADLVRAVDLSPHEVTVLVDGRPVPEDQSVEVDRVKVLRLIKGG | null | null | protein modification by small protein conjugation [GO:0032446] | null | nucleotide binding [GO:0000166]; protein tag activity [GO:0031386] | null | 4.10.410.50; | null | PTM: The C-terminal glycine is likely acyl-adenylated (-COAMP) by UbaA, and also probably thiocarboxylated (-COSH) to function in sulfur transfer. {ECO:0000269|PubMed:21368171}. | null | null | null | null | null | null | FUNCTION: Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in tRNA thiolation. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP2 C-terminal glycine carboxylate and the epsilon... | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4HRL0 | GH7B_LIMQU | MSLAVVFLLGFLAVSHGQQAGTETEEYHLPLTWERDGSSVSASVVIDSNWRWTHSTEDTTNCYDGNEWDSTLCPDADTCTENCAIDGVDQGTWGDTYGITASGSKLTLSFVTEGEYSTDIGSRVFLMADDDNYEIFNLLDKEFSFDVDASNLPCGLNGALYFVSMDEDGGTSKYSTNTAGAKYGTGYCDAQCPHDMKFIAGKANSDGWTPSDNDQNAGTGEMGACCHEMDIWEANSQAQSYTAHVCSVDGYTPCTGTDCGDNGDDRYKGVCDKDGCDYAAYRLGQHDFYGEGGTVDSGSTLTVITQFITGGGGLNEIRRI... | 3.2.1.91 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulose 1,4-beta-cellobiosidase activity [GO:0016162] | PF00840; | 2.70.100.10; | Glycosyl hydrolase 7 (cellulase C) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000269|PubMed:23733951}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2676.4 uM for p-nitrophenyl-beta-d-cellotrioside (pNP-G3) {ECO:0000269|PubMed:23733951}; KM=2121.7 uM for p-nitrophenyl-beta-d-cellopentaoside (pNP-G5) {ECO:0000269|PubMed:23733951}; Note=kcat is 10.57 min(-1) for p-nitrophenyl-beta-d-cellotrioside (pNP-G3). kcat i... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6.5 for p-nitrophenyl-beta-d-cellotrioside (pNP-G3), and 4-8 for p-nitrophenyl-beta-d-cellopentaoside (pNP-G5). {ECO:0000269|PubMed:23733951}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is approximately 25-45 degrees Celsius. High activity is maintained over a wide temperature range. {ECO:0000269|PubMed:23733951}; | FUNCTION: Exocellobiohydrolase (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (PubMed:23733951). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut inter... | Limnoria quadripunctata (Gribble) |
D4N500 | DIOX1_PAPSO | MEKAKLMKLGNGMEIPSVQELAKLTLAEIPSRYVCANENLLLPMGASVINDHETIPVIDIENLLSPEPIIGKLELDRLHFACKEWGFFQVVNHGVDASLVDSVKSEIQGFFNLSMDEKTKYEQEDGDVEGFGQGFIESEDQTLDWADIFMMFTLPLHLRKPHLFSKLPVPLRETIESYSSEMKKLSMVLFNKMEKALQVQAAEIKGMSEVFIDGTQAMRMNYYPPCPQPNLAIGLTSHSDFGGLTILLQINEVEGLQIKREGTWIAVKPLPNAFVVNVGDILEIMTNGIYHSVDHRAVVNSTNERLSIATFHDPSLESVI... | 1.14.11.31; 2.1.1.- | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:20228795}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:20228795}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | methylation [GO:0032259]; morphine biosynthetic process [GO:0097295] | null | (S)-tetrahydroprotoberberine N-methyltransferase activity [GO:0030782]; metal ion binding [GO:0046872]; oripavine 6-O-demethylase activity [GO:0102804]; thebaine 6-O-demethylase activity [GO:0102802] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + thebaine = CO2 + formaldehyde + neopinone + succinate; Xref=Rhea:RHEA:27477, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:59950, ChEBI:CHEBI:59953; EC=1.14.11.31; Evidence={ECO:0000269|PubMed:20228795, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.4 uM for oripavine {ECO:0000269|PubMed:20228795}; KM=20.3 uM for thebaine {ECO:0000269|PubMed:20228795}; KM=16.4 uM for 2-oxoglutarate {ECO:0000269|PubMed:20228795}; | PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Non-heme dioxygenase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products (PubMed:20228795, PubMed:29779229). Mediates the conversion of thebaine to neopinone (PubMed:20228795, PubMed:22098111). Catalyzes also, with lower efficiency, the 6-O-demethylation of orip... | Papaver somniferum (Opium poppy) |
D4N502 | DIOX3_PAPSO | METPILIKLGNGLSIPSVQELAKLTLAEIPSRYTCTGESPLNNIGASVTDDETVPVIDLQNLLSPEPVVGKLELDKLHSACKEWGFFQLVNHGVDALLMDNIKSEIKGFFNLPMNEKTKYGQQDGDFEGFGQPYIESEDQRLDWTEVFSMLSLPLHLRKPHLFPELPLPFRETLESYLSKMKKLSTVVFEMLEKSLQLVEIKGMTDLFEDGLQTMRMNYYPPCPRPELVLGLTSHSDFSGLTILLQLNEVEGLQIRKEERWISIKPLPDAFIVNVGDILEIMTNGIYRSVEHRAVVNSTKERLSIATFHDSKLESEIGPI... | 1.14.11.31; 1.14.11.32 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:20228795}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:20228795}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | methylation [GO:0032259]; morphine biosynthetic process [GO:0097295] | null | codeine O-demethylase activity [GO:0102805]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; thebaine 6-O-demethylase activity [GO:0102802]; thebane O-demethylase activity [GO:0102803] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + codeine + O2 = CO2 + formaldehyde + morphine + succinate; Xref=Rhea:RHEA:27413, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:57871, ChEBI:CHEBI:58097; EC=1.14.11.32; Evidence={ECO:0000269|PubMed:20228795, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=198 uM for (S)-scoulerine {ECO:0000269|PubMed:23928311}; KM=20.5 uM for codeine {ECO:0000269|PubMed:20228795}; KM=41.9 uM for thebaine {ECO:0000269|PubMed:20228795}; KM=19 uM for 2-oxoglutarate {ECO:0000269|PubMed:20228795}; Vmax=11.6 pmol/sec/mg enzyme with (S)-sc... | PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Non-heme dioxygenase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products (PubMed:29779229). Mediates the conversion of codeine to morphine (PubMed:20228795, PubMed:22098111, PubMed:29779229). Catalyzes also, with lower efficiency, the 3-O-demethylation of thebai... | Papaver somniferum (Opium poppy) |
D4NUX0 | HCT1_ACTRA | MVCIKSSCVVKPSEPTPNVKLFLPESDQVKPWTHAPVFFVYQPEVDNSVSTSLENLKFSLSRALVPYYPLAGRLNGIGGGRFELHCNTMGAVIIEAESDARLEDFGDFRPTSETTKLAPYVDYAKDVSELPLLLVQLTRFKCGGIGIGIAMSHIVSDGKGAFGFITTWAKINRGEKGIIEPFHDRTAFYKGDPTAKPRCDHVELKGYPVLLGNKSAKEERAKETTTRMLNLSKNQVDKLKEKSNLGKPKDYVGREYSRFEAMSGHIWRCASKARRHENEQLTSLRITIDCRNRLRPPLPPRYSGNATMVTTSIAESGELL... | 2.3.1.- | null | alkaloid metabolic process [GO:0009820]; phenylpropanoid metabolic process [GO:0009698]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to UV [GO:0009411] | null | hydroxycinnamoyltransferase activity [GO:0050734] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R,3S)-piscidate + (E)-4-coumaroyl-CoA = cimicifugate K + CoA; Xref=Rhea:RHEA:73319, ChEBI:CHEBI:57287, ChEBI:CHEBI:85008, ChEBI:CHEBI:192789, ChEBI:CHEBI:192790; Evidence={ECO:0000269|PubMed:31069522}; CATALYTIC ACTIVITY: Reaction=(2R,3S)-piscidate + (E)-caffeoyl-CoA = cimicifugate D + Co... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.8 uM for 4-coumaroyl-CoA (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31069522}; KM=10.5 uM for sinapoyl-CoA (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31069522}; KM=16.3 uM for caffeoyl-CoA (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|Pu... | PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:31069522}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:31069522}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:31069522}; | FUNCTION: Catalyzes the formation of cimicifugic acids. Uses hydroxycinnamoyl-CoA thioesters as hydroxycinnamoyl donor substrates. Has a strict specificity for piscidic acid as an acceptor substrate as none of the various other acceptors tested including 4-hydroxyphenyllactic acid, malate, spermidine or tetrahydroxyhex... | Actaea racemosa (Black cohosh) (Cimicifuga racemosa) |
D4P095 | CNPD3_PSEAI | MSRHSNTPATDASVLLVQLSDSHLFAEDGARLLGMDTAHSLEKVVERVAREQPRIDLILATGDVSQDGSLDSYTRFRRLSAPLAAPLRWFAGNHDEREPMQRATEGSDLLEQIVDVGNWRVVLLDSSIPGAVPGYLEDDQLDLLRRAIDSAGERFLLVSFHHHPVPIGSDWMDPIGLRNPQALFDLLAPYPQLRCLLWGHIHQEFDRQRGPLRLLASPSTCVQFAPGSSDFTLDRLAPGYRWLRLHDDGRLETGISRVDDVVFEVDYDTAGY | 3.1.4.53 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:20348254}; Note=Binds 2 metal cations per subunit. Site 1 may preferentially bind Fe(3+) ions, while site 2 may have a preference for Fe(2+) ions. {ECO:0000269|PubMed:20348254}; | null | null | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF00149; | 3.60.21.10; | Cyclic nucleotide phosphodiesterase class-III family | null | null | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000269|PubMed:20348254}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.2 uM for cAMP {ECO:0000269|PubMed:20348254}; Vmax=3.4 nmol/min/ng enzyme {ECO:0000269|PubMed:20348254}; | null | null | null | FUNCTION: Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Specifically required for regulation of virulence factors. Can also hydrolyze cGMP, but cGMP is unlikely to be synthesized by P.aeruginosa and cAMP... | Pseudomonas aeruginosa |
D4YWD1 | TPF_PELSA | FLGTINLSLCEEERDADEEERRDEPDESNVEVKKRFFFLSRIFGK | null | null | defense response to bacterium [GO:0042742]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | PF03032; | null | Frog skin active peptide (FSAP) family, Temporin subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20308076}. Target cell membrane {ECO:0000269|PubMed:20308076}. Note=Inserts into the lipid bilayer with an in-plane (parallel) orientation. {ECO:0000269|PubMed:20308076}. | null | null | null | null | null | FUNCTION: Non-amphipathic alpha-helical antimicrobial peptide with potent activity against some Gram-positive bacteria (including methicillin-resistant Staphylococcus aureus (MRSA)), weak activity against Gram-negative bacteria and no activity against fungi (PubMed:20308076, PubMed:26181487, PubMed:27915018). Permeabil... | Pelophylax saharicus (Sahara frog) (Rana saharica) |
D4Z2G1 | LINB_SPHIU | MSLGAKPFGEKKFIEIKGRRMAYIDEGTGDPILFQHGNPTSSYLWRNIMPHCAGLGRLIACDLIGMGDSDKLDPSGPERYAYAEHRDYLDALWEALDLGDRVVLVVHDWGSALGFDWARRHRERVQGIAYMEAIAMPIEWADFPEQDRDLFQAFRSQAGEELVLQDNVFVEQVLPGLILRPLSEAEMAAYREPFLAAGEARRPTLSWPRQIPIAGTPADVVAIARDYAGWLSESPIPKLFINAEPGALTTGRMRDFCRTWPNQTEITVAGAHFIQEDSPDEIGAAIAAFVRRLRPA | 3.8.1.5 | null | response to toxic substance [GO:0009636] | periplasmic space [GO:0042597] | haloalkane dehalogenase activity [GO:0018786] | PF00561; | 3.40.50.1820; | Haloalkane dehalogenase family, Type 2 subfamily | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10464214}. | CATALYTIC ACTIVITY: Reaction=1-haloalkane + H2O = a halide anion + a primary alcohol + H(+); Xref=Rhea:RHEA:19081, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:16042, ChEBI:CHEBI:18060; EC=3.8.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01231, ECO:0000269|PubMed:10100638, ECO:0000269|PubMed:9293022... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for 1,2-dibromoethane {ECO:0000269|PubMed:9293022}; KM=3.9 mM for 1-chloro-2-bromoethane {ECO:0000269|PubMed:9293022}; KM=0.9 mM for 1,2-dibromopropane {ECO:0000269|PubMed:9293022}; KM=0.05 mM for 1-bromo-2-methylpropane {ECO:0000269|PubMed:9293022}; KM=0.7 ... | PATHWAY: Xenobiotic degradation; gamma-hexachlorocyclohexane degradation. {ECO:0000305|PubMed:7691794}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2. {ECO:0000269|PubMed:9293022}; | null | FUNCTION: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and c... | Sphingobium indicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S) (Sphingobium japonicum) |
D5ARP7 | CCOP_RHOCB | MSKKPTTKKEVQTTGHSWDGIEELNTPLPRWWLWTFYATIVWGVAYSIAMPAWPIFASGATPGILGSSTRADVEKDIAKFAEMNKAVEDKLVATDLTAIAADPELVTYTRNAGAAVFRTWCAQCHGAGAGGNTGFPSLLDGDWLHGGSIETIYTNIKHGIRDPLDPDTLPVANMPAHLTDELLEPAQIDDVVQYVLKISGQPADEARATAGQQVFADNCVSCHGEDAKGMVEMGAPNLTDGIWLYGGDANTITTTIQLGRGGVMPSWSWAADGAKPRLSEAQIRAVASYVHSLGGGQ | null | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:8130227}; Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:8130227}; | oxidative phosphorylation [GO:0006119]; proton transmembrane transport [GO:1902600] | plasma membrane [GO:0005886]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF00034;PF13442;PF14715; | 6.10.280.130;1.10.760.10; | CcoP / FixP family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000305|PubMed:17143652, ECO:0000305|PubMed:18556791, ECO:0000305|PubMed:20952576, ECO:0000305|PubMed:8130227, ECO:0000305|PubMed:9473054}. | null | null | FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. CcoP subunit is required for transferring electrons from donor cytochrome c via its heme groups to CcoO subunit. From there, electrons are shuttled to the catalytic binuclear center of CcoN subunit where oxygen reduction takes place. The c... | Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) |
D5AUZ9 | CBIM_RHOCB | MHIMEGYLPVTHAIGWSLAAGPFVVAGAVKIRKIVAERPEARMTLAASGAFAFVLSALKIPSVTGSCSHPTGTGLGAVVFGPSVMAVLGVIVLLFQALLLAHGGLTTLGANAFSMAIVGPWVAWGVYKLAGKAGASMAVAVFLAAFLGDLATYVTTSLQLALAYPDPVSGFLGAALKFGSVFALTQIPLAIAEGFLTVIVVDALAGKVDDKDKLRILAGEAR | null | null | cobalamin biosynthetic process [GO:0009236]; cobalt ion transport [GO:0006824] | ATP-binding cassette (ABC) transporter complex [GO:0043190] | cobalt ion transmembrane transporter activity [GO:0015087] | PF01891; | 1.10.1760.20; | CbiM family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:20868747}; Multi-pass membrane protein {ECO:0000305|PubMed:20868747}. | null | null | PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. | null | null | FUNCTION: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity. A Cbi(MN) fusion protein has about 70% import capacity, but the holo-Cbi(MN)QO complex cannot be isol... | Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) |
D5CBA0 | CDIA_ENTCC | MMKQDQVRFSQRALSALLSVLLATQPLLPAVAASITPSGNTQMDKAANGVPVVNIATPNQSGISHNKYNDYNVGKEGLILNNATGQLNQTQLGGLIQNNPNLKAGQEAKGIINEVTGANRSNLQGYTEVAGKAANVIVANPYGITCNGCGFINTPNVTLTTGKPVLDASGKLQSLDVTQGAVTIEGAGLNGSQSDAVSIISRATEINVQLHAKDLRVVAGANRVAADGSVSALKGEGTAPKVAVDTGALGGMYANRIRLVSSETGVGVNLGNLNARQGDIALSSAGKVVLKNTLASGSTTVSAADVTLRGDHKAGGNVTV... | 3.1.-.- | null | null | host cell cytoplasm [GO:0030430] | RNA endonuclease activity [GO:0004521]; toxin activity [GO:0090729] | PF13332;PF15526;PF04829;PF05860; | 3.10.380.20;2.160.20.10; | CdiA toxin family | null | SUBCELLULAR LOCATION: Target cell, target cell cytoplasm {ECO:0000269|PubMed:24657090, ECO:0000269|PubMed:24889811, ECO:0000269|PubMed:25174572}. Note=Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner (Probable). Toxin translocation into the target cell depends on the proton motive f... | null | null | null | null | null | FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion; upon forced induction decreases E.cl... | Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56) |
D5EY13 | XYFA_XYLR2 | MKKLLVALSLIAGSLTASAQWGRPVDYAAGPGLKDAYKDYFTVGVAVNKFNISDPAQTAIVKKQFNSVTAENAWKPGEIHPKEGVWNFGLADSIANFCRENGIKMRGHCLCWHSQFADWMFTDKKGKPVKKEVFYQRLREHIHTVVNRYKDVVYAWDVVNEAMADDGRPFEFVDGKMVPASPYRQSRHFKLCGDEFIAKAFEFAREADPTGVLMYNDYSCVDEGKRERIYNMVKKMKEAGVPIDGIGMQGHYNIYFPDEEKLEKAINRFSEIVNTIHITELDLRTNTESGGQLMFSRGEAKPQPGYMQTLQEDQYARLFK... | 3.1.1.73; 3.2.1.8 | null | xylan catabolic process [GO:0045493] | null | endo-1,4-beta-xylanase activity [GO:0031176]; feruloyl esterase activity [GO:0030600] | PF00756;PF00331; | 3.40.50.1820;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 10 (cellulase F) family | null | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}; CATALYTIC ACTIVITY: Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000269|PubMed:19304844, ECO:00... | null | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for xylanase activity. {ECO:0000269|PubMed:19304844}; | null | FUNCTION: Involved in degradation of plant cell wall polysaccharides. Has endo-xylanase activity towards substrates such as oat spelt xylan (OSX), acetylated xylo-oligosaccharides and acetylated xylan, producing primarily xylobiose; cannot hydrolyze xylobiose to xylose. Also has feruloyl esterase activity, releasing fe... | Xylanibacter ruminicola (strain ATCC 19189 / DSM 19721 / CIP 105475 / JCM 8958 / 23) (Prevotella ruminicola) |
D5EY15 | XYL3A_XYLR2 | MKYQLFLSLALCVGLGASAQTLPYQNPNLSAKERAVDLCSRLTLEEKAMLMLDESPAIPRLGIKKFFWWSEALHGAANMGNVTNFPEPVGMAASFNPHLLFKVFDIASTEFRAQYNHRMYDLNGEDMKMRSLSVWTPNVNIFRDPRWGRGQETYGEDPYLTSVMGVQVVKGLQGPEDARYRKLWACAKHYAVHSGPEYTRHTANLTDVSARDFWETYMPAFKTLVKDAKVREVMCAYQRLDDDPCCGSTRLLQQILRDEWGFEYLVVSDCGAVSDFYENHKSSSDAVHGTSKAVLAGTDVECGFNYAYKSLPEAVRKGLL... | 3.2.1.37; 3.2.1.55 | null | arabinan catabolic process [GO:0031222]; xylan catabolic process [GO:0045493] | null | alpha-L-arabinofuranosidase activity [GO:0046556]; xylan 1,4-beta-xylosidase activity [GO:0009044] | PF14310;PF00933;PF01915;PF07691; | 3.40.50.1700;3.20.20.300;2.60.40.10; | Glycosyl hydrolase 3 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.; EC=3.2.1.37; Evidence={ECO:0000269|PubMed:19304844}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.; EC=3.... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 mM for pNP-beta-D-xylopyranoside (pNPX) (at 37 degrees Celsius and pH 5.0) {ECO:0000269|PubMed:19304844}; Note=kcat is 9.7 sec(-1) for the beta-xylosidase activity with pNPX as substrate (at 37 degrees Celsius and pH 5.0).; | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:19304844}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:19304844}; | null | FUNCTION: Involved in degradation of plant cell wall polysaccharides. Has beta-xylosidase activity via its capacity to hydrolyze glycosidic linkages of beta-1,4-xylo-oligosaccharides of various lengths (X2 to X6), releasing xylose monomers. To a much lesser extent, also has alpha-L-arabinofuranosidase activity. Does no... | Xylanibacter ruminicola (strain ATCC 19189 / DSM 19721 / CIP 105475 / JCM 8958 / 23) (Prevotella ruminicola) |
D5JWB3 | SARED_ESCCA | MADSSKKLTVLLSGASGLTGSLAFKKLKERSDKFEVRGLVRSEASKQKLGGGDEIFIGDISDPKTLEPAMEGIDALIILTSAIPRMKPTEEFTAEMISGGRSEDVIDASFSGPMPEFYYDEGQYPEQVDWIGQKNQIDTAKKMGVKHIVLVGSMGGCDPDHFLNHMGNGNILIWKRKAEQYLADSGVPYTIIRAGGLDNKAGGVRELLVAKDDVLLPTENGFIARADVAEACVQALEIEEVKNKAFDLGSKPEGVGEATKDFKALFSQVTTPF | 1.3.1.107 | null | response to toxic substance [GO:0009636] | chloroplast [GO:0009507] | oxidoreductase activity [GO:0016491] | PF13460; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=dihydrosanguinarine + NADP(+) = NADPH + sanguinarine; Xref=Rhea:RHEA:41656, ChEBI:CHEBI:17183, ChEBI:CHEBI:17209, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.107; Evidence={ECO:0000269|PubMed:17080644, ECO:0000269|PubMed:20378534}; CATALYTIC ACTIVITY: Reaction=dihydrosanguinarine + NAD(+... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.5 uM for sanguinarine (in the presence of 40 uM NADH) {ECO:0000269|PubMed:17080644}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:17080644}; | null | FUNCTION: Catalyzes the reduction of benzophenanthridines, preferentially sanguinarine, to the corresponding dihydroalkaloids. Involved in detoxifying the phytoalexins produced by plant itself. The sanguinarine produced by intact cells upon elicitation, after excretion and binding to cell wall elements, is rapidly reab... | Eschscholzia californica (California poppy) |
D5KXD2 | TPS12_SOLLC | MASSSANKCRPLANFHPTVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVEAPEGSEQKLVLIDAMQRLGVAYHFDNEIETSIQNIFDASSKQNDNDNNLYVVSLRFRLVRQQGHYMSSDVFKQFINQDGKFKETLTNDVQGLLSLYEASHLRVRDEEILEEALTFTTTHLESTVSNLSNNNSLKAEVTEAFSQPIRMTLPRVGARKYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVIQMASFFDDTFDAYATFDELEPFNNAIQR... | 4.2.3.-; 4.2.3.104; 4.2.3.106; 4.2.3.113; 4.2.3.15; 4.2.3.57 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.104; Evidence={ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; X... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:20431087, PubMed:21813655, PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E,8E)-alpha-humulene and (-)-(E)-beta-caryophyllene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into beta-b... | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
D5LGE0 | AIP_HYAAS | MNYLCLVVTLVAVAGAISGEKFSDDNTGYQSTPSLRIRTTPGRRRQTPRTIGPPYTRRTLRTTTDYSTTVENGNLTTPAANSTEKGNGLYGLRRQTPRTIGPPYTRRTLRTTTGYWTTVEKGNGTTPAANSTEKGNRPYGRRRQTPRTIGPPYTRRTTTDYWAAVEKGYLTTPAANSTEKESRPNATQRREISWTFGPLYTWRTTKGYGTTLETTNATSTS | null | null | null | extracellular region [GO:0005576] | null | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20178988}. | null | null | null | null | null | FUNCTION: [Hyalomin-A1]: Suppress host inflammatory response. Exerts significant anti-inflammatory functions, either by directly inhibiting host secretion of inflammatory factors such as tumor necrosis factor-alpha (TNF), monocyte chemotactic protein-1 (CCL2), and interferon-gamma (IFNG) or by indirectly increasing the... | Hyalomma asiaticum asiaticum (Tick) |
D5MP61 | 3XYN1_VIBSX | MKRTYLSLIAAGVMSLSVSAWSLDGVLVPESGILVSVGQDVDSVNDYASALGTIPAGVTNYVGIVNLDGLNSDADAGAGRNNIAELANAYPTSALVVGVSMNGEVDAVASGRYNANIDTLLNTLAGYDRPVYLRWAYEVDGPWNGHSPSGIVTSFQYVHDRIIALGHQAKISLVWQVASYCPTPGGQLDQWWPGSEYVDWVGLSYFAPQDCNWDRVNEAAQFARSKGKPLFLNESTPQRYQVADLTYSADPAKGTNRQSKTSQQLWDEWFAPYFQFMSDNSDIVKGFTYINADWDSQWRWAAPYNEGYWGDSRVQANALI... | 3.2.1.32 | null | cellulose catabolic process [GO:0030245]; xylan catabolic process [GO:0045493] | null | polysaccharide binding [GO:0030247]; xylan endo-1,3-beta-xylosidase activity [GO:0033905] | PF11606; | 2.60.40.2450;3.20.20.80; | Glycosyl hydrolase 26 family | null | null | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.; EC=3.2.1.32; Evidence={ECO:0000269|PubMed:15743273}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.4 mM for beta-1,3-xylotetraose {ECO:0000269|PubMed:15743273}; KM=7.5 mM for beta-1,3-xylopentaose {ECO:0000269|PubMed:15743273}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:15743273}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Inactive above 60 degrees Celsius. {ECO:0000269|PubMed:15743273}; | FUNCTION: Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylobiose, xylotriose and xylotetraose. Converts beta-1,3-xylotriose into xylose and xylobiose, converts beta-1,3-xylotetraose mainly into xylotriose and xylose, converts beta-1,3-xylopentaose into xylobiose and xylotriose. Does not hydr... | Vibrio sp |
D5MTF8 | HGL1D_WHEAT | MALLAAATLNPTTHLSLRSRAGRNSENLWLRSAASSQKSKGRFCNLTVRAGTPSKPAEPIGPVFTKLKPWQIPKRDWFDKDFLFGASTSAYQIEGAWNEDGKGPSTWDHFCHKYPERISDGTNGDVAADSYHLYEEDVKALKDMGMKVYRFSISWSRILPNGTGEVNQAGIDYYNKLINSLISHDIVPYVTIWHWDTPQALEDKYGGFLDPQIVDDYKQFAKLCFESFGDRVKNWFTFNEPHTYCCFSYGEGIHAPGRCSPGMDCAVPEGDSLREPYTAGHHILLAHAEAVEMFRTHYNMHGDSKIGMAFDVMGYEPYQD... | 3.2.1.182; 3.2.1.21 | null | carbohydrate metabolic process [GO:0005975] | chloroplast [GO:0009507] | beta-glucosidase activity [GO:0008422]; DIMBOA glucoside beta-D-glucosidase activity [GO:0102726]; scopolin beta-glucosidase activity [GO:0102483] | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; CATALYTIC ACTIVITY: Reaction=DIMBOA beta-D-glucoside + H2O = D-glucose + DIMBOA; Xref=Rhea:RHEA:33975, ChEBI:CHEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.34 mM for DIBOA-beta-D-glucoside (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=1.83 mM for DIBOA-beta-D-glucoside (with recombinant enzyme) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=0.272 mM for DIMBOA-b... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; | null | FUNCTION: Acts in defense of young plant parts against pests via the production of hydroxamic acids from hydroxamic acid glucosides. Enzymatic activity is highly correlated with plant growth. The preferred substrate is DIMBOA-beta-D-glucoside. {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}. | Triticum aestivum (Wheat) |
D5TM67 | CDAS_BACT1 | MHEWGLSEELKIQTKQMIEIAEKELSIMRNAIDKEDECILCKMEDIHHMLANVQTLAATYYIQAYLSPYTESSSFITTAIQHLSARKHGALIVVERNETLEALIQTGTTLNAHLTAPLLESIFYPGNPLHDGAVLVKNNHIVSAANILPLTKSTEVDPELGTRHRAAIGLSEKSDALILVVSEETGRTSFALNGILYTISL | 2.7.7.85 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26441857}; | cAMP biosynthetic process [GO:0006171]; sporulation resulting in formation of a cellular spore [GO:0030435] | null | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; diadenylate cyclase activity [GO:0106408] | PF10372;PF02457; | 3.40.1700.10;1.10.287.770; | Adenylate cyclase family, DacB/CdaS subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85; Evidence={ECO:0000255|HAMAP-Rule:MF_00838, ECO:0000269|PubMed:26441857}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:26441857}; | null | FUNCTION: One of 3 paralogous diadenylate cyclases (DAC) in this bacteria catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). It has slow DAC activity with ADP as a substrate and may have weak ADPase activity (PubMed:26441857). Required for efficient spore formation, whereas in B.subtilis, it ... | Bacillus thuringiensis (strain BMB171) |
D5VRB9 | ELP3_METIM | MKEKLMRCIIERILKEYKEGKTLDKKRIEQIKSECLRIYRIGIGHPSNSEILKYATEEEKKILIPILRKKPVRTISGVAVVAVMTSPAKCPHGKCIFCPGGLDSVFGDVPQSYTGREPATMRGLMFNFDPYLQTRARIEQLEKVGHPTDKIELIIMGGTFPAREIEYQDWFIKRCLDAMNERESKSLEEAQKINETAKHRCVALCIETRPDYCSEKEINQMLKLGATRVELGVQSIYNEILKLCKRGHSVEDTIKATQLLKDSGLKVSYHLMPGMPGSSIEMDKKMFKEIFTNPDFMPDMVKIYPCLVIEGTELYEMWKR... | 2.3.1.311 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q02908}; | tRNA acetylation [GO:0051391]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble uridine modification [GO:0002098] | cytoplasm [GO:0005737]; elongator holoenzyme complex [GO:0033588] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; S-adenosyl-L-methionine binding [GO:1904047]; tRNA binding [GO:0000049]; tRNA uridine(34) acetyltransferase activity [GO:0106261] | PF00583;PF04055;PF16199; | 3.40.630.30;3.20.20.70; | ELP3 family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:5... | null | PATHWAY: tRNA modification. {ECO:0000269|PubMed:25151136, ECO:0000269|PubMed:30733442}. | null | null | FUNCTION: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:25151136, PubMed:30733442). The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in th... | Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME) |
D6MZJ6 | NSMA5_MOUSE | MSLPDISRRRSPVPQEDWPLTPNALRPSPFPNPVLQALYSLSRVLLFPTYWSLDQLLGCWAPSVRSKSLGWFKVLAGSGVLLPLVVVGLPLALVGLALWLPLQVWRRPFCYQPPPACWVWPQPWHPPAERRRCFVFLTANLCLLPHGLAHFNNLSHSLQRAEAVGAALLDSLQSSQYRVSECSQPPPRVPGGELKATLPMGLDFVCLQEVFDLRAARRLVRVLVPNLGPVIYDVGTFGLMAGPYIKVLGSGLLLASRYPLLRATFRCFPNARREDAMASKGLLSVQAQLGIVDGHPIVGYLHCTHLHAPVEDGHIRCKQL... | 3.1.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20378533}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20378533}; | ceramide biosynthetic process [GO:0046513]; ceramide metabolic process [GO:0006672]; sphingomyelin catabolic process [GO:0006685]; sphingomyelin metabolic process [GO:0006684] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | metal ion binding [GO:0046872]; sphingomyelin phosphodiesterase activity [GO:0004767] | null | 3.60.10.10; | Neutral sphingomyelinase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:20378533}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:F1QG30}; Intermembrane side {ECO:0000250|UniProtKB:F1QG30}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20378533}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000269|PubMed:20378533}; PhysiologicalDirection=left-to-right; Xref=Rhea... | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:20378533}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:20378533}; | null | FUNCTION: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. {ECO:0000250|UniProtKB:F1QG30}. | Mus musculus (Mouse) |
D6PXE8 | VM3B_NAJAT | MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQLTNTPEQDRYLQDKKYIEFYVIVDNRMYRYYNNDKPAIKIRVYEMINAVNTKFRPLKIHIALIGLEIWSNKDKFEVKPAASVTLKSFGEWRETVLLPRKRNDNAQLLTGIDFNGNTVGRAYIGSLCKTNE... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF01562;PF01421; | 3.40.1620.60;3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc protease that inhibits the classical and alternative pathways of complement by cleaving factor B, C6, C7, and C8. Also slowly and selectively degrades alpha-chain of fibrinogen (FGA), and shows edema-inducing activity. {ECO:0000269|PubMed:20837040}. | Naja atra (Chinese cobra) |
D6R8X8 | HYUP_MICLQ | MNSTPIEEARSLLNPSNAPTRYAERSVGPFSLAAIWFAMAIQVAIFIAAGQMTSSFQVWQVIVAIAAGCTIAVILLFFTQSAAIRWGINFTVAARMPFGIRGSLIPITLKALLSLFWFGFQTWLGALALDEITRLLTGFTNLPLWIVIFGAIQVVTTFYGITFIRWMNVFASPVLLAMGVYMVYLMLDGADVSLGEVMSMGGENPGMPFSTAIMIFVGGWIAVVVSIHDIVKECKVDPNASREGQTKADARYATAQWLGMVPASIIFGFIGAASMVLVGEWNPVIAITEVVGGVSIPMAILFQVFVLLATWSTNPAANLL... | null | null | null | plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; nucleobase transmembrane transporter activity [GO:0015205] | PF02133; | 1.10.4160.10; | Purine-cytosine permease (2.A.39) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16621827}; Multi-pass membrane protein {ECO:0000305|PubMed:18927357, ECO:0000305|PubMed:20413494}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.6. {ECO:0000269|PubMed:16621827}; | null | FUNCTION: Nucleobase-proton symporter that mediates the sodium-dependent binding and uptake of 5-aryl-substituted hydantoin compounds (PubMed:16621827, PubMed:24952894). 5-indolyl methyl hydantoin and 5-benzyl hydantoin are the preferred substrates, with selectivity for a hydrophobic substituent in position 5 of hydant... | Microbacterium liquefaciens (Aureobacterium liquefaciens) |
D6RGH6 | MCIN_HUMAN | MQACGGGAAGRRAFDSICPNRMLALPGRALLCKPGKPERKFAPPRKFFPGCTGGSPVSVYEDPPDAEPTALPALTTIDLQDLADCSSLLGSDAPPGGDLAASQNHSHQTEADFNLQDFRDTVDDLISDSSSMMSPTLASGDFPFSPCDISPFGPCLSPPLDPRALQSPPLRPPDVPPPEQYWKEVADQNQRALGDALVENNQLHVTLTQKQEEIASLKERNVQLKELASRTRHLASVLDKLMITQSRDCGAAAEPFLLKAKAKRSLEELVSAAGQDCAEVDAILREISERCDEALQSRDPKRPRLLPEPANTDTRPGNLH... | null | null | cell cycle [GO:0007049]; centriole assembly [GO:0098534]; cilium assembly [GO:0060271]; motile cilium assembly [GO:0044458]; multi-ciliated epithelial cell differentiation [GO:1903251]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA replication [GO:0008156]; positive regulation of transcript... | nuclear body [GO:0016604]; nucleus [GO:0005634] | identical protein binding [GO:0042802] | PF07412; | 1.20.5.1180; | Geminin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21543332, ECO:0000269|PubMed:25048963}. Note=Excluded from the nucleolus. {ECO:0000269|PubMed:21543332}. | null | null | null | null | null | FUNCTION: Transcription regulator specifically required for multiciliate cell differentiation (PubMed:25048963). Acts in a multiprotein complex containing E2F4 and E2F5 that binds and activates genes required for centriole biogenesis. Required for the deuterosome-mediated acentriolar pathway (PubMed:25048963). Plays a ... | Homo sapiens (Human) |
D6VTK4 | STE2_YEAST | MSDAAPSLSNLFYDPTYNPGQSTINYTSIYGNGSTITFDELQGLVNSTVTQAIMFGVRCGAAALTLIVMWMTSRSRKTPIFIINQVSLFLIILHSALYFKYLLSNYSSVTYALTGFPQFISRGDVHVYGATNIIQVLLVASIETSLVFQIKVIFTGDNFKRIGLMLTSISFTLGIATVTMYFVSAVKGMIVTYNDVSATQDKYFNASTILLASSINFMSFVLVVKLILAIRSRRFLGLKQFDSFHILLIMSCQSLLVPSIIFILAYSLKPNQGTDVLTTVATLLAVLSLPLSSMWATAANNASKTNTITSDFTTSTDRFY... | null | null | cytogamy [GO:0000755]; pheromone-dependent signal transduction involved in conjugation with cellular fusion [GO:0000750] | G protein-coupled receptor homodimeric complex [GO:0038038]; plasma membrane [GO:0005886] | mating-type alpha-factor pheromone receptor activity [GO:0004934]; mating-type factor pheromone receptor activity [GO:0004932]; pheromone binding [GO:0005550] | PF02116; | 1.10.287.920; | G-protein coupled receptor 4 family | PTM: Undergoes hyperphosphorylation of the C-terminal cytoplasmic domain after binding of the alpha-factor, which leads to internalization by endocytosis. {ECO:0000269|PubMed:1330324, ECO:0000269|PubMed:8524302}.; PTM: Monoubiquitination at Lys-337 triggers internalization of STE2. {ECO:0000269|PubMed:9659916}.; PTM: N... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1330324, ECO:0000269|PubMed:14506226, ECO:0000269|PubMed:16313173, ECO:0000269|PubMed:2017168, ECO:0000269|PubMed:28073700, ECO:0000269|PubMed:2839507, ECO:0000269|PubMed:34627767, ECO:0000269|PubMed:35296853, ECO:0000269|PubMed:7935439}; Multi-pass membrane prote... | null | null | null | null | null | FUNCTION: Fungal class D1 G-protein-coupled receptor that acts as an alpha-factor pheromone receptor performing pheromone-dependent signal transduction involved in cellular conjugation, mating projection assembly, and in cell fusion (PubMed:10744981, PubMed:11495900, PubMed:12427030, PubMed:2556384, PubMed:2839507, Pub... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
D6WMX4 | PINK1_TRICA | MSVRAVGSRLFKHGRSLIQQFCKRDLNTTIGDKINAVSQATAAPSSLPKTQIPKNFALRNVGVQLGLQARRILIDNVLNRVTNSLSAELRKKATRRILFGDSAPFFALVGVSIASGTGILTKEEELEGVCWEIREAISKIKWQYYDIDESRFESNPITLNDLSLGKPIAKGTNGVVYSAKVKDDETDDNKYPFALKMMFNYDIQSNSMEILKAMYRETVPARMYYSNHDLNNWEIELANRRKHLPPHPNIVAIFSVFTDLIQELEGSKDLYPAALPPRLHPEGEGRNMSLFLLMKRYDCNLQSFLSTAPSTRTSLLLLAQ... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:26116755, ECO:0000269|PubMed:29991771}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:29991771}; | autophagy [GO:0006914]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of free ubiquitin chain polymerization [GO:1904544]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of protein ubiquitination [GO:0031398]; protein autophosphorylation [GO:0046777]; regulation of ap... | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674]; ubiquitin protein ligase binding [GO:0031625] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Proteolytically cleaved. In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (TcasGA2_TC013516). The short form is then released into the cytosol where it rapidly undergoes proteasome-depende... | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q0KHV6}. Note=Localizes mostly in mitochondrio... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22645651, ECO:000026... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=287.5 uM for Drp1 (at 30 degrees Celsius) {ECO:0000269|PubMed:32484300}; KM=84.4 uM for ubiquitin (at 30 degrees Celsius) {ECO:0000269|PubMed:32484300}; KM=391 uM for ubiquitin (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:29475881}; KM=36 uM for ubiquitin... | null | null | null | FUNCTION: Acts as a serine/threonine-protein kinase (PubMed:24751536, PubMed:25474007, PubMed:26116755, PubMed:26784449, PubMed:28980524, PubMed:29475881, PubMed:29991771, PubMed:32484300). Exhibits a substrate preference for proline at position P+1 and a general preference at several residues for basic residues such a... | Tribolium castaneum (Red flour beetle) |
D6XZ22 | GGP_BACIE | MHEIGEHLTTNTGWDIIKNRYEAAQAITEGSNFMIGNGFMGYRGTFAEDGKDAYAACIVTDTWDKADGKWEELSTVPNALLTLLHVDGEPFIMSEEAASFERTLDLSQGVTSRKVSQRMKNGATITIHEEKFASYRKKHAVLMKYTVESDQDTDAVLDTGIDYDVWSINGDHLQGHHYFSHPTGDGVTAKTVSYEDTVTVVETCSLDADASEEDYQNPDGSGRTFSLSLEAGKPVTLEKAMIIYSSNDVDNPQDEALLEAKHMQSYEEEKAANRLEWDNLWSHYDVTIQNNIIDQVALRFNIYHAIIATPVHKSLPIGAR... | 2.4.1.332 | null | trehalose catabolic process [GO:0005993] | cytosol [GO:0005829] | alpha,alpha-trehalase activity [GO:0004555]; carbohydrate binding [GO:0030246]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; protein-glucosylgalactosylhydroxylysine glucosidase activity [GO:0047402] | PF03633;PF03632;PF03636; | 1.50.10.10;2.70.98.40;2.60.420.10; | Glycosyl hydrolase 65 family | null | null | CATALYTIC ACTIVITY: Reaction=2-O-(alpha-D-glucopyranosyl)glycerol + phosphate = beta-D-glucose 1-phosphate + glycerol; Xref=Rhea:RHEA:43060, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57684, ChEBI:CHEBI:82766; EC=2.4.1.332; Evidence={ECO:0000269|PubMed:24466148, ECO:0000269|PubMed:24828502}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 mM for 2-O-alpha-D-glucopyranosyl-sn-glycerol {ECO:0000269|PubMed:24466148}; KM=0.57 mM for phosphate {ECO:0000269|PubMed:24466148}; Note=kcat is 95 sec(-1) with 2-O-alpha-D-glucopyranosyl-sn-glycerol. {ECO:0000269|PubMed:24466148}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:24466148}; | null | FUNCTION: Catalyzes both the (1) reversible phosphorolysis of 2-O-alpha-D-glucopyranosyl-sn-glycerol (GG) from beta-D-glucose 1-phosphate (betaGlc1P) and glycerol and (2) the hydrolysis of betaGlc1P. the betaGlc1P hydrolysis is a glucosyl-transfer reaction to an acceptor water molecule that produces an anomer-inverted ... | Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10) |
D7A5Q8 | YDDG_ANCN5 | MSRSSATLIGFTAILLWSTLALATSSTGAVPPFLLTALTFTIGGAVGIAAGLARGVGLSVLRQPWPVWVHGIGGLFGYHFFYFSALKLAPPAEAGLVAYLWPLLIVLFSAFLPGERLRPAHVAGALMGLAGTVVLLGARAGGFGFAPEYVPGYLAAAACAVIWSVYSVASRRFARVPTEVVAGFCLATAALSALCHILFEPSVWPVGSEWLAVVALGIGPVGIAFYTWDIGMKRGDVRLLGVLSYAAPVLSTLLLVVAGFAAPSGALAIACALIVGGAAVATLLARR | null | null | amino acid transport [GO:0006865] | plasma membrane [GO:0005886] | null | PF00892; | null | Drug/metabolite transporter (DMT) superfamily, Aromatic amino acid/paraquat exporter (ArAA/P-E) (TC 2.A.7.17) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:27281193}; Multi-pass membrane protein {ECO:0000269|PubMed:27281193}. | CATALYTIC ACTIVITY: Reaction=L-threonine(in) = L-threonine(out); Xref=Rhea:RHEA:35019, ChEBI:CHEBI:57926; Evidence={ECO:0000305|PubMed:27281193}; CATALYTIC ACTIVITY: Reaction=L-methionine(in) = L-methionine(out); Xref=Rhea:RHEA:70939, ChEBI:CHEBI:57844; Evidence={ECO:0000305|PubMed:27281193}; CATALYTIC ACTIVITY: Reacti... | null | null | null | null | FUNCTION: Amino acid transporter with broad substrate specificity (PubMed:27281193). Can transport various amino acids, including L-threonine, L-methionine, L-lysine and L-glutamate (PubMed:27281193). {ECO:0000269|PubMed:27281193}. | Ancylobacter novellus (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIMB 10456) (Starkeya novella) |
D7A6E5 | SOXA_ANCN5 | MRRFAAGCLALALLVLPFVLTGARAAEDESEKEIERYRQMIEDPMANPGFLNVDRGEVLWSEPRGTRNVSLETCDLGEGPGKLEGAYAHLPRYFADTGKVMDLEQRLLWCMETIQGRDTKPLVAKPFSGPGRTSDMEDLVAFIANKSDGVKIKVALATPQEKEMYAIGEALFFRRSSINDFSCSTCHGAAGKRIRLQALPQLDVPGKDAQLTMATWPTYRVSQSALRTMQHRMWDCYRQMRMPAPDYASEAVTALTLYLTKQAEGGELKVPSIKR | 2.8.5.2 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405, ECO:0000... | sulfur oxidation [GO:0019417] | cytochrome complex [GO:0070069]; periplasmic space [GO:0042597] | copper ion binding [GO:0005507]; electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor [GO:0016669]; protein heterodimerization activity [GO:0046982]; su... | PF21342; | 1.10.760.10; | SoxA family | PTM: Cysteine persulfide at Cys-236. {ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:21592966}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691, ChEBI:CHEBI:15378, ChEBI:CHEBI:2... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.49 mM for glutathione (at pH 6.0) {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; KM=0.19 mM for glutathione (at pH 7.0) {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; Vmax=0.124 u... | null | null | null | FUNCTION: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates... | Ancylobacter novellus (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIMB 10456) (Starkeya novella) |
D7EZN2 | LIPR2_PIG | MLPSWTIGLLLLATVRGKEICYQPFGCFSDETPWARTCHWPFKLFPWAPKDIDTHFLLYTNENPNNFQLINITNLDTIEASNFQLDRKTRFIIHGFIDKGEDSWPSEMCKKMFKVEKVNCICVDWRRGALTRYTQAVHNTRVVGAEIAFLIQGLSTKFDYNPENVHLIGHSLGAHTAAEAGRRLGGHVGRLTGLDPAQPCFQNTPEEVRLDPSDAMFVDVIHTDSAPFIPFLGFGMSQKVGHLDFYPNGGKEMPGCQKNTLSTIVDVDGIWEGIEDFAACNHLRSYKYYSSSIFSPDGFLGYPCASYDEFQEEENKCFPC... | 3.1.1.26; 3.1.1.3 | null | phospholipid catabolic process [GO:0009395]; phospholipid metabolic process [GO:0006644]; triglyceride catabolic process [GO:0019433] | extracellular space [GO:0005615]; neuron projection [GO:0043005]; zymogen granule membrane [GO:0042589] | 1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity [GO:0102549]; galactolipase activity [GO:0047714]; metal ion binding [GO:0046872]; phospholipase activity [GO:0004620]; 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:P54317}. Zymogen granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000250|UniProtKB:... | 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:0000269|PubMed:23770034}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:120... | null | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000269|PubMed:23770034}.; PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:23770034}. | null | null | FUNCTION: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:23770034). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (PubMed:23770034). Hydrolyzes short-, medium- and long-chain fatty acyls in trigl... | Sus scrofa (Pig) |
D7PC76 | S26A5_TURTR | MDHVEETEILAATQRYYVERPIFSHPVLQERLHKKDKISESIGDKLKQAFTCTPKKIRNIIYMFLPITKWLPAYRFKEYVLGDIVSGISTGVLQLPQGLAFAMLAAVPPVFGLYSSFYPVIMYCFFGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNSTEARDALRVKVAMSVTLLTGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFSLHESYNVDVVGT... | null | null | cochlear outer hair cell electromotile response [GO:0099129]; regulation of cell shape [GO:0008360]; sensory perception of sound [GO:0007605] | plasma membrane [GO:0005886] | bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; oxalate transmembrane transporter activity [GO:0019531]; secondary active sulfate transmembrane transporter activity [GO:0008271] | PF01740;PF00916; | 3.30.750.24; | SLC26A/SulP transporter (TC 2.A.53) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34695838}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=chloride(out) + 2 hydrogencarbonate(in) = chloride(in) + 2 hydrogencarbonate(out); Xref=Rhea:RHEA:72207, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q9EPH0}; | null | null | null | null | FUNCTION: Voltage-sensitive motor protein that drives outer hair cell (OHC) electromotility (eM) and participates in sound amplification in the hearing organ (PubMed:34695838). Converts changes in the transmembrane electric potential into mechanical displacements resulting in the coupling of its expansion to movement o... | Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) |
D7PDD4 | G6B_MOUSE | MALVLPLLPLLLSKVQGNPEVSLEGSPGDRVNLSCIGVSDPTRWAWAPSFPACKGLSKGRRPILWASTRGTPTVLQHFSGRLRSLDNGIKRLELLLSAGDSGTFFCKGRHENESRTVLQVLGDKAGCRPAGSTHGYEYPKVLIPLLGVGLVLGLGVAGVVWRRRRLSPPPPPPPPPGPLPTFAPVINAEPQRPLEQESKISGHLDQEPSLHYADLDHSVLGRHRRMSTVVSGDASTVYAVVV | null | null | blood coagulation [GO:0007596]; erythrocyte differentiation [GO:0030218]; integrin-mediated signaling pathway [GO:0007229]; megakaryocyte development [GO:0035855]; megakaryocyte differentiation [GO:0030219]; negative regulation of signal transduction [GO:0009968]; platelet formation [GO:0030220] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | null | PF15096; | null | null | PTM: N-glycosylated. {ECO:0000269|PubMed:23112346}.; PTM: May be O-glycosylated. {ECO:0000250|UniProtKB:O95866}.; PTM: Phosphorylated. {ECO:0000269|PubMed:23112346}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23112346}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O95866, ECO:0000255}. | null | null | null | null | null | FUNCTION: Inhibitory receptor that acts as a critical regulator of hematopoietic lineage differentiation, megakaryocyte function and platelet production (PubMed:23112346). Inhibits platelet aggregation and activation by agonists such as ADP and collagen-related peptide (By similarity). This regulation of megakaryocate ... | Mus musculus (Mouse) |
D7PF45 | SHIP2_PIG | MASACGAPGPGAGPGAALGSPAPAWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCVLYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVERERELDPPDERDASDGEDEKPPLPPRSGTSVSAPLGPSSPPAAPEPPTPAVESAPNGLSTVSHEYLKGSYGLDLEAVRGGASNLPHLTRTLAASCRRLHSEVDKVLSGLEILSKVFDQQSSPMVTRLLQQQNPPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPVQPSTRKAKTIPVQAFEVKLD... | 3.1.3.86 | null | establishment of mitotic spindle orientation [GO:0000132]; immune system process [GO:0002376]; negative regulation of insulin-like growth factor receptor signaling pathway [GO:0043569]; phosphatidylinositol dephosphorylation [GO:0046856]; regulation of actin filament organization [GO:0110053]; regulation of immune resp... | basal plasma membrane [GO:0009925]; cytosol [GO:0005829]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle pole [GO:0000922] | inositol-polyphosphate 5-phosphatase activity [GO:0004445]; phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:0034485]; SH3 domain binding [GO:0017124] | PF00536;PF00017; | 3.60.10.10;3.30.505.10;1.10.150.50; | Inositol 1,4,5-trisphosphate 5-phosphatase family | PTM: Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as insulin, growth factors such as EGF or PDGF, chemokines, integrin ligands and hypertonic and oxidative stress. May be phosphorylated upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-98... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15357}. Cytoplasm, cytoskeleton. Membrane {ECO:0000250|UniProtKB:O15357}; Peripheral membrane protein. Cell projection, filopodium {ECO:0000250|UniProtKB:O15357}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O15357}. Basal cell membrane {ECO:0000... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:57836; EC=3.1.3.86; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways (PubMed:12847108). Required for correct mitotic spindle ori... | Sus scrofa (Pig) |
D7RF80 | POLG_KFDV | MAKGAVLKGKGGGPPRRVPKETAKKTRQGPGRLPNGLVLMRMMGVLWHMVAGTARNPILKRFWATVPVRQAIAALRKIRKTVGLLLDSLNKRRGKRRSTTGLLTPILLACLATLVFSATVRRERTGNMVIRAEGKDAATQVEVMNGTCTILATDMGSWCDDSIMYECVTIDSGEEPVDVDCFCKGVERVSLEYGRCGKPAGGRNRRSVSIPVHAHSDLTGRGHKWLKGDSVKTHLTRVEGWVWKNKFLTAAFCAVVWMVTDSLPTRFIVITVALCLAPTYATRCTHLQNRDFVSGTQGTTRVSLVLELGGCVTLTAEGKP... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression ... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA he... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Kyasanur forest disease virus (KFDV) |
D7SFH9 | LRL26_ARATH | MNSQQSTRTKQMLQQSSTHLLCGVVLLQLFAAQVDAQRSTSPWQTLSGDAPLVIARGGFSGLFPDSSLAAYQFAMVVSVADVVLWCDVQLTKDGHGICFPDLNLANASNSEEVYPNRQKSYPVNGVTTKGWFPIDFSLTELQKVLFSLIRGILSRSGKFDENGYSISTVQNVATQMKPALFWLNVQHDEFYEQHNLSMSSFLLSTSRTVSIDFISSPEVNFFRKIAGGFGNNGPSFVFQFMGKEDFEPTTNRTYGSILSNLSFVKTFASGILVPKSYILPLDDKQYLLPHTSLVQDAHKAGLKLYASGFANDVDIAYNYS... | 2.7.11.1; 3.1.4.46 | null | cellular defense response [GO:0006968]; defense response [GO:0006952]; glycerol metabolic process [GO:0006071]; innate immune response [GO:0045087]; lipid metabolic process [GO:0006629]; phosphorylation [GO:0016310] | mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; glycerophosphodiester phosphodiesterase activity [GO:0008889]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF03009;PF07714; | 3.20.20.190;1.10.510.10; | Glycerophosphoryl diester phosphodiesterase family; Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20508139}; Single-pass type I membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597, ChEBI:CHEBI:83408; EC=3.1.4.46; Evidence={ECO:0000250|UniProtKB:Q7Y208}; CATALYTIC ACTIVITY: Reaction=ATP + L-... | null | null | null | null | FUNCTION: Atypical receptor-like kinase involved in disease resistance. {ECO:0000269|PubMed:20508139}. | Arabidopsis thaliana (Mouse-ear cress) |
D7SSD8 | MJE1_VITVI | MEKRERHFVLVHGACHGAWCWYKVTTFLRSAGHKVTALDLAAAGANGKRLDELNSISDYHEPLMKFMTSLVAGEKVILVAHSLGGVSVSVAMERFPQKISVAVFVSAYMPGPDFNLSTVYQELHQRRQGASKDTQYTFDRGSNNPPTSIIFSPEDLAAKLYQLSPPEDLTLATTLMRPTKLFRGENLLKETTVTREKYGTVRRVYIVCDKDNILKEDFQRWMIKNNPSDEVKVIMGSDHMPMFSKPLDLCAYLQEIVESYS | 3.1.1.- | null | jasmonic acid metabolic process [GO:0009694]; oxylipin biosynthetic process [GO:0031408]; response to cold [GO:0009409]; response to UV-B [GO:0010224]; salicylic acid metabolic process [GO:0009696] | null | methyl indole-3-acetate esterase activity [GO:0080030]; methyl jasmonate esterase activity [GO:0080032]; methyl salicylate esterase activity [GO:0080031] | PF12697; | 3.40.50.1820; | AB hydrolase superfamily, Methylesterase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + methyl (-)-jasmonate = H(+) + jasmonate + methanol; Xref=Rhea:RHEA:55372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15929, ChEBI:CHEBI:17790, ChEBI:CHEBI:58431; Evidence={ECO:0000269|PubMed:26934101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55373; Evidence={ECO:00... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92.9 uM for methyl jasmonate {ECO:0000269|PubMed:26934101}; | PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:26934101}.; PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000269|PubMed:26934101}. | null | null | FUNCTION: Methylesterase that catalyzes the hydrolysis of methyl jasmonate (MeJA) into jasmonate (JA) (PubMed:26934101). Can also use methyl salicylate (MeSA) as substrate with a lower efficiency (PubMed:26934101). {ECO:0000269|PubMed:26934101}. | Vitis vinifera (Grape) |
D7UNT2 | LCDH_RHISP | MSFITKAACVGGGVIGGAWVARFALAGIDVKIFDPHPEAERIIGEVMANAERAYAMLTMAPLPPKGKLTFCKSIEEAVEGADWIQESVPERLELKRGVITKIDAAARPDALIGSSTSGLLPSDLQSEMHHPERMFVAHPYNPVYLLPLVELVGGKKTSKATIERAMQGVEQIGMKGVVIAKEIEAFVGDRLLEALWREALWLIQDDICHTETLDNVMRYSFGMRWAQMGLFETYRIAGGEAGMRHFLAQFGPCLKWPWTKFTDVVDLDDALVEKIGAQSDAQAAGRSIRELERIRDENLVGIMHALKSGNGGEGWGAGKL... | 1.1.1.108 | null | carnitine catabolic process [GO:0042413]; fatty acid metabolic process [GO:0006631] | cytoplasm [GO:0005737] | carnitine 3-dehydrogenase activity [GO:0047728]; L-gulonate 3-dehydrogenase activity [GO:0050104]; NAD binding [GO:0051287]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF13279; | 3.10.129.10;3.40.50.720; | 3-hydroxyacyl-CoA dehydrogenase family, L-carnitine dehydrogenase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530902}. | CATALYTIC ACTIVITY: Reaction=carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH; Xref=Rhea:RHEA:19265, ChEBI:CHEBI:15378, ChEBI:CHEBI:17126, ChEBI:CHEBI:57540, ChEBI:CHEBI:57885, ChEBI:CHEBI:57945; EC=1.1.1.108; Evidence={ECO:0000269|PubMed:20530902}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 mM for L-carnithine {ECO:0000269|PubMed:20530902}; KM=0.087 mM for NAD(+) {ECO:0000269|PubMed:20530902}; KM=1.2 mM for 3-dehydrocarnitine {ECO:0000269|PubMed:20530902}; Vmax=18.9 umol/min/mg enzyme {ECO:0000269|PubMed:20530902}; | PATHWAY: Amine and polyamine metabolism; carnitine metabolism. | null | null | FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-dehydrocarnitine. Despite a high similarity to 3-hydroxyacyl-CoA dehydrogenases, cannot dehydrogenate 3-hydroxybutylate and 3-hydroxybutyl-CoA. Is probably involved in a L-carnitine degradation pathway that allows Rhizobium sp. YS-240 to grow on L-c... | Rhizobium sp |
D7UPN3 | RLK10_ORYSJ | MFSLPALLIGACAFAAAAVAASGDGCRAGCSLAIAAYYFSEGSNLTFIATIFAIGGGGYQALLPYNPAITNPDYVVTGDRVLVPFPCSCLGLPAAPASTFLAGAIPYPLPLPRGGGDTYDAVAANYADLTTAAWLEATNAYPPGRIPGGDGRVNVTINCSCGDERVSPRYGLFLTYPLWDGETLESVAAQYGFSSPAEMELIRRYNPGMGGVSGKGIVFIPVKDPNGSYHPLKSGGMGNSLSGGAIAGIVIACIAIFIVAIWLIIMFYRWQKFRKATSRPSPEETSHLDDASQAEGIKVERSIEFSYEEIFNATQGFSME... | 2.7.11.1 | null | innate immune response [GO:0045087]; phosphorylation [GO:0016310]; response to chitin [GO:0010200] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; chitin binding [GO:0008061]; protein self-association [GO:0043621]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transmembrane receptor protein kinase activity [GO:0019199] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {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=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | null | Oryza sativa subsp. japonica (Rice) |
D7UQM5 | AURK_PATPE | MTPTGPSHHSMAPKRVLPAASQSNMYGNIRSASTTSTTASTSSQALRLLQNAKTSKNADNRIAHAERQGPPSAHPAAMQKPAARVAPSNENRPDPAARQHQHQQQLQQQKATGHDRVLKESQAGNSTTTTMTSTQSKEANKWSLANFDIGRPLGKGKFGNVYLAREKKSKFIVALKVLFKSQLQKAKVEHQLRREIEIQSHLRHDHILRLYGYFYDDTRVYLILEYAARGELYKEMQAQKAGHFDEDRSAVYIYQLAKALLYCHEKKVIHRDIKPENLLLDLKGDLKIADFGWSVHAPSSRRATLCGTLDYLPPEMIEGK... | 2.7.11.1 | null | cell division [GO:0051301]; meiotic cell cycle [GO:0051321]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; regulation of cytokinesis [GO:0032465] | centrosome [GO:0005813]; chromosome passenger complex [GO:0032133]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole centrosome [GO:0031616] | ATP binding [GO:0005524]; 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, cytoskeleton, spindle {ECO:0000269|PubMed:21048162}. Midbody {ECO:0000269|PubMed:21048162}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21048162}. Nucleus {ECO:0000269|PubMed:21048162}. Chromosome {ECO:0000269|PubMed:21048162}. Chromosome, cent... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O14965}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine protein kinase that contributes to the regulation of cell cycle progression. Involved in meiotic apparatus formation and polar body extrusion. Contributes to Plk1 activation and phosphorylation of histone H3 at 'Ser-10' during meiosis I. Required for accurate progression of early embryonic M ... | Patiria pectinifera (Starfish) (Asterina pectinifera) |
D7URM0 | LCDH_PSESP | MPFITHIKTFAALGSGVIGSGWVARALAHGLDVIAWDPAPGAEQALRQRVANAWPALEKQGLAAGAAQHRLSFVSSIEECVRDADFIQESAPERLDLKLDLHAKISAAAKPDAIIASSTSGLLPSEFYESSSHPERCVVGHPFNPVYLLPLVEIVGGRHTAPEAIEAAKGIYTELGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGDAGMRHFMQQFGPALKLPWTYLPAPELTERLIDEVVDGTAAQVGERSIAELERYRDDTLLAVLEAIGTSKAKHGMTFS... | 1.1.1.108 | null | carnitine catabolic process [GO:0042413]; fatty acid metabolic process [GO:0006631] | cytoplasm [GO:0005737] | carnitine 3-dehydrogenase activity [GO:0047728]; L-gulonate 3-dehydrogenase activity [GO:0050104]; NAD binding [GO:0051287]; NAD+ binding [GO:0070403] | PF00725;PF02737; | 3.40.50.720; | 3-hydroxyacyl-CoA dehydrogenase family, L-carnitine dehydrogenase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530902}. | CATALYTIC ACTIVITY: Reaction=carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH; Xref=Rhea:RHEA:19265, ChEBI:CHEBI:15378, ChEBI:CHEBI:17126, ChEBI:CHEBI:57540, ChEBI:CHEBI:57885, ChEBI:CHEBI:57945; EC=1.1.1.108; Evidence={ECO:0000269|PubMed:20530902, ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for L-carnithine {ECO:0000269|Ref.2}; KM=8.5 mM for L-carnithine {ECO:0000269|PubMed:20530902}; KM=0.25 mM for NAD(+) {ECO:0000269|Ref.2}; KM=0.24 mM for NAD(+) {ECO:0000269|PubMed:20530902}; KM=1.71 mM for 3-dehydrocarnitine {ECO:0000269|Ref.2}; KM=4.5 mM fo... | PATHWAY: Amine and polyamine metabolism; carnitine metabolism. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5 for the oxidation reaction and 6.5 for the reduction reaction. {ECO:0000269|Ref.2}; | null | FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-dehydrocarnitine. Is specific for L-carnitine and NAD(+) as substrates since D-carnitine, other carnitine analogs such as choline and betaine, and NADP(+) are not substrates. Despite a high similarity to 3-hydroxyacyl-CoA dehydrogenases, cannot dehy... | Pseudomonas sp |
D7Y2H2 | CDNC_ECOM1 | MSTEHVDHKTIARFAEDKVNLPKVKADDFREQAKRLQNKLEGYLSDHPDFSLKRMIPSGSLAKGTALRSLNDIDVAVYISGSDAPQDLRGLLDYLADRLRKAFPNFSPDQVKPQTYSVTVSFRGSGLDVDIVPVLYSGLPDWRGHLISQEDGSFLETSIPLHLDFIKARKRAAPKHFAQVVRLAKYWARLMKQERPNFRFKSFMIELILAKLLDNGVDFSNYPEALQAFFSYLVSTELRERIVFEDNYPASKIGTLSDLVQIIDPVNPVNNVARLYTQSNVDAIIDAAMDAGDAIDAAFYAPTKQLTVTYWQKVFGSSFQ... | 2.7.7.-; 2.7.7.85 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:31932165}; | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | cytosol [GO:0005829]; membrane [GO:0016020] | 2'-5'-oligoadenylate synthetase activity [GO:0001730]; ATP binding [GO:0005524]; diadenylate cyclase activity [GO:0106408]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872] | null | 1.10.1410.20;3.30.460.10; | CD-NTase family, A01 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=3 ATP = 3',3',3'-c-tri-AMP + 3 diphosphate; Xref=Rhea:RHEA:72755, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:192523; Evidence={ECO:0000269|PubMed:31932165}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72756; Evidence={ECO:0000305|PubMed:31932165}; CATALYTIC ACTIVITY: Reactio... | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:31932165). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific s... | Escherichia coli (strain MS 115-1) |
D7Y2H4 | CAP6_ECOM1 | MNVKPSLDELFERRINFPDFEPQERLARLVGLDEHKDRLSKILGLLVNPYGIQEWAKKYHPDARAAVDTVLRRPPLVVLAGDVGSGKTELAETIGDAVARQEDIDITLYPLSLATRGQGRVGEMTQLVSAAFDYTIEAADKLKNTNGKARGAVLLLIDEADALAQSRENAQMHHEDRAGVNAFIRGIDRIANQKLPAAVLMCTNRLKALDPAVQRRAAEILTFSRPNDEQRHYLLHSKLTGLGLNSTAVEELVRLTGPRDPNSPGFTFSDITQRLIPSIILAAYPYNAVSVHSALQVVNKMTPTPAFIDRQ | null | null | defense response to virus [GO:0051607] | microtubule cytoskeleton [GO:0015630] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF00004; | 3.40.50.300; | AAA ATPase family | null | null | null | null | null | null | null | FUNCTION: Regulates complex assembly in a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate ... | Escherichia coli (strain MS 115-1) |
D7Y2H5 | NUCC_ECOM1 | MSDWSLSQLFASLHEDIQLRLGTARKAFQHPGAKGDASEGVWIEMLDTYLPKRYQAANAFVVDSLGNFSDQIDVVVFDRQYSPFIFKFNEQIIVPAESVYAVFEAKQSASADLVAYAQRKVASVRRLHRTSLPIPHAGGTYPAKPLIPILGGLLTFESDWSPALGMSFDKALNGDLSDGRLDMGCVASHGHFYFNNIDSKFNFEHGNKPATAFLFRLIAQLQFSGTVPMIDIDAYGKWLAN | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:31932164, ECO:0007744|PDB:6P7O}; | defense response to virus [GO:0051607] | null | endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF20247; | null | NucC endonuclease family | null | null | null | null | null | null | null | FUNCTION: Effector DNase of a CBASS antivirus system (PubMed:31932164, PubMed:31932165). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals... | Escherichia coli (strain MS 115-1) |
D8LQS7 | HPB_ECTSI | MQRVGAASPTCSSLQAPAAAPPILTISPHHRVKTAETAAEPDLLEPTGVHHPFHSLSPLTEARAWAAREGQYFNGLIEANGGASVSKGHPDLAVTFLTDHASCEWFFSQRQEVLDRQDGAYFGPLKCKKQYIGESLPTLASNQKESHQVLREHKLRVFRSRVPFAQSAMTNATDTFYKNLRDNGTGDYTVVYDFFLQQTIHFLHEWIYGLGVEGGQPLPPFKDFMNANPLDVSVLLELEMDTPVANLAAKLAQRSKKPSAEQLASVESIAEAIRSSDVWAGFVEMLEDSNVNTKDLERSFMFTTNFQSAGAIAKGMMPVV... | 4.2.1.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | fatty acid biosynthetic process [GO:0006633]; oxylipin biosynthetic process [GO:0031408]; sterol metabolic process [GO:0016125] | mitochondrion [GO:0005739] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; lyase activity [GO:0016829]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate = plasmodiophorol A; Xref=Rhea:RHEA:75603, ChEBI:CHEBI:58757, ChEBI:CHEBI:194366; Evidence={ECO:0000269|PubMed:35835431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75604; Evidence={ECO:0000269|PubMed:35835431}; CATALYTIC ACTIVITY: ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=133.3 uM for 13-HPOTE {ECO:0000269|PubMed:35835431}; KM=183 uM for 15-HPEPE {ECO:0000269|PubMed:35835431}; Note=kcat is 1446.7 sec(-1) with 13-HPOTE as substrate (PubMed:35835431). kcat is 1134.7 sec(-1) with 15-HPEPE as substrate (PubMed:35835431). {ECO:0000269|Pu... | PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000269|PubMed:35835431}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:35835431}; | null | FUNCTION: Cytochrome P450 hydroperoxide bicyclase involved in the metabolism of oxylipins 'ectocarpins' natural products, such as hybridalactone, ecklonilactones and derivatives (PubMed:35835431). Isomerizes the hydroperoxides into epoxyalcohols via epoxyallylic radical (PubMed:35835431). Can use alpha-linolenic acid 1... | Ectocarpus siliculosus (Brown alga) (Conferva siliculosa) |
D8QTR2 | MGH1_SELML | MAGPVRCLPPVVEATSIPHAPPVISKEVSEIVNNMLSVAIPAAAAASAQDQRFASQFRCGPEFTTMKAQALEACRKILAENDQGGYTIPAKGLYPYQWNWDSALVSLGLAEMEEERAWEELDRLMSAQWEDGMVPHIVFHKPSSTYFPGPEIWGSPDKPRNTTGITQPPVAAISVRRLLEEAKDKALALAMARKLFPKLLAWHRWFYRARDPEGTGLVATIHPWETGMDNSPAWDEALARVPIDDIPPYVRRDLGHVDAKMRPQKAEYDRYLTLLYRFRALDYDEAKLYYETPFRVTDLCTNCILHKANEDLLWLAGATG... | 3.2.1.170 | null | mannosylglycerate metabolic process [GO:0051478]; oligosaccharide metabolic process [GO:0009311]; protein N-linked glycosylation [GO:0006487] | endoplasmic reticulum membrane [GO:0005789] | Glc3Man9GlcNAc2 oligosaccharide glucosidase activity [GO:0004573]; glucosylglycerate hydrolase activity [GO:0102547]; mannosylglycerate hydrolase activity [GO:0102546] | null | 1.50.10.10; | Glycosyl hydrolase 63 family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2-O-(alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate + D-mannose; Xref=Rhea:RHEA:58456, ChEBI:CHEBI:4208, ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:57541; EC=3.2.1.170; Evidence={ECO:0000269|PubMed:23179444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58457; Evidenc... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.8 mM for 2-O-(alpha-D-mannosyl)-glycerate (at 40 degrees Celsius) {ECO:0000269|PubMed:23179444}; KM=5.9 mM for 2-O-(alpha-D-glucopyranosyl)-D-glycerate (at 40 degrees Celsius) {ECO:0000269|PubMed:23179444}; Vmax=40.5 umol/min/mg enzyme with 2-O-(alpha-D-mannosyl... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-6.50. {ECO:0000269|PubMed:23179444}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:23179444}; | FUNCTION: Catalyzes the hydrolysis of alpha-D-mannosyl-glycerate (MG) to D-glycerate and D-mannose (PubMed:23179444). Can also hydrolyze alpha-D-glucopyranosyl-glycerate (GG)with lower efficiency (PubMed:23179444). {ECO:0000269|PubMed:23179444}. | Selaginella moellendorffii (Spikemoss) |
D8VPP5 | AL11A_OLEEU | MSCIAVEAVLLGILLYIPIVLSDDRAPIPSNSAQLNSWFDGIIQPVAVRKATMDPALVTAEGQTKVIKLKSDGSGDFKSINEAIKSIPDDNTKRVILSLAPGNYSEKVKIGMYKHYITFYGEDPNNMPILVFGGTAAEYGTVDSATLIVESNYFSAVNLKIVNSAPRPDGKRVGAQAAALRISGDKASFYNVKIYGFQDTLCDDKGKHFYKDCYIEGTVDFIFGSGKSIFLNTELHAVPGDQPAIITAQARKTDSEDTGYYFVNCRVTGGGAFLGRSWMPAAKVVFAYTEMVDAIHPEGWILVKPEHESTVRFSEYNNKG... | 3.1.1.11 | null | cell wall modification [GO:0042545]; pectin catabolic process [GO:0045490] | extracellular region [GO:0005576] | aspartyl esterase activity [GO:0045330]; pectinesterase activity [GO:0030599] | PF01095; | 2.160.20.10; | Pectinesterase family | PTM: Glycosylated. {ECO:0000269|PubMed:20491902}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20491902}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;... | null | PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:20491902}; | null | FUNCTION: Catalyzes the demethylesterification of homogalacturonan components of pectin. May be involved in pollen tube development. {ECO:0000269|PubMed:20491902}. | Olea europaea (Common olive) |
D9I2F9 | NL1A1_RAT | MEESQSKQESNTRVAQHGSQQDVDPTFQTKRALEKERSKPRPRPLPRVQLQSLPGWSSTSNDVPLSQLIREMDHESRRCIHRSKKKLDRSEHISQGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQP... | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784... | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor ... | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1a allele 1]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain as... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (PubMed:33731929). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other dam... | Rattus norvegicus (Rat) |
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