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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A6NDG6 | PGP_HUMAN | MAAAEAGGDDARCVRLSAERAQALLADVDTLLFDCDGVLWRGETAVPGAPEALRALRARGKRLGFITNNSSKTRAAYAEKLRRLGFGGPAGPGASLEVFGTAYCTALYLRQRLAGAPAPKAYVLGSPALAAELEAVGVASVGVGPEPLQGEGPGDWLHAPLEPDVRAVVVGFDPHFSYMKLTKALRYLQQPGCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGATCGLKTILTLTGVSTLGDVKNNQESDCVSKKKMVPDFYVDSIADLLPALQ... | 3.1.3.21; 3.1.3.48 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8CHP8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHP8}; | glycerol biosynthetic process [GO:0006114]; glycerophospholipid metabolic process [GO:0006650]; negative regulation of gluconeogenesis [GO:0045721] | cytoplasm [GO:0005737] | ADP phosphatase activity [GO:0043262]; glycerol-1-phosphatase activity [GO:0000121]; glycerol-3-phosphatase activity [GO:0043136]; magnesium ion binding [GO:0000287]; phosphoglycolate phosphatase activity [GO:0008967]; protein tyrosine phosphatase activity [GO:0004725] | PF13344;PF13242; | 3.40.50.1000; | HAD-like hydrolase superfamily, CbbY/CbbZ/Gph/YieH family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q8CHP8}; CATALYTIC ACTIVITY: Reac... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for glycerol-3-phosphate {ECO:0000269|PubMed:26755581}; KM=1.5 mM for 2-phosphoglycolate {ECO:0000269|PubMed:26755581}; Vmax=100 nmol/min/mg enzyme with glycerol-3-phosphate as substrate {ECO:0000269|PubMed:26755581}; Vmax=500 nmol/min/mg enzyme with 2-phosp... | null | null | null | FUNCTION: Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase ... | Homo sapiens (Human) |
A6NDV4 | TMM8B_HUMAN | MNMPQSLGNQPLPPEPPSLGTPAEGPGTTSPPEHCWPVRPTLRNELDTFSVHFYIFFGPSVALPPERPAVFAMRLLPVLDSGGVLSLELQLNASSVRQENVTVFGCLTHEVPLSLGDAAVTCSKESLAGFLLSVSATTRVARLRIPFPQTGTWFLALRSLCGVGPRFVRCRNATAEVRMRTFLSPCVDDCGPYGQCKLLRTHNYLYAACECKAGWRGWGCTDSADALTYGFQLLSTLLLCLSNLMFLPPVVLAIRSRYVLEAAVYTFTMFFSTFYHACDQPGIVVFCIMDYDVLQFCDFLGSLMSVWVTVIAMARLQPVV... | null | null | cell-matrix adhesion [GO:0007160]; regulation of mitotic cell cycle [GO:0007346] | cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | null | PF12036; | null | TMEM8 family | PTM: Isoform 2 is N-glycosylated. {ECO:0000269|PubMed:15498789}. | SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17641538}; Multi-pass membrane protein {ECO:0000269|PubMed:17641538}. Cytoplasm {ECO:0000269|PubMed:17641538}. Nucleus {ECO:0000269|PubMed:17641538}. Mitochondrion {ECO:0000269|PubMed:17641538}. Endoplasmic reticulum {ECO:0000269|PubMed:17641538}. Not... | null | null | null | null | null | FUNCTION: May function as a regulator of the EGFR pathway. Probable tumor suppressor which may function in cell growth, proliferation and adhesion. {ECO:0000269|PubMed:15498789, ECO:0000269|PubMed:15723283, ECO:0000269|PubMed:17270023, ECO:0000269|PubMed:17641538}. | Homo sapiens (Human) |
A6NED2 | RCCD1_HUMAN | MAEERPGAWFGFGFCGFGQELGSGRGRQVHSPSPLRAGVDICRVSASWSYTAFVTRGGRLELSGSASGAAGRCKDAWASEGLLAVLRAGPGPEALLQVWAAESALRGEPLWAQNVVPEAEGEDDPAGEAQAGRLPLLPCARAYVSPRAPFYRPLAPELRARQLELGAEHALLLDAAGQVFSWGGGRHGQLGHGTLEAELEPRLLEALQGLVMAEVAAGGWHSVCVSETGDIYIWGWNESGQLALPTRNLAEDGETVAREATELNEDGSQVKRTGGAEDGAPAPFIAVQPFPALLDLPMGSDAVKASCGSRHTAVVTRTGE... | null | null | chromatin organization [GO:0006325] | chromosome [GO:0005694]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | null | PF00415; | 2.130.10.30; | null | PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of ARG-141 by KDM8. {ECO:0000269|PubMed:29563586}. | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:24981860}. Note=Colocalizes with trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000269|PubMed:24981860}. | null | null | null | null | null | FUNCTION: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with KDM8 (PubMed:24981860). Possibly together with KDM8, is involved in proper mitotic spindle organization and chromosome segregation (PubMed:24981860). Plays a ro... | Homo sapiens (Human) |
A6NEM1 | GG6L9_HUMAN | MWPQPRLPPHPAMSEKTQQGKLAAAKKKLKAYWQRKSPGIPAGANRKKKINGSSPDTFTSGGYHSPGDSATGIYGEGRASSTTLQDLESQYQELAVALDSSSAIISQLTENINSLVRTSKEEKKHEIHLVQKLGRSLFKLKNQTAEPLAPQPPAGPSKMEQLQDETNHLRKELESVGRQLQAEVENNQMLSLLNRRQEERLREQEERLREQEERLCEQEERLCEQEERLREQEERLCEQEKLPGQERLLEEVEKLLEQERRQEEQERLLERERLLDEVEELLEQERLRQQDERLWQQETLRELERLRELERMLELGWEAL... | null | null | null | null | null | PF15070; | null | GOLGA6 family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
A6NFA1 | TIKI2_HUMAN | MHAALAGPLLAALLATARARPQPPDGGQCRPPGSQRDLNSFLWTIRRDPPAYLFGTIHVPYTRVWDFIPDNSKAAFQASTRVYFELDLTDPYTISALASCQLLPHGENLQDVLPHELYWRLKRHLDYVKLMMPSWMTPAQRGKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTERDVRFRGVPVLDLYLAQQAEKMKKTTGAVEQVEEQCHPLNNGLNFSQVLFALNQTLLQQESVRAGSLQASYTTEDLIKHYNCGDLSAVIFNHDTSQLPNFINTTLPPHEQVTAQEIDSYFRQELIYKRNERMGKRVMALLRENED... | 3.4.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:22726442}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:22726442}; Note=Divalent metal cations. Mn(2+) or Co(2+). {ECO:0000269|PubMed:22726442}; | negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of protein oxidation [GO:1904808]; positive regulation of protein-containing complex assembly [GO:0031334]; proteolysis [GO:0006508]; Wnt signaling pathway [GO:0016055] | membrane [GO:0016020]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; Wnt-protein binding [GO:0017147] | PF01963; | null | TIKI family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22726442}; Single-pass type I membrane protein {ECO:0000269|PubMed:22726442}. | null | null | null | null | null | FUNCTION: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5... | Homo sapiens (Human) |
A6NFQ2 | TCAF2_HUMAN | MATIAAAAFEALMDGVTCWDVPRGPIPSELLLIGEAAFPVMVNDKGQVLIAASSYGRGRLVVVSHEGYLSHTGLAPFLLNAVSWLCPCPGAPVGVHPSLAPLVNILQDAGLEAQVKPEPGEPLGVYCINAYNDTLTATLIQFVKHGGGLLIGGQAWYWASQHGPDKVLSRFPGNKVTSVAGVYFTDTYGDRDRFKVSKKVPKIPLHVRYGEDVRQDQQQLLEGISELDIRTGGVPSQLLVHGALAFPLGLDASLNCFLAAAHYGRGRVVLAAHECLLCAPKMGPFLLNAVRWLARGQTGKVGVNTNLKDLCPLLSEHGLQ... | null | null | negative regulation of anion channel activity [GO:0010360]; positive regulation of cell migration [GO:0030335]; positive regulation of protein targeting to membrane [GO:0090314] | cell junction [GO:0030054]; plasma membrane [GO:0005886] | transmembrane transporter binding [GO:0044325] | PF17291;PF13402; | 3.40.390.80;1.10.390.30; | TCAF family | null | SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:25559186}. Note=Colocalizes with TRPM8 on the plasma membrane. {ECO:0000269|PubMed:25559186}. | null | null | null | null | null | FUNCTION: [Isoform 2]: Negatively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration stimulation in a TRPM8-dependent manner. {ECO:0000269|PubMed:25559186}. | Homo sapiens (Human) |
A6NFX1 | MFS2B_HUMAN | MAAPPAPAAKGSPQPEPHAPEPGPGSAKRGREDSRAGRLSFCTKVCYGIGGVPNQIASSATAFYLQLFLLDIAQIPAAQVSLVLFGGKVSGAAADPVAGFFINRSQRTGSGRLMPWVLGCTPFIALAYFFLWFLPPFTSLRGLWYTTFYCLFQALATFFQVPYTALTMLLTPCPRERDSATAYRMTVEMAGTLMGATVHGLIVSGAHRPHRCEATATPGPVTVSPNAAHLYCIAAAVVVVTYPVCISLLCLGVKERPDPSAPASGPGLSFLAGLSLTTRHPPYLKLVISFLFISAAVQVEQSYLVLFCTHASQLHDHVQG... | null | null | carbohydrate transport [GO:0008643]; lipid transport [GO:0006869]; positive regulation of platelet aggregation [GO:1901731]; sphingolipid biosynthetic process [GO:0030148]; sphingosine-1-phosphate receptor signaling pathway [GO:0003376] | plasma membrane [GO:0005886] | sphingolipid transporter activity [GO:0046624]; symporter activity [GO:0015293] | PF13347; | 1.20.1250.20; | Major facilitator superfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29045386, ECO:0000269|PubMed:29563527}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cell membrane and intracellular membranes. {ECO:0000269|PubMed:29045386}. | CATALYTIC ACTIVITY: Reaction=sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38667, ChEBI:CHEBI:60119; Evidence={ECO:0000305|PubMed:29563527}; CATALYTIC ACTIVITY: Reaction=sphinganine 1-phosphate(in) = sphinganine 1-phosphate(out); Xref=Rhea:RHEA:38671, ChEBI:CHEBI:57939; Evidence={ECO:... | null | null | null | null | FUNCTION: Lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets (PubMed:29045386). Sphingosine-1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology (By similarity). Sphingosine-1... | Homo sapiens (Human) |
A6NFY7 | SDHF1_HUMAN | MSRHSRLQRQVLSLYRDLLRAGRGKPGAEARVRAEFRQHAGLPRSDVLRIEYLYRRGRRQLQLLRSGHATAMGAFVRPRAPTGEPGGVGCQPDDGDSPRNPHDSTGAPETRPDGR | null | null | mitochondrial respiratory chain complex II assembly [GO:0034553] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | null | PF05347; | null | Complex I LYR family, SDHAF1 subfamily | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:19465911}. | null | null | null | null | null | FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with ... | Homo sapiens (Human) |
A6NGG8 | PCARE_HUMAN | MGCTPSHSDLVNSVAKSGIQFLKKPKAIRPGCQGGSERGSIPLLVKNSTCYDAGEGLAEEQPSPRRNQTTAKGLCQLMGDPASGKRKDMEGLIPGTKTSSSQLNKSQSHMAKDIPFKTQGSHGSQGADFSGDESEESSTQDTSKWKRTAKCHTSSTQSHCYQTIHPAHEPEGKVDFPEPLVKAHQQAYTYLHSSLSKYEAILCIIHQATQTRELLQPMVSFLLLCFEEISQLLGEISKDGEVLLQEVREDLAWPLKKREPQEQPNLLQQLLQYTVSKLQVLNGTVASLTGSFLEGSSSYLHSTATHLENKLSTKRNVDER... | null | null | photoreceptor cell outer segment organization [GO:0035845]; protein localization to photoreceptor outer segment [GO:1903546]; response to stimulus [GO:0050896]; visual perception [GO:0007601] | cilium [GO:0005929]; cone photoreceptor outer segment [GO:0120199]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | null | PF15449; | null | null | null | SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:20398886}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q6PAC4}. | null | null | null | null | null | FUNCTION: Plays an essential role for normal photoreceptor cell maintenance and vision. {ECO:0000269|PubMed:20398886}. | Homo sapiens (Human) |
A6NGQ2 | OOEP_HUMAN | MVDDAGAAESQRGKQTPAHSLEQLRRLPLPPPQIRIRPWWFPVQELRDPLVFYLEAWLADELFGPDRAIIPEMEWTSQALLTVDIVDSGNLVEITVFGRPRVQNRVKSMLLCLAWFHREHRARAEKMKHLEKNLKAHASDPHSPQDPVA | null | null | actin filament organization [GO:0007015]; embryonic pattern specification [GO:0009880]; establishment of spindle localization [GO:0051293]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of double-strand break ... | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; subcortical maternal complex [GO:0106333] | RNA binding [GO:0003723] | PF16005; | 3.30.1370.10; | KHDC1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25542835}. Nucleus {ECO:0000269|PubMed:25542835}. | null | null | null | null | null | FUNCTION: As part of the OOEP-KHDC3L scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart (By similarity). Positively regulates the homologous recombinatio... | Homo sapiens (Human) |
A6NGU5 | GGT3_HUMAN | MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCLEIGRDTLRDGGSAVDAAIAALLCVGLMNAHSMGIGVGLFLTIYNSTTRKAEVINAREVAPRLAFASMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAVLENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPRLADTYEMLAIEGAQAFYNGSLMAQIVKDIQAAGGIVTAEDLNNYCAELIEHPLNISLGDAVLYMPSARLSGPVLALILNILKGYNFSRESVETPEQKGLTYHRIVEAF... | 2.3.2.2; 3.4.19.13 | null | glutathione biosynthetic process [GO:0006750]; glutathione catabolic process [GO:0006751]; leukotriene D4 biosynthetic process [GO:1901750]; peptide modification [GO:0031179]; proteolysis [GO:0006508]; regulation of immune system process [GO:0002682]; regulation of inflammatory response [GO:0050727] | extracellular exosome [GO:0070062]; plasma membrane [GO:0005886] | glutathione hydrolase activity [GO:0036374]; leukotriene C4 gamma-glutamyl transferase activity [GO:0103068] | PF01019; | 1.10.246.130;3.60.20.40; | Gamma-glutamyltransferase family | PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250|UniProtKB:P19440}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07314}. | 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: Hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors. {ECO:0000250|UniProtKB:P19440}. | Homo sapiens (Human) |
A6NHL2 | TBAL3_HUMAN | MRECLSIHIGQAGIQIGDACWELYCLEHGIQPNGVVLDTQQDQLENAKMEHTNASFDTFFCETRAGKHVPRALFVDLEPTVIDGIRTGQHRSLFHPEQLLSGKEDAANNYARGRYSVGSEVIDLVLERTRKLAEQCGGLQGFLIFRSFGGGTGSGFTSLLMERLTGEYSRKTKLEFSVYPAPRISTAVVEPYNSVLTTHSTTEHTDCTFMVDNEAVYDICHRKLGVECPSHASINRLVVQVVSSITASLRFEGPLNVDLIEFQTNLVPYPRIHFPMTAFAPIVSADKAYHEQFSVSDITTACFESSNQLVKCDPRLGKYM... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing a... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Homo sapiens (Human) |
A6NHR9 | SMHD1_HUMAN | MAAADGGGPGGASVGTEEDGGGVGHRTVYLFDRREKESELGDRPLQVGERSDYAGFRACVCQTLGISPEEKFVITTTSRKEITCDNFDETVKDGVTLYLLQSVNQLLLTATKERIDFLPHYDTLVKSGMYEYYASEGQNPLPFALAELIDNSLSATSRNIGVRRIQIKLLFDETQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTRQGDFESDHSGYVRPVPVPRSLNSDISYFGVGGKQAVFFVGQSARMISKPADSQDVHELVLSKEDFEKKEKNKEAIYSGYIRNRKPSDSVHITNDDERFLHHLIIEEKEKDSFT... | 3.6.1.- | null | chromosome organization [GO:0051276]; dosage compensation by inactivation of X chromosome [GO:0009048]; double-strand break repair [GO:0006302]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; nose development [GO:0043584]; positive regulation of DNA repair [GO:0045739]; pos... | Barr body [GO:0001740]; site of double-strand break [GO:0035861] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; protein homodimerization activity [GO:0042803] | PF13589;PF06470; | 3.30.565.10; | SMC family | PTM: Sumoylated with SUMO1. {ECO:0000250|UniProtKB:Q6P5D8}. | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:24790221, ECO:0000269|PubMed:25294876}. Note=Recruited to inactivated chromosome X in females by Xist RNA (By similarity). Localizes at sites of DNA damage at double-strand breaks (DSBs) (PubMed:24790221, PubMed:25294876). {ECO:0000250|UniProtKB:Q6P5D8, ECO:0000269|P... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:29748383}; | null | null | null | null | FUNCTION: Non-canonical member of the structural maintenance of chromosomes (SMC) protein family that plays a key role in epigenetic silencing by regulating chromatin architecture (By similarity). Promotes heterochromatin formation in both autosomes and chromosome X, probably by mediating the merge of chromatin compart... | Homo sapiens (Human) |
A6NHX0 | CAST2_HUMAN | MELHILEHRLQVASVAKESIPLFTYGLIKLAFLSSKTRCKFFSLTETPEDYTIIVDEEGFLELPSSEHLSVADATWLALNVVSGGGSFSSSQPIGVTKIAKSVIAPLADQNISVFMLSTYQTDFILVRERDLPFVTHTLSSEFTILRVVNGETVAAENLGITNGFVKPKLVQRPVIHPLSSPSNRFCVTSLDPDTLPAVATLLMDVMFYSNGVKDPMATGDDCGHIRFFSFSLIEGYISLVMDVQTQQRFPSNLLFTSASGELWKMVRIGGQPLGFDECGIVAQISEPLAAADIPAYYISTFKFDHALVPEENINGVISA... | null | null | cellular response to L-arginine [GO:1903577]; negative regulation of TORC1 signaling [GO:1904262] | cytosol [GO:0005829] | identical protein binding [GO:0042802] | PF13840;PF21389;PF18700; | 3.30.2130.10; | GATS family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26972053}. | null | null | null | null | null | FUNCTION: Functions as a negative regulator of the TORC1 signaling pathway through the GATOR complex. As part of homodimers or heterodimers with CASTOR1, directly binds and inhibits the GATOR subcomplex GATOR2 and thereby mTORC1. Does not directly bind arginine, but binding of arginine to CASTOR1 disrupts the interacti... | Homo sapiens (Human) |
A6NI15 | MSGN1_HUMAN | MDNLRETFLSLEDGLGSSDSPGLLSSWDWKDRAGPFELNQASPSQSLSPAPSLESYSSSPCPAVAGLPCEHGGASSGGSEGCSVGGASGLVEVDYNMLAFQPTHLQGGGGPKAQKGTKVRMSVQRRRKASEREKLRMRTLADALHTLRNYLPPVYSQRGQPLTKIQTLKYTIKYIGELTDLLNRGREPRAQSA | null | null | cell differentiation [GO:0030154]; mesoderm formation [GO:0001707]; regulation of transcription by RNA polymerase II [GO:0006357]; segment specification [GO:0007379]; somitogenesis [GO:0001756] | chromatin [GO:0000785]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO... | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Involved in specifying the paraxial, but not dorsal, mesoderm. May regulate the expression of T-box transcription factors required for mesoderm formation and differentiation (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
A6NI61 | MYMK_HUMAN | MGTLVAKLLLPTLSSLAFLPTVSIAAKRRFHMEAMVYLFTLFFVALHHACNGPGLSVLCFMRHDILEYFSVYGTALSMWVSLMALADFDEPKRSTFVMFGVLTIAVRIYHDRWGYGVYSGPIGTAILIIAAKWLQKMKEKKGLYPDKSVYTQQIGPGLCFGALALMLRFFFEDWDYTYVHSFYHCALAMSFVLLLPKVNKKAGSPGTPAKLDCSTLCCACV | null | null | muscle organ development [GO:0007517]; myoblast fusion [GO:0007520]; myoblast fusion involved in skeletal muscle regeneration [GO:0014905]; plasma membrane fusion [GO:0045026]; positive regulation of skeletal muscle hypertrophy [GO:1904206] | Golgi membrane [GO:0000139]; plasma membrane [GO:0005886] | null | PF12036; | null | TMEM8 family | PTM: Palmitoylated at the C-terminus; palmitoylation promotes localization to the Golgi apparatus. {ECO:0000250|UniProtKB:Q9D1N4}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9D1N4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9D1N4}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9D1N4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9D1N4}. Note=Localizes on the plasma membrane of myoblasts, where it mediates myobl... | null | null | null | null | null | FUNCTION: Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers (PubMed:28681861). Actively participates in the membrane fusion reaction by mediating the mixing of cell membrane lipids (hemifusion) upstream of MYMX. Acts independently of MYMX (By s... | Homo sapiens (Human) |
A6NI73 | LIRA5_HUMAN | MAPWSHPSAQLQPVGGDAVSPALMVLLCLGLSLGPRTHVQAGNLSKATLWAEPGSVISRGNSVTIRCQGTLEAQEYRLVKEGSPEPWDTQNPLEPKNKARFSIPSMTEHHAGRYRCYYYSPAGWSEPSDPLELVVTGFYNKPTLSALPSPVVTSGENVTLQCGSRLRFDRFILTEEGDHKLSWTLDSQLTPSGQFQALFPVGPVTPSHRWMLRCYGSRRHILQVWSEPSDLLEIPVSGAADNLSPSQNKSDSGTASHLQDYAVENLIRMGMAGLILVVLGILIFQDWHSQRSPQAAAGR | null | null | cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; negative regulation of interleukin-12 production [GO:0032695]; negative regulation of interleukin-13 production [GO:0032696]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cell activation [GO:00508... | cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | inhibitory MHC class I receptor activity [GO:0032396] | PF13895; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12393390}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:12393390}. | null | null | null | null | null | FUNCTION: May play a role in triggering innate immune responses. Does not seem to play a role for any class I MHC antigen recognition. {ECO:0000269|PubMed:16675463}. | Homo sapiens (Human) |
A6NIH7 | U119B_HUMAN | MSGSNPKAAAAASAAGPGGLVAGKEEKKKAGGGVLNRLKARRQAPHHAADDGVGAAVTEQELLALDTIRPEHVLRLSRVTENYLCKPEDNIYSIDFTRFKIRDLETGTVLFEIAKPCVSDQEEDEEEGGGDVDISAGRFVRYQFTPAFLRLRTVGATVEFTVGDKPVSNFRMIERHYFREHLLKNFDFDFGFCIPSSRNTCEHIYEFPQLSEDVIRLMIENPYETRSDSFYFVDNKLIMHNKADYAYNGGQ | null | null | cilium assembly [GO:0060271]; lipoprotein transport [GO:0042953]; nervous system development [GO:0007399] | ciliary transition zone [GO:0035869]; cilium [GO:0005929]; cytosol [GO:0005829] | lipid binding [GO:0008289] | PF05351; | 2.70.50.40; | PDE6D/unc-119 family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:22085962}. Note=Enriched at the transition zone and extended into the proximal end of the cilium. | null | null | null | null | null | FUNCTION: Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated NPHP3 and plays a key role in localization of NPHP3 to the primary cilium membrane. Does not bind all m... | Homo sapiens (Human) |
A6NIX2 | WTIP_HUMAN | MQRSRAGADEAALLLAGLALRELEPGCGSPGRGRRGPRPGPGDEAAPALGRRGKGSGGPEAGADGLSRGERGPRRAAVPELSAQPAGSPRASLAGSDGGGGGGSARSSGISLGYDQRHGSPRSGRSDPRPGPGPPSVGSARSSVSSLGSRGSAGAYADFLPPGACPAPARSPEPAGPAPFPLPALPLPPGREGGPSAAERRLEALTRELERALEARTARDYFGICIKCGLGIYGAQQACQAMGSLYHTDCFTCDSCGRRLRGKAFYNVGEKVYCQEDFLYSGFQQTADKCSVCGHLIMEMILQALGKSYHPGCFRCSVCN... | null | null | cell projection organization [GO:0030030]; cytoskeleton organization [GO:0007010]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; miRNA-mediated post-transcriptional gene silencing [GO:0035195]; negative regulation of hippo signaling [GO:0035331]; positive regulation of miRNA-mediated gene sil... | adherens junction [GO:0005912]; nucleus [GO:0005634]; P-body [GO:0000932]; transcription regulator complex [GO:0005667] | metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714] | PF00412; | 2.10.110.10; | Zyxin/ajuba family | null | SUBCELLULAR LOCATION: Cell junction, adherens junction. Nucleus {ECO:0000250}. Cytoplasm, P-body. Note=Following podocyte injury, caused by treatment with LPS, puromycin aminonucleoside, ultraviolet or hydrogen peroxide, translocates from sites of cell-cell contacts into the cytosol and nucleus. The shift from cell con... | null | null | null | null | null | FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positi... | Homo sapiens (Human) |
A6NJ46 | NKX63_HUMAN | MESNLQGTFLLNNTPLAQFPEMKAPVCQYSVQNSFYKLSPPGLGPQLAAGTPHGITDILSRPVAAPNNSLLSGYPHVAGFGGLSSQGVYYSPQVGNFSKAGNEYPTRTRNCWADTGQDWRGGRQCSNTPDPLSDSIHKKKHTRPTFTGHQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKKSALEPSSSTPRAPGGAGAGAGGDRAPSENEDDEYNKPLDPDSDDEKIRLLLRKHRAAFSVLSLGAHSV | null | null | cell differentiation [GO:0030154]; cell fate determination [GO:0001709]; enteroendocrine cell differentiation [GO:0035883]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase ... | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA ... | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Putative transcription factor, which may be involved in patterning of central nervous system and pancreas. {ECO:0000250}. | Homo sapiens (Human) |
A6NJ78 | MET15_HUMAN | MLRYPYFCRMYKECLSCWLESGIPNLGVWPNRIHTTAEKYREYEAREQTDQTQAQELHRSQDRDFETMAKLHIPVMVDEVVHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDRDPTAYALAEHLSELYPKQIRAMLGQFSQAEALLMKAGVQPGTFDGVLMDLGCSSMQLDTPERGFSLRKDGPLDMRMDGGRYPDMPTAADVVNALDQQALASILRTYGEEKHAKKIASAIVQARSIYPITRTQQLASIVAGAFPPSAIYTRKDLLQRSTHIATKTFQALRIFVNNELNELYTGLKTAQKFLRPGGRLVALS... | 2.1.1.- | null | rRNA base methylation [GO:0070475] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | rRNA (cytosine-N4-)-methyltransferase activity [GO:0071424] | PF01795; | 1.10.150.170;3.40.50.150; | Methyltransferase superfamily, RsmH family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392}. | CATALYTIC ACTIVITY: Reaction=cytidine(839) in 12S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(839) in 12S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62524, Rhea:RHEA-COMP:16109, Rhea:RHEA-COMP:16110, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74506, ChEBI:CHEBI:82748; Evi... | null | null | null | null | FUNCTION: N4-methylcytidine (m4C) methyltransferase responsible for the methylation of position C839 in mitochondrial 12S rRNA (PubMed:31665743, PubMed:32371392). Involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits (PubMed:31665743, PubMed... | Homo sapiens (Human) |
A6NK06 | IRG1_HUMAN | MMLKSITESFATAIHGLKVGHLTDRVIQRSKRMILDTLGAGFLGTTTEVFHIASQYSKIYSSNISSTVWGQPDIRLPPTYAAFVNGVAIHSMDFDDTWHPATHPSGAVLPVLTALAEALPRSPKFSGLDLLLAFNVGIEVQGRLLHFAKEANDMPKRFHPPSVVGTLGSAAAASKFLGLSSTKCREALAIAVSHAGAPMANAATQTKPLHIGNAAKHGIEAAFLAMLGLQGNKQVLDLEAGFGAFYANYSPKVLPSIASYSWLLDQQDVAFKRFPAHLSTHWVADAAASVRKHLVAERALLPTDYIKRIVLRIPNVQYVN... | 4.1.1.6 | null | cellular response to interferon-beta [GO:0035458]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to molecule of bacterial origin [GO:0071219]; cellular response to progesterone stimulus [GO:0071393]; cellular response to tumor necrosis factor [G... | mitochondrion [GO:0005739] | aconitate decarboxylase activity [GO:0047613]; protein homodimerization activity [GO:0042803] | PF19305;PF03972; | 1.10.4100.10;3.30.1330.120; | PrpD family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P54987}. | CATALYTIC ACTIVITY: Reaction=cis-aconitate + H(+) = CO2 + itaconate; Xref=Rhea:RHEA:15253, ChEBI:CHEBI:15378, ChEBI:CHEBI:16383, ChEBI:CHEBI:16526, ChEBI:CHEBI:17240; EC=4.1.1.6; Evidence={ECO:0000269|PubMed:23610393, ECO:0000269|PubMed:31548418, ECO:0000269|PubMed:35662396}; PhysiologicalDirection=left-to-right; Xref=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.61 mM for cis-aconitate {ECO:0000269|PubMed:31548418}; Note=kcat is 0.94 sec(-1) for cis-aconitate. {ECO:0000269|PubMed:31548418}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:31548418}; | null | FUNCTION: Cis-aconitate decarboxylase that catalyzes production of itaconate and is involved in the inhibition of the inflammatory response (PubMed:23609450, PubMed:23610393, PubMed:31548418, PubMed:35662396). Acts as a negative regulator of the Toll-like receptors (TLRs)-mediated inflammatory innate response by stimul... | Homo sapiens (Human) |
A6NK58 | LIPT2_HUMAN | MRQPAVRLVRLGRVPYAELLGLQDRWLRRLQAEPGIEAPSGTEAGALLLCEPAGPVYTAGLRGGLTPEETARLRALGAEVRVTGRGGLATFHGPGQLLCHPVLDLRRLGLRLRMHVASLEACAVRLCELQGLQDARARPPPYTGVWLDDRKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSKELQRHVTVEEVMPPFLVAFKEIYKCTLISEDSPN | 2.3.1.181 | null | carboxylic acid metabolic process [GO:0019752]; positive regulation of oxygen metabolic process [GO:2000376]; protein lipoylation [GO:0009249] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ligase activity [GO:0016874]; lipoyl(octanoyl) transferase activity [GO:0033819] | null | null | LipB family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:28628643, ECO:0000269|PubMed:28757203}. | CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; ... | null | PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. | null | null | FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein (octanoyl-ACP) onto the lipoyl domains of lipoate-dependent enzymes such as the protein H of the glycine cleavage system (GCSH) (PubMed:28757203). Lipoyl-ACP can also act as a substrate although octanoyl-ACP is li... | Homo sapiens (Human) |
A6NK89 | RASFA_HUMAN | MDPSEKKISVWICQEEKLVSGLSRRTTCSDVVRVLLEDGCRRRRRQRRSRRLGSAGDPHGPGELPEPPNEDDEDDDEALPQGMLCGPPQCYCIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVLVRSEASLPNAGPRSAEARVVLSRERPCPARGAPARPSLAMTQEKQRRVVRKAFRKLAKLNRRRQQQTPSSCSSTSSSTASSCSSSPRTHESASVERMETLVHLVLSQDHTIRQQVQRLHELDREIDHYEAKVHLDRMRRHGVNYVQDTYLVGAGIELDGSRPGEEPEEVAAEAEEAAAAPPLAGEAQAAALE... | null | null | nervous system development [GO:0007399]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of neurogenesis [GO:0050769]; signal transduction [GO:0007165] | centrosome [GO:0005813]; cytosol [GO:0005829]; spindle pole [GO:0000922] | null | PF21712; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20956940}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20956940}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20956940}. Note=During interphase, predominantly cytoplasmic, although some nuclear staining... | null | null | null | null | null | FUNCTION: Plays an important role in regulating embryonic neurogenesis. {ECO:0000250|UniProtKB:Q8BL43}. | Homo sapiens (Human) |
A6NKB5 | PCX2_HUMAN | MVSQVLQLLRQGVWAALTGGWYHDPEQSKFTNSCHLYLWLFLLLLPLALHLAFPPNAIIVFFYCSAVTIFFTIIKLVSYRLHLMFDKGEVIQQKPSRKEEKPNKDKEAKGEHITNHRNPSNNRQIHNGKKEEASRNLSTPPLRCSSRGQSITSHHSSGPLELSAQETVEDLKGVILLEDHPIAPVSSTSPGIKVESLPASQAHMLETTTKSVIPVKPVATETLINGKGKERGGKGQPPLRHRSEGGLVDKGPLKKLPHLSLSQYDLLETDVSFQPWGSENSVLIPEPVSCPRGSIRERVQSKSPQDSLSSSCPQCDTIVA... | null | null | null | membrane [GO:0016020] | null | PF05041; | null | Pecanex family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: May play a role in tumorigenesis of colorectal carcinomas with high microsatellite instability (MSI-H). {ECO:0000269|PubMed:12140758, ECO:0000269|PubMed:14507650}. | Homo sapiens (Human) |
A6NMY6 | AXA2L_HUMAN | MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNIVTNRDNAQRQDIVFSYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDAQDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQRIQNKPLYFADQLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQ... | null | null | positive regulation of receptor-mediated endocytosis involved in cholesterol transport [GO:1905602] | basement membrane [GO:0005604]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; cytoskeletal protein binding [GO:0008092]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [G... | PF00191; | 1.10.220.10; | Annexin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane. In melanosome fractions from stage I to stage IV. Translocated from the cytoplasm to the cell surface through a Golgi-independent mechanis... | null | null | null | null | null | FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. {ECO:0000250}. | Homo sapiens (Human) |
A6NMZ7 | CO6A6_HUMAN | MMLLILFLVIICSHISVNQDSGPEYADVVFLVDSSDRLGSKSFPFVKMFITKMISSLPIEADKYRVALAQYSDKLHSEFHLSTFKGRSPMLNHLRKNFGFIGGSLQIGKALQEAHRTYFSAPANGRDKKQFPPILVVLASSESEDNVEEASKALRKDGVKIISVGVQKASEENLKAMATSQFHFNLRTVRDLSMFSQNMTHIIKDVIKYKEGAVDDIFVEACQGPSMADVVFLLDMSINGSEENFDYLKGFLEESVSALDIKENCMRVGLVAYSNETKVINSLSMGINKSEVLQHIQNLSPRTGKAYTGAAIKKLRKEVF... | null | null | cell adhesion [GO:0007155] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576] | extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01391;PF00092; | 1.20.5.320;3.40.50.410; | Type VI collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Deposed in the extracellular matrix of skeletal muscle. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}. | Homo sapiens (Human) |
A6NNB3 | IFM5_HUMAN | MDTAYPREDTRAPTPSKAGAHTALTLGAPHPPPRDHLIWSVFSTLYLNLCCLGFLALAYSIKARDQKVVGDLEAARRFGSKAKCYNILAAMWTLVPPLLLLGLVVTGALHLARLAKDSAAFFSTKFDDADYD | null | null | bone mineralization [GO:0030282]; bone morphogenesis [GO:0060349]; in utero embryonic development [GO:0001701]; regulation of bone mineralization [GO:0030500] | cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886] | null | PF04505; | null | CD225/Dispanin family | PTM: Palmitoylated. {ECO:0000250|UniProtKB:O88728}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24519609}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Required for normal bone mineralization. {ECO:0000269|PubMed:24519609}. | Homo sapiens (Human) |
A6NNM8 | TTL13_HUMAN | MEPSTCRTMESEEDYVEEKESEKCVKEGVTNPSNSSQQALLKADYKALKNGVPSPIMATKIPKKVIAPVDTGDLEAGRRKRRRKRRSLAINLTNCKYESVRRAAQMCGLKEVGEDEEWTLYWTDCAVSLERVMDMKRFQKINHFPGMTEICRKDLLARNLNRMYKLYPSEYNIFPRTWCLPADYGDFQSYGRQRKARTYICKPDSGCQGRGIFITRNPREIKPGEHMICQQYISKPLLIDGFKFDMRVYVLITSCDPLRIFTYEEGLARFATTPYMEPSHNNLDNVCMHLTNYAINKHNENFVRDGAVGSKRKLSTLNIW... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | microtubule cytoskeleton organization [GO:0000226]; protein modification process [GO:0036211] | cilium [GO:0005929]; cytosol [GO:0005829]; microtubule [GO:0005874] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.470.20; | Tubulin--tyrosine ligase family | null | null | CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEB... | null | null | null | null | FUNCTION: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates ATP-dependent polyglutamate side-chain elongation of the polyglutamylation reaction but not the initiation... | Homo sapiens (Human) |
A6NNN8 | S38A8_HUMAN | MEGQTPGSRGLPEKPHPATAAATLSSMGAVFILMKSALGAGLLNFPWAFSKAGGVVPAFLVELVSLVFLISGLVILGYAAAVSGQATYQGVVRGLCGPAIGKLCEACFLLNLLMISVAFLRVIGDQLEKLCDSLLSGTPPAPQPWYADQRFTLPLLSVLVILPLSAPREIAFQKYTSILGTLAACYLALVITVQYYLWPQGLVRESHPSLSPASWTSVFSVFPTICFGFQCHEAAVSIYCSMRKRSLSHWALVSVLSLLACCLIYSLTGVYGFLTFGTEVSADVLMSYPGNDMVIIVARVLFAVSIVTVYPIVLFLGRSV... | null | null | amino acid transmembrane transport [GO:0003333] | axon [GO:0030424]; cell cortex [GO:0005938]; membrane [GO:0016020] | L-amino acid transmembrane transporter activity [GO:0015179] | PF01490; | null | Amino acid/polyamine transporter 2 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q5HZH7}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q5HZH7}. Cell projection, axon {ECO:0000250|UniProtKB:Q5HZH7}. | CATALYTIC ACTIVITY: Reaction=L-glutamine(out) = L-glutamine(in); Xref=Rhea:RHEA:73419, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q5HZH7}; CATALYTIC ACTIVITY: Reaction=L-alanine(in) = L-alanine(out); Xref=Rhea:RHEA:70719, ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q5HZH7}; CATALYTIC ACTIVITY: Reaction=L... | null | null | null | null | FUNCTION: Electrogenic sodium-dependent amino acid transporter with a preference for L-glutamine, L-alanine, L-histidine, L-aspartate and L-arginine. May facilitate glutamine uptake in both excitatory and inhibitory neurons. The transport mechanism and stoichiometry remain to be elucidated. {ECO:0000250|UniProtKB:Q5HZH... | Homo sapiens (Human) |
A6NNY8 | UBP27_HUMAN | MCKDYVYDKDIEQIAKEEQGEALKLQASTSTEVSHQQCSVPGLGEKFPTWETTKPELELLGHNPRRRRITSSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCTSFWPMSPGRESSVNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAKQR... | 3.4.19.12 | null | defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of apoptotic process [GO:0043065]; positive regulation of type I interferon-mediated signaling pathway [GO:0060340]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linke... | cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; K48-linked deubiquitinase activity [GO:1990380]; K63-linked deubiquitinase activity [GO:0061578] | PF00443; | 3.90.70.10; | Peptidase C19 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CEG8}. Nucleus {ECO:0000250|UniProtKB:Q8CEG8}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:31534008, ECO:0000269|PubMed:32027733}; | null | null | null | null | FUNCTION: Deubiquitinase involved in innate antiviral immunity by mediating deubiquitination of CGAS and RIGI (PubMed:31534008, PubMed:32027733). Negatively regulates RIGI by mediating 'Lys-63'-linked deubiquitination of RIGI, inhibiting type I interferon signaling (PubMed:32027733). Also regulates 'Lys-63'-linked ubiq... | Homo sapiens (Human) |
A6NNZ2 | TBB8B_HUMAN | MREIVLTQTGQCGNQIGAKFWEVISDEHAIDSAGTYHGDSHLQLERINVHHHEASGGRYVPRAVLVDLEPGTMDSVHSGPFGQVFRPDNFISGQCGAGNNWAKGRYTEGAELTESVMDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIINTFSILPSPKVSDTVVEPYNATLSVHQLIENADETFCIDNEALYDICSRTLKLPTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVAELTQQMFDAKNMMAACDPRHGCYLTVAAIFRGR... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intercellular bridge [GO:0045171]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; mitotic spindle [GO:0072686] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Homo sapiens (Human) |
A6P320 | MARHB_RAT | MSDEGSKRGSRADSLEAEPPLPPPPPPPPPGESSLVPTSPRYRPPLPAPLERIVGSGEPPVELAPRRKGEPLPPLPPSRLPGDQEVSAAGDSCEGPRRLPEVKLPEAAAGKGSPAEPEAGACREGERRGTGDQPETRSVYSSRSSSSGGSGDQRSGHQHQHHQPICKICFQGAEQGELLNPCRCDGSVRYTHQLCLLKWISERGSWTCELCCYRYHVTAIKMKQPCQWQSISITLVEKVQMIAVILGSLFLIASVTWLLWSAFSPYAVWQRKDILFQICYGMYGFMDLVCIGLIVHEGAAVYRVFKRWRAVNLHWDVLNY... | 2.3.2.27 | null | protein ubiquitination [GO:0016567] | cytoplasmic vesicle membrane [GO:0030659] | ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF12906; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17604280}; Multi-pass membrane protein {ECO:0000269|PubMed:17604280}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase that mediates polyubiquitination of CD4. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May play a role in ubuquitin-dependent protein sorting in developmentin... | Rattus norvegicus (Rat) |
A6P3B2 | FMRF_MUSDO | MVAPLLVFLFSLQLCHTTSWAYVGGNSLNSNSLHASYSEFPAGTSNEVPEDAANGQDDNDDSQLTEPNDNNAPLVQSIDDETEMQFPKPIQWVSIDHLRNSIILRFQNPTPKILNKLDPEEMKRLRSLQENAMRWGKRSYESYPLNRNGLADKSSVGRMGFLSNHQVIRDSRGDNFMRFGRSVGGSGGNDDNFMRFGRASGSSDFMRFGRAGQDNFMRFGRAAGQDFMRFGRGSGQDFMRFGRSPGSQDFMRFGRNPGSQDFMRFGRSPGSQDFMRFGRNPGSQDFMRFGRNPGSQDFMRFGRNPGSQDFMRFGRASGGQ... | null | null | neuropeptide signaling pathway [GO:0007218] | extracellular region [GO:0005576] | null | PF01581; | null | FARP (FMRFamide related peptide) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | null | Musca domestica (House fly) |
A6P6V9 | CBDAS_CANSA | MKCSTFSFWFVCKIIFFFFSFNIQTSIANPRENFLKCFSQYIPNNATNLKLVYTQNNPLYMSVLNSTIHNLRFTSDTTPKPLVIVTPSHVSHIQGTILCSKKVGLQIRTRSGGHDSEGMSYISQVPFVIVDLRNMRSIKIDVHSQTAWVEAGATLGEVYYWVNEKNENLSLAAGYCPTVCAGGHFGGGGYGPLMRNYGLAADNIIDAHLVNVHGKVLDRKSMGEDLFWALRGGGAESFGIIVAWKIRLVAVPKSTMFSVKKIMEIHELVKLVNKWQNIAYKYDKDLLLMTHFITRNITDNQGKNKTAIHTYFSSVFLGGV... | 1.21.3.8 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q8GTB6}; Note=Binds 1 FAD per subunit in a bicovalent manner. {ECO:0000250|UniProtKB:Q8GTB6}; | cannabinoid biosynthetic process [GO:1901696]; terpenoid biosynthetic process [GO:0016114] | apoplast [GO:0048046] | cannabidiolate synthase activity [GO:0102779]; FAD binding [GO:0071949] | PF08031;PF01565; | 3.30.465.10;3.40.462.20;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | PTM: Glycosylated. {ECO:0000269|PubMed:17544411}.; PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:Q8GTB6}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8663284}. Secreted, extracellular space, apoplast {ECO:0000250}. Note=Probably sorted from the secretory cells into the storage cavity of glandular trichomes. | CATALYTIC ACTIVITY: Reaction=cannabigerolate + O2 = cannabidiolate + H2O2; Xref=Rhea:RHEA:34411, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:66962, ChEBI:CHEBI:67136; EC=1.21.3.8; Evidence={ECO:0000269|PubMed:17544411, ECO:0000269|PubMed:8663284}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34412; Eviden... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.137 mM for cannabigerolic acid {ECO:0000269|PubMed:8663284}; KM=0.206 mM for cannabinerolic acid {ECO:0000269|PubMed:8663284}; Vmax=2.57 nmol/sec/mg enzyme with cannabigerolic acid as substrate {ECO:0000269|PubMed:8663284}; Vmax=0.39 nmol/sec/mg enzyme with canna... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000303|PubMed:30468448}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:8663284}; | null | FUNCTION: Oxidoreductase involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (PubMed:17544411, PubMed:8663284). Catalyzes the stereoselective oxidative cyclization of the monoterpene moiety in cannabigerolic acid (CBGA), producing cannabidiolate (CB... | Cannabis sativa (Hemp) (Marijuana) |
A6P7H6 | FGF13_XENLA | MAAAIASSLIRQKRQAREREKSNACKCVSSPSKSKGNCEKNKLNVFSRVKLFGSKKRRRRRPEPQLKGIVTKLYSRQGYHLQLQPDGTIDGAKEEESSATVFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSEHFTPECKFKESVFENYYVTYSSMIYRQQHSGRSWFLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSQNDST | null | null | establishment of neuroblast polarity [GO:0045200]; head development [GO:0060322]; inhibitory synapse assembly [GO:1904862]; microtubule polymerization [GO:0046785]; negative regulation of collateral sprouting [GO:0048671]; negative regulation of microtubule depolymerization [GO:0007026]; neuron differentiation [GO:0030... | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; filopodium [GO:0030175]; growth cone [GO:0030426]; microtubule [GO:0005874]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383] | beta-tubulin binding [GO:0048487]; growth factor activity [GO:0008083]; microtubule binding [GO:0008017]; sodium channel regulator activity [GO:0017080]; transmembrane transporter binding [GO:0044325] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000250|UniProtKB:P70377}. Cell projection, growth cone {ECO:0000250|UniProtKB:P70377}. Cell projection, dendrite {ECO:0000250|UniProtKB:P70377}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P70377}. Cytoplasm {ECO:0000250|UniProtKB:P70377}. Note=Not secreted. ... | null | null | null | null | null | FUNCTION: Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules (By similarity). Through its action on microtubules, may participate in the refinement of axons by negatively regulating axonal and leading processes branching (By similarity). Pla... | Xenopus laevis (African clawed frog) |
A6PVC2 | TTLL8_HUMAN | MEPERKGLSLASSSDGDGREENKLKQGISQDLASSSRLDRYKIARQLTEKAIKEKKIFSIYGHYPVVRAALRRKGWVEKKFHFLPKVIPDVEDEGARVNDDTCAKVKENQEMALEKTDNIHDVMSRLVKNEMPYLLWTIKRDIIDYHSLTYDQMLNHYAKTASFTTKIGLCVNMRSLPWYVPANPDSFFPRCYSLCTESEQQEFLEDFRRTMASSILKWVVSHQSCSRSSRSKPRDQREEAGSSDLSSRQDAENAEAKLRGLPGQLVDIACKVCQAYLGQLEHEDIDTSADAVEDLTEAEWEDLTQQYYSLVHGDAFISN... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | cilium assembly [GO:0060271]; cilium movement [GO:0003341]; flagellated sperm motility [GO:0030317]; protein polyglycylation [GO:0018094] | axoneme [GO:0005930]; cilium [GO:0005929]; cytosol [GO:0005829]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; sperm flagellum [GO:0036126] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity [GO:0070735]; protein-glycine ligase activity, initiating [GO:0070736] | PF03133; | 3.30.470.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A4Q9F1}. Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9F1}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A4Q9F1}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A4Q9F1}. | CATALYTIC ACTIVITY: Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:45621... | null | null | null | null | FUNCTION: Monoglycylase which modifies both tubulin and non-tubulin proteins, adding a single glycine to the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of target proteins. Not involved in elongation step of the polyglycylation reaction. Preferenti... | Homo sapiens (Human) |
A6Q0K5 | CP12_CHLRE | MMLTKSVVISRPAVRPVSTRRAVVVRASGQPAVDLNKKVQDAVKEAEDACAKGTSADCAVAWDTVEELSAAVSHKKDAVKADVTLTDPLEAFCKDAPDADECRVYED | null | null | negative regulation of reductive pentose-phosphate cycle [GO:0080153]; positive regulation of protein-containing complex assembly [GO:0031334]; reductive pentose-phosphate cycle [GO:0019253] | chloroplast [GO:0009507]; protein-containing complex [GO:0032991]; supramolecular complex [GO:0099080] | copper ion binding [GO:0005507]; enzyme binding [GO:0019899]; molecular adaptor activity [GO:0060090]; nickel cation binding [GO:0016151] | PF02672; | null | CP12 family | PTM: Contains two disulfide bonds; only the oxidized protein, with two disulfide bonds, is active in complex formation. | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues. {ECO:0000269|PubMed:12846565}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A6QEK3 | HCHA_STAAE | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGINREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790] | PF01965; | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Staphylococcus aureus (strain Newman) |
A6QEP0 | CHDC_STAAE | MSQAAETLDGWYSLHLFYAVDWASLRIVPKDERDALVTEFQSFLENTATVRSSKSGDQAIYNITGQKADLLLWFLRPEMKSLNHIENEFNKLRIADFLIPTYSYVSVIELSNYLAGKSDEDPYENPHIKARLYPELPHSDYICFYPMNKRRNETYNWYMLTMEERQKLMYDHGMIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFFVGHIINTNEFDQFFAIS | 1.3.98.5 | COFACTOR: Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:27936663}; Note=Fe-coproporphyrin III acts both as a substrate and redox cofactor (Probable). Was originally thought to use heme as a cofactor (PubMed:23737523). {ECO:0000269|PubMed:23737523, ECO:... | heme biosynthetic process [GO:0006783] | null | heme binding [GO:0020037]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF06778; | null | ChdC family, Type 1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Fe-coproporphyrin III + 2 H(+) + 2 H2O2 = 2 CO2 + 4 H2O + heme b; Xref=Rhea:RHEA:56516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:60344, ChEBI:CHEBI:68438; EC=1.3.98.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:26083961, ECO:... | null | PATHWAY: Porphyrin-containing compound metabolism; protoheme biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:23737523, ECO:0000305|PubMed:26083961}. | null | null | FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:26083961). Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway (PubMed:26083961, PubMed:27936663, PubMed:27982566). The reaction occurs in a stepwise manner with a three-propi... | Staphylococcus aureus (strain Newman) |
A6QG31 | ISDA_STAAE | MTKHYLNSKYQSEQRSSAMKKITMGTASIILGSLVYIGADSQQVNAATEATNATNNQSTQVSQATSQPINFQVQKDGSSEKSHMDDYMQHPGKVIKQNNKYYFQTVLNNASFWKEYKFYNANNQELATTVVNDNKKADTRTINVAVEPGYKSLTTKVHIVVPQINYNHRYTTHLEFEKAIPTLADAAKPNNVKPVQPKPAQPKTPTEQTKPVQPKVEKVKPTVTTTSKVEDNHSTKVVSTDTTKDQTKTQTAHTVKTAQTAQEQNKVQTPVKDVATAKSESNNQAVSDNKSQQTNKVTKHNETPKQASKAKELPKTGLTS... | null | null | null | extracellular region [GO:0005576] | metal ion binding [GO:0046872] | PF00746;PF05031; | 2.60.40.1850; | IsdA family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:19398548}; Peptidoglycan-anchor {ECO:0000305}. Note=Encodes an LPXTG motif-containing sorting signal that targets to the cell wall, which is catalyzed by sortase A. {ECO:0000305|PubMed:12574635}. | null | null | null | null | null | FUNCTION: Cell wall-anchored surface receptor that participates in the extraction of heme from oxidized methemoglobin/metHb to enable growth on hemoglobin as a sole iron source (PubMed:12574635, PubMed:17229211). Receives heme from IsdB and transfers it to IsdC (By similarity). Plays also a role in the inhibition of ho... | Staphylococcus aureus (strain Newman) |
A6QGC0 | PRKC_STAAE | MIGKIINERYKIVDKLGGGGMSTVYLAEDTILNIKVAIKAIFIPPREKEETLKRFEREVHNSSQLSHQNIVSMIDVDEEDDCYYLVMEYIEGPTLSEYIESHGPLSVDTAINFTNQILDGIKHAHDMRIVHRDIKPQNILIDSNKTLKIFDFGIAKALSETSLTQTNHVLGTVQYFSPEQAKGEATDECTDIYSIGIVLYEMLVGEPPFNGETAVSIAIKHIQDSVPNVTTDVRKDIPQSLSNVILRATEKDKANRYKTIQEMKDDLSSVLHENRANEDVYELDKMKTIAVPLKKEDLAKHISEHKSNQPKRETTQVPIV... | 2.7.11.1 | null | cellular response to peptidoglycan [GO:0071224]; negative regulation of collateral sprouting [GO:0048671]; positive regulation of autophagy [GO:0010508]; protein phosphorylation [GO:0006468]; response to starvation [GO:0042594]; signal transduction [GO:0007165]; spore germination [GO:0009847] | autophagosome [GO:0005776]; cytosol [GO:0005829]; phagophore assembly site membrane [GO:0034045]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; peptidoglycan binding [GO:0042834]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF03793;PF00069;PF21160; | 2.60.40.2560;3.30.10.20;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Spore membrane; Single-pass type II membrane protein. Note=Is associated with the inner membrane of the spore. {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: Probable protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing either m-Dpm (meso-diaminopimelate) or L-lys, which act as spore germinants. Probably... | Staphylococcus aureus (strain Newman) |
A6QIG7 | CHIPS_STAAE | MKKKLATTVLALSFLTAGISTHHHSAKAFTFEPFPTNEEIESNKKMLEKEKAYKESFKNSGLPTTLGKLDERLRNYLKKGTKNSAQFEKMVILTENKGYYTVYLNTPLAEDRKNVELLGKMYKTYFFKKGESKSSYVINGPGKTNEYAY | null | null | null | extracellular region [GO:0005576] | null | PF11434; | 3.10.20.390; | CHIPS/FLIPr family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14993252}. | null | null | null | null | null | FUNCTION: Involved in countering the first line of host defense mechanisms. Specifically inhibits the response of human neutrophils and monocytes to complement anaphylatoxin C5a and formylated peptides, like N-formyl-methionyl-leucyl-phenylalanine (fMLP). Acts by binding directly to the C5a receptor (C5aR) and formylat... | Staphylococcus aureus (strain Newman) |
A6QL29 | AGNO1_BFPYV | MSTPARDPNTAGTAALSPFSTPNHELRAPGPGEAHSPFTPTAAPGSQPAGSLSDPEDGPDPTFNFYIQGHRRRPYDRQNRFGKLESEIRETKSQLETLRQELKHLQADVDDLKETVYAAGTSTASTSVPPSQPNSPTPTATTPEASPAAPTTESTETTGPSVATNATEPSESRPAR | null | null | null | host cell nucleus [GO:0042025]; virion component [GO:0044423] | null | null | null | null | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:11257197}. Host nucleus {ECO:0000269|PubMed:11257197}. | null | null | null | null | null | null | Budgerigar fledgling disease virus (BFPyV) (Aves polyomavirus 1) |
A6QLE5 | NLRP3_BOVIN | MRMVSVRCKLARYLEDLEDIDFKKFKMHLEDYPSQKGCTSIPRGQTEKADHVDLATLMIDFNGEEKAWAMAKWIFAAINRRDLYEKAKREEPEWENANISVLSQEESLEEEWMGLLGYLSRISICRKKKDYCKKYRKYVRSKFQCIKDRNARLGESVNLNKRFTRLRLIKEHRSQQEREHELLAIGRTWAKIQDSPVSSVNLELLFDPEDQHSEPVHTVVFQGAAGIGKTILARKIMLDWASEKLYQDRFDYLFYIHCREVSLGTQRSLGDLIASCCPGPNPPIGKIVSKPSRILFLMDGFDELQGAFDEHTEALCTNWR... | 3.6.4.- | null | detection of biotic stimulus [GO:0009595]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; NLRP3 inflammasome complex assembly [GO:0044546]; positive... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; interphase microtubule organizing center [GO:0031021]; membrane [GO:0016020]; mitochondrion [GO:0005739]; NLRP3 inflammasome complex [GO:0072559]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA-binding transcription factor binding [GO:0140297]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylinositol-4-phosphate binding [GO:0070273]; sequence-specific DNA binding [GO:0043565]; signaling adaptor activ... | PF14484;PF13516;PF05729;PF17776;PF17779;PF02758; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: Phosphorylation at Ser-198 by MAPK8/JNK1 increases inflammasome activation by promoting deubiquitination by BRCC3 and NLRP3 homooligomerization. Phosphorylation at Ser-801 by CSNK1A1 prevents inflammasome activation by preventing NEK7 recruitment. Phosphorylation at Ser-5 in the pyrin domain inhibits homomultimeri... | 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... | Bos taurus (Bovine) |
A6QLI1 | VGLU2_BOVIN | MESVKQRILTPGKEGLKNFAGKSLGQIYRVLEKKQDAGETIELTEDGKPLEVPEKKAPLCDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVDMVNNSTIHRGGKVIKEKAKFNWDPETVGMIHGSFFWGYIITQIPGGYIASRLAANRVFGAAILLTSTLNMLIPSAARVHYGCVIFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTSFCGSYAGAVIAMPLAGILVQYTGWSSVFYVYGSFGMIWYMFWLLVSYESPAKHPTITDEERRYIEESIGESANLLGAMEKFKTPWRKFFTSMPVYAIIVANF... | null | null | hyaloid vascular plexus regression [GO:1990384]; L-glutamate import [GO:0051938]; L-glutamate transmembrane transport [GO:0015813]; monoatomic anion transport [GO:0006820]; neurotransmitter loading into synaptic vesicle [GO:0098700]; phosphate ion homeostasis [GO:0055062]; phosphate ion transport [GO:0006817]; regulati... | chloride channel complex [GO:0034707]; excitatory synapse [GO:0060076]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672] | chloride channel activity [GO:0005254]; L-glutamate transmembrane transporter activity [GO:0005313]; L-glutamate uniporter activity [GO:0140788]; neurotransmitter transmembrane transporter activity [GO:0005326]; potassium:proton antiporter activity [GO:0015386]; sodium:phosphate symporter activity [GO:0005436] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Sodium/anion cotransporter family, VGLUT subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q8BLE7}; Multi-pass membrane protein {ECO:0000255}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q8BLE7}. Cell membrane {ECO:0000250|UniProtKB:Q8BLE7}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:Q9JI12}; CATALYTIC ACTIVITY: Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in); Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; Evidence={ECO:0000250|U... | null | null | null | null | FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as a uniporter which transports preferentially L-glutamate but also, phosphate from the cytoplasm into synaptic vesicle... | Bos taurus (Bovine) |
A6QLJ0 | ERCC2_BOVIN | MKLNVDGLLVYFPYDYIYPEQFSYMLELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLSFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQRDSSLPHCRFYEEFDVHGRQVPLPTGIYNLDDLKAVGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQANLETLQKTVLRIKETDEQRLREEYRRLVEGLREASAARETDAHLANPVLPDEVLKEAVP... | 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; | chromosome segregation [GO:0007059]; hair cell differentiation [GO:0035315]; nucleotide-excision repair [GO:0006289]; positive regulation of mitotic recombination [GO:0045951]; regulation of mitotic cell cycle phase transition [GO:1901990]; response to oxidative stress [GO:0006979]; transcription by RNA polymerase II [... | CAK-ERCC2 complex [GO:0070516]; cytoplasm [GO:0005737]; MMXD complex [GO:0071817]; nucleus [GO:0005634]; spindle [GO:0005819]; transcription factor TFIIH holo complex [GO:0005675] | 4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; metal ion binding [GO:0046872] | PF06733;PF06777;PF13307; | 3.40.50.300; | Helicase family, RAD3/XPD subfamily | PTM: ISGylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. | 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; | null | null | null | null | FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH a... | Bos taurus (Bovine) |
A6QLP2 | SAHH3_BOVIN | MSVQVVSAAAAAKVPEVELKDLSPSEAEPQLGLSTAAVSAMAPPAGGGDPEAPAPAAERPPAPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVKKQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNSKGNSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVEGWQPNMILDDGGDLTHWIYK... | 3.13.2.1 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Note=Binds 1 NAD(+) per subunit.; | one-carbon metabolic process [GO:0006730]; S-adenosylmethionine cycle [GO:0033353] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783] | hydrolase activity [GO:0016787] | PF05221;PF00670; | 3.40.50.1480;3.40.50.720; | Adenosylhomocysteinase family | PTM: Phosphorylated during neuronal differentiation at the LISN domain. {ECO:0000250|UniProtKB:Q68FL4}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24472682}. Microsome {ECO:0000250|UniProtKB:Q68FL4}. Note=Associates with membranes when phosphorylated, probably through interaction with ITPR1. {ECO:0000250|UniProtKB:Q68FL4}. | CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1; | null | PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. | null | null | FUNCTION: May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate (By similarity). {ECO:0000250|UniProtKB:Q96HN2, ECO:0000269|PubMed:24472682}. | Bos taurus (Bovine) |
A6QLT2 | MTMR2_BOVIN | MEKSSSCESLGSQPAVARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSAENFSPDLRVLRESNKLAEMEEPPLLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNNLSLFAFEYKEVFPENGWKLYDSLSEYRRQGIPNESWRITKVNERYELCDTYPALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFD... | 3.1.3.64; 3.1.3.95 | null | myelin assembly [GO:0032288]; negative regulation of myelination [GO:0031642]; neuron development [GO:0048666]; phosphatidylinositol dephosphorylation [GO:0046856]; regulation of phosphatidylinositol dephosphorylation [GO:0060304] | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; vacuolar membrane [GO:0005774] | identical protein binding [GO:0042802]; phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438] | PF02893;PF06602; | 2.30.29.30; | Protein-tyrosine phosphatase family, Non-receptor class myotubularin subfamily | PTM: Phosphorylation at Ser-58 decreases MTMR2 localization to endocytic vesicular structures. {ECO:0000250|UniProtKB:Q13614}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13614}. Early endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13614}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2D1}. Endosome membrane {ECO:0... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence={ECO:0000250|UniProtKB:Q13614}; CA... | null | null | null | null | FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity). Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and pho... | Bos taurus (Bovine) |
A6QLT4 | MTM1_BOVIN | MASAPTSKYNSHSLENESIKRTSRDGVNRDVGETLPRLPGEIRITDKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGVISRIEKMGGATSRGENSYGLDITCKDLRNLRFALKQEGHSRRDMFEILTRYAFPLAHSLPIFAFLNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRITFINKCYKLCDTYPALLVVPYRASDEDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKEDERYLDVIRETNRQVNKLTIYDARPNVNAVANKATGGGYESDDVYHNAELFFLDIHNIHVMRES... | 3.1.3.64; 3.1.3.95 | null | endosome to lysosome transport [GO:0008333]; intermediate filament organization [GO:0045109]; mitochondrion distribution [GO:0048311]; mitochondrion organization [GO:0007005]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of autophagosome assembly [GO:1902902]; phosphatidylinositol dephosphorylatio... | cytoplasm [GO:0005737]; filopodium [GO:0030175]; late endosome [GO:0005770]; membrane [GO:0016020]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; sarcomere [GO:0030017] | intermediate filament binding [GO:0019215]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphoprotein phosphatase activity [GO:0004721] | PF02893;PF06602; | 2.30.29.30; | Protein-tyrosine phosphatase family, Non-receptor class myotubularin subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13496}. Cell membrane {ECO:0000250|UniProtKB:Q13496}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13496}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q13496}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q13496}. Late endosome {ECO:0000250|UniProt... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence={ECO:0000250|UniProtKB:Q13496}; CA... | null | null | null | null | FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides. Negatively regulates EGFR degradation through regulation of EGFR traffickin... | Bos taurus (Bovine) |
A6QLW8 | S22A7_BOVIN | MGFEELLDKVGGFGPFQLRNVALLALPRVLLPMHFLLPIFLAAVPAHRCALPGVPDNFSNEDAWLEAHLPREPDGRLSACLRFTHPQALPNSTLWGEGQNSGEQPEGEPSTVPCPQGWEYNHSEFSSTIATEWDLVCEQKGLNKAISTFFFAGVLVGAEVYGYLSDRFGRRRLLLVAYVSSLALGLASAASVSYIMFAITRTLTGMALAGFTIIVMPLELEWLDVRHRTVAGVLSSTFWTGGVMLLALIGYLIRDWRWLLLTVTLPCVPGILTLWWVPESARWLLTQGRVEEAHRYLLRCARLNGPPVGEDSLSREALNK... | null | null | alpha-ketoglutarate transport [GO:0015742]; monoatomic ion transport [GO:0006811]; prostaglandin transport [GO:0015732] | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886] | alpha-ketoglutarate transmembrane transporter activity [GO:0015139]; organic anion transmembrane transporter activity [GO:0008514]; prostaglandin transmembrane transporter activity [GO:0015132]; sodium-independent organic anion transmembrane transporter activity [GO:0015347]; transmembrane transporter activity [GO:0022... | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-glutamate(in) + orotate(out) = L-glutamate(out) + orotate(in); Xref=Rhea:RHEA:72043, ChEBI:CHEBI:29985, ChEBI:CHEBI:30839; Evidence={ECO:0000250|UniProtKB:Q9Y694}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP(in) = 3',5'-cyclic GMP(out); Xref=Rhea:RHEA:76207, ChEBI:CHEBI:57746; Evidence=... | null | null | null | null | FUNCTION: Functions as a Na(+)-independent bidirectional multispecific transporter. Contributes to the renal and hepatic elimination of endogenous organic compounds from the systemic circulation into the urine and bile, respectively. Capable of transporting a wide range of purine and pyrimidine nucleobases, nucleosides... | Bos taurus (Bovine) |
A6QNM7 | UBP33_BOVIN | MSSFRSHCPHLDSVGEITKEDLIQKSHGSCQDCKVRGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTQPSLPHVKPLHQIQENGVQDFKIPSNTTLKTPLVAVFDDLDIEVEEEDELKARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEVEEDPQTIMTEETMEEDKSQSDVDFQSCESCSSSDKAENENGSRSFSEDNNETTMLIQ... | 3.4.19.12 | null | axon guidance [GO:0007411]; cell migration [GO:0016477]; centrosome duplication [GO:0051298]; endocytosis [GO:0006897]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; regulation of G protein-coupled rec... | centrosome [GO:0005813]; perinuclear region of cytoplasm [GO:0048471] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; zinc ion binding [GO:0008270] | PF06337;PF00443;PF02148; | 3.90.70.10;3.30.2230.10;3.30.40.10; | Peptidase C19 family, USP20/USP33 subfamily | PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; | null | null | null | null | FUNCTION: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period w... | Bos taurus (Bovine) |
A6QP16 | ZRAN1_BOVIN | MSERGIKWACEYCTYENWPSAIKCTMCRAQRPSGTIITEDPFKSGSSDVGRDWDPSSTEGGSSPLICPDSSARPRVKSSYSMENANKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGSRPVAFSVDPCEEYNDRNKLNTRTQHWTCSICTYENWAKAKKCVVCDHPRPNNIEAIEFAETEEASSIINEQDRARWRGSCSSGNSQRRSPPTMKRDSEVKMDFQRIELAGAVGSKEELEVDFKKLKQIKNRMKKTDWLFLNACVGVVEGDLAAIEAYKSSGGDIARQLTADEVRLLNRPSAFDVGYTLVHLAI... | 3.4.19.12 | null | cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; positive regulation of Wnt signaling pathway [GO:0030177]; protein K29-linked deubiquitination [GO:0035523]; protein K33-linked deubiquitination [GO:1990168]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; regulation of ce... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872] | PF18418;PF02338;PF00641; | 1.25.40.560;4.10.1060.10; | Peptidase C64 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UGI0}. Nucleus {ECO:0000250|UniProtKB:Q9UGI0}. Note=Enriched in punctate localization in the cytoplasm. {ECO:0000250|UniProtKB:Q9UGI0}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9UGI0}; | null | null | null | null | FUNCTION: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates AP... | Bos taurus (Bovine) |
A6QP84 | SOAT_BOVIN | MRANCSSGLACPANSSEEELPEGLKAFGNLDLVFTVVSALMIGLLMFSLGCSVEVQKLWGHIRRPWGIAVGMLCQFGLMPLIAYLLIISFSLKPLQAIAVLIMGCCPGGTVSNIFTFWVDGDMDLSISMTTCSTMAALGMMPLCLYLYTLSWNLEQNLTIPYQNIGITLVCLIIPVAFGIYVNYRWPKQSKIILKIGAIAGGLLFLVVTGAGMVLMKEFWSSDIILLMISFIFPLIGHATGFLLALLTHQSWQRCRTISLETGTQNVQMCFTMLQLSFTAEQLVQIFGFVLAYGLFQMLNGFFMVAAYKMYKRRLKNKHG... | null | null | bile acid and bile salt transport [GO:0015721] | membrane [GO:0016020] | bile acid:sodium symporter activity [GO:0008508] | PF01758; | 1.20.1530.20; | Bile acid:sodium symporter (BASS) (TC 2.A.28) family | PTM: Glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) + 2 Na(+)(out) = estrone 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71083, ChEBI:CHEBI:29101, ChEBI:CHEBI:60050; Evidence={ECO:0000250|UniProtKB:Q3KNW5}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 3-sulfate(out) + 2 Na(+)(out) = 17beta-estradiol 3-sulfate(in) + 2 ... | null | null | null | null | FUNCTION: Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis. Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids (By similari... | Bos taurus (Bovine) |
A6QPB3 | COHA1_BOVIN | MDITQKNKRDGTEVTERIITETVTTRLTSLPPKGGTSNGYAKTGSLGGGSRLEKQSLTHGSSGYINSSGSLRGNASTSSYRRAHSPASTLPNSPGSTFERKTHVTRHGTYEGSSSGNSSPEYPRKEFASSSTRGRSQTRESEIRVRLQSASPSTRWTELDDVKRLLKGSRSASVSPTRNSSNTLPIPKKGTVETKVVTASSQSVSGTYDTTILDANLPSHVWSSTLPAGSSMGTYHNNITTQSSSLLNTNAYSAGSVFGVPNNMASCSATLQPGISTSSSVFGMQNNLAPSSSTLSHGMAATSTAYGVKKNMPQSPTAVS... | null | null | extracellular matrix organization [GO:0030198]; hemidesmosome assembly [GO:0031581] | basement membrane [GO:0005604]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; hemidesmosome [GO:0030056]; membrane [GO:0016020] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; heparin binding [GO:0008201] | PF01391; | 1.20.5.320; | null | PTM: The intracellular/endo domain is disulfide-linked. {ECO:0000250}.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: The ectodomain is shedded from the surface of keratinocytes resulting in a 120-kDa soluble form, also named as 120 kDa... | SUBCELLULAR LOCATION: Cell junction, hemidesmosome {ECO:0000269|PubMed:9545306}. Membrane {ECO:0000269|PubMed:9545306}; Single-pass type II membrane protein {ECO:0000269|PubMed:9545306}. Note=Localized along the plasma membrane of the hemidesmosome. {ECO:0000250}.; SUBCELLULAR LOCATION: [120 kDa linear IgA disease anti... | null | null | null | null | null | FUNCTION: May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane. {ECO:0000250}.; FUNCTION: The 120 kDa linear IgA disease antigen homolog is an anchoring filament component involved in dermal-epidermal cohesion. {ECO:0000269|PubMed:12761182}. | Bos taurus (Bovine) |
A6QQJ8 | ZC12A_BOVIN | MSLWELEDRRSCQGTPRPAQEPTAEEATTAELQMKVDFFRKLGYSSAEIHSVLQKLGIQADTNTVLGELVKHGSAAERERQASPDPCPQLPLVPRGGGTPKAPTVETYPPEEDKEGSDLRPIVIDGSNVAMSHGNKDVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRDLEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAFESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTSEHKKQPCPYGRKCTYGIKCRFLHPERPSRPQRSVADE... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q5D1E8}; Note=Mg(2+) is required for RNase activity. {ECO:0000250|UniProtKB:Q5D1E8}; | 3'-UTR-mediated mRNA destabilization [GO:0061158]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; cellular response to chemokine [GO:1990869]; cellular response to ionomycin [GO:1904637]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to tumor necr... | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]; P-body [GO:0000932]; rough endoplasmic reticulum membrane [GO:0030867] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; miRNA binding [GO:0035198]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; nuclease activity [GO:0004518]; RNA endonuclease activity [GO:0004521]; RNA exonuclease acti... | PF18561;PF11977;PF18039; | 3.40.50.11980; | ZC3H12 family | PTM: Phosphorylated by IRAK1; phosphorylation is necessary for subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex. Phosphorylated by I-kappa-B-kinase (IKK) subunits IKBKB/IKKB and CHUK/IKKA at Ser-422 and Ser-426; these phosphorylations promote ubiquitin proteasome-mediated degradation of ZC3H12A and henc... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5D1E8}. Cytoplasm {ECO:0000250|UniProtKB:Q5D1E8}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q5D1E8}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5D1E7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5D1E7}; Cytoplasmic side {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay. Modulates the inflammat... | Bos taurus (Bovine) |
A6QQL0 | S15A4_BOVIN | MEGAGDERAPLLGARRTAFAGRRAACAAVLLTELLERAAFYGVTANLVLFLNGTAFGWEGAEASQALLLFMGLTYLVSPFGGWLADARLGRARAILLSLALYLLGMLAFPLLAAPATRSALCGAPGPTNVRNCSAPPCTDTPTRYCAPAVLSALALVGLGVGAVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAIVSLGGIAYIQQNVSFVTGYAIPAVCIGVAFVVFLCGQTFFITKPPDGSAFTDMFRILVYSCRPQKRIREHSPSGEGIGVFQQSSKHSLFDSCKMSRGGPFPEDKVEDVKALVKIVPVFLA... | null | null | dipeptide import across plasma membrane [GO:0140206]; histidine transport [GO:0015817]; innate immune response [GO:0045087]; mast cell homeostasis [GO:0033023]; peptidoglycan transport [GO:0015835]; positive regulation of innate immune response [GO:0045089]; positive regulation of nucleotide-binding oligomerization dom... | early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; lysosomal membrane [GO:0005765]; membrane [GO:0016020] | dipeptide transmembrane transporter activity [GO:0071916]; L-histidine transmembrane transporter activity [GO:0005290]; peptide:proton symporter activity [GO:0015333]; peptidoglycan transmembrane transporter activity [GO:0015647] | PF00854; | 1.20.1250.20; | Major facilitator superfamily, Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8N697}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q8N697}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q91W98}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=glycylglycylglycine(out) + n H(+)(out) = glycylglycylglycine(in) + n H(+)(in); Xref=Rhea:RHEA:76391, ChEBI:CHEBI:15378, ChEBI:CHEBI:195214; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76392; Evidence={ECO:0000250|UniProtKB:Q8N697}; CATALYTIC... | null | null | null | null | FUNCTION: Proton-coupled amino-acid transporter that mediates the transmembrane transport of L-histidine and some di- and tripeptides from inside the lysosome to the cytosol, and plays a key role in innate immune response. Able to transport a variety of di- and tripeptides, including carnosine and some peptidoglycans (... | Bos taurus (Bovine) |
A6QR55 | UBP4_BOVIN | MAEGGGYRERPDAETQKSELGALMRTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLYPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPAEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQNEDGTWPRQTQQSKSSTAPSRNFTTSPKSSASPYSSVSASPIANGDSTNTSGMHSSGVSRGGSGFSASYNCQESPLTHVQPGLCGLGNLGNTCFMNSALQCL... | 3.4.19.12 | null | negative regulation of protein ubiquitination [GO:0031397]; positive regulation of TORC1 signaling [GO:1904263]; protein deubiquitination [GO:0016579]; protein localization to cell surface [GO:0034394]; proteolysis [GO:0006508]; regulation of protein stability [GO:0031647]; spliceosomal tri-snRNP complex assembly [GO:0... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872] | PF06337;PF14836;PF00443; | 3.90.70.10;3.30.2230.10; | Peptidase C19 family, USP4 subfamily | PTM: Phosphorylated at Ser-445 by PKB/AKT1 in response to EGF stimulus, promoting its ability deubiquitinate RHEB. {ECO:0000250|UniProtKB:Q13107}.; PTM: Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated. {ECO:0000250|UniProtKB:Q13107}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Nucleus {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Note=Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alph... | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q13107}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins. Deubiquitinates PDPK1. Deubiquitinates TRIM21. Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface. Deubiquitinates HAS2. Deubiquitinates RHEB in response to EGF signaling, promot... | Bos taurus (Bovine) |
A6R8Q8 | ARO1_AJECN | MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYVLISDTNLTPLYLEGFQKSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECISIGMVKEAELARHLGILNNVSVSRISKCL... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum) |
A6RYB8 | ATG1_BOTFB | MASTTTSTSSLSSRRQKTGVGSFTINEQIGKGSFATVYRGTHMPSGNLVAIKSVNLSRLNKKLKDNLYVEIEILKSLYHPHIVALIDCRESASHIHLMMEYCELGDLSYFIKKRDRLADNPTLYDMVQKYPMPVEGGLNQVVVRHFFKQLSSAMEFLRERDFVHRDVKPQNLLLIPSPEWIAKRAKGGPEAMKASKESVVAMVGINSLPMLKLADFGFARSLPSTSLAETLCGSPLYMAPEILRYEKYDARADLWSIGTVLYEMMTGRPPFKAINHVQLLQKIEKNQDEIRFPSRGIYSRDLKDIVRRLLKKKPEDRITF... | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:004259... | Atg1/ULK1 kinase complex [GO:1990316]; autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; phagophore [GO:0061908]; phagophore assembly site membrane [GO:0034045]; vacuole-isolation membrane contact site [GO:0120095] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | 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:P53104}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective a... | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
A6T7D6 | PYRC_KLEP7 | MTAQSQVLKIRRPDDWHIHLRDDDMLKTVVPYTSEFYGRAIVMPNLVPPVTTVAAAIAYRQRIMDAVPAGHDFTPLMTCYLTDSLDPAELERGFNEGVFTAAKLYPANATTNSSHGVTSTDAIMPVLERMEKLGMPLLVHGEVTHAEIDIFDREARFIETVMEPLRQRLPGLKVVFEHITTKDAAEYVRDGNELLAATITPQHLMFNRNHMLVGGIRPHLYCLPVLKRNIHQQALRELVASGFSRAFLGTDSAPHARHRKEASCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSLNGPRFYGLPVNESYVELVREET... | 3.5.2.3 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00219}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:20676924}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20676924}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:20676924}... | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205] | cytosol [GO:0005829] | dihydroorotase activity [GO:0004151]; zinc ion binding [GO:0008270] | PF01979; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, DHOase family, Class II DHOase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for dihydroorotate {ECO:0000269|PubMed:20676924}; Vmax=8.87 umol/min/mg enzyme {ECO:0000269|PubMed:20676924}; | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00219}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:20676924}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 60 degrees Celsius. {ECO:0000269|PubMed:20676924}; | FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6T923 | HPXO_KLEP7 | MKAIVIGAGIGGLSAAVALKQSGIDCDVYEAVKEIKPVGAAISVWPNGVKCMAHLGMGDIMETFGGPLRRMAYRDFRSGENMTQFSLAPLIERTGSRPCPVSRAELQREMLDYWGRDSVQFGKRVTRCEEDADGVTVWFTDGSSASGDLLIAADGSHSALRPWVLGFTPQRRYAGYVNWNGLVEIDEALAPGDQWTTFVGEGKRVSLMPVSAGRFYFFFDVPLPAGLAEDRDTLRADLSRYFAGWAPPVQKLIAALDPQTTNRIEIHDIEPFSRLVRGRVALLGDAGHSTTPDIGQGGCAAMEDAVVLGAVFRQTRDIAA... | 1.14.13.113 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:19260710}; | purine nucleobase metabolic process [GO:0006144]; urate catabolic process [GO:0019628] | null | FAD binding [GO:0071949]; FAD-dependent urate hydroxylase activity [GO:0102099]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; urate oxidase activity [GO:0004846] | PF01494; | 3.50.50.60; | FAD-dependent urate hydroxylase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + O2 + urate = 5-hydroxyisourate + H2O + NAD(+); Xref=Rhea:RHEA:27329, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.113; Evidence={ECO:0000269|PubMed:19260710}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42 uM for urate {ECO:0000269|PubMed:19260710}; Note=kcat is 42 sec(-1). {ECO:0000269|PubMed:19260710}; | PATHWAY: Purine metabolism; urate degradation. {ECO:0000269|PubMed:19260710}. | null | null | FUNCTION: Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU). {ECO:0000269|PubMed:19260710}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TB83 | MTFA_KLEP7 | MFKWPWKADDESGNAEMPWEQALAIPVLAHLSSTEQHKLTQMAARFLQQKRLVALQGLELTPLHQARIAMLFCLPVLELGIEWLDGFHEVLIYPAPFIVDDEWEDDIGLVHNQRVVQSGQSWQQGPVVLNWLDIQDSFDASGFNLVVHEVAHKLDTRNGDRASGVPLIPLREVAGWEHDLHAAMNNIQDEIDLVGESAASIDAYAATDPAECFAVLSEYFFSAPELFAPRFPALWQRFCHFYRQDPLARRRENGLQDEGDRRIVH | 3.4.11.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01593, ECO:0000269|PubMed:22467785}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01593, ECO:0000269|PubMed:22467785}; | proteolysis [GO:0006508] | cytosol [GO:0005829] | aminopeptidase activity [GO:0004177]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270] | PF06167; | 3.40.390.10;1.10.472.150; | MtfA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01593}. | null | null | null | null | null | FUNCTION: Involved in the modulation of the activity of the glucose-phosphotransferase system (glucose-PTS). Interacts with the transcriptional repressor Mlc, preventing its interaction with DNA and leading to the modulation of expression of genes regulated by Mlc, including ptsG, which encodes the PTS system glucose-s... | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TBV3 | NUDI_KLEP7 | MRHRTIVCPLIENKGHYLLCKMAADRGVFPGQWALSGGVEPGERIEEALRREIREELGEKLILTHIAPWCFRDDTRVKTYPDGHQETIYMIYLIFNCVSANRDVTINEEFDDYAWVKAEDLKNYDLNAATRVTLSLKGLL | 3.6.1.-; 3.6.1.12; 3.6.1.23; 3.6.1.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; | DNA repair [GO:0006281] | null | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity [GO:0035539]; 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity [GO:0008413]; 8-oxo-dGDP phosphatase activity [GO:0044715]; 8-oxo-GDP phosphatase activity [GO:0044716]; dCTP diphosphatase activity [GO:0047840]; dTTP diphosphatase activ... | PF00293; | 3.90.79.10; | Nudix hydrolase family, NudI subfamily | null | null | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01846}; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP). {ECO:0000255|HAMAP-Rule:MF_01846}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TF07 | CYSG2_KLEP7 | MDHLPIFCQLRQRDCLLVGGGDVAERKARLLLDAGANVTVNALDFTPQFQVWADSQMLTLVQGEFIPSLLDNCWLAIAATDDETVNQQVSEAAEARRIFCNVVDAPRQASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESILPLHLGQLARYAGHLRARVKQQFATVGERRRFWEKLFVNDRLAQSLANDDRQAVADTTEQLLTEPLEHRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRSGYHCVPQEEINQILLREAQKGRRVVRLKGGDPFIFGRGGEELETLCEA... | 1.3.1.76; 2.1.1.107; 4.99.1.4 | null | cobalamin biosynthetic process [GO:0009236]; methylation [GO:0032259]; siroheme biosynthetic process [GO:0019354] | null | NAD binding [GO:0051287]; precorrin-2 dehydrogenase activity [GO:0043115]; sirohydrochlorin ferrochelatase activity [GO:0051266]; uroporphyrin-III C-methyltransferase activity [GO:0004851] | PF10414;PF13241;PF14824;PF00590; | 3.40.50.720;1.10.8.210; | Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family; Precorrin methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856, ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107; Evidence={ECO:0000255|HAMAP-Rule:MF_01646}; CATALYTIC ACTIV... | null | PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01646}.; PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01646}.; PATHWAY: Porphyrin-contain... | null | null | FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlo... | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TGM4 | FADB_KLEP7 | MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGHALDVLEKQSDLKGLLLRSEKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTISAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIAAGKDVGADQALKIGLVDGVVAAEKLRDGALAILRQAMNGDLDWKAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARLGREEALVLENKSFVPLAHTNEARALVGIFLNDQYVKAKAKKLTKDVETPKHAAVLG... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
A6TZ28 | HCHA_STAA2 | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790] | PF01965; | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Staphylococcus aureus (strain JH1) |
A6WE36 | XPB_KINRD | MTDGPLIVQSDKTLLLEVDHPRAGACRAAIAPFAELERAPEHVHTYRLTPLGLWNARAAGHDAEQVVDTLLEFSRYSVPHALLVDVAETMARYGRLQLVKDEEHGLVLRSLDPAVLEEVLRSRKSAPLLGTRIAPDAVLVHPSERGNLKQVLLKLGWPAEDLAGYVDGEAHAIDLAEDGWALRPYQSEAVDNFWNGGSGVVVLPCGAGKTLVGAAAMAKARATTLILVTNTVSARQWRDELLKRTSLTEDEIGEYSGARKEIRPVTIATYQVVTTKRKGVYPHLELFDARDWGLILYDEVHLLPAPIFRMTADLQARRRL... | 5.6.2.4 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19199647}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19199647}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:19199647}; Note=ATPase activity has a small preference for Mn(2+) over Mg(2+) or Ca(2+). C... | transcription initiation at RNA polymerase II promoter [GO:0006367] | transcription preinitiation complex [GO:0097550] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787] | PF16203;PF13625;PF04851; | 3.40.50.300; | Helicase family, RAD25/XPB subfamily | null | null | 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:0000269|PubMed:19199647}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:3061... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for 21-mer ssDNA substrate {ECO:0000269|PubMed:19199647}; KM=50 uM for 10-mer ssDNA substrate {ECO:0000269|PubMed:19199647}; | null | null | null | FUNCTION: ATP-dependent 3'-5' DNA helicase, unwinds 3'-overhangs, 3'- flaps, and splayed-arm DNA substrates but not 5'-overhangs or 5'-flap substrates (PubMed:19199647). Requires ATP hydrolysis for activity; the ATPase activity is DNA-dependent and requires a minimum of 4 single-stranded nucleotides (nt) with 6-10 nt p... | Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) |
A6X8Z5 | RHG31_MOUSE | MKNKGAKQKLKRKGAASAFGCDLTEYLESSGQDVPYVLKSCAEFIETHGIVDGIYRLSGITSNIQRLRQEFGSDQCPDLTREVYLQDIHCVGSLCKLYFRELPNPLLTYELYEKFTEAVSHRPEEGQLARIQNVILELPPPHYRTLEYLIRHLAHIASFSSKTNMHARNLALVWAPNLLRSKKIEATICNGDAAFLAVRVQQVVIEFILNHADQIFNGGAPGALQQDESRTITKSLTLPALSLPMKLVSLEEAQARSLATNHPARKERRENSLPEIVPPPFHTVLELPDNKRKLSSKSKKWKSIFNLGRSGSDSKSKLSR... | null | null | small GTPase-mediated signal transduction [GO:0007264] | focal adhesion [GO:0005925]; lamellipodium [GO:0030027] | GTPase activator activity [GO:0005096]; SH3 domain binding [GO:0017124] | PF00620; | 1.10.555.10; | null | PTM: Phosphorylated on Thr-776 by GSK3; which reduces GAP activity. {ECO:0000269|PubMed:16024771, ECO:0000269|PubMed:17158447}. | SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell junction, focal adhesion. | null | null | null | null | null | FUNCTION: Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration. {ECO:0000269|PubMed:16860736, ECO:0000269|PubMed:9786927}. | Mus musculus (Mouse) |
A6X935 | ITIH4_MOUSE | MKSPAPAHMWNLVLFLPSLLAVLPTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYSAAVGRGESAGIVKTTGRQTEKFEVSVNVAPGSKITFELIYQELLQRRLGMYELLLKVRPQQLVKHLQMDIYIFEPQGISILETESTFMTPELANALTTSQNKTKAHIRFKPTLSQQQKSQSEQDTVLNGDFIVRYDVNRSDSGGSIQIEEGYFVHHFAPENLPTMSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEAN... | null | null | acute-phase response [GO:0006953]; hyaluronan metabolic process [GO:0030212]; response to cytokine [GO:0034097] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF06668;PF08487;PF00092; | 3.40.50.410; | ITIH family | PTM: May be O-glycosylated (By similarity). N-glycosylated. {ECO:0000250, ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:17330941}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration. | Mus musculus (Mouse) |
A6XA80 | LTC4S_CAVPO | MKDEVALLATVTLLGVLLQAYFSLQVIRARRAHRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGVYFHEGAAALCGLVYLFTRLRYFWGYARSAQLRLAPLYASARALWLLLALATLGLLAHFLPAAARAALLRLLRALLRTA | 2.5.1.-; 4.4.1.20 | null | leukotriene biosynthetic process [GO:0019370]; leukotriene metabolic process [GO:0006691]; long-chain fatty acid biosynthetic process [GO:0042759] | endoplasmic reticulum membrane [GO:0005789]; nuclear membrane [GO:0031965]; nuclear outer membrane [GO:0005640] | enzyme activator activity [GO:0008047]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; leukotriene-C4 synthase activity [GO:0004464] | PF01124; | 1.20.120.550; | MAPEG family | PTM: Phosphorylation at Ser-36 by RPS6KB1 inhibits the leukotriene-C4 synthase activity. {ECO:0000250|UniProtKB:Q16873}. | SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Nucleus membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass ... | CATALYTIC ACTIVITY: Reaction=leukotriene C4 = glutathione + leukotriene A4; Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925, ChEBI:CHEBI:57973; EC=4.4.1.20; Evidence={ECO:0000250|UniProtKB:Q16873}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17619; Evidence={ECO:0000250|UniProtKB:Q16873}; CATALYTIC ... | null | PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis. {ECO:0000250|UniProtKB:Q16873}. | null | null | FUNCTION: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity. Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioacti... | Cavia porcellus (Guinea pig) |
A6XH05 | CINS1_SALFT | MSSLIMQVVIPKPAKFFHNNLFSLSSKRHRFSTTTTTRGGRWARCSLQTGNEIQTERRTGGYQPTLWDFSTIQSFDSEYKEEKHLMRAAGMIDQVKMMLQEEVDSIRRLELIDDLRRLGISCHFEREIVEILNSKYYTNNEIDERDLYSTALRFRLLRQYDFSVSQEVFDCFKNAKGTDFKPSLVDDTRGLLQLYEASFLSAQGEETLRLARDFATKFLQKRVLVDKDINLLSSIERALELPTHWRVQMPNARSFIDAYKRRPDMNPTVLELAKLDFNMVQAQFQQELKEASRWWNSTGLVHELPFVRDRIVECYYWTTG... | 4.2.3.-; 4.2.3.108; 4.2.3.111; 4.2.3.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | alpha-pinene biosynthetic process [GO:0046248]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; monoterpenoid biosynthetic process [GO:0016099] | chloroplast [GO:0009507] | 1,8-cineole synthase activity [GO:0102313]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; pinene synthase activity [GO:0050550]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate; Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32544; Evidence={ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=65.4 uM for (2E)-geranyl diphosphate {ECO:0000269|PubMed:17557809}; Note=kcat is 3.18 min(-1) with (2E)-geranyl diphosphate as substrate. {ECO:0000269|PubMed:17557809}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:17557809}. | null | null | FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products, components of the chemical defense arsenal (PubMed:17557809). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into 1,8-cineole, and, as minor products, alpha-terpineol, beta-pinene, alpha-pinene, sabinene and m... | Salvia fruticosa (Greek sage) |
A6XH06 | SABS1_SALPM | MPLNSLHNLERKPSKAWSTSCTAPAARLQASFSLQQEEPRQIRRSGDYQPSLWDFNYIQSLNTPYKEQRYVNRQAELIMQVRMLLKVKMEAIQQLELIDDLQYLGLSYFFPDEIKQILSSIHNEHRYFHNNDLYLTALGFRILRQHGFNVSEDVFDCFKTEKCSDFNANLAQDTKGMLQLYEASFLLREGEDTLELARRFSTRSLREKLDEDGDEIDEDLSSWIRHSLDLPLHWRIQGLEARWFLDAYARRPDMNPLIFKLAKLNFNIVQATYQEELKDVSRWWNSSCLAEKLPFVRDRIVECFFWAIGAFEPHQYSYQR... | 4.2.3.-; 4.2.3.15 | 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]; green leaf volatile biosynthetic process [GO:0010597]; monoterpenoid biosynthetic process [GO:0016099] | chloroplast [GO:0009507] | magnesium ion binding [GO:0000287]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene; Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17557809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637; Evidence={ECO:0000269|PubMed:17557809}; CATALYTIC ACTIVITY: R... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:17557809}. | null | null | FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products, components of the chemical defense arsenal (PubMed:17557809). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into sabinene, and, as minor products, myrcene (PubMed:17557809). {ECO:0000269|PubMed:17557809}. | Salvia pomifera (Apple sage) |
A6XIP3 | GP_HAZVJ | MEGSYWWLSLLALLAWGANGESTSPAETSPAPTTPNPPVVNPSLRRKIVNQRILSAMGMDSDPSNEALNGVCQSIHSNGCNANELKLRLADFFIDTNSSQCYDEILVKKPCSSLTPAHNSHWVPRGLDKSEVDKIFDTKLKLFFSQSRKVTCLSASALNPSQFVKHFQVKIQETSGPAKQSLRSLHCVNLVWSHSHKGEKEVVHVLQSAVPVKLKNCLAMLNFRQCYYNQQSEGPVVVPSYQHNGEKWVTGAYTMTVEVDKHADGPCEISTTCITEGSEIKPGVHSLRGFKTTLVIHGKRNTGRRLLSSSNARQECSSGT... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF20682;PF01561;PF20726;PF07948; | 1.10.8.1320; | Nairovirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavage by host MBTPS1/S1P/SKI-1 endopeptidase yield glycoprotein N. Specific enzymatic cleavages by host furin-like protease and MBTPS1/S1P endopeptidase yield GP38. {ECO:0000250|UniProtKB:Q8JSZ3}.; PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}.... | SUBCELLULAR LOCATION: [Envelopment polyprotein]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8JSZ3}.; SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JSZ3}. Host Golgi apparatus membrane {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Glycoprotein N and glycoprotein C interact with each other and are present at the surface of the virion. Glycoprotein N probably locks the Gn-Gc complex in a prefusion state. Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptors. This attachment induces virio... | Hazara virus (isolate JC280) |
A6XKM2 | CXA1_URSAM | MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRM... | null | null | cell-cell signaling [GO:0007267]; establishment of mitotic spindle orientation [GO:0000132]; heart development [GO:0007507]; microtubule-based transport [GO:0099111]; negative regulation of cell growth [GO:0030308]; negative regulation of gonadotropin secretion [GO:0032277]; negative regulation of trophoblast cell migr... | apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; connexin complex [GO:0005922]; endoplasmic reticulum [GO:0005783]; intercalated disc [GO:0014704]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; tight junction [GO:0070160] | beta-catenin binding [GO:0008013]; gap junction channel activity involved in cell communication by electrical coupling [GO:1903763]; gap junction hemi-channel activity [GO:0055077]; monoatomic ion transmembrane transporter activity [GO:0015075]; tubulin binding [GO:0015631] | PF00029;PF03508; | 1.20.5.1130;1.20.1440.80; | Connexin family, Alpha-type (group II) subfamily | PTM: Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates gap junction assembly. Phosphorylated at Ser-368 by PRKCG; phosphorylation induces disassembly of gap junction plaques and inhibition of gap junction activity. Phosphorylation at Ser-368 by PRKCD triggers its internalization into small vesicles leadi... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17302}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000250|UniProtKB:P17302}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD ... | null | null | null | null | null | FUNCTION: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by part... | Ursus americanus (American black bear) (Euarctos americanus) |
A6XMY0 | ARA1_HYAAR | MERRTLLVVLLVCSCVVAAAAEASPSRWPSPGRPRPFPGRPKPIFRPRPCNCYAPPCPCDRWRH | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; immune system process [GO:0002376]; killing of cells of another organism [GO:0031640] | null | chitin binding [GO:0008061] | null | null | null | PTM: Disulfide bonds are important for activity especially against Gram-negative bacteria, since the linearization of the peptide causes a strong decrease of activity on these bacteria. {ECO:0000269|PubMed:23326415}. | null | null | null | null | null | null | FUNCTION: Antimicrobial peptide that has a large activity spectrum with activity against Gram-positive, Gram-negative bacteria, as well as against fungi (PubMed:17658600, PubMed:23326415). Shows activity at micromolar concentrations (PubMed:17658600, PubMed:23326415). Displays minimal inhibitory concentration (MIC) val... | Hyas araneus (Atlantic lyre crab) (Great spider crab) |
A6XNC6 | UGFGT_MEDTR | MSTFKNEMNGNNLLHVAVLAFPFGTHAAPLLSLVKKIATEAPKVTFSFFCTTTTNDTLFSRSNEFLPNIKYYNVHDGLPKGYVSSGNPREPIFLFIKAMQENFKHVIDEAVAETGKNITCLVTDAFFWFGADLAEEMHAKWVPLWTAGPHSLLTHVYTDLIREKTGSKEVHDVKSIDVLPGFPELKASDLPEGVIKDIDVPFATMLHKMGLELPRANAVAINSFATIHPLIENELNSKFKLLLNVGPFNLTTPQRKVSDEHGCLEWLDQHENSSVVYISFGSVVTPPPHELTALAESLEECGFPFIWSFRGDPKEKLPKG... | 2.4.1.- | null | flavonoid biosynthetic process [GO:0009813]; phenylpropanoid metabolic process [GO:0009698] | null | UDP-glycosyltransferase activity [GO:0008194] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=89.8 uM for kaempferol {ECO:0000269|PubMed:17437063}; KM=28.7 uM for quercitin {ECO:0000269|PubMed:17437063}; KM=52 uM for pelargonidin {ECO:0000269|PubMed:17437063}; KM=71.8 uM for cyanidin {ECO:0000269|PubMed:17437063}; KM=1.5 uM for apigenin {ECO:0000269|PubMed:... | PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis. | null | null | FUNCTION: Catalyzes the glycosylation of flavonoids at the 3-O-position. Glycosylates the 7-O-position if the 3-O-position is not available. Also able to perform 3-O-glycosylation of anthocyanidins. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A6Y9S5 | LGA1_HYPJE | MAPPSLPCGIYAPTMTFFHPESEDIDIPTIKHHAQRLAKAGLAGLVVMGSNGEAVHCTRDEKIAVLSATREALDAAGFQSVPVLFGATEGSVRGTIELCKLAAAAGAAAALVLPPSYYRAQTDEASIEAYFVAVADASPIPLVLYNYPGAVSGIDMDSDLLIRLAQHKNIVGTKFTCGNTGKLTRVALATDAKTPFRDGSGYMAFGGMCDFTLQTLVSGGSGIIAGGANVMPKLCVKVWDSYSQGNRDEAEKLQKVLSRGDWPLTKAAIAGTKSAIQTYYGYGGYPRRPLKRLEQARVSAIEEGIREAMEIEKTL | 4.1.2.54 | null | D-galacturonate catabolic process [GO:0019698] | null | 4-hydroxy-tetrahydrodipicolinate synthase activity [GO:0008840]; aldehyde-lyase activity [GO:0016832] | PF00701; | 3.20.20.70; | DapA family | null | null | CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-L-galactonate = L-glyceraldehyde + pyruvate; Xref=Rhea:RHEA:38107, ChEBI:CHEBI:15361, ChEBI:CHEBI:27975, ChEBI:CHEBI:75545; EC=4.1.2.54; Evidence={ECO:0000269|PubMed:17609199}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.5 mM for 2-dehydro-3-deoxy-L-galactonate {ECO:0000269|PubMed:17609199}; KM=3.8 mM for D-glycero-3-deoxy-pentulosonate {ECO:0000269|PubMed:17609199}; KM=0.5 mM for pyruvate {ECO:0000269|PubMed:17609199}; KM=1.2 mM for L-glyceraldehyde {ECO:0000269|PubMed:17609199}... | PATHWAY: Carbohydrate acid metabolism. {ECO:0000269|PubMed:17609199}. | null | null | FUNCTION: Mediates the conversion of 2-dehydro-3-deoxy-L-galactonate to pyruvate and L-glyceraldehyde in D-galacturonate catabolic process. {ECO:0000269|PubMed:17609199, ECO:0000269|PubMed:18768163}. | Hypocrea jecorina (Trichoderma reesei) |
A6YFB5 | HTRA1_XENLA | MTMLWLAVLLTCGAPAALLPTSGVGCPARCDPSSCSPAPTNCQSGETALRCGCCSVCAAAENERCGEGPEDPLCASGLRCVRNGGVTRCQCPSNQPVCGSDGKTYSSLCRLQAESKAVQGRGVAAIIPIQRGDCQQGQKDPDSPRYKYNFIADVVEKIAPAVVHIELFRILPFFKREVPAASGSGFIVSEDGLILTNAHVVTNKHRLKVERSDGSTYDAQIIDVDEKADIALIKIKAKGKLPVLLLGRSEELRPGEFVVAIGSPFSLQNTVTTGIVSTAQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVVG... | 3.4.21.- | null | positive regulation of apoptotic process [GO:0043065]; programmed cell death [GO:0012501]; proteolysis [GO:0006508] | collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | growth factor binding [GO:0019838]; serine-type endopeptidase activity [GO:0004252] | PF00219;PF07648;PF17820;PF13365; | 2.30.42.10;2.40.10.120;3.30.60.30;4.10.40.20; | Peptidase S1C family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92743}. Secreted {ECO:0000269|PubMed:17681134}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92743}. Note=Predominantly secreted. Also found associated with the plasma membrane. {ECO:0000250|UniProtKB:Q92743}. | null | null | null | null | null | FUNCTION: Serine protease with a variety of targets, including extracellular matrix proteins and proteoglycans such as biglycan, syndecan-4 and glypican-4. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular spac... | Xenopus laevis (African clawed frog) |
A6YP92 | ARX_RAT | MSNQYQEEGCSERPECKSKSPTLLSSYCIDSILGRRSPCKMRLLGAAQSLPAPLASRTDQEKAMQGSPKGSSAPFEAELHLPPKLRRLYGPGGGRLLQGAAAAAAAAAAAAAAAATATGTAGPRGEVPPPPPPAARPGERQDSAGAVAAAAAAAWDTLKISQAPQVSISRSKSYRENGAPFVPPPPALDELGGPGGVAHPEERLSAASGPGSAPAAGGGTGTEEDEEELLEDEEDEDEEEELLEDDEEELLEDDARALLKEPRRCSVATTGTVAAAAAAAAAAAAVATEGGELSPKEELLLHPEDAEGKDGEDSVCLSAG... | null | null | axon guidance [GO:0007411]; cell proliferation in forebrain [GO:0021846]; cerebral cortex GABAergic interneuron migration [GO:0021853]; cerebral cortex tangential migration [GO:0021800]; embryonic olfactory bulb interneuron precursor migration [GO:0021831]; epithelial cell fate commitment [GO:0072148]; forebrain develo... | nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulato... | PF00046;PF03826; | 1.10.10.60; | Paired homeobox family, Bicoid subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35137, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. | null | null | null | null | null | FUNCTION: Transcription factor. Binds to specific sequence motif 5'-TAATTA-3' in regulatory elements of target genes, such as histone demethylase KDM5C. Positively modulates transcription of KDM5C. Activates expression of KDM5C synergistically with histone lysine demethylase PHF8 and perhaps in competition with transcr... | Rattus norvegicus (Rat) |
A6YQT5 | RPOA_PRRSV | MSGILDRCTCTPNARVFVAEGQVYCTRCLSARSLLPLNLQVPELGVLGLFYRPEEPLRWTLPRAFPTVECSPAGACWLSAIFPIARMTSGNLNFQQRMVRVAAEIYRAGQLTPTVLKTLQVYERGCRWYPIVGPVPGVGVYANSLHVSDKPFPGATHVLTNLPLPQRPKPEDFCPFECAMADVYDIGRGAVMYVAGGKVSWAPRGGNEVKFEPIPKELKLVANRLHTSFPPHHVVDMSRFTFMTPGSGVSMRVEYQHGCLPADTVPEGNCWWRLFDSLPPEVQYKEIRHANQFGYQTKHGVPGKYLQRRLQVNGLRAVTD... | 2.7.7.48; 3.4.19.12; 3.4.21.-; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | null | induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host ISG15-protein conjugation [GO:0039579]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [... | host cell endoplasmic reticulum [GO:0044165]; host cell membrane [GO:0033644]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]; protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA helicase activity [GO:0003724]; RNA nuclease activity [GO:0004540]; RNA-depen... | PF16749;PF19215;PF14757;PF14756;PF05410;PF05411;PF05412;PF05579;PF00680;PF01443; | 3.90.70.160;4.10.80.390;3.30.1330.220;2.30.31.30;3.90.70.70;3.40.50.300;3.90.70.60;2.40.10.10; | Arteriviridae polyprotein family | PTM: [Replicase polyprotein 1ab]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. Nsp1 is autocleaved into two subunits, Nsp1-alpha and Nsp1-beta. There are two alternative pathways for processing. Either nsp4-5 is cleaved, which represents the major pathway or the nsp5-6 and nsp6-7 are... | SUBCELLULAR LOCATION: [Nsp1]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Nsp1-beta pap... | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALY... | null | null | null | null | FUNCTION: [Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.; FUNCTION: [Nsp1-alpha papain-like cysteine protei... | Porcine reproductive and respiratory syndrome virus (PRRSV) |
A6YRY8 | RSSA_SHEEP | MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTAAQPEVADWSEGVQVPSVPIQQFPTEDWSARPFTEDWSAAPTAQATEWVGTTSELS | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | 90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | laminin binding [GO:0043236]; laminin receptor activity [GO:0005055]; structural constituent of ribosome [GO:0003735] | PF16122;PF00318; | null | Universal ribosomal protein uS2 family | PTM: Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association. {ECO:0000255|HAMAP-Rule:MF_03016}.; PTM: Cleaved by stromelysin-3 (ST3) at the cell surface... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_03016}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03016}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03016}. Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the c... | null | null | null | null | null | FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement mem... | Ovis aries (Sheep) |
A6YSL1 | RNC1_MAIZE | MGPPAMAFQALTLTPLPFSLHSSSRRVRVLAVAADQTPPPAPPSEPANSPSRLLRELAQRKKAVSPKKKHPPRRFILKPPLDDERLTRRFLSSPQLSLKALPLLSSCLPSAPLSTADRTWMDEYLLEAKQALGYPLAPSETLGEGDDCPARHFDVLFYLAFQHLDPSSERTRMRHVRNGHSRLWFLGQYVLELAFCEFFLQRYPRESPGPMRERVFALIGKKVLPRWLKAASLHNLVFPYDDLDKMIRKDREPPSKAVFWAIFGAIYLCFGMPEVYRVLFEAFGMDPDDESCQPKLRRQLEDVDYVSVEFEKRQLTWQDV... | null | null | Group II intron splicing [GO:0000373]; mRNA processing [GO:0006397]; regulation of gene expression [GO:0010468]; ribosome biogenesis [GO:0042254]; RNA processing [GO:0006396] | chloroplast stroma [GO:0009570]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | double-stranded RNA binding [GO:0003725]; ribonuclease III activity [GO:0004525]; single-stranded RNA binding [GO:0003727] | PF00636; | 1.10.1520.10; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:17693527}. | null | null | null | null | null | FUNCTION: Binds specific group II introns in chloroplasts and facilitates their splicing. Acts on both subgroup IIA and subgroup IIB introns. The substrates of the subgroup II also require the CRM domain proteins CAF1 or CAF2. Binds both single-stranded and double-stranded RNA non-specifically, but lacks endonuclease a... | Zea mays (Maize) |
A6ZM04 | PIF1_YEAS7 | MPKWIRSTLNHIIPRRPFICSFNSFLLLKNVSHAKLSFSMSSRGFRSNNFIQAQLKHPSILSKEDLDLLSDSDDWEEPDCIQLETEKQEKKIITDIHKEDPVDKKPMRDKNVMNFINKDSPLSWNDMFKPSIIQPPQLISENSFDQSSQKKSRSTGFKNPLRPALKKESSFDELQNSSISQERSLEMINENEKKKMQFGEKIAVLTQRPSFTELQNDQDDSNLNPHNGVKVKIPICLSKEQESIIKLAENGHNIFYTGSAGTGKSILLREMIKVLKGIYGRENVAVTASTGLAACNIGGITIHSFAGIGLGKGDADKLYK... | 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03176}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03176}; Note=Mg(2+). To a lesser extent, can also use Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03176}; | DNA recombination [GO:0006310]; DNA repair [GO:0006281]; mitochondrial genome maintenance [GO:0000002]; negative regulation of telomere maintenance via telomerase [GO:0032211]; telomere maintenance [GO:0000723] | mitochondrial inner membrane [GO:0005743]; nucleolus [GO:0005730] | 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; G-quadruplex DNA binding [GO:0051880]; telomerase inhibitor activity [GO:0010521] | PF05970;PF21530; | 3.40.50.300; | Helicase family, PIF1 subfamily | PTM: Phosphorylated. Undergoes RAD53-dependent phosphorylation in response to loss of mtDNA (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus, nucleolus {ECO:0000250}. Note=Mainly concentrated in the nucleolus, and occasionally redistributes to single nuclear foci outside the nucleolus, probably sites of DNA repair. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion inner membrane {EC... | 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:0000255|HAMAP-Rule:MF_03176}; | null | null | null | null | FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule o... | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
A6ZU07 | ATG1_YEAS7 | MGDIKNKDHTTSVNHNLMASAGNYTAEKEIGKGSFATVYRGHLTSDKSQHVAIKEVSRAKLKNKKLLENLEIEIAILKKIKHPHIVGLIDCERTSTDFYLIMEYCALGDLTFLLKRRKELMENHPLLRTVFEKYPPPSENHNGLHRAFVLSYLQQLASALKFLRSKNLVHRDIKPQNLLLSTPLIGYHDSKSFHELGFVGIYNLPILKIADFGFARFLPNTSLAETLCGSPLYMAPEILNYQKYNAKADLWSVGTVVFEMCCGTPPFRASNHLELFKKIKRANDVITFPSYCNIEPELKELICSLLTFDPAQRIGFEEFF... | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:0042594]; reticulophagy [GO:0061709... | autophagosome [GO:0005776]; cytosol [GO:0005829]; phagophore assembly site membrane [GO:0034045] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | PTM: Autophosphorylated at Thr-226 and Ser-390. The phosphorylation state may play a role in the induction of protein degradation upon starvation. Phosphorylation at Thr-226 within the activation loop is required for protein kinase activity whereas phosphorylation at Ser-34 leads to inhibition of kinase activity. Phosp... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. Note=Formes punctate structures in starvation conditions only when ATG13 and ATG17 were both present. Localizes to both the iso... | 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:P53104}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective a... | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
A6ZXH8 | ATG9_YEAS7 | MERDEYQLPNSHGKNTFLSRIFGLQSDEVNPSLNSQEMSNFPLPDIERGSSLLHSTNDSREDVDENDLRVPESDQGTSTEEEDEVDEEQVQAYAPQISDGLNGDHQLNSVTSKENVLETEKSNLERLVEGSTDDSVPKVGQLSSEEEEDNEFINNDGFDDDTPLFQKSKIHEFSSKKSNTIEDGKRPLFFRHIYQNNRPQRDTQKLFTSSNAIHHDKDKSANNGPRNINGNQKHGTKYFGSATQPRFTGSPLNNTNRFTKLFPLRKPNLLSNISVLNNTPEDRINTLSVKERALWKWANVENLDIFLQDVYNYYLGNGFY... | null | null | lipid transport [GO:0006869]; protein localization to phagophore assembly site [GO:0034497] | autophagosome [GO:0005776]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; mitochondrial membrane [GO:0031966]; phagophore assembly site membrane [GO:0034045] | null | PF04109; | null | ATG9 family | PTM: Phosphorylated by ATG1; phosphorylation is required for autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Phosphorylation by ATG1 regulates ATG18 interaction and preautophagosome elongation. Phosphorylation at Ser-122 is required for selective autophagy by regulating anterograde trafficking and... | SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Golgi apparatus membrane {ECO:0000250|UniProtKB:... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-s... | null | null | null | null | FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key ro... | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
A6ZY89 | ARO1_YEAS7 | MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQ... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) |
A7B558 | NANY_MEDG7 | MKTVGYAIVGTGYFGAELGRIMKEQEGARIVAVLDPENGQTIAEELDCDVETDLDTLYSREDVEAVIVATPNYLHKEPVIKAAEHGVNVFCEKPIALSYQDCDEMVRTCQEHGVIFMAGHVMNFFHGVRYAKKLINDGVIGKVLYCHSARNGWEEQQPTISWKKIREKSGGHLYHHIHELDCVQFLMGGMPEEVTMTGGNVAHQGEAFGDEDDMLFVNMQFSDNRYAVLEWGSAFHWPEHYVLIQGTKGAIKIDMCDCGGTLKVDGREEHFLVHESQEEDDDRTRIYHGTEMDGAIMYGKPGKKPPMWLHSIMKNEMKYL... | 4.2.1.- | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:32669363}; Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:32669363}; | null | null | biliverdin reductase (NAD(P)+) activity [GO:0004074]; lyase activity [GO:0016829]; nucleotide binding [GO:0000166] | PF01408;PF02894; | 3.40.50.720; | Gfo/Idh/MocA family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-2,7-anhydro-alpha-neuraminate = N-acetyl-alpha-neuraminate; Xref=Rhea:RHEA:78519, ChEBI:CHEBI:15377, ChEBI:CHEBI:58770, ChEBI:CHEBI:229228; Evidence={ECO:0000269|PubMed:32669363}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.074 mM for 2,7-AN {ECO:0000269|PubMed:31636419}; Note=kcat is 0.0824 sec(-1). {ECO:0000269|PubMed:31636419}; | null | null | null | FUNCTION: Hydratase involved in the degradation of sialic acids, which are present in the host mucus layer and represent a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota (PubMed:31636419, PubMed:32669363). Catalyzes the reversible conversion of the dehydrated form of N-ac... | Mediterraneibacter gnavus (strain ATCC 29149 / DSM 114966 / JCM 6515 / VPI C7-9) (Ruminococcus gnavus) |
A7BFV8 | SPT_BACTC | MKHNLQDNLQGEQMANTNSNGGKKPFSDAKIIERANLLRDNDLYFFFRAIEETEASTVTVKGKKQIMIGSNNYLGLTHHPAVKEAAIKAVEKYGTGCTGSRFLNGNLNIHEELDEKLAAYLGHEKAIVFSTGMQANLGALSAICGPKDLMLFDSENHASIIDASRLSLGTTFKYKHNDMASLEELLESNMSRFNRVIIVADGVFSMTGDILRLPEVVKLAKKYGAYVYVDDAHGLGVMGPQGRGTMAHFDVTKDVDFNMGTFSKSFASIGGVISGSKDAIDYVRHSARSFMFSASMPPAAVATVSACIDVVQNDETILNN... | 2.3.1.50 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:17557831}; | ceramide biosynthetic process [GO:0046513]; sphingosine biosynthetic process [GO:0046512] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | 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 | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17557831}. Cell inner membrane {ECO:0000269|PubMed:17557831}; Peripheral membrane protein {ECO:0000269|PubMed:17557831}. Note=Predominantly concentrated in a limited region near the inner membrane or organelle-like multilayered membrane structure. {ECO:0000269|PubMed:... | 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:0000269|PubMed:17557831}; PhysiologicalDirection=left-to-righ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.7 mM for L-serine {ECO:0000269|PubMed:17557831}; Note=kcat is 0.03 sec(-1) (in the presence of 100 uM of palmitoyl-CoA). {ECO:0000269|PubMed:17557831}; | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305|PubMed:17557831}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 to 8.0. {ECO:0000269|PubMed:17557831}; | null | FUNCTION: Catalyzes the condensation of L-serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-oxosphinganine. {ECO:0000269|PubMed:17557831}. | Bacteriovorax stolpii (Bdellovibrio stolpii) |
A7BHQ9 | TYRO_PHONA | MSRVVITGVSGTIANRLEINDFVKNDKFFSLYIQALQVMSSVPPQENVRSFFQIGGIHGLPYTPWDGITGDQPFDPNTQWGGYCTHGSVLFPTWHRPYVLLYEQILHKHVQDIAATYTTSDKAAWVQAAANLRQPYWDWAANAVPPDQVIVSKKVTITGSNGHKVEVDNPLYHYKFHPIDSSFPRPYSEWPTTLRQPNSSRPNATDNVAKLRNVLRASQENITSNTYSMLTRVHTWKAFSNHTVGDGGSTSNSLEAIHDGIHVDVGGGGHMGDPAVAAFDPIFFLHHCNVDRLLSLWAAINPGVWVSPGDSEDGTFILPP... | 1.14.18.1 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:17617709}; Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:17617709}; | melanin biosynthetic process [GO:0042438] | null | copper ion binding [GO:0005507]; tyrosinase activity [GO:0004503] | PF18132;PF00264; | 2.60.310.20;1.10.1280.10; | Tyrosinase family | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17617709}. | null | CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; Evidence={ECO:0000269|PubMed:17617709}; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1930 uM for L-dopa {ECO:0000269|PubMed:17617709}; KM=119 uM for t-butylphenol {ECO:0000269|PubMed:17617709}; KM=30.6 uM for p-cresol {ECO:0000269|PubMed:17617709}; KM=163 uM for t-butylcatechol {ECO:0000269|PubMed:17617709}; KM=1240 uM for 3-(3,4-dihydroxyphenyl) p... | null | null | null | FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. {ECO:0000250|UniProtKB:Q92396}. | Pholiota nameko |
A7DTF0 | MRG1_CAEEL | MSSKKNFEVGENVACIYKGKPYDAKITDIKTNSDGKELYCVHFKGWNNRYDEKIPVGEEKDRIFKGTASEYAEKHNAELPTTALKPKKKSLAAEAPRDDRDDTPGTSKGKKAKSVTIAPVMTADDMKVELPKPLRKILIDDYDLVCRYFINIVPHEYSVDQIIEDYIKTIPVSNEQMRTVDDLLIEYEEADIKITNLALICTARGLVDYFNVTLGSSYQLLYKFERPQYNDLVKKRAMEKGIDITNPTALQDSGFRPSQEYGIVHFLRMLAKLPDYLKLTQWNDHVINRIMIGVHDLIVFLNKNHGKYYRGSSDYQGASN... | null | null | chromosome attachment to the nuclear envelope [GO:0097240]; chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA repair [GO:0006281]; embryo development ending in birth or egg hatching [GO:0009792]; germ cell development [GO:0007281]; heterochromatin formation [GO:0031507]; negative regulation of tr... | autosome [GO:0030849]; chromatin [GO:0000785]; euchromatin [GO:0000791]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634] | null | PF05712;PF11717; | 2.30.30.140;1.10.274.30; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:22172672}. Chromosome {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:31118512}. Note=Concentrated on euchromatic regions marked by H3K36me2/me3 and probably enriched on autosomes. {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:31118512}. | null | null | null | null | null | FUNCTION: Protein involved in the remodeling of chromatin thereby regulating various processes including transcription, chromosome synapsis and genome integrity (PubMed:17215300, PubMed:22172672, PubMed:22212480, PubMed:30929290). Mainly binds genomic loci carrying trimethylated histone H3 'Lys-36' (H3K36me3) or 'Lys-4... | Caenorhabditis elegans |
A7DY56 | TRN1_COCOF | MANLRESSRDKSRWSLEGMTALVTGGSKGIGEAVVEELAMLGARVHTCARDETQLQESLREWQAKGFQVTTSVCDVSSRDQREKLMETVSSLFQGKLNILVNNAGTCITKPTIDYTSEDFSFLMSTNLESSFHLSQLAHPLLKSSGLGSIVLISSVASVVHVNVGSIYGATKGAMNQLARNLACEWASDSIKVNSVCPGFISTPLASNYFRNEEFKKEVENIIPTGRVGEANEVSSLVAYLCLPAASYVTGQTICVDGGFSVNGFTFKSLPLR | 1.1.1.206; 1.1.1.236 | null | null | null | tropine dehydrogenase activity [GO:0050356]; tropinone reductase activity [GO:0050358] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family, SDR65C subfamily | null | null | CATALYTIC ACTIVITY: Reaction=NADP(+) + tropine = H(+) + NADPH + tropinone; Xref=Rhea:RHEA:18357, ChEBI:CHEBI:15378, ChEBI:CHEBI:57554, ChEBI:CHEBI:57783, ChEBI:CHEBI:57851, ChEBI:CHEBI:58349; EC=1.1.1.206; Evidence={ECO:0000269|PubMed:18221363}; CATALYTIC ACTIVITY: Reaction=NADP(+) + pseudotropine = H(+) + NADPH + trop... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3290 uM for tropinone {ECO:0000269|PubMed:18221363}; KM=2002 uM for nortropinone {ECO:0000269|PubMed:18221363}; KM=42 uM for 8-thiabicyclo[3.2.1]octan-3-one {ECO:0000269|PubMed:18221363}; KM=2636 uM for quinuclidinone {ECO:0000269|PubMed:18221363}; KM=1342 uM for N... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. The pH has no influence on the tropine to pseudotropine product ratio. {ECO:0000269|PubMed:18221363}; | null | FUNCTION: Oxidoreductase having both tropinone reductase I and II activities. Involved in the tropane alkaloids calystegines and cochlearine biosynthesis. Can use tropinone and nortropinone as substrates and produces both tropine and pseudotropine. Able to oxidize pseudotropine in the reverse reaction. {ECO:0000269|Pub... | Cochlearia officinalis (Common scurvygrass) |
A7E2V4 | ZSWM8_HUMAN | MELMFAEWEDGERFSFEDSDRFEEDSLCSFISEAESLCQNWRGWRKQSAGPNSPTGGGGGGGSGGTRMRDGLVIPLVELSAKQVAFHIPFEVVEKVYPPVPEQLQLRIAFWSFPENEEDIRLYSCLANGSADEFQRGDQLFRMRAVKDPLQIGFHLSATVVPPQMVPPKGAYNVAVMFDRCRVTSCSCTCGAGAKWCTHVVALCLFRIHNASAVCLRAPVSESLSRLQRDQLQKFAQYLISELPQQILPTAQRLLDELLSSQSTAINTVCGAPDPTAGPSASDQSTWYLDESTLTDNIKKTLHKFCGPSPVVFSDVNSMY... | null | null | positive regulation of miRNA catabolic process [GO:2000627]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; target-directed miRNA degradation [GO:0140958] | Cul2-RING ubiquitin ligase complex [GO:0031462]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytosol [GO:0005829] | ubiquitin ligase-substrate adaptor activity [GO:1990756]; zinc ion binding [GO:0008270] | PF21055; | null | ZSWIM8 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q3UHH1}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:33184234, ECO:0000269|PubMed:33184237}. | null | null | FUNCTION: Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs) (PubMed:33184234, PubMed:33184237). The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquit... | Homo sapiens (Human) |
A7E2Y1 | MYH7B_HUMAN | MSGNKRGSRASCPHRGAECLLPWAALNLQGFQLLLLHPSATAMMDVSELGESARYLRQGYQEMTKVHTIPWDGKKRVWVPDEQDAYVEAEVKSEATGGRVTVETKDQKVLMVREAELQPMNPPRFDLLEDMAMMTHLNEASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIF... | null | null | null | cytoplasm [GO:0005737]; membrane [GO:0016020]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15755502}; Peripheral membrane protein {ECO:0000269|PubMed:15755502}. | null | null | null | null | null | FUNCTION: Involved in muscle contraction. {ECO:0000269|PubMed:11919279}. | Homo sapiens (Human) |
A7E320 | UHRF1_BOVIN | MWIQVRTMDGKVAHTVDSLSRLTKVEELRKKIQELFHVEPGLQRLFYRGKQMEDGHTLFDYDVRLNDTIQLLVRQSLVLPVPVPSSSGGSKERDSELSDTDSGCGLAQSESDKSSNSGEAANEPEGKADEDECDETELGLYKVGEYVDARDTNMGAWFEAKVIRVTRKAPAHDQPSSSSSKPEDDIIYHVTYDDYPENGVVQMTSQNVRARARHTIKWEDLQVGQVVMVNYNPDLPKDRGFWYDAEILRKRETRTARELHANVRIGGDSLNDCRIVFVDEVFKIERPGEGNPMVENPMRRKSGPSCKHCKDDERKLCRMC... | 2.3.2.27 | null | cell cycle [GO:0007049]; DNA repair [GO:0006281]; heterochromatin formation [GO:0031507]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein ubiquitination [GO:0016567]; ubiquitin-dependent pro... | chromatin [GO:0000785]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleus [GO:0005634]; replication fork [GO:0005657] | hemi-methylated DNA-binding [GO:0044729]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00628;PF02182;PF12148;PF00240; | 2.30.30.1150;2.30.30.140;2.30.280.10;3.30.40.10; | null | PTM: Phosphorylation at Ser-302 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-645 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: Ubiquitinated; which leads to proteasomal... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VDF2, ECO:0000255|PROSITE-ProRule:PRU00358}. Note=Associated, through the YDG domain (also called SRA domain), with replicating DNA from early to late S phase, including at replicating pericentric heterochromatin (By similarity). Also localizes to euchromatic regio... | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q96T88}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns t... | Bos taurus (Bovine) |
A7E3N2 | NCF2_RAT | MSLAEAIRLWNEGVQAADKKDWKGALEAFSEVQDPHSRICFNIGCMYTILDNLQEAEQAFTKSINRDKHLAVAYFQRGMLYYSMEKYRPASVGRKAALLFLGSYNLVARIIVGYPLSPGKVLYNIALMHAKKEEWKKAEEQLALATNMKSEPRHSKIDKAMESIWKRCPTSHLPLDPPQVTMALWFEEGGVGKRSVVASVVHQDNFSGFAPLQPQSAEPPPRPKTPEIFRALEGEAHRVLFGFVPETPEELQVMPGNIVFVLKKGSDNWATVMFNGQKGLVPCNYLEPVELRIHPQSQPQEDTSLESDIPPPPNSSPPER... | null | null | cellular response to hormone stimulus [GO:0032870]; phagocytosis [GO:0006909]; positive regulation of blood pressure [GO:0045777]; positive regulation of neuron apoptotic process [GO:0043525]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; respiratory burst [GO:0045730]; response to activity [... | acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; NADPH oxidase complex [GO:0043020] | small GTPase binding [GO:0031267]; superoxide-generating NADPH oxidase activator activity [GO:0016176] | PF00564;PF00018;PF13181; | 2.30.30.40;1.25.40.10; | NCF2/NOXA1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19878}. | null | null | null | null | null | FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000250|UniProtKB:P19878}. | Rattus norvegicus (Rat) |
A7E3S4 | RAF1_BOVIN | MEHIQGAWKTISNGFGFKDTVFDGTSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTVGDGGVPALPSLTMRRMRESVSRIPPGSQHRYSTPHAFTFSASSPSSEGSLSQRQRSTSTPNVHMVSATLPVDSRMIEDAIRSHSESGSPSALSSSPNNLSPTGWSQPKTPAPAQRERAP... | 2.7.11.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P04049}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P04049}; | death-inducing signaling complex assembly [GO:0071550]; ERBB2-ERBB3 signaling pathway [GO:0038133]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; face development [GO:0060324]; insulin receptor signaling pathway [GO:0008286]; insulin secretion involved in cellular response to glucose st... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; small GTPase binding [GO:0031267] | PF00130;PF00069;PF02196; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily | PTM: Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation. Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation. Phosphorylation at Ser-259 induces the interaction with YWHAZ and inactivates kinase activity. Dephosphory... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with RGS14 and BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-259 impairs its membrane accumulation. Recruited to the cell membrane by the active Ras protein... | 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:P04049}; Physiolo... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformatio... | Bos taurus (Bovine) |
A7EK16 | MYO1_SCLS1 | MGISRRPKADKNASAADSAPGGKPNIQKAQFDTTKKKEVGVSDLTLISKVSNEAINENLKKRFDNREIYTYIGHVLVSVNPFRDLGIYTDAVLESYKGKNRLEMPPHVFAVAESAYYNMNAYKDNQCVIISGESGAGKTEAAKRIMQYIANVSGGSNSSIQETKEMVLATNPLLESFGNAKTLRNNNSSRFGKYLQLQFNAQGEPVGADITNYLLEKTRVVTQIKDERNFHIFYQFTKGASQAYRESYGIQQPSQYLYTSKAGCFDVDGIDDLAEYQDTLQAMKVIGLSQAEQDEIFRMLAAILWTGNIQFREGDDGYAT... | null | null | actin cortical patch assembly [GO:0000147]; actin cortical patch localization [GO:0051666]; actin filament organization [GO:0007015]; endocytosis [GO:0006897]; mitotic cytokinesis [GO:0000281]; vesicle transport along actin filament [GO:0030050] | actin cortical patch [GO:0030479]; actin cytoskeleton [GO:0015629]; cell cortex of cell tip [GO:0051285]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; mating projection tip [GO:0043332]; medial cortex [GO:0031097]; myosin I complex [GO:0045160]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; prospor... | actin filament binding [GO:0051015]; Arp2/3 complex binding [GO:0071933]; ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; microfilament motor activity [GO:0000146] | PF00063;PF06017;PF00018; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720;2.30.30.40; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch {ECO:0000250}. | null | null | null | null | null | FUNCTION: Type-I myosin implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions as actin nucleation-promoting ... | Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) |
A7F0W2 | ATG1_SCLS1 | MASKTPSSSSSRRPRNVGVGSFTINEEIGKGSFATVYRGTHVPSGSLVAIKSVNLGRLNKKLKDNLYVEIEILKSLHHPHIVALMDCRESTSHIHLMMEYCELGDLSYFIKKRDKLADNPSLFDMIRKYPMPVDGGLNQVVVRHFFKQLSSAMEFLRDRDFVHRDVKPQNLLLIPSPDWMAKSKNGPEAMKASKESIVPMVGINSLPMLKLADFGFARSLPSTSLAETLCGSPLYMAPEILRYEKYDARADLWSIGTVLYEMMTGKPPFRAANHVELLRKIEQNEDEIRFPSKTVFSRDLKDIARRFLKKRPEDRITFPE... | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; regulation of autophagy [GO:00105... | Atg1/ULK1 kinase complex [GO:1990316]; autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; phagophore [GO:0061908]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]; vacuole-isolation membrane contact site [GO:0120095] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | 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:P53104}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective a... | Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) |
A7F7H0 | ARO1_SCLS1 | MGSTTFENPTRIEILGKEDIIVDFDIWRNFVAEDLLSDLPSSTYVLITDTNLSPLYVPAFQQSFEALAAKSSSTPRLLTYEIPPGENSKSRETKAEIEDWMLSHQCTRDSVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLVGAFWQPQRIYIDLRFLETLPVREFINGMAEVVKTAAIWDEAEFSALEDNANLIMTTIRAKNTDCSTRLGPIRDILKRIVLGSAKTKADVVSADEREGGLRNILNFGHSIGHAFEAILTPQVLHGEAVAIGMVKEAELARHLGVLKPGAVARLV... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) |
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