Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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F5HSE3 | NIPLA_DANRE | MNGDMPHVPITTLAGIAGLTDLLNQLPLPSPLPGTTTKSLLYNGRVAEDVGHLLGCRDETLVSQLANSLSQVSTEHIELKDSLGSDELEGDVPVLLQLLMSRNPNIFRNKTAPNTPQYPAQAGISQQSMAPPYKITHGSMQGSPASANYQQASMSHSPSGHFVPGQSGPGGRFLPQQGSPVPSPYAPQSPATGYRQYPHPPAYSQHQHLQQGSVASPMIPGAMRNVHENKDQMRMGFTSHLLQSSPPYTPPCDGTKDLHLGSQDKQRGQKSSEGEQDSPDKATVYDIVGSPAKDHTKLILRPSRARPAEVELGGMYPGSD... | null | null | brain development [GO:0007420]; digestive tract development [GO:0048565]; embryonic pectoral fin morphogenesis [GO:0035118]; embryonic viscerocranium morphogenesis [GO:0048703]; establishment of mitotic sister chromatid cohesion [GO:0034087]; establishment of protein localization to chromatin [GO:0071169]; heart develo... | Scc2-Scc4 cohesin loading complex [GO:0090694] | chromatin binding [GO:0003682]; chromatin loop anchoring activity [GO:0140587] | PF12765;PF12830; | 1.25.10.10; | SCC2/Nipped-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6KCD5}. | null | null | null | null | null | FUNCTION: May play a structural role in chromatin. Involved in sister chromatid cohesion, possibly by facilitating the cohesin complex loading. Transcription factor, which may promote cortical neuron migration during brain development by regulating the transcription of crucial genes in this process (By similarity). {EC... | Danio rerio (Zebrafish) (Brachydanio rerio) |
F6NXI9 | TRNT1_DANRE | MWAKLFLRPSFVNRVHLTWSCRALLTMQLKTKEFESLFTDGLVGLAEIFQKNQFELRIAGGAVRDLLSGKRPEDVDFATTATPEEMKSMFQTAGVRMINNKGEKHGTITARLHEENFEVTTLRVDVQTDGRHAEVEFTTDWQKDAERRDLTINSMFLGLDGTLYDYFQGYEDLKNRKVRFVGSASLRIQEDYLRILRYFRFYGRVAAEPGQHEPETLEAIRENARGLAGISGERIWVELKKMLVGNHAGHLLELVYELGLAQYTGLPADGDVEEMKQVWQRAHVSSPKPMTVLAALFRKQADVENLDQRLKVSREEKNLG... | 2.7.7.72 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O66728}; | eye development [GO:0001654]; mitochondrial tRNA 3'-end processing [GO:1990180]; thigmotaxis [GO:0001966]; tRNA 3'-terminal CCA addition [GO:0001680]; tRNA processing [GO:0008033]; visual behavior [GO:0007632] | mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP binding [GO:0005524]; CCA tRNA nucleotidyltransferase activity [GO:0004810]; CCACCA tRNA nucleotidyltransferase activity [GO:0160016]; metal ion binding [GO:0046872]; tRNA binding [GO:0000049] | PF01743;PF12627; | 3.30.460.10;1.10.3090.10; | TRNA nucleotidyltransferase/poly(A) polymerase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96Q11}. Cytoplasm {ECO:0000250|UniProtKB:Q96Q11}. Nucleus {ECO:0000250|UniProtKB:Q96Q11}. | CATALYTIC ACTIVITY: Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72; Evidence={ECO:0000250|UniProtKB:Q96Q11}; P... | null | null | null | null | FUNCTION: Nucleotidyltransferase that catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs, which is necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates (PubMed:26494905). tRNA 3'-terminal CCA addition is required both for tRN... | Danio rerio (Zebrafish) (Brachydanio rerio) |
F6Q1T7 | FUT1_BOVIN | MWAPGHHHLCLIFLLTCVFACVFFLLIHQNLFHSGLDLFLPCPDRSRVRSPVAILCLSGTLMNPNATFTCPRHSASVSGTWTIDPKGRFGNQMGQYATLLALAQLNGRQAFIQPSMHAVLAPVFRITLPVLAPEVDRHAPWQELELHDWMSEEYAHLKEPWLKLTGFPCSWTFFHHLRDQIRSEFTLHEHLRQEAQRSLSGLRFPRTGGRPSTFVGVHVRRGDYLQVMPLHWKGVVGDRAYLQQAMDWFRARHKAPIFVVTSNGMKWCRENIDTSRGDVIFAGDGQEGAPNKDFALLTQCNHTIMTIGTFGFWAAYLAGG... | 2.4.1.344; 2.4.1.69 | null | carbohydrate metabolic process [GO:0005975]; fucosylation [GO:0036065]; lipid metabolic process [GO:0006629]; olfactory bulb development [GO:0021772]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell-matrix ... | Golgi cisterna membrane [GO:0032580] | alpha-(1,2)-fucosyltransferase activity [GO:0031127]; galactoside 2-alpha-L-fucosyltransferase activity [GO:0008107] | PF01531; | null | Glycosyltransferase 11 family | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O09160}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O09160}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250|UniProtKB:O09160}. | CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 + GDP-beta-L-fucose = a ganglioside Fuc-GM1 + GDP + H(+); Xref=Rhea:RHEA:48292, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82639, ChEBI:CHEBI:90189; Evidence={ECO:0000269|PubMed:10814703}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.26 uM for Galacto-N-biose {ECO:0000269|PubMed:10814703}; KM=1.29 uM for ganglioside GM1a {ECO:0000269|PubMed:10814703}; Vmax=48.6 pmol/min/mg enzyme towards Galacto-N-biose {ECO:0000269|PubMed:10814703}; Vmax=58.5 pmol/min/mg enzyme towards ganglioside GM1a {ECO:... | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P19526}. | null | null | FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose residue of glycoconjugates through an alpha(1,2) linkage leading to H antigen synthesis that is an intermediate substrate in the synthesis of ABO blood group antigens (PubMed:10814703). H antigen is essen... | Bos taurus (Bovine) |
F6RG56 | MCLN3_CALJA | MANPEIVISSCSSHEEENRCNFNQHTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTVAFKHLFLKGYIDRMDDTYAVYTQSDVYDQIIFAVNQYLQLYNVSVGNHAYENKGTDQSAMAICQHFYKRGNIYPGNDTFDIDPEIETDCFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHNMMIFDAFVILTCLVSLILCIRSVISGLQLQQEFVNF... | null | null | monoatomic cation transmembrane transport [GO:0098655]; protein homotetramerization [GO:0051289] | autophagosome membrane [GO:0000421]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; stereocilium membrane [GO:0060171] | identical protein binding [GO:0042802]; intracellularly phosphatidylinositol-3,5-bisphosphate-gated monatomic cation channel activity [GO:0097682]; NAADP-sensitive calcium-release channel activity [GO:0072345]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025] | PF21381;PF08016; | 1.10.287.70; | Transient receptor (TC 1.A.4) family, Polycystin subfamily, MCOLN3 sub-subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8TDD5}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:29019979}; Multi-pass membrane protein {ECO:0000269|PubMed:29019979}. Early endosome membrane {ECO:0000250|UniProtKB:Q8TDD5}; Multi-pass membrane protein {ECO:0000269|PubMed:29019979}. Late endosome membrane {ECO:0000250|UniProtKB:Q8R4F0}; Multi-pass membrane ... | null | null | null | null | null | FUNCTION: Nonselective ligand-gated cation channel probably playing a role in the regulation of membrane trafficking events (PubMed:29019979). Acts as a Ca(2+)-permeable cation channel with inwardly rectifying activity (By similarity). Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal... | Callithrix jacchus (White-tufted-ear marmoset) |
F6SEU4 | SYGP1_MOUSE | MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDRPGWNPRFCIISGNQLLMLDEDEIHPLLIRDRRSESSRNKLLRRTVSVPVEGRPHGEHEYHLGRSRRKSVPGGKQYSMEAAPAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRSASGDTVFWGEHFEFNNLPAV... | null | null | axonogenesis [GO:0007409]; dendrite development [GO:0016358]; maintenance of postsynaptic specialization structure [GO:0098880]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of axonogenesis [GO:0050771]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation ... | dendritic shaft [GO:0043198]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density, intracellular component [GO:0099092]; synapse [GO:0045202] | GTPase activator activity [GO:0005096]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124] | PF00168;PF12004;PF00616; | 2.60.40.150;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Note=Mostly in excitatory glutamatergic synapses (By similarity). receptor activation or SYNGAP1/MPDZ complex disruption. Phosphorylation by PLK2 promotes its activity (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Major constituent of the PSD essential for postsynaptic signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses, it may play a role in NMDAR-dependent control of AMPAR potentiation, AMPAR membrane trafficking and synaptic plasticity. Regulates AMPA... | Mus musculus (Mouse) |
F6SZT2 | KHDC3_MACMU | MDTPRRFPTLVQLMQPKAMPVEVLGHLPKRFSWFHSEFLKNPKVVRLEVWLVEKIFGRDRERIPHVQGMSQILIHVNRLDPNGEAEILVFGRPSYQEDTIKMIMNLADYHRQLQAKGSGKALAQDVATKKAEIQLSSTEVREAGTQRSVEVREVGTQGSPVEVRETGTQQSLEAANQSGTQRSPEAASKAVTQRFSEDTRAPVTRL | null | null | positive regulation of dendrite development [GO:1900006]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of neurogenesis [GO:0050769]; regulation of protein localization [GO:0032880] | cell cortex [GO:0005938]; centrosome [GO:0005813]; chromosome [GO:0005694]; mitochondrion [GO:0005739]; 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, cell cortex {ECO:0000250|UniProtKB:Q9CWU5}. Nucleus {ECO:0000250|UniProtKB:Q9CWU5}. Mitochondrion {ECO:0000250|UniProtKB:Q9CWU5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9CWU5}. Chromosome {ECO:0000250|UniProtKB:Q587J8}. Note=Localized ... | null | null | null | null | null | FUNCTION: As part of the OOEP-KHDC3 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 (PubMed:33115731). Regulates homologous recombination-mediated DNA... | Macaca mulatta (Rhesus macaque) |
F6TQD1 | RN212_MOUSE | MASWVFCNRCFQSPHRKSSFSLTSCGHVYCHSCLLKGTKNECVICQAPCQTVLLSKHTNSNIQTFFLGIDGLCKKYSQETSQISEFQEKHRRRLVAFYQEKISQLEESLRKSVLQIKQLQSMRSSQQPAFNKIKNSVSTKPNGYLFLPPNSSLPDRIESMDIDLTPPARKPEMSAGPSRISVISPPQDGRMGSVTCRGPQHLSLTPSHASMTKASRVPPLQMPYKELSPPPASQLSSRATQGPSPSVSSSWTGPPRQPISISGLLQRQCAGSASPRGMDTEKMSPFLPSTPTNLRSVASPWHACVHR | 2.3.2.- | null | chiasma assembly [GO:0051026]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic gene conversion [GO:0006311]; protein sumoylation [GO:0016925]; reciprocal meiotic recombination [GO:0007131] | synaptonemal complex [GO:0000795] | metal ion binding [GO:0046872]; SUMO transferase activity [GO:0019789] | PF14634; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates to the synaptonemal complex. Localizes to a minority of double-strand breaks (DSBs) sites. Marks crossover sites during midpachynema. | null | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: SUMO E3 ligase that acts as a regulator of crossing-over during meiosis: required to couple chromosome synapsis to the formation of crossover-specific recombination complexes. Localizes to recombination sites and stabilizes meiosis-specific recombination factors, such as MutS-gamma complex proteins (MSH4 and ... | Mus musculus (Mouse) |
F6UA42 | UHRF1_XENTR | MWIQVRTMDGRDTRRIDSLSKLTKVEDLRARIQQIFGVALESQRLFYRGKQMENGHTLFDYSVGLNDIVQLLVRQIPDSVPTKDKECGISDADSGCGSGQGESDKNSSCGEGATDVDGQPAGINSENVGPSLYKKNDLVDARDLNMGAWFEAQIVSVSKRVNPDGMSAEILDTSAASDDIIYHVKYEDYPENGVVQLTYKDVRLRARTTLPWHDLKVGQVVMVNYNPDEPKERGYWYDAEILRKRETRTIKEIYVKVLLGDAGDSLNDCRIRFVDEIYKIEEPGSAYITTESPQKRQNGPECKHCKDNPKRACRMCACYV... | 2.3.2.27 | null | cell cycle [GO:0007049]; 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 protein catabolic process [G... | 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 | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}. Note=Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions (By similarity). {ECO:0000250}. | 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: 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... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
F6UH96 | SPRTN_XENTR | MQLSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGIEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINKRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGEFVKIKEPENYSQKRKRNNDPTKSELGNSSHVKINKGKSNGVDIRTVIPFSGTGYKLFEPSKSDAQLKIQNDNPTKDKAVMHHTPPSTNQTDSTFLSRKIVSAKKISVANTKVFINLNGSPIKLPSSSNNKSHQDSSKQ... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; | DNA damage response [GO:0006974]; positive regulation of protein ubiquitination [GO:0031398]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]; response to UV [GO:0009411]; translesion synthesis [GO:0019985] | chromatin [GO:0000785]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; single-stranded DNA binding [GO:0003697]; ubiquitin binding [GO:0043130] | PF10263; | 3.30.160.60; | Spartan family | PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:A0A1L8G2K9}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress. {ECO:0000250|UniProtKB:Q9H040}. | null | null | null | null | null | FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication an... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
F6VAN0 | ATF6A_MOUSE | MESPFSPVLPHGPDEDWESTLFAELGYFTDTDDVHFDAAHEAYENNFDHLNFDLDLMPWESDLWSPGSHFCSDMKAEPQPLSPASSSCSISSPRSTDSCSSTQHVPEELDLLSSSQSPLSLYGDSCNSPSSVEPLKEEKPVTGPGNKTEHGLTPKKKIQMSSKPSVQPKPLLLPAAPKTQTNASVPAKAIIIQTLPALMPLAKQQSIISIQPAPTKGQTVLLSQPTVVQLQSPAVLSSAQPVLAVTGGAAQLPNHVVNVLPAPVVSSPVNGKLSVTKPVLQSATRSMGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLG... | null | null | endoplasmic reticulum unfolded protein response [GO:0030968]; eye development [GO:0001654]; positive regulation of apoptotic process [GO:0043065]; positive regulation of ATF6-mediated unfolded protein response [GO:1903893]; positive regulation of autophagy [GO:0010508]; positive regulation of transcription by RNA polym... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulato... | PF00170; | 1.20.5.170; | BZIP family, ATF subfamily | PTM: During unfolded protein response, a fragment of approximately 50 kDa containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases (By similarity). {ECO:0000250|UniProtKB:P18850}.; PTM: N... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22682248}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P18850}; Single-pass type II membrane protein {ECO:0000255}. Note=Translocates from the endoplasmic reticulum to the Golgi, where it is ... | null | null | null | null | null | FUNCTION: [Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcrip... | Mus musculus (Mouse) |
F6Y5S8 | IMPA3_CALJA | MAPMGIRLSPLGVAVFCLLGLGVLYHLYSGFLAGRFSLFGLGGEPAGGAAGPPAAADGGTVDLREMLAVSVLAAVRGGDEVRRVRESNVLHEKSKGKTREGADDKMTSGDVLSNRKMFYLLKTAFPSVQINTEEHVDAADQEVILWDHKIPEDILKEVTAPKEVPAESVTVWIDPLDATQEYTEDLRKYVTTMVCVAVNGKPVLGVIHKPFSEYTAWAMVDGGSNVKARSSYNEKTPRIVVSRSHSGMVKQVALQTFGNQTTIIPAGGAGYKVLALLDVPDKSQEKADLYIHVTYIKKWDICAGNAILKALGGHMTTLSG... | 3.1.3.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | phosphatidylinositol phosphate biosynthetic process [GO:0046854]; skeletal system development [GO:0001501] | trans-Golgi network membrane [GO:0032588] | 3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; 3',5'-nucleotide bisphosphate phosphatase activity [GO:0097657]; 3'-nucleotidase activity [GO:0008254]; metal ion binding [GO:0046872] | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | PTM: Contains N-linked glycan resistant to endoglycosydase H. {ECO:0000250|UniProtKB:Q9NX62}. | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NX62}. Note=The catalytic core is predicted to res... | CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000250|UniProtKB:Q80V26}; | null | PATHWAY: Sulfur metabolism. {ECO:0000250|UniProtKB:Q80V26}. | null | null | FUNCTION: Exhibits 3'-nucleotidase activity toward adenosine 3',5'-bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',... | Callithrix jacchus (White-tufted-ear marmoset) |
F6ZDS4 | TPR_MOUSE | MTSGGSASRSGHRGVPMTSRGFDGSRRGSLRRAGARETASEAADGAAPAAGLRASPCSLASPSAAAAVAAIPADMAAVLQQVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVTETRECQNLRLELEKLNNQVKVLTEKTKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVAVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVLRLEEQMNGLKTS... | null | null | cell division [GO:0051301]; cellular response to heat [GO:0034605]; cellular response to interferon-alpha [GO:0035457]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mRNA export from nucleus [GO:0006406]; mRNA export from nucleus in response to heat stress [GO:0031990]; negative regulation of RNA export f... | chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; mitotic spindle [GO:0072686]; nuclear envelope [GO:0005635]; nuclear inclusion body [GO:0042405]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore nuclear b... | chromatin binding [GO:0003682]; dynein complex binding [GO:0070840]; heat shock protein binding [GO:0031072]; mitogen-activated protein kinase binding [GO:0051019]; mRNA binding [GO:0003729]; protein homodimerization activity [GO:0042803]; structural constituent of nuclear pore [GO:0017056]; tubulin binding [GO:0015631... | PF07926; | 1.10.287.1490; | TPR family | PTM: Phosphorylated. Phosphorylation occurs on serine and threonine residues (comprised in the C-terminal region) by MAPK1/ERK2 and stabilizes the interaction between these two proteins (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side {ECO:0000250|UniProtKB:P12270}. Nucleus envelope {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:12513910}. Nucleus, nuclear pore... | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral ch... | Mus musculus (Mouse) |
F7B113 | SL9A9_HORSE | MERQRRFMSEKDEYQFQHQGAVELLVFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIESGTVYDCGKLAFSPSTLLINITDQVYEYKYKREISQHNINPHLGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCIVIGLIMYGFVKAMVYAGQLKNGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLNDAVAIVLTYSISIYSPKENPNAFDAAAFFQSVGNFLGIFAGSFAMGSAYAVVTALLTKFTKLCEFPMLETGLFFLLS... | null | null | potassium ion transmembrane transport [GO:0071805]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]; sodium ion import across plasma membrane [GO:0098719]; sodium ion transmembrane transport [GO:0035725] | early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038] | potassium:proton antiporter activity [GO:0015386]; protein homodimerization activity [GO:0042803]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | null | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Early endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pas... | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:33118634}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.5 mM for Na(+) {ECO:0000269|PubMed:33118634}; | null | null | null | FUNCTION: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+) (PubMed:33118634). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH... | Equus caballus (Horse) |
F7BJB9 | MORC3_MOUSE | MAAQPPTGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAMVFTKNGETMSVGFLSQTYLEVIKAEHVVVPIVTFNKHRQMINLTESKASLAAILEHSLFSTEQKLLAELNAIMGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDETAGRKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIIIRGQKVKTQLVSKSLAYIERDVYRPKFLTRTVRITFGFNCRNKDHYGIMMYHK... | null | null | antiviral innate immune response [GO:0140374]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulatio... | chromatin [GO:0000785]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; methylated histone binding [GO:0035064]; protein-macromolecule adaptor activity [GO:0030674]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270] | PF13589;PF17942;PF07496; | 3.30.40.100;3.30.565.10; | null | PTM: Sumoylation is involved in interaction with PML and localization to PML nuclear bodies. {ECO:0000250|UniProtKB:Q14149}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17332504}. Nucleus matrix {ECO:0000250|UniProtKB:Q14149}. Nucleus, PML body {ECO:0000269|PubMed:17332504}. Chromosome {ECO:0000269|PubMed:27528681}. Note=Also found in PML-independent nuclear bodies. Localization to nuclear bodies is ATP-dependent. {ECO:000... | null | null | null | null | null | FUNCTION: Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response. Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFN... | Mus musculus (Mouse) |
F7BWT7 | TSN15_MOUSE | MPRGDSEQVRYCARFSYLWLKFSLIIYSTVFWLIGGLVLSVGIYAEAERQKYKTLESAFLAPAIILILLGVVMFIVSFIGVLASLRDNLCLLQSFMYILGICLVMELIGGIVALIFRNQTIDFLNDNIRRGIENYYDDLDFKNIMDFVQKKFKCCGGEDYRDWSKNQYHDCSAPGPLACGVPYTCCIRNTTDVVNTMCGYKTIDKERLNAQNIIHVRGCTNAVLIWFMDNYTIMAGLLLGILLPQFLGVLLTLLYITRVEDIILEHSVTDGLLGPGAKSRTDTAGTGCCLCYPD | null | null | negative regulation of Notch signaling pathway [GO:0045746]; protein localization to plasma membrane [GO:0072659]; protein maturation [GO:0051604]; regulation of membrane protein ectodomain proteolysis [GO:0051043] | cell junction [GO:0030054]; cell surface [GO:0009986]; cytosol [GO:0005829]; late endosome membrane [GO:0031902]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; tetraspanin-enriched microdomain [GO:0097197] | enzyme binding [GO:0019899] | PF00335; | 1.10.1450.10; | Tetraspanin (TM4SF) family | PTM: Palmitoylated. {ECO:0000250|UniProtKB:O95858}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30463011}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:O95858}. | null | null | null | null | null | FUNCTION: Part of TspanC8 subgroup, composed of 6 members that interact with the transmembrane metalloprotease ADAM10. This interaction is required for ADAM10 exit from the endoplasmic reticulum and for enzymatic maturation and trafficking to the cell surface as well as substrate specificity. Different TspanC8/ADAM10 c... | Mus musculus (Mouse) |
F7D4X9 | SIR5_MONDO | MSLLHFATRRLILQVLRELGLKAPPVHKTLKICIAMSRPSSNMADFRRFFARAKHIAIITGAGVSAESGVPTFRGPGGFWRKWKAEDLATPEAFAQNPSLVWEFYHYRREVILKKHPNAAHVAIAACEERLSLQGRRVVVITQNIDEFHTKAGTKNILELHGSLFKTRCCSCGNVRVNYNNPICPALEGKGLPDPNAPDAQIPLENLPRWKTTGDFSVLFLLDASPLYPSNLSCSHPVGAPALSEVADLGRWVGTSSLVYPAGMFGPHVALRGIPVAEFNTVTTPVTQNFRFHFSGLCGTTIPEALSPHESEKTG | 2.3.1.- | null | negative regulation of reactive oxygen species metabolic process [GO:2000378]; protein demalonylation [GO:0036046]; protein desuccinylation [GO:0036048]; regulation of ketone biosynthetic process [GO:0010566] | cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; protein-glutaryllysine deglutarylase activity [GO:0061697]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]; transferase activity [GO:0016740]; zinc ion binding [GO:00... | PF02146; | 3.30.1600.10;3.40.50.1220; | Sirtuin family, Class III subfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160}. Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03160}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03160}. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus... | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-malonyl-L-lysyl-[protein] + NAD(+) = 2''-O-malonyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47672, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11878, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87831, ChEBI:CHEBI:87833; E... | null | null | null | null | FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS... | Monodelphis domestica (Gray short-tailed opossum) |
F7E540 | TTLL7_XENTR | MPSLPNESDHQATCSLSLHSDLPYQPSSSIKRKVRKKKKNGAITANVVGTKYEIVRLVTEEMMFTKARDDDETANLIWNDCAVQHEKIAELRNYQRINHFPGMGEICRKDCLARNMTKMIKCQPHEYNFIPRTWIFPAEYTQFQTYIKELKKKRRQKTFIIKPANGAMGHGISLTRNGEKLQAQDHLIVQEYLEKPFLLESYKFDLRIYILVTSCDPLRIFLYNDGLVRMGTEKYHPPSESNLSQLYMHLTNYSVNKHNENFERDETENRGSKRSIKWFTEFLRANDYDISKFWNDISDLVVKTLIVAEPHVLHAYRMCR... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | cell differentiation [GO:0030154]; microtubule cytoskeleton organization [GO:0000226]; nervous system development [GO:0007399]; protein polyglutamylation [GO:0018095] | cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; microtubule [GO:0005874]; perikaryon [GO:0043204] | 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 | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9F0}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:A4Q9F0}. Cell projection, dendrite {ECO:0000250|UniProtKB:A4Q9F0}. Perikaryon {ECO:0000250|UniProtKB:A4Q9F0}. Note=In cells with primary cilia, found in both cilia and basal bo... | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChE... | 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 (PubMed:26875866, PubMed:28576883). Mediates both ATP-dependent initiation and elongation steps of the polyglutamyla... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
F7EQ49 | GPER1_MACMU | MEVTSQARGMGLEMYPGTMQPAAPNTTSPELNLSHPLLGASLANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHEQYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLN... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic chromosome condensation [GO:0030263]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to estradiol stimulus [GO:0071392]; cellular response to glucose stimulus [GO:0071333]; cellular response ... | axon [GO:0030424]; axon terminus [GO:0043679]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine head [GO:0044327]; dendritic spine membrane [GO:0032591]; early endosome [GO:0005769]; endoplas... | chromatin binding [GO:0003682]; G protein-coupled estrogen receptor activity [GO:0038054]; nuclear estrogen receptor activity [GO:0030284]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane and leads to proteasome-mediated degradation. {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Basolat... | null | null | null | null | null | FUNCTION: G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth f... | Macaca mulatta (Rhesus macaque) |
F7EZ75 | SIR5_MACMU | MRPLQIVPSRLISQLYCGLKPPASTRNQICLKMARPSSSMADFRKCFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPLAFAHNPSRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAGTKNLLEIHGSLFKTRCTSCGIVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDKELGRCDLCLVVGTSSVVYPAAMFAPQVAARGVPVAEFNTETTPATNRFRFHFQGPCGTTLPEALARHENETVS | 2.3.1.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03160}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03160}; | protein demalonylation [GO:0036046]; protein desuccinylation [GO:0036048]; regulation of ketone biosynthetic process [GO:0010566] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; protein-glutaryllysine deglutarylase activity [GO:0061697]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]; transferase activity [GO:0016740]; zinc ion binding [GO:00... | PF02146; | 3.30.1600.10;3.40.50.1220; | Sirtuin family, Class III subfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160}. Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03160}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03160}. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus... | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-malonyl-L-lysyl-[protein] + NAD(+) = 2''-O-malonyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47672, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11878, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87831, ChEBI:CHEBI:87833; E... | null | null | null | null | FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS... | Macaca mulatta (Rhesus macaque) |
F7FIH8 | NNRE_MONDO | MSGLRTLLGLGLLVSSSRFPRVVARGGPRCPGPAWWAARPMHLGDSTMAGGTVKYLSQEEAQAVDEELFNEYKFSVDQLMELAGLSCATAIAKAYPLSSFGSNPPAVLVICGPGNNGGDGLVCARHLKLFGYEPKIHYPKKPNKPLFDALVTQCQKMDIPFLPEVPPEPMLIDELYELVVDAIFGFSFKGAVREPFGTILSIMNGLTVPIASIDIPSGWDVEKGNPEGIRPDLLISLTAPKKAATLFKGRHHYLGGRFVPSDLEKKYQLNLPPYPGTDCVLQLQ | 5.1.99.6 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_03159}; Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03159}; | lipid transport [GO:0006869]; membrane raft distribution [GO:0031580]; negative regulation of angiogenesis [GO:0016525]; nicotinamide nucleotide metabolic process [GO:0046496]; regulation of cholesterol efflux [GO:0010874]; sprouting angiogenesis [GO:0002040] | cell body [GO:0044297]; cilium [GO:0005929]; extracellular space [GO:0005615]; mitochondrion [GO:0005739] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; NADHX epimerase activity [GO:0052856]; NADPHX epimerase activity [GO:0052857]; nucleotide binding [GO:0000166] | PF03853; | 3.40.50.10260; | NnrE/AIBP family | PTM: Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation. {ECO:0000255|HAMAP-Rule:MF_03159}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159}. Note=In sperm, secretion gradually increases during capacitation. {ECO:0000255|HAMAP-Rule:MF_03159}. | CATALYTIC ACTIVITY: Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215, ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6; Evidence={ECO:0000250|UniProtKB:Q8NCW5}; CATALYTIC ACTIVITY: Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227, ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6; Evidence={ECO:0000250|U... | null | null | null | null | FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothe... | Monodelphis domestica (Gray short-tailed opossum) |
F7FQM7 | APOA1_MACMU | MKATVLTLAVLFLTGSQARHFWQQDEPPQTPWDRVKDLVTVYVEALKDSGKDYVSQFEGSALGKQLNLKLLDNWDSVTSTVSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELHEGTRQKLHELHEKLSPLGEEVRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKASEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLSTQ | null | null | acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of cholesterol efflux [GO:0010875]; positive regulatio... | chylomicron [GO:0042627]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361] | cholesterol transfer activity [GO:0120020]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000250|UniProtKB:P02647}... | Macaca mulatta (Rhesus macaque) |
F7IX06 | PETH2_THEAE | MSVTTPRRETSLLSRALRATAAAATAVVATVALAAPAQAANPYERGPNPTESMLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAIAISPGYTGTQSSIAWLGERIASHGFVVIAIDTNTTLDQPDSRARQLNAALDYMLTDASSAVRNRIDASRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKSWRDITVPTLIIGAEYDTIASVTLHSKPFYNSIPSPTDKAYLELDGASHFAPNITNKTIGMYSVAWLKRFVDEDTRYTQFLCPGPRTGLLSDVEEYRSTCPF | 3.1.1.101; 3.1.1.74 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:30761732, ECO:0000269|Ref.5, ECO:0000305|PubMed:22183084}; Note=Can also bind other divalent metal ions with lower efficiency (PubMed:22183084). Calcium ion binding contributes to the thermostability of the protein (PubMed:22183084). {ECO:00002... | null | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | cutinase activity [GO:0050525]; metal ion binding [GO:0046872] | PF12146; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G8GER6}. Periplasm {ECO:0000250|UniProtKB:G8GER6}. | CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; PhysiologicalDirection=left-to-right; Xref=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.22 mM for pNP-acetate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; KM=3.41 mM for pNP-butyrate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; KM=2.37 mM for pNP-hexanoate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:221... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:20393707}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:20393707}; | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed:33387709). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed... | Thermobifida alba (Thermomonospora alba) |
F7J0M4 | RGA4R_ORYSJ | MEAALLSGFIKAILPRLFSLVDDKHKLHKGVKGDIDFLIKELRMIVGAIDDDLSLDHPAAAAVQTLCMEDLRELAHGIEDCIDGVLYRAARDQQQSPVRRAVQAPKKLQRNLQLAQQLQRLKRMAAEANQRKQRYTAAAPGQHGQVYSSAAAQVDEPWPSCSSASDPRIHEADLVGVDADREELLEQLAERQPEQLKVIAIVGFCGLGKTALAAEAYNRETGGGRFERHAWVCAGHRSAREVLGELLRRLDADGRSFHGDSDAGQLCVDIRQQLEKNRYFIVIDDIQTEDQWKSIKSAFPTDKDIGSRIVVTTTIQSVAN... | null | null | defense response to bacterium [GO:0042742]; innate immune response-activating signaling pathway [GO:0002758]; plant-type hypersensitive response [GO:0009626] | cytoplasm [GO:0005737] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; protein self-association [GO:0043621] | PF00931;PF18052; | 1.20.5.4130;1.10.8.430;3.40.50.300;3.80.10.10;1.10.10.10; | Disease resistance NB-LRR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25024433}. | null | null | null | null | null | FUNCTION: Disease resistance (R) protein. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Contribution... | Oryza sativa subsp. japonica (Rice) |
F7J0N2 | RGA5R_ORYSJ | MDAPASFSLGAMGPLLRKLDSLLVAPEIRLPKPLKEGIELLKEDLEEIGVSLVEHSVVDSPTHKARFWMDEVRDLSYHIEDCIDTMFSMRSGGDDGKPRSERRHKVGRAKIDGFSKKPKPCTRMARIAELRALVREASERLERYQLGDVCGSSSPVVFTADGRARPLHHGVSANLVGVDEFKTKLNRWLSDEEGPHLKVAAIVGPAGIGKTALATELYRDHRWQFECRAFVRASRKPDMQRLLGGILSQVQRRQRSSDAYADSTVQSLIDNLREHLQDRRYLIIIDGLWETAVWNIANSAFPDVNSFSRILITADIEQVA... | null | null | defense response to bacterium [GO:0042742]; innate immune response-activating signaling pathway [GO:0002758]; plant-type hypersensitive response [GO:0009626] | cytoplasm [GO:0005737] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein self-association [GO:0043621] | PF00931;PF18052; | 1.20.5.4130;3.30.70.100;1.10.8.430;3.40.50.300;3.80.10.10; | Disease resistance NB-LRR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25024433}. | null | null | null | null | null | FUNCTION: Disease resistance (R) protein that recognizes the AVR-Pia and AVR1-CO39 effector avirulence proteins from M.oryzae. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system inc... | Oryza sativa subsp. japonica (Rice) |
F8G0M4 | HSPB_PSEP6 | MSMKQRVIIVGGGPVGLLTALGLAKAGTNVVVLEAESQPSDSPRALVYHFPVLPHLKRLGVLDDCVAAGLMRQNFAWRVHSTSEMIFWDLSCLEGDVELPYALHLGQDKLSRILIEHLKALPNVEVRYSSPVVDCEVGPRSVRVVLGGESPGVIVEGDWLIGADGANSFVRREVLNQNFFGITWPQRYVATNTRFDFDKLGFGKTTMQVDDVYGSVICNIDADSLWRVTFMEDPNLPMEGIRGRIDQVFKELLPTNDPYEVVAFSPYRMHQRVTDRMRNGRVILIGDAAHVTNPTGGLGLTGGMFDAFALTSVLNQVIHD... | 1.14.13.163 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305|PubMed:21949128}; Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:21949128}; | alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608] | null | FAD binding [GO:0071949]; monooxygenase activity [GO:0004497] | PF01494; | 3.30.70.2450;3.50.50.60; | PheA/TfdB FAD monooxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 H(+) + 2 NADH + O2 = 2,5-dihydroxypyridine + H2O + 2 NAD(+) + succinate semialdehyde; Xref=Rhea:RHEA:33927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57706, ChEBI:CHEBI:57945, ChEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.175 mM for HSP {ECO:0000269|PubMed:21949128}; KM=0.2 mM for NADH {ECO:0000269|PubMed:21949128}; Note=kcat is 2 sec(-1). {ECO:0000269|PubMed:21949128}; | PATHWAY: Alkaloid degradation; nicotine degradation. {ECO:0000305|PubMed:21949128}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. At pH below 7.0 or above 9.0, there is substantial loss of activity. {ECO:0000269|PubMed:21949128}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. The enzyme activity measured at 5 degrees Celsius is maintained up to 25 degrees Celsius but is lost quickly at higher temperatures. {ECO:0000269|PubMed:21949128}; | FUNCTION: Involved in the nicotine degradation (PubMed:21949128). Catalyzes the cleavage of 6-hydroxy-3-succinoylpyridine (HSP) by incorporation of oxygen at the 3-position to produce to 2,5-dihydroxypyridine (DHP) and succinic semialdehyde (PubMed:21949128). {ECO:0000269|PubMed:21949128}. | Pseudomonas putida (strain DSM 28022 / S16) |
F8G0P1 | PNAO_PSEP6 | MTKDGDEGSKSGVSRRKFLGSAAVGVATAGIASQLLTLSAPAEAAVKTNVGPSRAGVGYDVIVIGGGFAGVTAAREASRSGLKTLILEGRSRLGGRTFTSKLQNQKVELGGTWVHWTQPNVWTEIMHYGLEVEETVGLANPETVIWVTEDNVKRAPAAEAFEIFGSACNEYYKEARNIYPRPFEPFFERKKLQHVDGLSAADYLEKLPLTREQKDMMDSWLSGNGHNYPETIAYSEIMRWFALSNFNMPTMFDSIARYKIKTGTHSLLEAIMADGNSEVKLSTPVTKVNQDKDKVTVTTEDGVFTASAVIVAVPINTLHD... | 1.4.2.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26634650, ECO:0000269|PubMed:35835223}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:35835223}; | alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608] | periplasmic space [GO:0042597] | oxidoreductase activity [GO:0016491] | PF01593; | 3.90.660.10;3.50.50.60; | Flavin monoamine oxidase family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:35835223}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + H2O + pseudooxynicotine = 4-oxo-4-(pyridin-3-yl)butanal + 2 Fe(II)-[cytochrome c] + 2 H(+) + methylamine; Xref=Rhea:RHEA:75351, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:5933... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.073 mM for pseudooxynicotine (at 30 degrees Celsius) {ECO:0000269|PubMed:26634650}; Note=kcat is 0.790 sec(-1) (at 30 degrees Celsius). {ECO:0000269|PubMed:26634650}; | PATHWAY: Alkaloid degradation; nicotine degradation. {ECO:0000269|PubMed:24204321}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:26634650}; | null | FUNCTION: Involved in nicotine degradation (PubMed:26634650, PubMed:35835223). Catalyzes the deamination of pseudooxynicotine to 3-succinoylsemialdehyde-pyridine (PubMed:26634650, PubMed:35835223). Functions as a dehydrogenase that uses the c-type cytochrome protein CycN as the physiological electron acceptor (PubMed:3... | Pseudomonas putida (strain DSM 28022 / S16) |
F8G0P2 | NICA2_PSEP6 | MSDKTKTNEGFSRRSFIGSAAVVTAGVAGLGAIDAASATQKTNRASTVKGGFDYDVVVVGGGFAGATAARECGLQGYRTLLLEARSRLGGRTFTSRFAGQEIEFGGAWVHWLQPHVWAEMQRYGLGVVEDPLTNLDKTLIMYNDGSVESISPDEFGKNIRIAFEKLCHDAWEVFPRPHEPMFTERARELDKSSVLDRIKTLGLSRLQQAQINSYMALYAGETTDKFGLPGVLKLFACGGWNYDAFMDTETHYRIQGGTIGLINAMLTDSGAEVRMSVPVTAVEQVNGGVKIKTDDDEIITAGVVVMTVPLNTYKHIGFTP... | 1.4.2.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:24204321, ECO:0000269|PubMed:27933790, ECO:0000269|PubMed:29812904, ECO:0000269|PubMed:32873764, ECO:0000269|PubMed:33432238, ECO:0000269|PubMed:33464876}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:27933790, ECO:0000269|PubMed:29812904, EC... | alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608] | periplasmic space [GO:0042597] | nucleotide binding [GO:0000166]; oxidoreductase activity [GO:0016491] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(S)-nicotine + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome c] + 2 H(+) + N-methylmyosmine; Xref=Rhea:RHEA:73655, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:59806, ChEBI:CHEBI:193521; EC=1.4.2.2; Evidence={ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43.5 nM for nicotine (at room temperature) {ECO:0000269|PubMed:26237398}; KM=91.9 nM for nicotine (at 37 degrees Celsius) {ECO:0000269|PubMed:26237398}; KM=114 nM for nicotine (at 22 degrees Celsius) {ECO:0000269|PubMed:29812904}; Note=kcat is 0.00664 sec(-1) with ... | PATHWAY: Alkaloid degradation; nicotine degradation. {ECO:0000269|PubMed:24204321}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:26237398}; | FUNCTION: Involved in nicotine degradation (PubMed:24204321, PubMed:26237398, PubMed:29812904, PubMed:33432238). Catalyzes the conversion of nicotine to N-methylmyosmine (PubMed:24204321, PubMed:29812904, PubMed:33432238, PubMed:33464876). N-methylmyosmine undergoes spontaneous hydrolysis to form pseudooxynicotine (PN)... | Pseudomonas putida (strain DSM 28022 / S16) |
F8J4S0 | TOP4A_OXYTA | MKISQVFIFVFLLMISVAWANEAYEEESNYLSERFDADVEEITPEFRGIRCPKSWKCKAFKQRVLKRLLAMLRQHAF | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; hemolysis in another organism [GO:0044179] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21933345, ECO:0000303|PubMed:21933345}. Target cell membrane {ECO:0000305|PubMed:21933345}. Note=Probably forms a transmembrane alpha-helix in the target cell membrane. {ECO:0000269|PubMed:21933345, ECO:0000303|PubMed:21933345}. | null | null | null | null | null | FUNCTION: Disrupts cell membranes through the formation of pores (Probable). Has antibacterial activity against Gram-positive bacteria S.aureus (MIC=10 uM) and B.subtilis (MIC=0.5 uM) as well as Gram-negative bacteria P.fluorescens (MIC=1 uM) and E.coli (MIC=0.5 uM). Has hemolytic activity against human erythrocytes (E... | Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) |
F8KAY7 | RSAKS_PSESP | MSRFIRASQRRTLLATLIAATLAQPLLAAESLDSKPASAITAAKNAEVLKNLPFADREEFEAAKRGLIAPFSGQIKNAEGQVVWDMGAYQFLNDKDAADTVNPSLWHQAQLNNIAGLFEVMPKLYQVRGLDPANMTIIEGDSGLVLIDTLTTAETARAALDLYFQHRPKKPIVAVVYSHSHIDHFGGARGIIDEADVKAGKVKVFAPSGFMEHAVSENILAGTAMARRGQYQSGVMVPRGAQAQVDSGLFKTTATNATNTLVAPNVLIEKPYERHTVDGVELEFQLTLGSEAPSDMNIYLPQFKVLNTADNAPPAMHNLL... | 3.1.6.19 | null | dodecyl sulfate metabolic process [GO:0018909] | outer membrane-bounded periplasmic space [GO:0030288] | linear primary-alkylsulfatase activity [GO:0018741]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983] | PF14864;PF14863;PF00753; | 1.25.40.880;3.60.15.30;3.30.1050.10; | Metallo-beta-lactamase superfamily, Type III sulfatase family | null | null | CATALYTIC ACTIVITY: Reaction=an (R)-secondary-alkyl sulfate + H2O = an (S)-secondary-alcohol + sulfate.; EC=3.1.6.19; Evidence={ECO:0000269|PubMed:21770430, ECO:0000269|PubMed:23061549, ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=151 uM for (R)-2-octyl sulfate {ECO:0000269|PubMed:23061549}; KM=651 uM for 1-octyl sulfate {ECO:0000269|PubMed:23061549}; Note=kcat is 262 min(-1) with (R)-2-octyl sulfate as substrate. kcat is 52 min(-1) with 1-octyl sulfate as substrate. {ECO:0000269|PubMed:2306... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Is very stable at 20-30 degrees Celsius. {ECO:0000269|Ref.2}; | FUNCTION: Alkylsulfatase that catalyzes the enantioselective hydrolysis of secondary-alkylsulfates with strict inversion of configuration, leading to the formation of homochiral (S)-configurated alcohols and nonreacted sulfate esters (PubMed:21770430, PubMed:23061549, Ref.2). The substrate spectrum includes a range of ... | Pseudomonas sp |
F8QN53 | PA2A2_VIPRE | MRILWIVAVCLIGVEGNLYQFGKMIRYKTGKSALLSYSDYGCYCGWGGQGKPKDATDRCCFVHDCCYGRVNGCDPKLTIYSYSFENGDIVCGGDDSCKRAVCECDRVAAICFGENLNTYDKKYKNYPSSQCTETEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21185324}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=3592 umol/min/mg enzyme (Vur-PL2B) {ECO:0000269|PubMed:21185324}; Note=Vmax=1736 umol/min/mg enzyme (Vur-PL2A). {ECO:0000269|PubMed:21185324}; | null | null | null | FUNCTION: Snake venom phospholipase A2 that causes internal bleeding, shows very strong anticoagulant activities and inhibits ADP-induced platelet aggregation (PubMed:21185324). Shows very low cytotoxicity (PubMed:21185324). Is not able (or very weakly) to suppress the acetylcholine (ACh)-evoked current mediated by alp... | Vipera renardi (Steppe viper) (Vipera ursinii renardi) |
F8QN54 | PA2B_VIPRE | MRTLWIVAVCLIGVEGSLLEFGMMILEETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCNPKIDRYKYHRKNGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNHIYKYYPDFLCKKESEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21185324}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=0.7 mmol/min/umol enzyme {ECO:0000269|PubMed:25522251}; | null | null | null | FUNCTION: Snake venom phospholipase A2 that may have a strong anticoagulant activity (PubMed:21185324). Is able to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7 (CHRNA7)-similar nAChRs in L.stagnalis neurons (IC(50)=10.5 uM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7... | Vipera renardi (Steppe viper) (Vipera ursinii renardi) |
F8S296 | ATG2_ARATH | MVFPWNIAKSAEEAFSRWAVKRVVKFLLKKKLGKLILGDIDLDQLDIQLRDGTIQLSDLAINVDYLNDKFDAPLVIKEGSIGSLLVKMPWKTNGCQVEVDELELVLAPRLESNKSSSNEASTSASTREDLHNIRLEIGKHENEMLMNAAKSASIDVHEGVKTVAKIVKWFLTSFHVKIKNLIIAFDPDFGKKQSEAGPRPTLVLRMTEIECGISEEQVSANEVSPDNFLGINRLANCVKFQGAVVELLNMDDDDDGDKTCDKKTSNDVTLIMTGVGGGFSGSLNFSIPWKNGSLDIRKVDADISIDPVEVRFQPSTIRWF... | null | null | autophagosome assembly [GO:0000045]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; leaf senescence [GO:0010150]; lipid transport [GO:0006869]; piecemeal microautophagy of the nucleus [GO:0034727]; protein transport [GO:0015031]; reticulophagy [GO:0061709] | endoplasmic reticulum membrane [GO:0005789]; phagophore assembly site membrane [GO:0034045] | phosphatidylinositol-3-phosphate binding [GO:0032266] | PF09333;PF13329;PF12624; | null | ATG2 family | null | SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q96BY7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96BY7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53855}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q2TAZ0}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phos... | null | null | null | null | FUNCTION: Lipid transfer protein involved in autophagosome assembly (PubMed:21645148). Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion (By similarity). Binds to the ER exit site (ERES), which is the membrane source for a... | Arabidopsis thaliana (Mouse-ear cress) |
F8VPJ6 | RFX7_MOUSE | MAEEQQQPPPQQLDAPQQLPLSAPNPGVALPALVPGLPGTEANALQHKIKNSICKTVQSKVDCILQEVEKFTDLEKLYLYLQLPSGLSSAEKSDQNAMSSSRAQQMHAFSWIRNTLEEHPETSLPKQEVYDEYKSYCDNLGYHPLSAADFGKIMKNVFPNMKARRLGTRGKSKYCYSGLRKKAFVHMPTLPNLDFHKTGDGLEGVEPSGQLQNIDEEVISSACRLVCEWAQKVLSQPFDTVLELAHFLVKSHYIGTKSMAALTVMAAAPAGLKGIPQPSAFIPTAESNSFQPQVKTLPSPIDAKQQLQRKIQKKQQEQKL... | null | null | positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979] | PF18326;PF02257; | 6.10.140.1290;1.10.10.10; | RFX family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29967452}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:29967452). Acts as a transcriptional activator by binding to promoter regions of target genes, such as Rec8, Mxd4 and Ddit4 (PubMed:29967452). Plays a role in natural killer (NK) cell maintenance and immunity (PubMed:29967452). May play a role in the process of ciliogenesis in the... | Mus musculus (Mouse) |
F8VPN2 | TEX15_MOUSE | MTYFFIYVSTERACSLNNCTIAKRIGKGKDATVIFEHFRKPVDPFVQENCPCKALNSEMGPFSSDTSSSYGNVQNGNNSVLEAYNRQTENSSNLRDASQVYTHNSGFSFIPTGNTASGNGDLFSVTYLRSILSSISAAFPSHNNTGSSTVITSKLIKDPRLMKREQSMRNKSDTAGLSDVLPLDKSLGCGDSQIKLTCMPTSSISSSEVPADNTITSCLNASCFKFSSESSHYQAHNSSSKGHDCIASSSIAVTEQFKEQHSSSFPSSLSNAFSDVRKQKHSEEQVQRAQMRSNVPVLTALSSESRNSDESENTCSNDSQ... | null | null | cell differentiation [GO:0030154]; DNA methylation-dependent heterochromatin formation [GO:0006346]; DNA repair [GO:0006281]; fertilization [GO:0009566]; homeostasis of number of cells within a tissue [GO:0048873]; homologous chromosome pairing at meiosis [GO:0007129]; male genitalia development [GO:0030539]; male meio... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF15326; | null | TEX15 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18283110, ECO:0000269|PubMed:32381626}. Nucleus {ECO:0000269|PubMed:18283110, ECO:0000269|PubMed:32381626, ECO:0000269|PubMed:32719317}. | null | null | null | null | null | FUNCTION: Required during spermatogenesis for normal chromosome synapsis and meiotic recombination in germ cells. Necessary for formation of DMC1 and RAD51 foci on meiotic chromosomes, suggesting a specific role in DNA double-stranded break repair (PubMed:18283110). Essential executor of PIWIL4-piRNA pathway directed t... | Mus musculus (Mouse) |
F8VPQ2 | ARI4A_MOUSE | MKAADEPAYLTVGTDVSAKYRGAFCEAKIKTVKRLVKVKVLLKQDNTTQLVQDDQVKGPLRVGAIVETRTSDGSIQEAIISKLTDASWYTVVFDDGDERTLRRTSLCLKGERHFAESETLDQLPLTNPEHFGTPVIAKKTNRGRRSSLPITEDEKEEESSEEEDEDKRRLNDELLGKVVSVASTAESTGWYPALVVSPSCNDDVTVKKDQCLVRSFIDSKFYSIARKDIKELDILTLPESELCARPGLRRASVFLKGRIVPDNWKMDISEILESSSSDDEECPAEEHEEEKEKEAKKEEEELPEEELDPEERDNFLQQLY... | null | null | chromatin organization [GO:0006325]; erythrocyte development [GO:0048821]; establishment of Sertoli cell barrier [GO:0097368]; genomic imprinting [GO:0071514]; negative regulation of cell migration [GO:0030336]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription b... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; transcription repressor complex [GO:0017053] | transcription cis-regulatory region binding [GO:0000976] | PF01388;PF08169;PF11717; | 2.30.30.140;1.10.150.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305|PubMed:17043311, ECO:0000305|PubMed:23487765}. | null | null | null | null | null | FUNCTION: DNA-binding protein which modulates activity of several transcription factors including RB1 (retinoblastoma-associated protein) and AR (androgen receptor) (PubMed:17043311, PubMed:23487765). May function as part of an mSin3A repressor complex (By similarity). Has no intrinsic transcriptional activity (PubMed:... | Mus musculus (Mouse) |
F8VPU2 | FARP1_MOUSE | MGEIEQKPTPASRLGAPENSGISTLERGQKPPPTPSGKLMTVKIQMLDDTQEAFEVPQRAPGKVLFDAVCNHLNLVEGDYFGLEFPDHRKIVVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYVPQQDALEDRIMEFHHSHVGQTPAESDFQLLEVARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDVNSSYQDTLEFLMAGRDFCKSFWKICVEHHAFFRLFE... | null | null | dendrite morphogenesis [GO:0048813]; enzyme-linked receptor protein signaling pathway [GO:0007167]; positive regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904395]; postsynaptic actin cytoskeleton organization [GO:0098974]; Rac protein signal transduction [GO:0016601]; regulation of presynaps... | cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extrinsic component of postsynaptic membrane [GO:0098890]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978] | cytoskeletal protein binding [GO:0008092]; guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267] | PF08736;PF09380;PF00373;PF09379;PF00169;PF00621; | 1.20.80.10;1.20.900.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23209303}; Peripheral membrane protein {ECO:0000269|PubMed:23209303}; Cytoplasmic side {ECO:0000269|PubMed:23209303}. Synapse {ECO:0000269|PubMed:23209303}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell projection, filopodium {ECO:0000... | null | null | null | null | null | FUNCTION: Functions as a guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
F8VPZ5 | ERCC6_MOUSE | MFHEEVPNSTHPQEQDCLPSQHANAYKDMPVGQENGGVSEAGECLSSTSCEYGPSTSAEACVLAATRRGPTLLHIDRHQIPAVEPSAQALELQGLGVDVYDQAVLEQGVLQQVDSAMHEASCVAQLADAEKEYQSVLDDLMSCTTSLRQINKIIEQLSPQAASNRDINRKLDSVKRQKYNKEQQLKKITAKQKRLQAILGGAGVQVELDHASLEEDDAEPGPSCLGSMLMPAQETAWEELIRTGQMTPFGTPAPQKQEKKPRKIMLNEASGFEKYLAEQAQLSFERKKQAATKRTAKKAIVISESSRAAIETKADQRSQV... | 3.6.4.- | null | base-excision repair [GO:0006284]; chromatin remodeling [GO:0006338]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA protection [GO:0042262]; DNA repair [GO:0006281]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; double-strand break repair via synt... | B-WICH complex [GO:0110016]; nucleolus [GO:0005730]; nucleus [GO:0005634]; site of DNA damage [GO:0090734]; transcription elongation factor complex [GO:0008023] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]; protein tyrosine k... | PF00271;PF00176; | 3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | PTM: Phosphorylated in a cell cycle-dependent manner at Ser-158 by cyclin A-CDK2 in response to DNA damage (By similarity). Phosphorylation at this site promotes the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain, thereby probably releasing the inhibitory effect of the N-termin... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03468}. | 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:Q03468}; | null | null | null | null | FUNCTION: Essential factor involved in transcription-coupled nucleotide excision repair which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (By similarity). Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby mod... | Mus musculus (Mouse) |
F8VQ03 | ADAM3_MOUSE | MLPLFLVLSYLGQVIAAGKDVETPLLQITVPEKIDTNIQDAKEAETQVTYVVRIEGKAYTLQLEKQSFLHPLFGTYLRDKLGTLQPYFSLVKTHCFYQGHAAEIPVSTVTLSTCSGLRGLLQLENITYGIEPLESSATFEHILYEIKNNKIDYSPLKENFANSEQESQSYRILVKPEKGSNSTLTKRILRIKIIMDKAMFDHMGSEVGVATQKVVHIFGLINTMFSQLKMTVMLNSLEIWSEQDKIETNGDADEVLQRFLLWKSKEISQKAQDITYLLLYKDHPDYVGATYHGMACNPNFTAGIALHPKTLAVEGFAIVL... | null | null | binding of sperm to zona pellucida [GO:0007339]; cell adhesion [GO:0007155]; fertilization [GO:0009566]; flagellated sperm motility [GO:0030317]; male gonad development [GO:0008584]; positive regulation of gene expression [GO:0010628]; proteolysis [GO:0006508]; regulation of mRNA processing [GO:0050684]; single fertili... | cell surface [GO:0009986]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sperm head [GO:0061827] | metalloendopeptidase activity [GO:0004222] | PF08516;PF00200;PF07974;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | null | PTM: Initially synthesized as a 110-kDa precursor in round spermatids, and the precursor is then processed into a 42-kDa mature protein during the sperm transport into and/or once in the epididymis. {ECO:0000269|PubMed:15514464, ECO:0000269|PubMed:24501175}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15514464}; Single-pass membrane protein {ECO:0000255}. Note=Localized in round and elongating spermatids. Localized on the anterior part of the sperm head, and is removed during the acrosome reaction. {ECO:0000269|PubMed:15514464}. | null | null | null | null | null | FUNCTION: Involved in fertilization by controlling sperm migration into the oviduct (PubMed:19339711). Promotes the binding of sperm to the oocyte zona pellucida (PubMed:32529245). {ECO:0000269|PubMed:19339711, ECO:0000269|PubMed:32529245}. | Mus musculus (Mouse) |
F8VQB6 | MYO10_MOUSE | MDSFFPEGARVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITNQKVTAMHPLHEEGVDDMASLAELHGGSIMYNLFQRYKRNQIYTYIGSIIASVNPYQPIAGLYERATMEEYSRCHLGELPPHIFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSVISQQTLDLGLQEKTSSVEQAILQSSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQQGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLDQGEREEFYLSLPENYHYLNQSGCTEDKTISDQESFRQVITAMEVMQFSK... | null | null | cell motility [GO:0048870]; cytoskeleton-dependent intracellular transport [GO:0030705]; positive regulation of cell-cell adhesion [GO:0022409]; regulation of cell shape [GO:0008360]; regulation of filopodium assembly [GO:0051489] | cell cortex [GO:0005938]; cytosol [GO:0005829]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; filopodium tip [GO:0032433]; lamellipodium [GO:0030027]; myosin complex [GO:0016459]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; ruffle [GO:0001726] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; plus-end directed microfilament motor activity [GO:0060002]; spectrin binding [GO:0030507] | PF00373;PF00612;PF16735;PF00063;PF00784;PF00169;PF18597; | 1.10.10.820;1.20.5.170;1.20.5.190;1.20.58.530;1.20.80.10;6.20.240.20;3.40.850.10;1.20.120.720;1.25.40.530;2.30.29.30; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | PTM: The initiator methionine for isoform Headless is removed. | SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cytoskeleton. Cell projection, filopodium tip. Cytoplasm, cell cortex. Cell projection, filopodium membrane; Peripheral membrane protein. Note=May be in an inactive, monomeric confor... | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments ... | Mus musculus (Mouse) |
F8VQN3 | GPR31_MOUSE | MERTNCSAASTVVETAVGTMLTLECVLGLMGNAVALWTFFYRLKVWKPYAVYLFNLVVADLLLATSLPFFAAFYLKGKTWKLGHMPCQVLLFLLAFSRGVGVAFLTTVALDRYLRVVHPRLRVNLLSLRAAWGISSLIWLLMVVLTPQNLLTCRTTQNSTECPSFYPTGGAKAIATCQEVLFFLQVLLPFGLISFCNSGLIRTLQKRLRESDKQPRIRRARVLVAIVLLLFGLCFLPSVLTRVLVHIFQEFKSCSVQQAIVRASDIAGSLTCLHSTLSPAIYCFSNPAFTHSYRKVLKSLRGRRKAAESPSDNLRDSYS | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of inflammatory response [GO:0050728]; positive regulation of immune response [GO:0050778]; response to acidic pH [GO:0010447]; response to ischemia [GO:0002931]; response to molecule of bacterial origin [GO:0002237] | plasma membrane [GO:0005886] | arachidonic acid binding [GO:0050544]; bioactive lipid receptor activity [GO:0045125]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00270}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: High-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12-S-HETE), with much lower affinities for other HETE isomers (By similarity) (PubMed:29227475). 12-S-HETE is a eicosanoid, a 12-lipoxygenase (ALOX12) metabolite of arachidonic acid, involved in many physiologic and pathologic processe... | Mus musculus (Mouse) |
F8W2M1 | HACE1_DANRE | MERAMEHLNVQLNRLTRSLRRARTVELPEDSETAVYTLMPMVMADQHRSVSELLLNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKRGANPNYQDISGCTPLHLAARNGQKKCMGRLLEYNADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLPDRNGVTPLDLCVQGGYGETCEILIQHHGRLFQTLIQMTQNDDIKENMLRQVLEHVSQQNDSNYQRILTSLAEVATTNGHKLLSLSSNFEVQ... | 2.3.2.26 | null | atrioventricular valve formation [GO:0003190]; cardiac ventricle morphogenesis [GO:0003208]; cell cycle [GO:0007049]; Golgi organization [GO:0007030]; heart looping [GO:0001947]; membrane fusion [GO:0061025]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; protein K48-linked ubiquitina... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | small GTPase binding [GO:0031267]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF12796;PF13637;PF00632; | 1.25.40.20;3.30.2160.10;3.30.2410.10;3.90.1750.10; | null | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. | 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=2.3.2.26; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golg... | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W2M8 | TPP1_DANRE | MRVAVFVLSFIWLVNGELLEADQDAVVPGDWTFLGRVGPLEEVELTFALKQQNVSKMEELLKLVSDPDSHQYGKYLSLDEVAALSRPSPLTEKVVENWLRSHGVMDCHTIITRDFLQCVMTVEVAEALLPGSKFHRFSKNTKTLLRSTSQYSVHEDVHQHLDFVGGVHRFPQKRKIVSKGWEGARQAILGYHLGVTPAVIRNRYNLTAKDVGTAANNSQAVAQFLEQYYHPADLAEFMSLFGGGFTHMSTVERVVGTQGGGKAGIEASLDVEYIMSSGANISTWVFTNPGRHESQEPFLQWMLLLSNMSAVPWVHTISYG... | 3.4.14.9 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O14773}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:O14773}; | central nervous system development [GO:0007417]; locomotory behavior [GO:0007626]; neurogenesis [GO:0022008]; proteolysis [GO:0006508] | lysosome [GO:0005764] | endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]; tripeptidyl-peptidase activity [GO:0008240] | PF00082;PF09286; | 3.40.50.200; | null | PTM: Activated by autocatalytic proteolytical processing. {ECO:0000250|UniProtKB:O14773}. | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:O14773}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.; EC=3.4.14.9; Evidence={ECO:0000269|PubMed:23587805}; | null | null | null | null | FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:23587805). May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (By similarity). Requires substrates with an unsubstituted N-terminus (By similarity). {ECO... | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W3R9 | ALK_DANRE | MIARILYFFLWSAAFLPELQCASQRTADALTTFPTSAFINGTDRKDSNQTSTSRIKRKTLSVDFAVPSLLRYYLALFIKRPLNGDCLSFNGCYTVRANLLMRCVPLQKTIAGLLDAKLAAMNVNRSSTGQLPYRQKRPVPKVLNLGLTSASRKSNQVVVEVGEEMVKTGCGGLHVYEDAPVVFLEMDLTRILEWWLGAEGGRLRVRLMPERKVQVPGKEDKYSAAIRASDARLFIQIASSERPSSTISRNPTVAPKYWNFSWIAEDELTFPEDPVSTSDCTSKAKSCDRRPDGYYPEFAWSLTSAEDSWAIDQTMVKTKA... | 2.7.10.1 | null | phosphorylation [GO:0016310]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neurogenesis [GO:0050769]; regulation of cell population proliferation [GO:0042127]; regulation of neuron differentiation [GO:0045664]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF12810;PF00629;PF07714; | 2.60.120.200;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UM73}; Single-pass type I membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000250|UniProtKB:Q9UM73}; | null | null | null | null | FUNCTION: Receptor tyrosine kinase required for neurogenesis in the developing central nervous system (PubMed:23667670). Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response (PubMed:29078341). Ligand-binding to the extr... | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W3X3 | PCD19_DANRE | MHSKDMDFVQMFVCFLLCWTGVDAVFNLKYTVEEELRAGTKIANVTADAKVAGFALGNRQPYLRVISNSEPRWVNLSPAGLLITKQKIDRDAVCRQTPKCFISLEVMSNSMEICVIKIEIIDVNDNAPRFPTNHIDIEISENAAPGTRFPLEGASDPDSGSNGIQTYTITPNDIFGLEIKTRGDGSKIAELVVEKTLDRETQSRYTFELTAEDGGDPPKSGTVQLNIKVIDSNDNNPVFDEPVYTVNVLENSPINTLVIDLNATDPDEGTNGEVVYSFINFVSNLTKQMFKIDPKTGVITVNGVLDHEELHIHEIDVQAK... | null | null | brain morphogenesis [GO:0048854]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; excitatory postsynaptic potential [GO:0060079]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; neural tube formation [GO:0001841]; regulation of neuronal action potential [GO:0098908]; visual pe... | membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynapse [GO:0098794] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802] | PF00028;PF08266; | 2.60.40.60; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21115806}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Calcium-dependent cell-adhesion protein (PubMed:21115806). Essential for the early stages of neurulation in the anterior neural plate (PubMed:19615992). Shows little cell adhesion activity on its own but exhibits robust homophilic cell adhesion when in a complex with cadherin cdh2 and appears to mediate the a... | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W463 | P2X4A_DANRE | MSESVGCCDSVSQCFFDYYTSKILIIRSKKVGTLNRFTQALVIAYVIGYVCVYNKGYQDTDTVLSSVTTKVKGIALTNTSELGERIWDVADYIIPPQEDGSFFVLTNMIITTNQTQSKCAENPTPASTCTSHRDCKRGFNDARGDGVRTGRCVSYSASVKTCEVLSWCPLEKIVDPPNPPLLADAENFTVLIKNNIRYPKFNFNKRNILPNINSSYLTHCVFSRKTDPDCPIFRLGDIVGEAEEDFQIMAVHGGVMGVQIRWDCDLDMPQSWCVPRYTFRRLDNKDPDNNVAPGYNFRFAKYYKNSDGTETRTLIKGYGI... | null | null | calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; monoatomic cation transport [GO:0006812]; response to ATP [GO:0033198] | membrane [GO:0016020]; monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; transmembrane transporter complex [GO:1902495] | ATP binding [GO:0005524]; ATP-gated ion channel activity [GO:0035381]; CTP binding [GO:0002135]; extracellularly ATP-gated monoatomic cation channel activity [GO:0004931]; ligand-gated monoatomic ion channel activity [GO:0015276]; purine nucleotide binding [GO:0017076]; purinergic nucleotide receptor activity [GO:00016... | PF00864; | 1.10.287.940;2.60.490.10; | P2X receptor family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99571}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q99571}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q99571}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q99571}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out... | null | null | null | null | FUNCTION: ATP-gated nonselective transmembrane cation channel permeable to potassium, sodium and calcium (By similarity). CTP, but not GTP or UTP, functions as a weak affinity agonist for P2RX4 (PubMed:28332633). Activated by extracellularly released ATP, it plays multiple role in immunity and central nervous system ph... | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W4H9 | MRP2A_DANRE | MPRFQLSNSTSVPNHNYEWSYEYYDDEEPVSFEGLKAHRYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHPEAAEPYEKRMRLTSCADGLGRQRETDGRTGLSRPLLEESRSLFHCYINEEEREGGRAATDAGALTHGRSGIGNSRGQVEEVGLVVQNMVLESRAEREAALLAHFNIPNFVNSELNSALGDEDLLLGDPPIIMEEARPRCTHHIID | null | null | developmental growth [GO:0048589]; energy homeostasis [GO:0097009]; energy reserve metabolic process [GO:0006112]; negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106072]; protein localization to cell surface [GO:0034394]; protein localization to plasma membrane [GO... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | corticotropin hormone receptor binding [GO:0031780]; signaling receptor regulator activity [GO:0030545]; type 1 melanocortin receptor binding [GO:0070996]; type 3 melanocortin receptor binding [GO:0031781]; type 4 melanocortin receptor binding [GO:0031782]; type 5 melanocortin receptor binding [GO:0031783] | PF15183; | null | MRAP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Inhibitor of melanocortin receptor 4 (mc4r), a receptor involved in energy homeostasis. Plays a role during larval development in the control of energy homeostasis and body weight regulation by decreasing ligand-sensitivity of mc4r and mc4r-mediated generation of cAMP, leading to stimulate growth during larva... | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8WQK8 | DPP11_POREA | MNKRFFPTLLLAFVCSTLAYADGGMWLMQQINGQVARMKSLGMQLEAADIYNPNGSSLKDAVVMFDGGCTGVLVSNQGLLLTNHHCGYDQIQKHSSVQHNYLKDGFWSYSLAEELVNPGLEVEIVDEITDVTAAVKKELERIKKPSGLEFLSPRYLSSLAPEIVGKKAASRPGYRYEIKAFYGGNRYYMFTKKVFRDVRLVAAPPSSIGKFGSDTDNWAWPRHTGDFSIFRLYADKNGNPAEYSKDNVPYRPKRWVKVNAQGVKEGDFALIMGYPGTTYKFFTADEVTEWSEIDNNIRIEMRGILQDVMLREMLADPKIN... | 3.4.14.- | null | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cell surface [GO:0009986]; extracellular region [GO:0005576] | dipeptidyl-peptidase activity [GO:0008239]; serine-type aminopeptidase activity [GO:0070009] | PF10459; | 2.40.10.10; | Peptidase S46 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21896480}. Cell surface {ECO:0000269|PubMed:21896480}. Note=Is observed in both cell-associated and soluble extracellular forms. {ECO:0000269|PubMed:21896480}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:21896480}; | null | FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Is likely involved in amino acid metabolism and bacterial growth/survival of asaccharolytic P.e... | Porphyromonas endodontalis (strain ATCC 35406 / DSM 24491 / JCM 8526 / CCUG 16442 / BCRC 14492 / NCTC 13058 / HG 370) (Bacteroides endodontalis) |
F9FRH4 | MNLOX_FUSOF | MVALLIFLGIFTCVETLPLSDSPSSYIPEEVPSSQTADIGLPPPTEFTLPNEDDEILIRKLNIQKTRKEILYGPSLIGKTSFFISGPLGDQISQRDQTLWSRDAAPVVQAVSHDAAAALHDIQIHGGLQNLDDYKILYQGHWSSSVPGGIAKGQFSNFTSDLLFSMERLSTNPYILRRLHPHADELPFAVDSKIVQKLTGSTLPSLHKAGRLFLADHSYQKDYVAQEGRYAAACQALFYLDDRCHQFLPLAIKTNVGSNLTYTPLDEPNDWLLAKVMFNVNDLFHGQMYHLASTHAVAEIVHLAALRTMSSRHPVLALLQ... | 1.13.11.-; 1.13.11.45 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:26113537}; Note=Three His residues, the carboxyl oxygen of the C-terminal Ile or Val residue, and a fifth residue, usually Asn, ligate the metal, which binds water to form a catalytic base Mn(2+)OH(2) for hydrogen abstraction. {ECO:0000250|UniP... | arachidonic acid metabolic process [GO:0019369]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372] | extracellular region [GO:0005576] | linoleate 11-lipoxygenase activity [GO:0050584]; linoleate 13S-lipoxygenase activity [GO:0016165]; metal ion binding [GO:0046872] | PF00305; | 3.10.450.60; | Lipoxygenase family, Manganese lipoxygenase subfamily | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:26113537}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8X151}. | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (11S)-hydroperoxy-(9Z,12Z)-octadecadienoate; Xref=Rhea:RHEA:18993, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57467; EC=1.13.11.45; Evidence={ECO:0000250|UniProtKB:Q8X151}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (11R)-hydroperox... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29 uM for linoleate {ECO:0000269|PubMed:26113537}; | null | null | null | FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9-, 11- and 13-hydroperoxy fatty acids. Oxidizes linoleic acid to mainly 11R-, 13S- and racemic 9-HPODE, and alpha-linolenic acid to 11-HPOTrE. {ECO:0000269|PubMed:26113537}. | Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt) |
F9UMS6 | MLES_LACPL | MTKTASEILNNPFLNKGTAFTKEERQALGLTGTLPSKVQTIDEQATQAYAQFKSKPSRLEQRIFLMNLFNENRTLFFHLMDEHVVEFMPIVYDPVVADSIEQYNELFLDPQNAAFVSVDAPEDIEATLKNAADGRDIRLVVVTDAEGILGMGDWGVNGVDIAIGKLMVYTAAAGIDPSQVLPVSIDAGTNNQKLLDDPLYLGNRHKCVSGEQYYDVIDKFVAAEQQLFPDSLLHFEDFGRDNAQVILDKYKDQIATFNDDIQGTGMVVLAGILGALNISKESIKDQKILSFGAGTAGMGIANQILDELMQAGLTEEEAKQ... | 4.1.1.101 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:6833282}; COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:6833282}; | malate metabolic process [GO:0006108]; malolactic fermentation [GO:0043464]; pyruvate metabolic process [GO:0006090] | cytosol [GO:0005829] | carboxy-lyase activity [GO:0016831]; malate dehydrogenase (decarboxylating) (NAD+) activity [GO:0004471]; malolactic enzyme activity [GO:0043883]; manganese ion binding [GO:0030145]; NAD binding [GO:0051287] | PF00390;PF03949; | 3.40.50.10380;3.40.50.720; | Malic enzymes family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-malate + H(+) = (S)-lactate + CO2; Xref=Rhea:RHEA:46276, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:16651; EC=4.1.1.101; Evidence={ECO:0000269|PubMed:6833282}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.012 mM for manganese {ECO:0000269|PubMed:6833282}; KM=0.059 mM for NAD {ECO:0000269|PubMed:6833282}; KM=9.5 mM for (S)-malate {ECO:0000269|PubMed:6833282}; | null | null | null | FUNCTION: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate. {ECO:0000269|PubMed:6833282}. | Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum) |
F9UPU7 | KT3K_LACPL | MHLTKTWLAQLPLTDIQQVQPVSGGDINAAFQIITRHHQYFLKVQPHNDVTFFDHEVAGLRLLGAVTKTPRVIASGTIATDGYLLLDWLATGTGSQSALGAAVAKVHHQHHAQFGLDHDFTAGKLPKINHWQTDWATFYTQQRLDVLVNLAKEHHLWSETREMHYHRLRQQLLQDSHMHTVKPSLLHGDLWSGNYLFDTTGTPVLIDPDVFYGDREMDLAMTTIFGGFDTDFYQAYQAAYPVAPGMQDRLPSYQLYYLLAHLNLFGETYGPAVDRILMQY | 2.7.1.- | null | phosphorylation [GO:0016310] | null | ATP binding [GO:0005524]; kinase activity [GO:0016301]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]; protein-ribulosamine 3-kinase activity [GO:0102193] | PF03881; | 3.90.1200.10; | Fructosamine kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + N(6)-(D-ribulosyl)-L-lysine = ADP + H(+) + N(6)-(3-O-phospho-D-ribulosyl)-L-lysine; Xref=Rhea:RHEA:61400, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144590, ChEBI:CHEBI:144611, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17681011}; PhysiologicalDirection=left-to-right; Xre... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for free ribuloselysine {ECO:0000269|PubMed:17681011}; KM=340 uM for free ribulosecadaverine {ECO:0000269|PubMed:17681011}; KM=60 uM for free erythruloselysine {ECO:0000269|PubMed:17681011}; KM=63 uM for free erythrulosecadaverine {ECO:0000269|PubMed:1768101... | null | null | null | FUNCTION: Ketoamine kinase that phosphorylates ketoamines, such as erythruloselysine, erythrulosecadaverine, ribuloselysine and ribulosecadaverine, on the third carbon of the sugar moiety to generate ketoamine 3-phosphate (PubMed:17681011). Has higher activity on free lysine (erythruloselysine and ribuloselysine), than... | Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum) |
F9USS9 | LARA_LACPL | MVAIDLPYDKRTITAQIDDENYAGKLVSQAATYHNKLSEQETVEKSLDNPIGSDKLEELARGKHNIVIISSDHTRPVPSHIITPILLRRLRSVAPDARIRILVATGFHRPSTHEELVNKYGEDIVNNEEIVMHVSTDDSSMVKIGQLPSGGDCIINKVAAEADLLISEGFIESHFFAGFSGGRKSVLPGIASYKTIMANHSGEFINSPKARTGNLMHNSIHKDMVYAARTAKLAFIINVVLDEDKKIIGSFAGDMEAAHKVGCDFVKELSSVPAIDCDIAISTNGGYPLDQNIYQAVKGMTAAEATNKEGGTIIMVAGAR... | 5.1.2.1 | COFACTOR: Name=Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide; Xref=ChEBI:CHEBI:137373; Evidence={ECO:0000269|PubMed:26138974}; Note=Was originally shown to use Ni(2+) as a cofactor (PubMed:24710389), but in fact, the cofactor is a (SCS)Ni pincer complex, a nicotinic acid mononucleotide derivative that is cova... | null | null | lactate racemase activity [GO:0050043]; metal ion binding [GO:0046872] | PF09861;PF21113; | 3.40.50.11440;3.90.226.30; | Lactate racemase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-lactate = (R)-lactate; Xref=Rhea:RHEA:10960, ChEBI:CHEBI:16004, ChEBI:CHEBI:16651; EC=5.1.2.1; Evidence={ECO:0000269|PubMed:24710389, ECO:0000269|PubMed:26138974}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46 mM for L-lactate {ECO:0000269|PubMed:24710389}; KM=11 mM for D-lactate {ECO:0000269|PubMed:24710389}; Note=kcat is 4745 sec(-1) for conversion of L-lactate to D-lactate. kcat is 1333 sec(-1) for conversion of D-lactate to L-lactate. {ECO:0000269|PubMed:24710389}... | null | null | null | FUNCTION: Catalyzes the interconversion between the D- and L-isomers of lactate (PubMed:24710389, PubMed:26138974). May act as a rescue enzyme to ensure D-lactate production in physiological conditions where its production by the D-lactate dehydrogenase LdhD is not sufficient (PubMed:16166538). D-Lactate is absolutely ... | Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum) |
F9UST4 | LARE_LACPL | MATLATKKATLVAALKDLQRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHIKNNTPDSWYYAKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQELGLTNWNKVASCSVSSRFPYGTTLTHDNIAQVMAAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLVFNDRVNRQLQSLGFRYVTLDLGGFRSGRMNDTLTKAQLATFA | 4.4.1.37 | null | null | null | ATP binding [GO:0005524]; lyase activity [GO:0016829]; sulfurtransferase activity [GO:0016783] | PF02540; | 3.40.50.620; | LarE family | null | null | CATALYTIC ACTIVITY: Reaction=[LarE protein]-L-cysteine + ATP + pyridinium-3,5-dicarboxylate mononucleotide = [LarE protein]-dehydroalanine + AMP + diphosphate + H(+) + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide; Xref=Rhea:RHEA:54788, Rhea:RHEA-COMP:13982, Rhea:RHEA-COMP:13985, ChEBI:CHEBI:15378, ChEBI:CH... | null | null | null | null | FUNCTION: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Catalyzes the ATP-dependent incorporation of two sulfur atoms in pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN) to yield pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN). The source of sulfur is the en... | Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum) |
F9VMT6 | FBPAP_SULTO | MKTTISVIKADIGSLAGHHIVHPDTMAAANKVLASAKEQGIILDYYITHVGDDLQLIMTHTRGELDTKVHETAWNAFKEAAKVAKDLGLYAAGQDLLSDSFSGNVRGLGPGVAEMEIEERASEPIAIFMADKTEPGAYNLPLYKMFADPFNTPGLVIDPTMHGGFKFEVLDVYQGEAVMLSAPQEIYDLLALIGTPARYVIRRVYRNEDNLLAAVVSIERLNLIAGKYVGKDDPVMIVRLQHGLPALGEALEAFAFPHLVPGWMRGSHYGPLMPVSQRDAKATRFDGPPRLLGLGFNVKNGRLVGPTDLFDDPAFDETRR... | 3.1.3.11; 4.1.2.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15274916}; Note=Can also use Zn(2+) or Mn(2+) in vitro, although with much less efficiency than Mg(2+). {ECO:0000269|PubMed:15274916}; | dephosphorylation [GO:0016311]; gluconeogenesis [GO:0006094]; NADPH regeneration [GO:0006740] | null | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; fructose-bisphosphate aldolase activity [GO:0004332]; magnesium ion binding [GO:0000287] | PF01950; | null | FBP aldolase/phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983966}; ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.027 mM for D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 80 degrees Celsius) {ECO:0000269|PubMed:15274916}; KM=0.027 mM for D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 48 degrees Celsius) {ECO:0000269|PubMed:21983966}; ... | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305|PubMed:20348906, ECO:0000305|PubMed:21983966}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:15274916}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is over 100 degrees Celsius. {ECO:0000269|PubMed:15274916}; | FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P). {ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:20348906, EC... | Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) |
F9VN79 | RNH_SULTO | MIIGYFDGLCEPKNPGGIATFGFVIYLDNRKIEGYGLAEKPFSINSTNNVAEYSGLICLMETMLRLGISSPIIKGDSQLVIKQMNGEYKVKAKRIIPLYEKAIELKKKLNATLIWVPREENKEADRLSRVAYELVRRGKLRDIGCIILT | 3.1.26.4 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15520465}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15520465}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:15520465}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:15520465}; No... | null | cytoplasm [GO:0005737] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF13456; | 3.30.420.10; | null | PTM: The disulfide bond confers considerable stability to the protein. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408, ECO:0000269|PubMed:15520465}; | null | null | null | null | FUNCTION: Nuclease that specifically degrades the RNA of RNA-DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. In the presence of Mn(2+) or Co(2+) can also cleave an RNA-RNA hybrid; the dsRNase activity is 10- 100-fold lower than RNase H activity. Co... | Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) |
F9W301 | KN1_ORYSJ | MSNVTVCVRFRPLSHKERKTNGDKVCFKRLDSESFVFKDEREEDVIFSFDRVFYEDAEQSDVYNFLAVPIVADAISGINGTIITYGQTGAGKTYSMEGPSILHCNKQKTGLVQRVVDELFQSLQSSESMAMWSVKLSMVEIYLEKVRDLLDLSKDNLQIKESKTQGIYISGATEVSIQNSSDALECLSEGIANRAVGETQMNLASSRSHCLYIFSVQQGSTSDERVRGGKIILVDLAGSEKVEKTGAEGRVLDEAKTINKSLSVLGNVVNALTTGKPNHVPYRDSKLTRILQDALGGNSRAALLCCCSPSASNAPESLST... | null | null | anterograde dendritic transport of neurotransmitter receptor complex [GO:0098971]; axon guidance [GO:0007411]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; synaptic vesicle transport [GO:0048489] | cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, KIN-1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21282525}. | null | null | null | null | null | FUNCTION: Kinesin-like motor protein that exhibits microtubule-stimulated ATPase activity. Plays an essential role in male meiotic chromosomal dynamics, male gametogenesis and anther dehiscence. May play a minor and nonessential role in regulating meiotic spindle formation. {ECO:0000269|PubMed:21282525}. | Oryza sativa subsp. japonica (Rice) |
F9WWF1 | GGS2_ZYMTI | MLDVRGSLPGQVNTGTISPYRRIDRSNDTIGTSDLAADEQVLLGPFNHLDARPGKEIRSQLIDAFDSWLQVPTASLAVIKNVVRMLHNASLLIDDIQDNSELRRGAPAAHHAFGTAQTINSANYVYFRALRELSTLHNPVMVQIYTAELLNLHHGQGMDLFWRETGTCPTESRYLEMVGNKTGGLFRLAIRCMCVEGSPKQSSADYIRLATMIGILFQILDDFRNLTDGSYTSSKGFCEDLTEGKFSFPIVHAIRSNPGDSFLHDILRQHTDDPAVKKEAVSYLERCGSLIYTQGVIHQLAGDVLTLADEVDAGQGRAQA... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | null | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster 3 that mediates the biosynthesis of an isoprenoid secondary metabolite. {ECO:0000269|PubMed:28818040}. | Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch fungus) (Septoria tritici) |
F9WZD2 | GSS1_ZYMTI | MDKFSQSPPLRDDLVRGSSLNWTKEKENILKGPFNYLESHPGKDIRSQLIAAFNAWLDVPEESLNVIRRVVAMLHTASLLIDDVEDNSQLRRGIPVAHNVFGTAQTINSANYVYFCALKELAILNNPAVIQIYTEELVNLHRGQGMDLFWRDTLTCPSEDDYLEMVGNKTGGLFRLAIKLMCAESPSHNAHPDPFQRNDYVPLVNTIGLLFQILDDYKNLSDTIYTQNKGLCEDLTEGKFSFPIIHAIRADPGNLVLINILKQKTTDDEVKKYAVAYMDRAGSFSYTRKVLRGLTKKALTQVDEVDAGRGRGEQMKTILE... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | null | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster 4 that mediates the biosynthesis of an isoprenoid secondary metabolite. {ECO:0000269|PubMed:28818040}. | Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch fungus) (Septoria tritici) |
F9XLC1 | GGS3_ZYMTI | MHISTIKTAGSSGMSHMNEAYSSTTATEMVARGAGSEIIHTEIDSNGSKELAPNGAQSRVQKPSEDAVRAPYDYIRTLPSKRIRETFIDALDSWLAVPAGSSTSIKSIIGMLHQSSLMLDDIEDDSTLRRGKPTAHTLFGTAQTINSANWVFVCAFEELRQLRGVDAATVFVEELKNLHCGQALDLHWKHHTYIPSVDEYLNMVDHKTGGLFRLCVRLMQGESSTSCHHIDAERFITLLGRYFQIRDDYQNLVSDEYTNQKGFCEDLDEGKISLPLIYCLAGSDPTQIMIKGILQHKRTGEMPLSMKKLILEKMRSGGAL... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | null | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster 25 that mediates the biosynthesis of an isoprenoid secondary metabolite. {ECO:0000269|PubMed:28818040}. | Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch fungus) (Septoria tritici) |
G0HV10 | PYRG_HALHT | MPTEPETDYDPELGRKFIFVTGGVMSGLGKGITAASTGRLLKNAGFDVTAVKIDPYLNVDAGTMNPFQHGEVYVLKDGGEVDLDLGNYERFLDIDMTFDHNVTTGKTYQHVIEKERSGDYLGRTVQIIPHITDDIKRRIREAAEGNDVCIIEVGGTVGDIEGMPYLEALRQFAHEEDEDDILFTHVTLVPYSKNGEQKTKPTQHSVKELRSIGLQPDILVGRCSDKLDIDTKEKIALFCDVPTEAVFSNPDVDDIYHVPLMVEEEGLDQYVMEELDIATEALPEDERENRWRDLVTQNTEGEVDIALVGKYDLEDAYMSV... | 6.3.4.2 | null | 'de novo' CTP biosynthetic process [GO:0044210]; glutamine metabolic process [GO:0006541]; pyrimidine nucleobase biosynthetic process [GO:0019856] | cytoophidium [GO:0097268]; cytosol [GO:0005829] | ATP binding [GO:0005524]; CTP synthase activity [GO:0003883]; glutaminase activity [GO:0004359]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF06418;PF00117; | 3.40.50.880;3.40.50.300; | CTP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32507415}. Note=Localizes to the cytoophidium, a short subcellular filamentary structure where CTP synthase is compartmentalized. Only a few cells form cytoophidia under standard growth conditions, they are observed in late log phase. Stress conditions such as treatme... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; Evidenc... | null | PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01227}. | null | null | FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. {ECO:0000255|HAMAP-Rule:MF_01227}. | Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755) |
G0L322 | AGAA_ZOBGA | MKKNYLLLYFIFLLCGSIAAQDWNGIPVPANPGNGMTWQLQDNVSDSFNYTSSEGNRPTAFTSKWKPSYINGWTGPGSTIFNAPQAWTNGSQLAIQAQPAGNGKSYNGIITSKNKIQYPVYMEIKAKIMDQVLANAFWTLTDDETQEIDIMEGYGSDRGGTWFAQRMHLSHHTFIRNPFTDYQPMGDATWYYNGGTPWRSAYHRYGCYWKDPFTLEYYIDGVKVRTVTRAEIDPNNHLGGTGLNQATNIIIDCENQTDWRPAATQEELADDSKNIFWVDWIRVYKPVAVSGGGNNGNDGATEFQYDLGTDTSAVWPGYTR... | 3.2.1.81 | null | carbohydrate metabolic process [GO:0005975] | extracellular region [GO:0005576] | beta-agarase activity [GO:0033916] | PF21254;PF18962; | 2.60.120.200;2.60.120.430; | Glycosyl hydrolase 16 family | PTM: Proteolytically cleaved into mature beta-agarase A catalytic chain (AgaAc). {ECO:0000269|PubMed:15456406}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15456406}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.; EC=3.2.1.81; Evidence={ECO:0000269|PubMed:15456406}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for agarose {ECO:0000269|PubMed:15456406}; Note=kcat is 150 sec(-1).; | null | null | null | FUNCTION: Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place. {ECO:0000269|P... | Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij) |
G0LXV8 | LATA_LATHA | SLVRMRREGEEDLTLEEKAELCSELELQQKYVDIGSNIIGDLSSLPIVGKIVGTIAAAAMAVTHVASGRLDIEQTLGGCSDVPFDQIKEILEERFNEIDRKLESHSAALEEITKLVEKSISAVEKTRKQMNKRFDEVMRSIQDAKVSPLVSKINNFARYFDTEKERIRGLKLSDYILKLEEPNGILLHFKESRTPRDDSLQAPLFSIIQERYAVPKSIDDELAFKVLYALLYGTQTYVSVMFFLLEQYSFLANHYYEKGDLEKYDEYFNSLNNVFLDFKSSLVGTGTSNNEGLLDRVLQVLVTVKNSEFLGLEKNGVNEM... | null | null | exocytosis [GO:0006887] | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF00023;PF12796; | 1.25.40.20; | Cationic peptide 01 (latrotoxin) family, 03 (alpha-latrotoxin) subfamily | PTM: Processed by furin-like proteases at both the N- and C-termini. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22001442}. Target cell membrane {ECO:0000250|UniProtKB:P23631}. Note=Forms a membrane channel in the prey. {ECO:0000250|UniProtKB:P23631}. | null | null | null | null | null | FUNCTION: Presynaptic neurotoxin that causes massive release of neurotransmitters from vertebrate (but not invertebrate) nerve terminals and endocrine cells via a complex mechanism involving activation of receptor(s) and toxin insertion into the plasma membrane with subsequent pore formation. Binds to neurexin-1-alpha ... | Latrodectus hasselti (Redback spider) |
G0R6T8 | LP9A_HYPJQ | MIQKLSNLLVTALAVATGVVGHGHINDIVINGVWYQAYDPTTFPYESNPPIVVGWTAADLDNGFVSPDAYQNPDIICHKNATNAKGHASVKAGDTILFQWVPVPWPHPGPIVDYLANCNGDCETVDKTTLEFFKIDGVGLLSGGDPGTWASDVLISNNNTWVVKIPDNLAPGNYVLRHEIIALHSAGQANGAQNYPQCFNIAVSGSGSLQPSGVLGTDLYHATDPGVLINIYTSPLNYIIPGPTVVSGLPTSVAQGSSAATATASATVPGGGSGPTSRTTTTARTTQASSRPSSTPPATTSAPAGGPTQTLYGQCGGSGY... | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:28900033}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:28900033}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulose binding [GO:0030248]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF03443;PF00734; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | PTM: N-glycosylation at position Asn-158 is important to determine C1/C4-oxidation ratios. {ECO:0000269|PubMed:30238672}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26285758}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:26285758, ECO:0000269|PubMed:28110665, ECO:0000269|PubMed:28900033, ECO:0000269|PubMed:30238672}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (PubMed:26285758, PubMed:28110665, PubMed:28900033, PubMed:30238672). Catalysis by LPMOs requires th... | Hypocrea jecorina (strain QM6a) (Trichoderma reesei) |
G0RUP7 | XYN2_HYPJQ | MVSFTSLLAGVAAISGVLAAPAAEVESVAVEKRQTIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS | 3.2.1.8 | null | xylan catabolic process [GO:0045493] | extracellular region [GO:0005576] | endo-1,4-beta-xylanase activity [GO:0031176] | PF00457; | 2.60.120.180; | Glycosyl hydrolase 11 (cellulase G) family | PTM: Glycosylated. {ECO:0000269|PubMed:8975597}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8975597}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000250|UniProtKB:P36217}; | null | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01097}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6. {ECO:0000269|PubMed:8975597}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:8975597}; | FUNCTION: Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose. {ECO:0000... | Hypocrea jecorina (strain QM6a) (Trichoderma reesei) |
G0RV93 | GCE_HYPJQ | MASRFFALLLLAIPIQAQSPVWGQCGGIGWSGPTTCVGGATCVSYNPYYSQCIPSTQASSSIASTTLVTSFTTTTATRTSASTPPASSTGAGGATCSALPGSITLRSNAKLNDLFTMFNGDKVTTKDKFSCRQAEMSELIQRYELGTLPGRPSTLTASFSGNTLTINCGEAGKSISFTVTITYPSSGTAPYPAIIGYGGGSLPAPAGVAMINFNNDNIAAQVNTGSRGQGKFYDLYGSSHSAGAMTAWAWGVSRVIDALELVPGARIDTTKIGVTGCSRNGKGAMVAGAFEKRIVLTLPQESGAGGSACWRISDYLKSQG... | 3.1.1.117 | null | carbohydrate metabolic process [GO:0005975]; lignin catabolic process [GO:0046274] | extracellular region [GO:0005576] | carboxylic ester hydrolase activity [GO:0052689]; cellulose binding [GO:0030248] | PF00734; | 3.40.50.1820; | Carbohydrate esterase 15 (CE15) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+); Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668; EC=3.1.1.117; Evidence={ECO:0000269|PubMed:1767865... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside {ECO:0000269|PubMed:17678650}; Vmax=5.5 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside {ECO:000... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:17678650}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-60 degrees Celsius. {ECO:0000269|PubMed:17678650}; | FUNCTION: Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin. Does not hydrolyze substrates of... | Hypocrea jecorina (strain QM6a) (Trichoderma reesei) |
G0S0Y3 | PAN3_CHATD | MAPLDLTRGQTDACSTENKDILCRNVLIYGHCRYEDQGCTYNHDQNKNSSQPEAPSKKMFNVDSPSFTPSGQSTVLPKKTTLSSQAASAAPFTPRGGGTPTLQTTAESTMFNPAAIREFTPQNYDLGNNNANGISQENGLYPDPFTMSTMGTALPTAGQYNLPLYGDHSGLAAPGAPFYPPHAAYPTGPIQPPHYHLYQPFGPYRQELQPWQRATYDFFMPQNLREDLQKKQFATLQVIPNSGLPQLEHWHSLVPLDTSNRKNTSCFGYPSWVYKAQNSRNGRHYALRRLEGYRLTNEKAILNVMKDWKKIKNASIVTIH... | null | null | mRNA processing [GO:0006397]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289] | P-body [GO:0000932]; PAN complex [GO:0031251] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) binding [GO:0008143]; protein kinase activity [GO:0004672] | PF18101; | 1.10.287.3700;1.20.5.5160;6.10.250.3160;1.10.510.10; | Protein kinase superfamily, PAN3 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03181}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the s... | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0S196 | ATC5_CHATD | MAPPQEEGGGNGTELSMQRSRWATRRLTVKSGARKRLSLMTRAQAKNSATEKRQSGVTDDGSPAADGDQKEGSISSSNNGGSAPRKLYFNLPLPPELKDEEGHPIQQFPRNKIRTAKYTPLSFIPKNLWFQFHNIANIFFLFLVILVIFPIFGGVNPGLNSVPLIVIITVTAIKDAIEDYRRTILDIELNNAPVHRLQGWENVNVEKDNVSLWRRFKKANSRFFGSIWHLIERLWKEDAQSMRQRFASADPRMSIETRTAPWDPSHRRSVASHTEEIQMTPVPSPVPHDPDVPTVSSAIENEATLLQNLKGDLINHEIPV... | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32303992}; | Golgi organization [GO:0007030]; phospholipid translocation [GO:0045332] | endosome membrane [GO:0010008]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; phosphatidylcholine floppase activity [GO:0090554]; phosphatidylethanolamine flippase activity [GO:0090555]; phosphatidylserine floppase activity [GO:0090556] | PF13246;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32660}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32660}. Endosome membrane {ECO:0000250|UniProtKB:P32660}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32660}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P32660}; Mult... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000305|PubMed:32303992}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphat... | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:32303992). May... | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0S3J5 | RIO1_CHATD | MTPAPEPQDPPTIHEPVATEQTDDISDWDVESDYEDGYGAPSKSQAQGGASAADRPKINAHARIDDQMTDLARHASKIRLDNLTMQQIFRDKDRTDNATSDQVLDNHTRMIILNMLNRNIISEIYGTISTGKEANVYNAVAYDNNGERIERAVKVYKTIILGFKDRERYLAGEQRFKTIVDKALSAPRKMIKLWAEKEFRNLKRLHTAGIPCPEPIYLKYNVMVMGFLGDHTNGYAFPRLHDTKITGETLEETEAEWRRLYINLLSMMRRMYQVCGLVHGDLSEYNILYNEGVLYIIDVSQSVEHDHIEATNFLRMDIRN... | 2.7.11.1; 3.6.3.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:G0S5R3, ECO:0000250|UniProtKB:Q9BRS2}; | maturation of SSU-rRNA [GO:0030490]; phosphorylation [GO:0016310] | cytosol [GO:0005829]; preribosome, small subunit precursor [GO:0030688] | ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF01163; | 1.10.510.10; | Protein kinase superfamily, RIO-type Ser/Thr kinase family | PTM: Autophosphorylated. {ECO:0000269|PubMed:24948609}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | 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:0000255|PIRNR:PIRNR038147}; CATALYT... | null | null | null | null | FUNCTION: Involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit (By similarity). In vitro, has strong ATPase activity and only low protein kinase activity (PubMed:24948609). {ECO:0000250|UniProtKB:Q12196, ECO:0000269|PubMed:24948609}. | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0S4X6 | ODP2_CHATD | MLAQVLRRQALQHVRLARAAAPSLTRWYASYPPHTIVKMPALSPTMTSGNIGAWQKKPGDAITPGEVLVEIETDKAQMDFEFQEEGVLAKILKETGEKDVAVGSPIAVLVEEGTDINAFQNFTLEDAGGDAAAPAAPAKEELAKAETAPTPASTSAPEPEETTSTGKLEPALDREPNVSFAAKKLAHELDVPLKALKGTGPGGKITEEDVKKAASAPAAAAAAPGAAYQDIPISNMRKTIATRLKESVSENPHFFVTSELSVSKLLKLRQALNSSAEGRYKLSVNDFLIKAIAVACKRVPAVNSSWRDGVIRQFDTVDVS... | 2.3.1.12 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000255|PROSITE-ProRule:PRU01066}; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000255|PROSITE-ProRule:PRU01066}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086] | mitochondrial pyruvate dehydrogenase complex [GO:0005967] | dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=68 uM for coenzyme A {ECO:0000269|PubMed:33567276}; | null | null | null | FUNCTION: The 10-megadalton pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) and catalyzes the overall oxidative decarboxylation of pyruvate to form acetyl-CoA and CO(2) (PubMed:33... | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0SAK3 | NU145_CHATD | MSFGFGSGGFGQNNNSSTFGGFGSTPTTNTGFGSTGTTAFGSTSNTTGGGLFGGGGGGFGSGNTFGSGFGSKPAFGTPATTSSTSLFGSTTTTAGGTGFGSGGFGSTNTSSPFGGGGTSLFGNKTTTGFGSGTSTFGSNTGGGLFGGGSTTTGFGATNNPGIGTNVGDPPGTAVVPFSPTVEKEVNNPSQSNSYQNILFMDAYKKWSAEELRLADYNQGRKTAAPGGTGAFGSSGFGGFGTTSNTGGFGSNTGGGLFGNTQQNTGGFGTTNTTGSAFGSGGGLFGNKPATGGLFGTSSSQPAQSGGLFGSGTASTFGSSN... | 3.4.21.- | null | mRNA transport [GO:0051028]; post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery [GO:0000973]; protein import into nucleus [GO:0006606]; RNA export from nucleus [GO:0006405]; telomere tethering at nuclear periphery [GO:0034398] | nuclear membrane [GO:0031965]; nuclear pore cytoplasmic filaments [GO:0044614] | hydrolase activity [GO:0016787]; nuclear localization sequence binding [GO:0008139]; RNA binding [GO:0003723]; structural constituent of nuclear pore [GO:0017056] | PF04096;PF13634;PF12110; | 1.10.10.2360;1.25.40.690;3.30.1610.10; | Nucleoporin GLFG family | PTM: NUP145 is autocatalytically cleaved in NUP145N and NUP145C. {ECO:0000250|UniProtKB:P49687}. | SUBCELLULAR LOCATION: [Nucleoporin NUP145C]: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Cytoplasmic side {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Periph... | null | null | null | null | null | FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured ... | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0SAK8 | PAN2_CHATD | MDADWDEVTRIAYPAPGTNDFPRPATAVAFDPIAELLWAGFDRGRVCSFYGRDLTRYTAFKIQPASEGPVRQFLFHDKGVIVLGTRSVHMAMRRGPALWNIRHENMKDLRCMSFTSKGTQEIIVAGWQDTMLVIDVLKGDIIKQIPAQHHYSIMKKSRYICAATKTGSVDLIDPLSFKIVRSWQAHASYINDMDAQNDFIVTCGGSLKQQAAQTYMLDPYVNVFDLKNMASMKPMPFPPLAAHVRLHPRMLTTAIVTSQHGQMHVVDIMNPNSSTVRYANISSYVKLFEIAPSGEALVIGDADCNIHLWGSPTKIHFTDM... | 3.1.13.4 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03182}; Note=Binds 2 metal cations per subunit in the catalytic exonuclease domain. {ECO:0000255|HAMAP-Rule:MF_03182}; | mRNA processing [GO:0006397]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289] | P-body [GO:0000932]; PAN complex [GO:0031251] | metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; poly(A)-specific ribonuclease activity [GO:0004535] | PF20770;PF00929;PF13423; | 3.90.70.10;3.30.420.10;2.130.10.10; | Peptidase C19 family, PAN2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24872509}; | null | null | null | null | FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the sh... | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0SGC7 | MGM1_CHATD | MSAQLRAAAAITPAARRVISGPAAVRRFHHYHHLPTGGIQRVEIAARGLRRSVQFPALANAYHNNAVIVRNASFTRLLPKLALKFIRVPALFGGMMLGAVGWVQYQAIKVSNSAQEFYGNIKATVADTAFSVWSSAVDIAEQTKRGWENTKNQFEIPEWLDRIMKGEGLAGEGSGSGEGGPNGGPEPPRQSRAGAATVAGASATVYGYGASDNDDRTPEEIMRDDNMMFITKKMIEIRNLLQKVGQGSTVTLPSIVVIGSQSSGKSSVLEAIVGHEFLPKGSNMITRRPIELTLVNDPEAKVDYGEFPDLGLARVTDFSL... | 3.6.5.5 | null | defense response to virus [GO:0051607]; mitochondrial fusion [GO:0008053] | cytoplasm [GO:0005737]; membrane [GO:0016020]; microtubule [GO:0005874]; nucleus [GO:0005634] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; microtubule binding [GO:0008017] | PF01031;PF00350; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | PTM: Cleavage of the transit peptide by mitochondrial processing protease (MPP) produces a long integral membrane form of MGM1 (L-MGM1) (By similarity). Further processing by the rhomboid protease PCP1 produces a short peripheral membrane form of MGM1 (S-MGM1) (By similarity). Both forms are required for full activity ... | SUBCELLULAR LOCATION: [Dynamin-like GTPase MGM1, long form]: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P32266}; Single-pass type II membrane protein {ECO:0000255}; Intermembrane side {ECO:0000250|UniProtKB:P32266}.; SUBCELLULAR LOCATION: [Dynamin-like GTPase MGM1, small form]: Mitochondrion intermembrane spac... | 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; EC=3.6.5.5; Evidence={ECO:0000269|PubMed:31292547}; | null | null | null | null | FUNCTION: Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function (PubMed:31292547). Exists in two forms: the transmembrane, long form (Dynamin-like GTPase MGM1, long f... | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0SHW7 | RAD50_CHATD | MSKIEKLSILGVRSFGPHHPETIAFNTPLTLIVGYNGSGKTTVIECLKYATTGELPPNSTRNGAFIHDPDLVGEKEVRAQVKLSFRSTIGESYVVTRNIQLLVQRNNKRTQKTLEGSLLLRNNGERTVISTRVAELDKLVSEKLGVPPAILDAVIFCHQDDSLWPMSEPAALKKRFDEIFEAQKYTKVIENIRLLKKKKGDELKILKEREVQDKANKERAEKVDRLMAQLTREILEAREKCNELSKQMEEESAKIKDKYEQANSFLKIMNDLQTKTEKLEYKKDAIVELRSRIEELPDPDEVLRNTLDEYEQTINRIVAD... | 3.6.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:36577401}; Note=Binds 1 zinc ion per homodimer. {ECO:0000269|PubMed:36577401}; | chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA duplex unwinding [GO:0032508]; double-strand break repair [GO:0006302]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via telomerase [GO:0007004] | condensed nuclear chromosome [GO:0000794]; Mre11 complex [GO:0030870] | ATP hydrolysis activity [GO:0016887]; double-stranded DNA binding [GO:0003690]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [GO:0051880]; guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; single-stranded telomeric DNA binding [GO:0043047] | PF13476;PF13558; | 3.40.50.300; | SMC family, RAD50 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}. | 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:36577401}; | null | null | null | null | FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (By similarity). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanis... | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0WXL9 | CS2H_ACIS1 | MVSEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHIEQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKEIIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLPAFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHPLIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIVKE | 3.13.1.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22012399}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22012399}; | hydrogen sulfide biosynthetic process [GO:0070814] | null | carbonate dehydratase activity [GO:0004089]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270] | PF00484; | 3.40.1050.10; | Beta-class carbonic anhydrase family | null | null | CATALYTIC ACTIVITY: Reaction=carbon disulfide + 2 H2O = CO2 + 2 H(+) + 2 hydrogen sulfide; Xref=Rhea:RHEA:38143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:23012, ChEBI:CHEBI:29919; EC=3.13.1.5; Evidence={ECO:0000269|PubMed:22012399}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=130 uM for carbon disulfide {ECO:0000269|PubMed:22012399}; KM=22 uM for carbonyl sulfide {ECO:0000269|PubMed:22012399}; Vmax=40 nmol/min/ug enzyme towards hydrogen sulfide formation from carbon disulfide {ECO:0000269|PubMed:22012399}; Vmax=74 nmol/min/ug enzyme tow... | PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis. {ECO:0000269|PubMed:22012399}. | null | null | FUNCTION: Catalyzes the conversion of carbon disulfide into hydrogen sulfide and carbon dioxide, with carbonyl sulfide as an intermediate. Likely plays a key role in sulfur metabolism that allows Acidianus sp. A1-3 to grow on carbon disulfide as the main carbon and energy source. Does not show carbonic anhydrase activi... | Acidianus sp. (strain A1-3) |
G0Y7D3 | TPS3_LITCU | MALQLLTPSFSFQHSPSPHRLTTLRYTHHTIRCTASAPSYSDLVGRRSANYKPSKWDSNFVETLESDYKKENHEMYIEKLMGDVKHLMKKVVNPIEKMELVDTIQRLGLGYLFNKEIKEVLNTIATSKATFKTKKDLHAVALQFRLLRQHGYEVSPDAFHKFKDEKGGFKESLCMDIKGMLSLYEASHLSFQGEVVLDEAREFTSTHLKAIEGNIDPVLLKKVRHSLEMPLHWRMLRLEARWYIETYDEEDRKNPSLAELAKHDFNSVQTIYQRSLKRMSRWWRDLGLGERLEFSRDRLVECFFWTTGVIFDPQFERCRG... | 4.2.3.-; 4.2.3.110 | 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]; monoterpene biosynthetic process [GO:0043693] | chloroplast [GO:0009507] | alpha-thujene synthase activity [GO:0102700]; 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 = alpha-thujene + diphosphate; Xref=Rhea:RHEA:68644, ChEBI:CHEBI:33019, ChEBI:CHEBI:50031, ChEBI:CHEBI:58057; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68645; Evidence={ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=(2E)-ge... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|Ref.1}. | null | null | FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products used by traditional Chinese medicine to treat headache, inflammation and intoxication (Ref.1). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-thujene and (1R,5R)-sabinene (Ref.1). {ECO:0000269|Ref.1}... | Litsea cubeba (Aromatic litsea) (Laurus cubeba) |
G1FC92 | MIG21_CAEEL | MERDSNTAKSEIFYSNPAIWRHLKDGKGEGMSKSEKRNKHGCRNFTYSIWNCIRPGGWSTWSKWSKCREGIRKRRRTCNNPLPIGTTCSGQKVEKQSCAISSNVPEYLFGSWTSWNPWSRCDCDRSLRIRTRHCKGNSCEGCDKDYEDCRPDECPISKKWSEWTDWVNYGIEQVRFSAWCSSSNVANTEVGIRKETQDSMKHANWSEWHMHPGVAYRYRLLHNSSISIEHHLLSRFTSSCLPLHFAIPIFCFCILTGFLLQNIIYCVVNRFKRRFIRLNYSYDSNPRDYPSHLIRSPGSPKDESFW | null | null | determination of left/right asymmetry in nervous system [GO:0035545]; neuroblast migration [GO:0097402]; neuron migration [GO:0001764]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of cell migration [GO:0030334] | plasma membrane [GO:0005886] | signaling receptor activity [GO:0038023] | PF00090; | 2.20.100.10; | null | PTM: Glycosylated via C-mannosylation by dpy-19 at Trp-58 and Trp-61. {ECO:0000269|PubMed:23562325}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for determination of left/right asymmetry in nervous system. Acts together with unc-40 to control an initial left-right asymmetric polarization of the Q neuroblasts. Mig-21 and unc-40 may control the asymmetry in Wnt signaling response by restricting posterior polarization to one of the 2 Q neuroblas... | Caenorhabditis elegans |
G1FNI6 | TFP_THLAR | MARTLQGEWMKVEQKGGQVPAPRSSHGIAVIGDKLYCFGGEDPPYESIDNDLYVFDFNTHTWSIAPANGDVPKTRVLGTRMVAVGTKLYVFGGRNKQLEFEDFYSYDTVKEEWKFLTKLDEKGGPEARTFHSMTSDENHVYVFGGVSKGGLNATPFRFRTIEAYNIAEGKWAQLPDPGEDFEKRGMAGFLVVQGKLWVFYGFATANDPKIPTLYGSQDYESNRVHCYDPATQKWTEVETTGFEKPSRRSCFAHAAVGKYIIIFGGEIERDPEAHQGPGTLSREGFALDTETLVWERYEGGPIKPSNRGWVASTTTTINGK... | 4.8.1.8 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:21783213, ECO:0000269|PubMed:26260516, ECO:0000269|PubMed:30900313}; | glucosinolate metabolic process [GO:0019760]; nitrile biosynthetic process [GO:0080028] | cytosol [GO:0005829]; nucleus [GO:0005634] | enzyme regulator activity [GO:0030234]; identical protein binding [GO:0042802]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF01344;PF13964; | 2.120.10.80; | null | null | null | CATALYTIC ACTIVITY: Reaction=(Z)-N-(sulfonatooxy)prop-2-enimidothioate = allyl thiocyanate + sulfate; Xref=Rhea:RHEA:69316, ChEBI:CHEBI:16189, ChEBI:CHEBI:183062, ChEBI:CHEBI:183082; EC=4.8.1.8; Evidence={ECO:0000269|PubMed:21783213}; CATALYTIC ACTIVITY: Reaction=(Z)-N-(sulfonatooxy)prop-2-enimidothioate = 2-(thiiran-2... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6. {ECO:0000269|PubMed:21783213}; | null | FUNCTION: Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation (By similarity). Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase (PubMed:21783213, PubMed:23999604, PubMed:26260516, PubMed:30900313). C... | Thlaspi arvense (Field penny-cress) |
G1JSL4 | PXG1_AVESA | MAEDAVVSDAVVVSDAMSSVAKGAPVTAQRPVRDDLEKHIPKPYLARALVAVDVNNPEGTKGGRHEHGQKSVLQQHVSFFDQNGDGIIYPWETFRGLRRLGFNLIVSFIVAIGIHTGLSYPTLPTWRPSLLFPVYIDRIHKAKHGSDTATFDTEGRFMPVNFENIFSKNARSQPDKLTLREIWMMTNDHRLAYDPFGWVANKGEWILLYMLAKDDEGYLPKEAIRGVYDGSLFEFLAEQRTKKAHGKQH | 1.11.2.3 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | null | endoplasmic reticulum [GO:0005783]; lipid droplet [GO:0005811]; membrane [GO:0016020] | 18-hydroxyoleate peroxygenase activity [GO:0102070]; calcium ion binding [GO:0005509]; monooxygenase activity [GO:0004497]; plant seed peroxidase activity [GO:1990137] | PF05042; | null | Caleosin family | null | SUBCELLULAR LOCATION: Microsome membrane. Lipid droplet. | CATALYTIC ACTIVITY: Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3; Evidence={ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:16956885, ECO:0000269|PubMed:21784965}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.07 uM for 9-HPOD {ECO:0000269|PubMed:21784965}; KM=10.42 uM for 9-HPOT {ECO:0000269|PubMed:21784965}; KM=25.18 uM for 13-HPOD {ECO:0000269|PubMed:21784965}; KM=7.25 uM for 13-HPOT {ECO:0000269|PubMed:21784965}; KM=215.76 uM for cumene hydroperoxide {ECO:0000269|... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:21784965}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:21784965}; | FUNCTION: Calcium-binding peroxygenase involved in cutin monomers biosynthesis. Can catalyze epoxidation of fatty acid and sulfoxidation reactions that can proceede competitively, although in favor of the sulfoxidation. Can only use unsaturated fatty acids with double bonds in the cis configuration as substrates. The p... | Avena sativa (Oat) |
G1JUH1 | TPS3_SOLLC | MSIFSTRYLVTPFSSFSPPKAFVSKACSLSTGQPLNYSPNISTNIISSSNGIINPIRRSGNYEPTMWNYEYIQSTHNHHVGEKYMKRFNELKAEMKKHLMMMLHEESQELEKLELIDNLQRLGVSYHFKDEIIQILRSIHDQSSSEATSANSLYYTALKFRILRQHGFYISQDILNDFKDEQGHFKQSLCKDTKGLLQLYEASFLSTKSETSTLLESANTFAMSHLKNYLNGGDEENNWMVKLVRHALEVPLHCMMLRVETRWYIDIYENIPNANPLLIELAKLDFNFVQAMHQQELRNLSRWWKKSMLAEKLPFARDRI... | 4.2.3.105; 4.2.3.117; 4.2.3.15; 4.2.3.16 | 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] | chloroplast [GO:0009507] | (4S)-limonene synthase activity [GO:0050552]; camphene synthase activity [GO:0102703]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; tricyclene synthase activity [GO:0102701] | 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 + tricyclene; Xref=Rhea:RHEA:32687, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:64266; EC=4.2.3.105; Evidence={ECO:0000269|PubMed:21813655}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (1S,4R)-camphene + diphosphate; Xref=Rhea:RHEA:25... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. | null | null | FUNCTION: Monoterpene synthase that catalyzes the formation of camphene and tricyclene from geranyl diphosphate. Produces also lower amounts of limonene and beta-myrcene, and traces of several other monoterpenoids. {ECO:0000269|PubMed:21813655}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
G1NJB6 | MYG_MELGA | MGLSDQEWQQVLTIWGKVEADIAGHGHEVLMRLFHDHPETLDRFDKFKGLKTPDQMKGSEDLKKHGATVLTQLGKILKQKGNHESELKPLAQTHATKHKIPVKYLEFISEVIIKVIAEKHAADFGADSQAAMKKALELFRNDMASKYKEFGFQG | 1.11.1.-; 1.7.-.- | null | removal of superoxide radicals [GO:0019430] | extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 6.10.140.2100;6.10.140.2110; | Globin family | null | SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:00002... | null | null | null | null | FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of... | Meleagris gallopavo (Wild turkey) |
G1SJB4 | RACK1_RABIT | MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR | null | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; gastrulation [GO:0007369]; positive regulation of protein phosphorylation [GO:0001934]; rescue of stalled ribosome [GO:0072344]; rhythmic process [GO:0048511] | cytosol [GO:0005829]; dendrite [GO:0030425]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840] | protein kinase C binding [GO:0005080]; ribosome binding [GO:0043022]; translation regulator activity [GO:0045182] | PF00400; | 2.130.10.10; | WD repeat G protein beta family, Ribosomal protein RACK1 subfamily | PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC. {ECO:0000250|UniProtKB:P63244}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:000... | null | null | null | null | null | FUNCTION: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules (By similarity). Interacts with a wide variety of proteins and plays a role in many cellular processes (By similarity). Component of the 40S ribosomal subunit involved in translational repression (P... | Oryctolagus cuniculus (Rabbit) |
G1SK22 | RS27A_RABIT | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK | null | null | modification-dependent protein catabolic process [GO:0019941]; protein ubiquitination [GO:0016567]; translation [GO:0006412] | cytosolic ribosome [GO:0022626]; nucleolus [GO:0005730]; ribonucleoprotein complex [GO:1990904] | metal ion binding [GO:0046872]; protein tag activity [GO:0031386]; structural constituent of ribosome [GO:0003735]; ubiquitin protein ligase binding [GO:0031625] | PF01599;PF00240; | 6.20.50.150; | Ubiquitin family; Eukaryotic ribosomal protein eS31 family | PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects de... | SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31]: Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, ECO:0000269|PubMed:30517857, ECO:0000269|Pub... | null | null | null | null | null | FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polyme... | Oryctolagus cuniculus (Rabbit) |
G1SPE9 | GNPAT_RABIT | MDSSSSSNYFSVGSTNPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVYKGITPCKPSDIKNSVLNSEEIHYVIKQLSMESLQSVDVLREEVCEILDEMSHKLRLGAIRFFAFALSKIFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDLPVPVIAAGMDFLGMKMIGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEFFLEGTRSRSAKTLTPKFGLLSIVMEPFFKREVFDTYLVPISISYDKILEETLYAYELLGVPKPKESTTGLLKARRILSENF... | 2.3.1.42 | null | cerebellum morphogenesis [GO:0021587]; ether lipid biosynthetic process [GO:0008611]; fatty acid metabolic process [GO:0006631]; glycerol-3-phosphate metabolic process [GO:0006072]; glycerophospholipid metabolic process [GO:0006650]; membrane organization [GO:0061024]; paranodal junction assembly [GO:0030913]; phosphol... | mitochondrial membrane [GO:0031966]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; plasma membrane [GO:0005886] | glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; glycerone-phosphate O-acyltransferase activity [GO:0016287] | PF01553;PF19277; | null | GPAT/DAPAT family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:Q9ES71}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9ES71}; Matrix side {ECO:0000250|UniProtKB:Q9ES71}. Note=Exclusively localized to the lumenal side of the peroxisomal membrane. {ECO:0000250|UniProtKB:Q9ES71}. | CATALYTIC ACTIVITY: Reaction=an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone 3-phosphate + CoA; Xref=Rhea:RHEA:17657, ChEBI:CHEBI:57287, ChEBI:CHEBI:57534, ChEBI:CHEBI:57642, ChEBI:CHEBI:58342; EC=2.3.1.42; Evidence={ECO:0000269|PubMed:9459311}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17658; E... | null | PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000269|PubMed:9459311}. | null | null | FUNCTION: Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical prope... | Oryctolagus cuniculus (Rabbit) |
G1SRW8 | SLN14_RABIT | MEIPKTGVETLYPEFVVEVGRVTFGEENRKKMTNSCLKRTENLNIIKATCALLNSGGGVIKAEIHDKNYNYQCHGLGHDLETSFQKLLPFGSQKYLDYMQQGHELLIFVKSWNPDVSSLLPLRICSLRSNLYQRDVTSAINLSASSALELLREKQHAAQRGRRRLHPPRASNSNLQEEEDMKMLASEVFKKDRLMYKEKLNFTESTHVEFKRFTTKKVVPRIKEMLPHYVSAFANTQGGYLIIGVDDKSKEVFGCKKEKVNPDLLKKEIENCIEKLPTFHFCHEKPKINFITKILNVYQKDVLYGYVCVVQVEPFCCAVF... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25996083}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25996083}; Note=C-terminally truncated SLFN14 endoribonuclease: Requires manganese and magnesium for its endoribonuclease activity. {ECO:0000269|PubMed:25996083}; | cellular response to magnesium ion [GO:0071286]; cellular response to manganese ion [GO:0071287]; mRNA catabolic process [GO:0006402]; platelet maturation [GO:0036345]; rRNA catabolic process [GO:0016075] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ribosome binding [GO:0043022]; RNA endonuclease activity [GO:0004521] | PF17057;PF04326;PF21026; | 3.30.950.30; | null | null | SUBCELLULAR LOCATION: [Protein SLFN14]: Nucleus {ECO:0000250|UniProtKB:P0C7P3}. | null | null | null | null | null | FUNCTION: [Protein SLFN14]: Shows no ribosome-associated and endoribonuclease activities. {ECO:0000269|PubMed:25996083}.; FUNCTION: [C-terminally truncated SLFN14 endoribonuclease]: Displays polysome-associated endoribonuclease activity towards mRNAs and rRNAs (PubMed:25996083). May play a role in RNA surveillance path... | Oryctolagus cuniculus (Rabbit) |
G1SW77 | SERB1_RABIT | MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPNVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDRPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQKQISYNCSDLDQSNVTEETPEGEEHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKK... | null | null | negative regulation of translation [GO:0017148]; PML body organization [GO:0030578]; ribosome hibernation [GO:0141014] | cytosol [GO:0005829]; non-membrane-bounded organelle [GO:0043228]; nucleus [GO:0005634] | mRNA 3'-UTR binding [GO:0003730]; ribosome binding [GO:0043022]; SUMO binding [GO:0032183]; translation elongation factor binding [GO:0061770]; translation repressor activity [GO:0030371] | PF04774;PF16174; | null | SERBP1-HABP4 family | PTM: Phosphorylation by MTOR inhibits SERBP1 and relieves ribosome hibernation. {ECO:0000250|UniProtKB:Q8NC51}. | null | null | null | null | null | null | FUNCTION: Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (PubMed:30355441). Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting rib... | Oryctolagus cuniculus (Rabbit) |
G1T469 | NOD2_RABIT | MCSQEAFQAQRSQLVGLLVSGSLEGFESILDLLLSWEVLSWEDYEGLRLVGQPLSHLARRLLDTVWNKGTWGCQKLIAAVQEAQDSSQCPELHGCWDPHSLHPAQDLQSHRPAIVRRLYSHVEGVLDLALEQGFISQYECDEIRLPIFTSSQRARRLLDLATVKANGLAAFLLQHVQKLPVSLSLPFEAAACKKYMSKLRTIVAAQSRFLSTYDGAENLCLEDIYTENTLEVRTEVGMAGPLHKSPAALGLEELFSPNGHLNEDADTVLVVGEAGSGKSTLLQQVHLLWATGQDFQEFLFVFPFSCRQLQCVARPLSVMT... | null | null | adaptive immune response [GO:0002250]; antibacterial innate immune response [GO:0140367]; biosynthetic process of antibacterial peptides active against Gram-positive bacteria [GO:0002815]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to muramyl dipeptide [GO:0071225]; cellular response to pep... | basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of plasma membrane [GO:0019897]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; phagocytic vesicle [GO:0045335]; protein-containing complex [GO:0032991] | actin binding [GO:0003779]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; CARD domain binding [GO:0050700]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; muramyl dipeptide binding [GO:0032500]; pattern recognition receptor activity [GO:0038187]; peptidoglycan binding [GO:0042834]; protei... | PF00619;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NOD1-NOD2 family | PTM: Palmitoylated by ZDHHC5; palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection. Palmitoylation promotes localization to the cell membrane. Palmitoylation protects from SQSTM1/p62-dependent autophagic degradation. {ECO:00002... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HC29}; Lipid-anchor {ECO:0000250|UniProtKB:Q9HC29}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9HC29}. Cytoplasm {ECO:0000250|UniProtKB:Q9HC29}. Mitochondrion {ECO:0000250|UniProtKB:Q9HC29}. Note=Palmitoylation promotes localization to the cell membran... | null | null | null | null | null | FUNCTION: Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and plays an important role in gastrointestinal immunity. Specifically activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan found in every bacterial peptidoglycan type. NOD2 specif... | Oryctolagus cuniculus (Rabbit) |
G1T6D1 | RL23_RABIT | MSKRGRGGSSGAKFRISLGLPVGAVINCADNTGAKNLYIISVKGIKGRLNRLPAAGVGDMVMATVKKGKPELRKKVHPAVVIRQRKSYRRKDGVFLYFEDNAGVIVNNKGEMKGSAITGPVAKECADLWPRIASNAGSIA | null | null | cellular response to actinomycin D [GO:0072717]; G1 to G0 transition [GO:0070314]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; positive regulation of cell population proliferation [GO:0008284]; positive regula... | cytosolic large ribosomal subunit [GO:0022625]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; synapse [GO:0045202] | large ribosomal subunit rRNA binding [GO:0070180]; structural constituent of ribosome [GO:0003735]; transcription coactivator binding [GO:0001223]; ubiquitin ligase inhibitor activity [GO:1990948]; ubiquitin protein ligase binding [GO:0031625] | PF00238; | 2.40.150.20; | Universal ribosomal protein uL14 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:3329666... | null | null | null | null | null | FUNCTION: Component of the large ribosomal subunit (PubMed:26245381, PubMed:27863242, PubMed:30517857). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:26245381, PubMed:27863242, PubMed:30517857). {ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ... | Oryctolagus cuniculus (Rabbit) |
G1T7U7 | NAAA_RABIT | MQGTGHPVRPVLELLLLLLLLAGVGGSTTASTPGPPLFNVSLDVAPERWLPVLRHYDVELVRAAVAQVIGDRVPKWVLALIEKGALKLERLLPPPFTAEIRGMCDFLNLSLADGLLVNLAYEYSAFCTSIVAQDSRGHVYHGRNLDYPYGSILRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDERDRGWWWENLVAALFLRHSPISWLLRTTLSEAESFEAAVYRLAKTPLIADVYYIVGGTNPREGVVITRNRDGPADIWPLDPLKGVWFLVETNYDHWKPAPEEDDRRTPAIKALNATGQAKLSLE... | 3.5.1.23; 3.5.1.60 | null | fatty acid metabolic process [GO:0006631]; lipid catabolic process [GO:0016042]; N-acylethanolamine metabolic process [GO:0070291]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; sphingosine metabolic process [GO:0006670] | lysosome [GO:0005764]; membrane [GO:0016020] | ceramidase activity [GO:0102121]; fatty acid amide hydrolase activity [GO:0017064]; N-(long-chain-acyl)ethanolamine deacylase activity [GO:0047412]; N-acylsphingosine amidohydrolase activity [GO:0017040] | PF02275;PF15508; | null | Acid ceramidase family | PTM: N-glycosylated (PubMed:30301806). Tunicamycin treatment causes a reduction in specific activity against N-palmitoylethanolamine (By similarity). {ECO:0000250|UniProtKB:Q02083, ECO:0000269|PubMed:30301806}.; PTM: Autoproteolytic cleavage at pH 4.5 gives rise to the alpha and beta subunit (PubMed:30301806). Cleavage... | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q02083}. Membrane {ECO:0000250|UniProtKB:Q02083}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02083}. | CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoylethanolamine = ethanolamine + hexadecanoate; Xref=Rhea:RHEA:45064, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:57603, ChEBI:CHEBI:71464; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45065; Evidence={ECO:0000250|UniPro... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:Q02083}. | null | null | FUNCTION: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine. {ECO:0000250|UniProtKB:Q5KTC7}. | Oryctolagus cuniculus (Rabbit) |
G1TGF1 | TEBP_RABIT | MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE | 5.3.99.3 | null | chaperone-mediated protein complex assembly [GO:0051131]; positive regulation of telomerase activity [GO:0051973]; prostaglandin biosynthetic process [GO:0001516]; protein folding [GO:0006457]; telomerase holoenzyme complex assembly [GO:1905323]; telomere maintenance via telomerase [GO:0007004] | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA polymerase binding [GO:0070182]; Hsp90 protein binding [GO:0051879]; prostaglandin-E synthase activity [GO:0050220]; protein-folding chaperone binding [GO:0051087] | PF04969; | 2.60.40.790; | P23/wos2 family | PTM: Proteolytically cleaved by caspase-7 (CASP7) in response to apoptosis, leading to its inactivation. {ECO:0000250|UniProtKB:Q15185}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3ZBF7}. | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893, ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3; Evidence={ECO:0000250|UniProtKB:Q15185}; | null | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:Q15185}. | null | null | FUNCTION: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassemb... | Oryctolagus cuniculus (Rabbit) |
G1TLT8 | RSSA_RABIT | MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTATQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGTTTEWS | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | 90S preribosome [GO:0030686]; 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]; virus receptor activity [GO:0001618] | 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:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35709277, ECO:00... | null | null | null | null | null | FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit (PubMed:23873042, PubMed:25601755). Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits (PubMed:23873042, PubMed:25601755). Also functions as a cell surface r... | Oryctolagus cuniculus (Rabbit) |
G1TM55 | RS6_RABIT | MKLNISFPATGCQKLIEVDDERKLRTFYEKRMATEVAADALGEEWKGYVVRISGGNDKQGFPMKQGVLTHGRVRLLLSKGHSCYRPRRTGERKRKSVRGCIVDANLSVLNLVIVKKGEKDIPGLTDTTVPRRLGPKRASRIRKLFNLSKEDDVRQYVVRKPLNKEGKKPRTKAPKIQRLVTPRVLQHKRRRIALKKQRTKKNKEEAAEYAKLLAKRMKEAKEKRQEQIAKRRRLSSLRASTSKSESSQK | null | null | activation-induced cell death of T cells [GO:0006924]; cytoplasmic translation [GO:0002181]; erythrocyte development [GO:0048821]; G1/S transition of mitotic cell cycle [GO:0000082]; gastrulation [GO:0007369]; glucose homeostasis [GO:0042593]; mammalian oogenesis stage [GO:0022605]; negative regulation of apoptotic pro... | cell body [GO:0044297]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; small-subunit processome [GO:00320... | protein kinase binding [GO:0019901]; structural constituent of ribosome [GO:0003735] | PF01092; | 1.20.5.2650; | Eukaryotic ribosomal protein eS6 family | PTM: Ribosomal protein S6 is the major substrate of protein kinases in eukaryote ribosomes. The phosphorylation is stimulated by growth factors, tumor promoting agents, and mitogens. It is dephosphorylated at growth arrest. Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites fac... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:3160947... | null | null | null | null | null | FUNCTION: Component of the 40S small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA (PubMed:23873042, PubMed:25601755, PubMed:262... | Oryctolagus cuniculus (Rabbit) |
G1TNM3 | RS3_RABIT | MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPSGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA | 4.2.99.18 | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell division [GO:0051301]; DNA repair [GO:0006281]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of protein-containing complex assembly [GO:0031334]; regulation of translation [GO:0006417]; translation [GO:0006412] | cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; mitochondrial inner membrane [GO:0005743]; nucleolus [GO:0005730]; spindle [GO:0005819]; synapse [GO:0045202] | class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; DNA binding [GO:0003677]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF07650;PF00189; | 3.30.300.20;3.30.1140.32; | Universal ribosomal protein uS3 family | PTM: Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly. {ECO:0000250|UniProtKB:P23396}.; PTM: Sumoylation by SUMO1 enhances protein stability through increased resistance to proteolysis. Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230. {... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:3228622... | CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RH... | null | null | null | null | FUNCTION: Component of the small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). Has endonuclease activity... | Oryctolagus cuniculus (Rabbit) |
G1TZ76 | RS27_RABIT | MPLAKDLLHPSPEEEKRKHKKKRLVQSPNSYFMDVKCPGCYKITTVFSHAQTVVLCVGCSTVLCQPTGGKARLTEGCSFRRKQH | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P42677}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P42677}; | ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412] | cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730] | metal ion binding [GO:0046872]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF01667; | 2.20.25.100; | Eukaryotic ribosomal protein eS27 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:3329666... | null | null | null | null | null | FUNCTION: Component of the small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). Required for proper rRNA ... | Oryctolagus cuniculus (Rabbit) |
G1TZA0 | PLM_RABIT | MAYLHHTLLVCMGLLAMANAEAPQEQDPFTYDYQSLRIGGLIIAGILFILGILIILKRGAWERFDTARRTGEPDEEEGTFRSSIRRLSTRRR | null | null | negative regulation of protein glutathionylation [GO:0010734]; potassium ion transport [GO:0006813]; regulation of monoatomic ion transport [GO:0043269]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; caveola [GO:0005901]; intercalated disc [GO:0014704]; T-tubule [GO:0030315] | sodium channel regulator activity [GO:0017080] | PF02038; | 1.20.5.780; | FXYD family | PTM: Major plasma membrane substrate for cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) in several different tissues. Phosphorylated in response to insulin and adrenergic stimulation. Phosphorylation at Ser-88 stimulates sodium/potassium-transporting ATPase activity while the unphosphorylated form inhib... | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589}; Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule... | null | null | null | null | null | FUNCTION: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B... | Oryctolagus cuniculus (Rabbit) |
G1UB11 | ERG5_CANAL | MNSTEVDNLPFQQQLTSFVELAVAKATGSPITTLFTIIFLILSYDQLSYQINKGSIAGPRFKFYPIIGPFLESLDPKFEEYKAKWDSGELSCVSIFHKFVVIASSRDLARKILSSPKYVKPCVVDVAIKILRPTNWVFLDGKQHTDYRRSLNGLFSSKALEIYIPVQEKYMDIYLERFCKYDGPREFFPEFRELLCALSLRTFCGDYITEDQIALVADNYYRVTAALELVNFPIIIPYTKTWYGKKIADDTMKIFENCAAMAKKHINENNGTPKCVMDEWIHLMKEAREKHSEDPDSKLLVREFSNREISEAIFTFLFAS... | 1.14.19.41 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | cellular response to starvation [GO:0009267]; ergosterol biosynthetic process [GO:0006696]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to starvation [GO:... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | C-22 sterol desaturase activity [GO:0000249]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity [GO:0016491] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=5-dehydroepisterol + H(+) + NADPH + O2 = ergosta-5,7,22,24(28)-tetraen-3beta-ol + 2 H2O + NADP(+); Xref=Rhea:RHEA:33467, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18249, ChEBI:CHEBI:52972, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.19.41; Evidence={ECO:0000250|... | null | PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from zymosterol: step 4/5. {ECO:0000305|PubMed:20547793}. | null | null | FUNCTION: C-22 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (Probable). ERG5 converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (By similarity). The third modul... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UB61 | CDC11_CANAL | MNYSTENVSSAALRKRKTLKKSINFSIMIIGESGSGRSTLINTLCGGNSIVPTSSTATQDPFTKKLTLRHENVELEDNEGHKISLNIIDTPNFANSINCDDDFKIIVDFIRHQFDEVLLEESRVKRNPRFKDGRIHVLIYMINPTGHGLSDIDVKFLQHVNNLVNIIPIISKADSLTPKELKLNKELILEDLNNYGINFYKFNEYDYEQDYIDEEIIEYNKYLNSLIPFAIIGANEYRSNPNGSEDEDDILKLRILNKDFKPIDIDNAEINDFTILKNVLLVTHLNEFKDITHDSIYENYRTEALSGKQFQYVNKDSAKQ... | null | null | actomyosin contractile ring assembly [GO:0000915]; cellular bud neck septin ring organization [GO:0032186]; chitin localization [GO:0006033]; chlamydospore formation [GO:0001410]; cytoskeleton-dependent cytokinesis [GO:0061640]; division septum assembly [GO:0000917]; growth of unicellular organism as a thread of attach... | ascospore wall [GO:0005619]; cell division site [GO:0032153]; cellular bud neck [GO:0005935]; cellular bud neck septin ring [GO:0000144]; cellular bud neck septin structure [GO:0000399]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Gin4 complex [GO:1990317]; hyphal septin ring [GO:0032168]; hyphal tip [G... | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; structural constituent of cytoskeleton [GO:0005200] | PF00735; | 3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family | PTM: Hyphal induction causes immediate phosphorylation at Ser-395 by GIN4 and at Ser-394 by CDC28-CCN1. GIN4 phosphorylation at Ser-395 primes CDC11 for further phosphorylation by CDC28-CCN1. CDC28-HGC1 then maintains CDC11 phosphorylation throughout hyphal growth. Ser-4 is also phosphorylated in yeast cells but not hy... | SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:11454197, ECO:0000269|PubMed:12181342, ECO:0000269|PubMed:19915075, ECO:0000269|PubMed:22687514}. Note=Localizes to a tight ring at the bud and pseudohyphae necks and as a more diffuse array in emerging germ tubes of hyphae. | null | null | null | null | null | FUNCTION: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just bef... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UB63 | CSA1_CANAL | MLPSIVISIVLASFVSAESSITEAPTTTAEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVASSSEQPVETSSEPAGSSQSVESSQPAETSSSEPAETSSSEPAETSSETSSEQPASSEPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVP... | null | null | intracellular iron ion homeostasis [GO:0006879]; single-species biofilm formation on inanimate substrate [GO:0044011] | cell surface [GO:0009986]; cellular bud [GO:0005933]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; hyphal cell wall [GO:0030446]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF05730; | null | RBT5 family | PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the... | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10652105, ECO:0000269|PubMed:19555771, ECO:0000269|PubMed:23243062, ECO:0000269|PubMed:23728625}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. | null | null | null | null | null | FUNCTION: Heme-binding protein involved in heme-iron utilization. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation. {ECO:0000269|PubMed:15306022, ECO:0000269|PubMed:17042757, ECO:0000269|PubMed:21205162}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UB67 | EED1_CANAL | MERRQFNTSNIRNGTGRPRKTPRSKLYMVYPPLSGEDSTNPEPEEGSSQENNPTEPSSSQSNSVQNQDQSEDQSQLPQQESNTQQESNTQQESNTPSPRASNTSTETPAPLSPIQPGIRNIPSGLLLPQEKVGRLMGYPFYRDFNFTLNPERYQKLIYVFQILKNAARNHRNGASLLRKYFSLARRSKRTTDMFVTTIEEMRKRSLENSRKRELEEAQEREESNKRQHTESSAEPNAESSTESTTESNAESGAEPNAEPSAESTTESNVESGAEPNAESGAESGAEPTAESNAELKQRIWEILSYRLEQSNNETNNTGES... | null | null | cell adhesion involved in single-species biofilm formation [GO:0043709]; development of symbiont in host [GO:0044114]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; positive regulation of cell adhesion involved in single-species biofilm formation [GO:1900189]... | nucleus [GO:0005634] | null | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcriptional regulator involved in extension of germ tubes into elongated hyphae and maintenance of filamentous growth. Regulates expression of UME6. Acts in a pathway that regulates maintenance of hyphal growth by repressing hyphal-to-yeast transition and allows dissemination within host epithelial tissue... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UBC2 | PGA47_CANAL | MKVSQILPLAGAISVASGFWIPDFSNKQNSNSYPGQYKGKGGYQDDCGDDYKKGYKSKTYSKVKPITSTDCTTPIQPTGTTTGYTKDVVESTSYTTDTAYTTTVITVTKCDGGSCSHTAVTTGVTIITVTTNDVITEYTTYCPLTSTPATESTPATESTPATESTPATESTPATESTPATESTPCTTSTETTPATESTPATESTPATESTPATESTPATESTPATESTPATESTPATESTPCTTSTETTPATESTASTETASSTPVESTVIVPSTTVITVSSCYEDKCSVSSVTTGVVTISSEETIYTTYCPITSSITIP... | null | null | adhesion of symbiont to host [GO:0044406]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; single-species biofilm formation in or on host organism [GO:0044407]; single-species biofilm formation on inanimate substrate [GO:0044011] | extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; side of membrane [GO:0098552] | cell adhesion molecule binding [GO:0050839] | PF13928; | null | PGA18 family | PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the... | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:17416898, ECO:0000269|PubMed:18375812}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. | null | null | null | null | null | FUNCTION: Cell wall protein which mediates cell-cell and cell-substrate adhesion. Required for biofilm formation and plays a role in virulence. {ECO:0000269|PubMed:14665461, ECO:0000269|PubMed:16321041, ECO:0000269|PubMed:17416898, ECO:0000269|PubMed:18375812, ECO:0000269|PubMed:20709785}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UBD1 | PMOB_METCA | MKTIKDRIAKWSAIGLLSAVAATAFYAPSASAHGEKSQAAFMRMRTIHWYDLSWSKEKVKINETVEIKGKFHVFEGWPETVDEPDVAFLNVGMPGPVFIRKESYIGGQLVPRSVRLEIGKTYDFRVVLKARRPGDWHVHTMMNVQGGGPIIGPGKWITVEGSMSEFRNPVTTLTGQTVDLENYNEGNTYFWHAFWFAIGVAWIGYWSRRPIFIPRLLMVDAGRADELVSATDRKVAMGFLAATILIVVMAMSSANSKYPITIPLQAGTMRGMKPLELPAPTVSVKVEDATYRVPGRAMRMKLTITNHGNSPIRLGEFYTA... | 1.14.18.3 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245, ECO:0000269|PubMed:22013879}; Note=Binds 3 copper ions per subunit. Two of these (copper ion 1 and 3) form a binuclear cluster. {ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245, ECO:0000269|PubMed... | null | membrane [GO:0016020] | metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497] | PF04744; | 1.10.287.710;2.60.120.570;2.60.40.1580; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245}; Multi-pass membrane protein {ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245}. Note=Located in intracellular membranes. | CATALYTIC ACTIVITY: Reaction=a quinol + methane + O2 = a quinone + H2O + methanol; Xref=Rhea:RHEA:30355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16183, ChEBI:CHEBI:17790, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.14.18.3; Evidence={ECO:0000269|PubMed:7646068}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=24.2 nmol/min/mg enzyme (with NADH as reductant) {ECO:0000269|PubMed:7646068}; Vmax=4.4 nmol/min/mg enzyme (with decyl-plastoquinol as reductant) {ECO:0000269|PubMed:7646068}; Vmax=2.9 nmol/min/mg enzyme (with duroquinol as reductant) {ECO:0000269|PubMed:7646068}... | null | null | null | FUNCTION: Methane monooxygenase is responsible for the initial oxygenation of methane to methanol in methanotrophs. At least in vitro, specific quinols can replace NADH as reductants. {ECO:0000269|PubMed:10376840, ECO:0000269|PubMed:17002291, ECO:0000269|PubMed:20410881}. | Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) |
G1UH28 | CHIT_PUNGR | MAKTLPFSRALLLSLSILLVARAISAGDIAIYWGQNGGEGTLASTCDTGRYAYVIVSFVTTFGNFRAPVVNLAGHCDPAAGTCTGLSDEIRSCQGKDIKVLMSIGGGAGDYSLVSEADADNFADYLWNNFLGGQSSSRPLGDAVLDGIDFDIELGTTTFYDTLARALSSRSTQAAKVYLTAAPQCPHPDSHLDAALNTGLFDNVWIQFYNNPLAQCQYSSGNTNDILSSWNTWTSSTTAGKIFLGLPAAPEAAGSGYIPPDVLTGQILPQIKTSAKYGGVMLYSKFYDTTYSTTIKDQV | 3.2.1.14 | null | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272]; seed germination [GO:0009845]; seedling development [GO:0090351] | amyloplast [GO:0009501]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; chitinase activity [GO:0004568] | PF00704; | 3.20.20.80; | Glycosyl hydrolase 18 family, Chitinase class III subfamily | null | SUBCELLULAR LOCATION: Plastid, amyloplast {ECO:0000269|PubMed:21790816, ECO:0000269|PubMed:22112454}. Note=Localizes to stroma in amyloplasts of the embryonic cells of the seed. {ECO:0000269|PubMed:21790816, ECO:0000269|PubMed:22112454}. | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000269|PubMed:21790816}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat/KM is 0.119 M(-1)sec(-1) for native protein, 0.130 M(-1)sec(-1) for native protein with 10 mM Ca(2+) and 0.116 M(-1)sec(-1) for EDTA-treated protein, using 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside (4-MU(GlcNAc)(3)) as substrate at pH 4.5 a... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 2.5 and 5.0. Removal of Ca(2+) from the protein by EDTA treatment narrows the pH range to 2.5-3.5. {ECO:0000269|PubMed:21790816}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is approximately 45 degrees Celsius. Removal of Ca(2+) from the protein by EDTA treatment decreases the optimum temperature to 35 degrees Celsius. {ECO:0000269|PubMed:21790816}; | FUNCTION: Hydrolyzes chitin. Probable calcium storage protein of the seeds. Binds calcium ions with high capacity and low affinity. Involved in seed germination. {ECO:0000269|PubMed:21790816}. | Punica granatum (Pomegranate) |
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