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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G5EFY4 | EGL46_CAEEL | MVPMNDFWVKAILSSTNPSPVPSTTSTVSNDENLDKTLDFDCSTQTVFPTLPMFWNPTLVQQMLALYQIQQQQIQFSAKLAPQPLFQEPTIQKEFLPFPHQSRKRPLPIDPKKTKLRKLNEDTVTSSPVSGMFIKEEADVKSVEELQKEADLLDETAAYVEVTEESRQKIDEIPNVIGDCICRLCKVKYEDVFKLAQHKCPRIAHEEYKCPDCDKVFSCPANLASHRRWHKPRNELGGSPPAQSSTIVSCSTCFNSFPTKKMLKLHSSTCQRSPLQDLLSRVIPTM | null | null | axon guidance [GO:0007411]; cell cycle [GO:0007049]; cell fate commitment [GO:0045165]; detection of carbon dioxide [GO:0003031]; detection of oxygen [GO:0003032]; male mating behavior [GO:0060179]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroblast division [GO:0055057]; neuron differen... | nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-bi... | null | 3.30.160.60; | INSM1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11274062, ECO:0000269|PubMed:23946438}. Note=Localized to nucleus during interphase and evenly distributed in the cytoplasm of dividing Q.a and Q.p neuroblasts. {ECO:0000269|PubMed:23946438}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:30291162). Represses expression of genes involved in differentiation of touch receptor neurons (TRN), probably acting as a heterodimer with egl-44, perhaps by occupying similar cis-regulatory elements as an unc-86/mec-3 heterodimer (PubMed:30291162). Plays a role in cell fate spec... | Caenorhabditis elegans |
G5EFY5 | NOB1_CAEEL | MISVMQQMINNDSPEDSKESITSVQQTPFFWPSAAAAIPSIQGESRSERESETGSSPQLAPSSTGMVMPGTAGMYGFGPSRMPTANEFGMMMNPVYTDFYQNPLASTGWYSYGQPYQFTANYSIPSLDGNLSDITIPTTAGSSAATTPNAAMHLPWAISHDGKKKRQPYKKDQISRLEYEYSVNQYLTNKRRSELSAQLMLDEKQVKVWFQNRRMKDKKLRQRHSGPFPHGAPVTPCIERLIN | null | null | animal organ morphogenesis [GO:0009887]; anterior/posterior axis specification [GO:0009948]; anterior/posterior pattern specification [GO:0009952]; cell differentiation [GO:0030154]; embryonic body morphogenesis [GO:0010172]; embryonic pattern specification [GO:0009880]; nematode male tail tip morphogenesis [GO:0045138... | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00046; | 1.10.10.60; | Abd-b homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU000682}. | null | null | null | null | null | FUNCTION: Transcription factor, involved in posterior embryonic patterning, morphogenetic movements of the posterior hypodermis, and cell fate specification (PubMed:10781051, PubMed:16824957, PubMed:20824072, PubMed:21408209). Binds to the 5'-TAGT-3' motif in regulatory elements of genes, including Meis protein psa-3 a... | Caenorhabditis elegans |
G5EFY7 | PQM1_CAEEL | MSFLNNDFGSPPATSSPPTTMPKLPTIQDMLNNIGASTVNLMQPNPYLMQNQIPLPVPNLPLNPFLHLNPAISQEIIQQFIAMSFNTPNVLASIANMGDDEGPSCNPKMRRGDLLKSVSMDSTEDPPSITLDNNGDMIVPNNDKEGWCRNKKYIEQTENGYMCTVCRKVYGRYNSVSYHVTIYHRNPPIKCNVPNCQFTTREARYIHFHKNYRHGIPLPESIDQGSRKCPHCRHVSKSPAMLEKHIRRHQIKDGLSNINEAIRERTSTICDEAMEIEPAETEVDPIETKPRSCTL | null | null | cellular lipid metabolic process [GO:0044255]; cellular response to heat [GO:0034605]; defense response to Gram-negative bacterium [GO:0050829]; determination of adult lifespan [GO:0008340]; glycogen metabolic process [GO:0005977]; innate immune response [GO:0045087]; intracellular oxygen homeostasis [GO:0032364]; nega... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin insulator sequence binding [GO:0043035]; metal ion binding [GO:0046872] | null | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30956009}. Nucleus {ECO:0000269|PubMed:23911329, ECO:0000269|PubMed:29949773, ECO:0000269|PubMed:31532389}. Cytoplasm {ECO:0000269|PubMed:23911329, ECO:0000269|PubMed:31532389}. Note=Nuclear localization under normal conditions, cytoplasmic as a result of heat-stress... | null | null | null | null | null | FUNCTION: Zinc finger transcription factor which acts as both a transcriptional activator and repressor (PubMed:23911329, PubMed:30956009). Binds to the promoters of genes that contain the 5'-CTTATCA-3' DNA consensus sequence in their regulatory region (PubMed:23911329, PubMed:31532389). Functions downstream of the Ins... | Caenorhabditis elegans |
G5EFZ1 | GPMI_CAEEL | MFVALGAQIYRQYFGRRGMAMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQIEAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTNESLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPELYLHFYGDGRDTSPNSGVGFLEQTLEFLEKTTGYGKLATVVGRYYAMDRDNRWERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGEKGRVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGMTQ... | 5.4.2.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17897734}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17897734}; Note=Binds 2 manganese or magnesium ions per subunit (By similarity). Cobalt and nickel are less efficient (PubMed:17897734). {ECO:0000250|UniProtKB:Q9X519,... | carbohydrate metabolic process [GO:0005975]; glucose catabolic process [GO:0006007]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity [GO:0046537]; manganese ion binding [GO:0030145] | PF06415;PF01676; | 3.40.720.10;3.40.1450.10; | BPG-independent phosphoglycerate mutase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.12; Evidence={ECO:0000269|PubMed:15234973, ECO:0000269|PubMed:17897734}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.508 mM for 3-phosphoglycerate {ECO:0000269|PubMed:17897734}; | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. {ECO:0000305|PubMed:15234973}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:17897734}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. Active between 17 and 32 degrees Celsius. {ECO:0000269|PubMed:17897734}; | FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. {ECO:0000269|PubMed:15234973, ECO:0000269|PubMed:17897734}. | Caenorhabditis elegans |
G5EFZ3 | ASH2_CAEEL | MRSSKGGRGRQAAPKTAPTTVCYCDGKRELGSVEVVCSTCLKWFHGRCLKEFHELNSNGVPFMICYTFTCKQCRPTAEDWKAKKADLVQMCVTVLATLSAERLKADGKLSAEHVPEDFTYLSLKDEIVPYMNENWYMLTAIKQKKEWHQNLAPTLLKEKNIFVQHNDDDDLFALAEKNLSLLGPLHEAVKLIGKRPIERENREPRHIELPPIEGPKTRGASKRRHAEAPVTGKKQKLAADYSSTAAPNGVQIDIPFSKDNYRYYLTEVDPNVPEDPAWNQNQSSAYVIPSFHYRELLNPTVNVSSNDRAFQLSINGNSIT... | null | null | chromatin organization [GO:0006325]; determination of adult lifespan [GO:0008340]; programmed cell death [GO:0012501] | nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188] | metal ion binding [GO:0046872]; transcription cis-regulatory region binding [GO:0000976] | PF21198;PF00622; | 2.60.120.920;3.90.980.20; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20555324}. | null | null | null | null | null | FUNCTION: Component of the set-2/ash-2 histone methyltransferase (HMT) complex (Probable). Required for the di- and trimethylation at 'Lys-4' of histone H3, a mark associated with epigenetic transcriptional activation (PubMed:20555324, PubMed:21527717). Implicated in the epigenetic inheritance of lifespan over several ... | Caenorhabditis elegans |
G5EG11 | FAT4_CAEEL | MVLREQEHEPFFIKIDGKWCQIDDAVLRSHPGGSAITTYKNMDATTVFHTFHTGSKEAYQWLTELKKECPTQEPEIPDIKDDPIKGIDDVNMGTFNISEKRSAQINKSFTDLRMRVRAEGLMDGSPLFYIRKILETIFTILFAFYLQYHTYYLPSAILMGVAWQQLGWLIHEFAHHQLFKNRYYNDLASYFVGNFLQGFSSGGWKEQHNVHHAATNVVGRDGDLDLVPFYATVAEHLNNYSQDSWVMTLFRWQHVHWTFMLPFLRLSWLLQSIIFVSQMPTHYYDYYRNTAIYEQVGLSLHWAWSLGQLYFLPDWSTRIM... | 1.14.19.37; 1.14.19.44 | null | lipid metabolic process [GO:0006629]; unsaturated fatty acid biosynthetic process [GO:0006636] | membrane [GO:0016020] | acyl-CoA delta5-desaturase activity [GO:0062076]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [GO:0016717]; stearoyl-CoA 9-desaturase activity [GO:0004768] | PF00487; | 3.10.120.10; | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(11Z,14Z)-eicosadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46524, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHE... | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9845325, ECO:0000269|PubMed:9917342}. | null | null | FUNCTION: Can function as a Delta(5) fatty acid desaturase and behaves as a (8-3) desaturase. Introduces a double bond in the fatty acid chain 5 carbons away from carboxy terminal to biosynthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiolo... | Caenorhabditis elegans |
G5EG14 | CATIN_CAEEL | MGKDSKKHKKERRRERSPSTSDSDEERLQKRLAEQRSLKKDEKRRQKEEMKKNESAEEKRARRMEKKMRKDAKRKDADAEDTLIPPELNYTNLNNPFNDTKLTQTFVWGKKLEREGKSGLTQDEITKQTSQRIRKNLHEAAEFKRIRDSRAAAKEDMEMMKRDADLRAGQISDTKEREFQMDQIKERTRIRIDQGRAKAIDLLSRYARFADENPHTAKIPDFELENPMEYLKASCKSVDDYEDLIEDIKTYREVDGWAKNETWWMDVTRIAEDEIQKKAAQNRGDVHASVQTEVQNMFKNKSIDELLKLEDQMDAKIRGN... | null | null | gonad development [GO:0008406]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of cell migration [GO:0030335]; regulation of cell migration [GO:0030334]; regulation of gene expression [GO:0010468]; regulation of Wnt signaling pathway [GO:0030111] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681] | RNA binding [GO:0003723] | PF10312;PF09732; | null | CACTIN family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20188721}. Cytoplasm {ECO:0000269|PubMed:20188721}. | null | null | null | null | null | FUNCTION: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (By similarity). Plays a role during early embryonic development (PubMed:20188721). Required for the distal tip cell migration at the end of larval development and for gonad morphogenesis (PubMed:20188721). {ECO:0000250|UniProtK... | Caenorhabditis elegans |
G5EG17 | SMC6_CAEEL | MGKRDIPSPNENIAPRTIGMRDVDLTAAPAKKAKLDTGERIAVSGRVASVKLTNFMCHANLQIDFKTAQNNCFYIGGPNGSGKSALFAAINLGLGGRGSDNDRGNTVKSYIKDGTTQSKITITLTNAGLNAHPDFDDLISIERTINQASSTYIMKSVKVTSSDNHVERIVSRKKADVDRIVSRFSIHLSNPAFWMSQDRSRSFLANFKPANVYKLYLESTNLENIRLSYIRFADALDECFALIQLKAGEILNEQKKLKRMQEQRDLQAKLDQDRALVASFCWKLLFCKVRDYNDQIELTLKKQEAQKTLQDETKKEYAKN... | null | null | chromosome organization [GO:0051276]; DNA replication [GO:0006260]; double-strand break repair via homologous recombination [GO:0000724]; meiotic cell cycle [GO:0051321] | condensed nuclear chromosome [GO:0000794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]; Smc5-Smc6 complex [GO:0030915] | ATP binding [GO:0005524]; damaged DNA binding [GO:0003684]; single-stranded DNA binding [GO:0003697] | PF02463; | 3.40.50.300; | SMC family, SMC6 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20661436}. Chromosome {ECO:0000269|PubMed:20661436}. Note=Nucleoplasmic in the distal gonad arm and localizes on chromosomes during pachytene, diplotene and diakinesis in oocytes. {ECO:0000269|PubMed:20661436}. | null | null | null | null | null | FUNCTION: Core component of the smc-5/smc-6 complex (PubMed:20661436). Involved in DNA double-strand break repair by promoting sister-chromatid homologous recombination during meiosis (PubMed:20661436, PubMed:24939994, PubMed:27010650). Also plays a role in the DNA damage repair of ultraviolet (UV) radiation-induced DN... | Caenorhabditis elegans |
G5EG38 | CDC16_CAEEL | MSAISPDTKSFAIPTLADEGSSSKPASSLDLPKHESIRFKPIKTLASRIDGSEYYDEASMEKVMEMLEIGRTDEAVAYADTLYSNIIDDEQQDIVTIAEYVKILVVLRQWRRISHIIARGNYHQIHIVFAYYAATALFQRKLYEDVAELSVGHLLPSNGQIGPLPVRTLSQVTGRYVEEERMKYSFANMAELDNSSKKLRMVPALMITIAESFLKLMNRDAAMICINYALSLDNTTLHVERLMAKYNLVEPAMWEKYRKVRNEQLKLHEGNHDPRILMERAQRAYEMGRFRETKKITDELFDLFGPHPECIILRIHCLTM... | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; asymmetric cell division [GO:0008356]; cell division [GO:0051301]; eggshell formation [GO:0030703]; meiotic cell cycle [GO:0051321]; neurotransmitter transport [GO:0006836]; polarity specification of anterior/posterior axis [GO:0009949]; positive regu... | anaphase-promoting complex [GO:0005680]; anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; synapse [GO:0045202] | null | PF14559; | 1.25.40.10; | APC6/CDC16 family | null | SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:24321454}. Synapse {ECO:0000269|PubMed:24321454}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}. | null | null | FUNCTION: Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (By similarity). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins (By ... | Caenorhabditis elegans |
G5EG44 | MDL1_CAEEL | MEQQLNLGHLLTAARLLDIGALDISSLDLGALTSTSSSPGSSSPAMFDLSNESELRSLFCGKLKVDKKQSSCASNASTSSQPYCSSPPARKSSKHSRTAHNELEKTRRANLRGCLETLKMLVPCVSDATRNTTLALLTRARDHIIELQDSNAAQMKKLNDLRDEQDELVAELAQLQADEEVAQATSQACQTLSQSRPESRASSFTSTSSRDSPCYLEYSPSSKPMDSHKPTIIDLYAEGLIPRGPITFPRPLVYPHNVFDLMNLPPTPFDVSQFLPINLQV | null | null | determination of adult lifespan [GO:0008340]; regulation of cell differentiation [GO:0045595]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:27402359}. | null | null | null | null | null | FUNCTION: Transcriptional regulator which binds to the E box motif 5'-CACGTG-3', when in a heterodimeric complex with mxl-1 (PubMed:9764821). Involved in the control of lifespan in response to dietary restriction, the decline in protein homeostasis associated with normal aging, germline signaling and may overlap with t... | Caenorhabditis elegans |
G5EG59 | EXOS5_CAEEL | MAGRLREMRCELSFLKNADGSACFSQGATCIWASCSGPGDVHASKASDEAMTLDISYRANCGDNKFNVLNNIIHSTLSNAINLELFPHTTISVTVHGIQDDGSMGAVAINGACFALLDNGMPFETVFCGVLIVRVKDELIIDPTAKQEAASTGRVLFSVCKGSDGHPEVCAMDAIGHWDFIQLEAAWSLAQPSASAIFDFYKTVMKRKLSVDEQ | null | null | apoptotic DNA fragmentation [GO:0006309]; nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; RNA processing [GO:0006396]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364... | cytoplasmic exosome (RNase complex) [GO:0000177]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730] | 3'-5' exonuclease activity [GO:0008408]; double-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899] | PF01138;PF03725; | 3.30.230.70; | RNase PH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQT4}. Nucleus {ECO:0000250|UniProtKB:Q9NQT4}. | null | null | null | null | null | FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events (By similarity). Involved in apoptotic DNA degradation (PubMed:12718884). In vitro, does not bind or digest single-stranded RNA (PubMed... | Caenorhabditis elegans |
G5EG78 | PXDN2_CAEEL | MLLEFLLLIGISLSTACPSECRCAGLDVHCEGKNLTAIPGHIPIATTNLYFSNNLLNSLSKSNFQALPNLQYLDLSNNSIRDIEETLLDSFPGLKYLDLSWNKIRYVPKLSTAPNALVSLNLVHNEISRLDNDLVSHSPYMQTFLIQRNRIQSLPHDFFNSRMVPTLKTVKMAGNPWSCDCRMVNVKQFADSLFAHSNQNIFIVGKCFFPKGLRNYVFRNLSIENLECEKPEYSKTDDGMFKMSCPNNEMEGYHYDSIFLENNKEARHTAHFARDKDGSLLSNGQFTRNYQCAFYRQKQSIHMQKKMQASSSTEPPITTT... | 1.11.2.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX... | axon guidance [GO:0007411]; basement membrane organization [GO:0071711]; embryonic body morphogenesis [GO:0010172]; muscle attachment [GO:0016203]; negative regulation of axon regeneration [GO:0048681]; regulation of basement membrane organization [GO:0110011]; response to oxidative stress [GO:0006979] | basement membrane [GO:0005604]; extracellular space [GO:0005615] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF03098;PF07679;PF13855; | 1.10.640.10;2.60.40.10;3.80.10.10; | Peroxidase family, XPO subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20876652, ECO:0000269|PubMed:25475546}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:20876652}. Note=Localizes to the basement membrane in between the epidermis and muscles. {ECO:0000269|PubMed:20876652}. | CATALYTIC ACTIVITY: Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O; Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:... | null | null | null | null | FUNCTION: Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer (By similarity). Required for ... | Caenorhabditis elegans |
G5EG86 | BRC2_CAEEL | MGDSSKKVKDSFDTISEPDSFDEPKGVPISMEPVFSTAAGIRIDVKQESIDKSKKMLNSDLKSKSSSKGGFSSPLVRKNNGSSAFVSPFRREGTSSTTTKRPASGGFEDFEAPPAKKSTSSSSKKSKKHSKKEKKKEFKEIHADVLRVSRIYEKDKFRIILQESSSTPLILATCSYNRGSDIKFGDRIHVDAEVCKKSSSGDVTEIYIDRVLKNKENGAKSGIRRHSIAKKPFCIKPRFIHELSDTKIKKTVVQVNLLDLNLDFYAGCSKCKHSLPEAANQCEFCKDSQGKSELSMYSRVRVMDFSGQMFINVTTKNMKK... | null | null | DNA strand invasion [GO:0042148]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via single-strand annealing [GO:0045002]; egg-laying behavior [GO:0018991]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic... | condensed nuclear chromosome [GO:0000794]; nucleus [GO:0005634] | single-stranded DNA binding [GO:0003697] | null | 2.40.50.140; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15798199}. Chromosome {ECO:0000269|PubMed:15798199}. Note=Diffusely localized in the nucleus. Recruited to sites of DNA damage upon induction of DNA double strand breaks by ionizing radiation (IR) or in meiosis. {ECO:0000269|PubMed:15798199}. | null | null | null | null | null | FUNCTION: Required for the homologous recombination repair of DNA double strand breaks, thereby playing a role in chromosome integrity (PubMed:15798199, PubMed:16843491). Acts by targeting rad-51 to sites of DNA damage and stabilizing rad-51-DNA filaments by blocking ATP hydrolysis catalyzed by rad-51 (PubMed:15798199,... | Caenorhabditis elegans |
G5EG88 | ACH23_CAEEL | MHRIYTFLIFISQLALGLSNNPDIPIQYELANNIMENYQKGLIPKVRKGSPINVTLSLQLYQIIQVNEPQQYLLLNAWAVERWVDQMLGWDPSEFDNETEIMARHDDIWLPDTTLYNSLEMDDSASKKLTHVKLTTLGKNQGAMVELLYPTIYKISCLLNLKYFPFDTQTCRMTFGSWSFDNSLIDYFPRTFTNGPIGLANFLENDAWSVLGTKVNREEKKYTCCPVNYTLLHYDVVIQRKPLYYVLNLIAPTAVITFISIIGFFTSVNPFTNFCNVSSSVHDLRQEKITLGITTLLSMSIMIFMVSDKMPSTSTCVPLI... | null | null | null | neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23950710, ECO:0000269|PubMed:24212673}; Multi-pass membrane protein {ECO:0000269|PubMed:24212673, ECO:0000305|PubMed:23950710}. | null | null | null | null | null | FUNCTION: Betaine receptor that functions as a ligand-gated non-selective monovalent cation channel in mechanosensory neurons to maintain basal levels of locomotion. The channel is permeable to Na(+) and K(+) but not to Ba(2+) or Ca(2+) ions. Elicits current in response to betaine, very weak current in response to chol... | Caenorhabditis elegans |
G5EGA3 | ANKL1_CAEEL | MPPNGAITTTPRSRMPPTTPSSGKSRPKKETLHYLAASSSTTSVDAARTLLERGANVNAIDRDGATPLHYACTHDNVAMAQLLLTFGADPMSADKLGRTAYSIAKGNTLRFLRRYKKSSNRQRLGFFRRFFACHSRNETFFIVRNNQEVAPLRPTALAEAASISFNRGNVLTNSYRCAKKKIRATFHAIRRSRSNSTATLQDVVLTSEGIRTVTTPSRRAPKATVYAKRSMSVSDLLLIPDRRDIKNEDVKTRGSPVKKTRGTGRSRTPEAILNPRKQRTPVNHHKRSKSQETKLVAMPSPNSMAYYNTSRARNAGLRPA... | 3.1.-.- | null | cell division [GO:0051301]; cellular response to hydroxyurea [GO:0072711]; cellular response to ionizing radiation [GO:0071479]; DNA catabolic process [GO:0006308]; DNA damage response [GO:0006974]; double-strand break repair via homologous recombination [GO:0000724]; embryo development ending in birth or egg hatching ... | condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; midbody [GO:0030496]; mitotic spindle midzone [GO:1990023]; nucleoplasm [GO:0005654]; spindle midzone [GO:0051233] | DNA endonuclease activity [GO:0004520] | PF13637;PF03020; | 1.10.720.40;1.25.40.20; | null | PTM: Phosphorylated. Phosphorylated during telophase when localized at the midbody. {ECO:0000269|PubMed:29463814}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22383942, ECO:0000269|PubMed:29463814, ECO:0000269|PubMed:29879106}. Nucleus {ECO:0000269|PubMed:29879106}. Chromosome {ECO:0000269|PubMed:29463814}. Midbody {ECO:0000269|PubMed:29463814}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:29463814}. Note=Localizes ... | null | null | null | null | null | FUNCTION: Endonuclease which, in association with baf-1, plays an essential role during embryogenesis in the DNA repair response following DNA damage probably by ensuring proper chromosome segregation (PubMed:22383942). Also required during postembryonic cell divisions after DNA damage caused by ionizing radiation to e... | Caenorhabditis elegans |
G5EGA5 | FAT2_CAEEL | MTIATKVNTNKKDLDTIKVPELPSVAAVKAAIPEHCFVKDPLTSISYLIKDYVLLAGLYFAVPYIEHYLGWIGLLGWYWAMGIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDKGHPWVTEEDYNNRTAIEKYFAVIPISGWLRWNPIYTIVGLPDGSHFWPWSRLFETTEDRVKCAVSGVACAICAYIAFVLCDYSVYTFVKYYYIPLLFQGLILVIITYLQHQNEDIEVYEADEWGFVRGQTQTIDRHWGFGLDNIMHNITNGHVAHHFFFTKIPHYHLLEATPAIKKA... | 1.14.19.-; 1.14.19.6 | null | collagen and cuticulin-based cuticle development [GO:0040002]; fatty acid elongation [GO:0030497]; innate immune response [GO:0045087]; reproduction [GO:0000003]; unsaturated fatty acid biosynthetic process [GO:0006636] | membrane [GO:0016020] | delta12-fatty-acid desaturase activity [GO:0102985]; oxidoreductase activity [GO:0016491]; palmitoleic acid delta 12 desaturase activity [GO:0102987]; stearoyl-CoA 9-desaturase activity [GO:0004768] | PF11960;PF00487; | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:25856, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,... | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:26806391}. | null | null | FUNCTION: Can function as a Delta(12)/Delta(15) bifunctional desaturase and behaves as a nu +3' desaturase. Introduces a double bond in the fatty acid chain three carbons away from an existing double bond to biosynthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and m... | Caenorhabditis elegans |
G5EGB2 | LIN29_CAEEL | MDQTVLDSAFNSPVDSGIAGTTTGSGSTTHFGVGTNFKVSVRSSSRSTDGTDSTDGANSDNVTGSTGSTPAHHSITNLNMALSQHSIDSATAASSTNPFPHFNQADLLNFHQNSLLPHHMFSQFGRYPQFEQKPDVGVLQQQMQMREAKPYKCTQCVKAFANSSYLSQHMRIHLGIKPFGPCNYCGKKFTQLSHLQQHIRTHTGEKPYKCKFTGCDKAFSQLSNLQSHSRCHQTDKPFKCNSCYKCFTDEQSLLDHIPKHKESKHLKIHICPFCGKSYTQQTYLQKHMTKHADRSKASNFGNDVVPADPFDPSLLSWNPM... | null | null | cell fate specification [GO:0001708]; cell-cell fusion [GO:0140253]; cellular lipid metabolic process [GO:0044255]; collagen biosynthetic process [GO:0032964]; cuticle development [GO:0042335]; cuticle pattern formation [GO:0035017]; exit from mitosis [GO:0010458]; male genitalia morphogenesis [GO:0048808]; molting cyc... | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA b... | PF00096; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32223899, ECO:0000269|PubMed:8756296, ECO:0000269|PubMed:9334281, ECO:0000269|PubMed:9986728}. Note=Accumulates in nuclei of hypodermal cells in a temporally restricted fashion, beginning during the larval L4 stage. {ECO:0000269|PubMed:8756296}. | null | null | null | null | null | FUNCTION: Transcription factor which regulates the expression of various genes, including those involved in cuticle synthesis and maintenance, such as collagens, and in lipid metabolism (PubMed:27401555, PubMed:29604168, PubMed:31974205, PubMed:7671813). Binds to promoter regions of genes, at 5'-[(T/G)TTTTTT(A/T/C/G)]-... | Caenorhabditis elegans |
G5EGC9 | PES1_CAEEL | MTSSIKSDAPQFLLDLDNCSSLPPTPPKTASPGNSKMKGFNISDLCLDLDSSTSSSCSVSPASSFHTRSESVGQQQSGRNSPVSSSTESPTKRPKYSYNALIAMAIQSSPFKSLRVSEIYKYISSNFSYYKNQKPLQWQNSVRHNLSLHKEFRKVRTLDGKGSYWAMTADLGTDVYISNNCGKLRRQKSKVAKFPPMQQHFPIPQLPTQNIHQLCMQNPQILATLLQNMYLQNMQNLQNIPMVPGFPIIPVPINPTSFHFPKSS | null | null | anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; embryo development ending in birth or egg hatching [GO:0009792]; nematode larval development [GO:0002119]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; 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] | PF00250; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:8162851}. Cytoplasm {ECO:0000269|PubMed:8162851}. | null | null | null | null | null | FUNCTION: Transcription factor (By similarity). Plays a role in embryogenesis and later development, perhaps acting redundantly with forkhead protein fkh-2 (PubMed:11044397). {ECO:0000250|UniProtKB:Q12952, ECO:0000269|PubMed:11044397}. | Caenorhabditis elegans |
G5EGD2 | HIF1_CAEEL | MEDNRKRNMERRRETSRHAARDRRSKESDIFDDLKMCVPIVEEGTVTHLDRIALLRVAATICRLRKTAGNVLENNLDNEITNEVWTEDTIAECLDGFVMIVDSDSSILYVTESVAMYLGLTQTDLTGRALRDFLHPSDYDEFDKQSKMLHKPRGEDTDTTGINMVLRMKTVISPRGRCLNLKSALYKSVSFLVHSKVSTGGHVSFMQGITIPAGQGTTNANASAMTKYTESPMGAFTTRHTCDMRITFVSDKFNYILKSELKTLMGTSFYELVHPADMMIVSKSMKELFAKGHIRTPYYRLIAANDTLAWIQTEATTITH... | null | null | apoptotic process [GO:0006915]; cellular response to caloric restriction [GO:0061433]; cellular response to hypoxia [GO:0071456]; determination of adult lifespan [GO:0008340]; heat acclimation [GO:0010286]; negative regulation of apoptotic process [GO:0043066]; phosphorelay signal transduction system [GO:0000160]; posi... | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding tra... | PF00989;PF14598; | 3.30.450.20; | null | PTM: Hydroxylation on Pro-621 by egl-9 during normoxia conditions is required for vhl-1-mediated proteasomal degradation. {ECO:0000269|PubMed:11595184}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:19889840}. | null | null | null | null | null | FUNCTION: A transcription factor which is a key regulator in various cellular processes; including environment stress resistance (oxygen levels, hydrogen sulfide and cyanide levels and heat), negative regulation of cell apoptosis in ASJ neurons by inhibition of cep-1 via transcriptional activation of tyr-2, resistance/... | Caenorhabditis elegans |
G5EGE9 | DPY26_CAEEL | MDVPSSSNVTGRRKRQVLDDDEDDGFRSTPLRKVRGTKKIRPADVVPETIMTKIGAHIDDIVNKKKVGELNCFEYKSPLEIHTIEDMIKAKASIQEMAVVLEGAQCIIGYRVDRLHHDVRQIDSALSSGTVMRDSNGEEIHLTLESRKAKKKMAVVDGMNGMLDFLNNMDDALTTTELDADNDKNWKEDEENIAGEPRIDFKANSKDVDAFLQRDIFPEKLIYALSIKRATDLRADLLSDVSNYISADDTAHDLKDANIDWLRANPTFQKATKGSVCNSSNSFHSLNYYGIHSPDGRTLMLHNRIADKNADDRFFTSDVS... | null | null | cell division [GO:0051301]; chromosome condensation [GO:0030261]; dosage compensation by hypoactivation of X chromosome [GO:0042464]; meiotic chromosome segregation [GO:0045132]; meiotic sister chromatid segregation [GO:0045144]; mitotic sister chromatid segregation [GO:0000070]; negative regulation of gene expression ... | condensed nuclear chromosome [GO:0000794]; condensin complex [GO:0000796]; dosage compensation complex [GO:0046536]; nuclear chromosome [GO:0000228]; X chromosome [GO:0000805] | null | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11937488, ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:8939869}. Chromosome {ECO:0000269|PubMed:11937488, ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:8939869}. Note=During meiosis and mitosis, localizes to condensed chromosomes (PubMed:8939869). In interphase cel... | null | null | null | null | null | FUNCTION: Required for both chromosome condensation and segregation and for X-chromosome dosage compensation depending on its binding partners (PubMed:19119011, PubMed:19781752, PubMed:2917714, PubMed:8939869, PubMed:8939870). Member of the condensin I complex, a complex required for conversion of interphase chromatin ... | Caenorhabditis elegans |
G5EGF4 | EGL18_CAEEL | MSISIMTETRPESAEQQHHEVLQRPSDEPCSGCKQLQKDVAKTISMVMERMDKLQYRLDELLKENNELKSSSVSSGKASPSPAESRSSPKLVETVVAPVSGARKRKPKERSPPAAASPLPDFSNLMNGFMFDPLNMSNPNGMMQLLSMVQQQQQQQQHHQHIENQQSVSPPQSKSVKIEDPMDQDVKQEESERSDIPTATEAQNLLDALTAQFSSNGQATSTTSPPSSSSQVQAVIEAVATPSSQSQDSSMFEKTETSGDPNAARCSNCRTDKTTAWRRDAEGKLVCNPCGLYYRLHKVRRPIEMRKNHIQQRYRRKNKE... | null | null | cell fate commitment [GO:0045165]; cell fate specification [GO:0001708]; membrane fusion [GO:0061025]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode larval development [GO:0002119]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF00320; | 3.30.50.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Probable transcription factor (PubMed:11532911, PubMed:24885717). Involved in embryonic development and in vulval development in larvae, acting redundantly, at least in part, with elt-6 (PubMed:11532911, PubMed:12399309, PubMed:14975731, PubMed:24885717). Perhaps acting together with elt-6, may form a positiv... | Caenorhabditis elegans |
G5EGH6 | FAT7_CAEEL | MTVKTRASIAKKIEKDGLDSQYLFMDPNEVLQVQEESKKIPYKMEIVWRNVALFAALHVAAAIGLYELVFHAKWQTAVFSFALYVFSGFGITAGAHRLWSHKSYKATTPMRIFLMLLNNIALQNDIIEWARDHRCHHKWTDTDADPHNTTRGFFFTHMGWLLVRKHPQVKEHGGKLDLSDLFSDPVLVFQRKHYFPLVILFCFILPTIIPVYFWKETAFIAFYVAGTFRYCFTLHATWCINSAAHYFGWKPYDTSVSAVENVFTTVVAVGEGGHNFHHTFPQDYRASEYSLIYNWTRVLIDTAAVLGLVYDRKTIADEFI... | 1.14.19.-; 1.14.19.1 | null | fatty acid biosynthetic process [GO:0006633]; intracellular oxygen homeostasis [GO:0032364]; post-embryonic development [GO:0009791]; response to hypoxia [GO:0001666]; unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum membrane [GO:0005789] | 16:0 monogalactosyldiacylglycerol desaturase activity [GO:0009979]; iron ion binding [GO:0005506]; stearoyl-CoA 9-desaturase activity [GO:0004768] | null | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI... | null | PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis. {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}. | null | null | FUNCTION: Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols (PubMed:10872837, PubMed:16839188, PubMe... | Caenorhabditis elegans |
G5EGJ5 | IDA1_CAEEL | MRFFHSIIVLLFSISTGSAFLLYGCNLSENLCDNDESCYPDGVFGQCYSSESGSPEPTVLDNLDDTQLELLKLELTRLAAKDKDWGDEETQCVLAYFKMSMFYQLQYDPDFCQVRKPANVWALIQLIDTGLTEDPTILDEDVNPENVTDEDMAQIIEQLKEPSLPTEEDIEEALNAQNEDVDDEILDQYVQAVVNNENPDFSELSDGQLNILIGRLVDLKKNVENEEAQLLTGDGEQEMAVPLDDLEERGEQAILKKDIEQVGEINQGLDNTEHKIVKGRKDQVVTRVDANRVYLKVHLKNEDQLMPLIEFLQNTIAIPN... | null | null | dephosphorylation [GO:0016311]; exocytosis [GO:0006887]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; positive regulation of anterior/posterior axon guidance [GO:1905488]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of secretion [GO:0051046]; ventral c... | axon [GO:0030424]; cytoplasmic vesicle membrane [GO:0030659]; dendrite [GO:0030425]; dense core granule [GO:0031045]; perikaryon [GO:0043204]; secretory granule [GO:0030141]; synapse [GO:0045202]; trans-Golgi network transport vesicle [GO:0030140] | transmembrane receptor protein tyrosine phosphatase activity [GO:0005001] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 8 subfamily | PTM: Proteolytically cleaved probably at a dibasic consensus sequence by egl-3. {ECO:0000269|PubMed:15180830}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:15180830, ECO:0000305|PubMed:15044551}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830}. Cell projection, axon {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830}. Cell ... | null | null | null | null | null | FUNCTION: Regulates dense-core vesicle (DCV) trafficking and/or secretion (PubMed:19343207). Probably by controlling DCV trafficking, plays a role in the AVG neuron-mediated formation of the right axon tract of the ventral nerve cord (PubMed:27116976). Involved in locomotion by regulating acetylcholine release (PubMed:... | Caenorhabditis elegans |
G5EGJ9 | DEP1_CAEEL | MIRWKYELHSLIWLFLVLHLSKCQSDSLTTSAEQHELFAIKKDSLSPWSQILVSLPRRHPLYQSFAAKIQDVTENISDEVRDSNKTFVSSDDAPYSIRIHALRAGHRYSIAIHGQKDGSTSLIKEESVVMDPRAPDFRSMDSDIQVAEHNITMRTIKNDSYLQDSFSIEYRQINPDKKFPVLQILDIPEQKNLEFYLGNLNSGFDYSVRVIAHKDGMSSRPWISTLTTKPSPLKEVNINQNAGSCVEVSWQNDEFSGADFYTIQYSLQSTPNNSTNMTIPSTESSISICDSMLQGEAYQIIATVQKGGQVSEPLITKFQL... | 3.1.3.48 | null | positive regulation of vulval development [GO:0040026]; protein dephosphorylation [GO:0006470]; vulval cell fate specification [GO:0072327] | membrane [GO:0016020]; receptor complex [GO:0043235] | phosphatase activity [GO:0016791]; protein tyrosine phosphatase activity [GO:0004725] | PF00041;PF18861;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 3 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes in intracellular punctate structures in vulva cell precursors which partially colocalize with let-23. {ECO:0000269|PubMed:15901674}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:28135265}; | null | null | null | null | FUNCTION: Phosphatase which may dephosphorylate receptor let-23 and thereby regulate cell fate during the development of the vulva and the excretory system (PubMed:15901674). By inhibiting let-23 signaling prevents the establishment of a primary cell fate in the descendants of vulva precursor cells P5.p and P7.p (PubMe... | Caenorhabditis elegans |
G5EGK5 | CAM1_CAEEL | MSPRPEDDDLVIEPADDEGLHYGNASMEGTSTGQRPYIRLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRVNNVPDAVKLSQKKGSHHSTKHIAFDEYEDYEMMDRGRLPDEEDADLYRVPDSAAGSNYAPVAVSERWLDGIKYRVGDCVQYRGEACRQYLSNKFVMMTNESREEMYDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVCESDSNNQIVSICKHDCDVIQNDECPSELALAAQHELVGDTPKALFPLC... | 2.7.10.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25029443}; Note=Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305}; | axon guidance [GO:0007411]; cell migration [GO:0016477]; cellular response to nerve growth factor stimulus [GO:1990090]; establishment of neuroblast polarity [GO:0045200]; interneuron migration [GO:1904936]; motor neuron migration [GO:0097475]; neuroblast migration [GO:0097402]; neuron migration [GO:0001764]; phosphory... | axon [GO:0030424]; cell projection [GO:0042995]; dendrite [GO:0030425]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; neuronal cell body membrane [GO:0032809]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; frizzled binding [GO:0005109]; metal ion binding [GO:0046872]; neurotrophin binding [GO:0043121]; neurotrophin receptor activity [GO:0005030]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147] | PF07679;PF00051;PF07714; | 1.10.2000.10;2.60.40.10;2.40.20.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, ROR subfamily | PTM: Autophosphorylated at tyrosine residues which are probably located in the activation loop (residues 724-732). Autophosphorylation does not increase kinase activity in vitro. {ECO:0000269|PubMed:25029443}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10476968, ECO:0000269|PubMed:15944127}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:10476968, ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:19561603}. Cell projection, dendrite {ECO:0000269|PubMed:10476968, ECO:00... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PIRNR:PIRNR000624, ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.53 mM for ATP (in the presence of Mg(2+) at 20 degrees Celsius) {ECO:0000269|PubMed:25029443}; KM=0.45 mM for ATP (in the presence of Mn(2+) at 20 degrees Celsius) {ECO:0000269|PubMed:25029443}; Note=Autophosphorylation gives similar KM values for ATP. {ECO:00002... | null | null | null | FUNCTION: Tyrosine-protein kinase receptor for Wnt ligands egl-20, mom-2 and cwn-1 (PubMed:17942487, PubMed:25029443). Involved in the final positioning of migrating ALM, CAN, BDU and HSN neurons during development (PubMed:10476968, PubMed:14651925, PubMed:9165130, PubMed:9475729). Involved in the anterior-posterior mi... | Caenorhabditis elegans |
G5EGK6 | DIN1_CAEEL | MVQVPSTNTVKESRHVAISGLPSTLPDDRLQLHFTKFGEIQRLVRQHGNPEIVLVSYMDARGALRARSTKPQFEDSIEYKISAYIPEPTQNSSMASMSSTPSSGQSSSPRNAELSPQRYGDTRGAEVKSPSFRNQMEARRGGPHLSVQSQQRHSREYWPIPEFPSESTACVVYEIQSGSTPERDLFELVKKHSKRSGVPIDIQLESTTEPGWKKARVHYYRLDTDGLKADKSLILGRPPKFRVYYPTSGEQKHPQCHPSTSYAIPKLKGDHLLKASCSVHVPHLDRHSPDHYRRRFESYGQVIDVDMVKSNDNKAFAVVQ... | null | null | protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | nucleus [GO:0005634] | RNA binding [GO:0003723]; ubiquitin protein ligase activity [GO:0061630] | PF00076;PF07744; | 2.40.290.10;3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15314028}. | null | null | null | null | null | FUNCTION: [Isoform d]: Probable transcriptional corepressor which modulates activity of the nuclear hormone receptor daf-12 to regulate the dauer diapause. {ECO:0000269|PubMed:15314028}. | Caenorhabditis elegans |
G5EGK8 | PP2A_CAEEL | MAAAPPSADPLDKALIVDVDQWIEQLYECKPLSENQVKTLCEKAKEILEKEPNVQEVRCPVTVCGDVHGQFHDLMELFKMGGKSPDTNYLFMGDYVDRGYYSVETVSLLVCLKIRYKDRVTLLRGNHESRQITQVYGFYDECLRKYGNSNVWKYFTDLFDCFPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRIQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHSNGLTLISRAHQLVMEGYNWSHDRNVVTVFSAPNYCYRCGNQAAMVELDDDLKYSFLQFDPAPRRGEPHVTRRTPDYFL | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P36873}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:P36873}; | centriole assembly [GO:0098534]; centrosome separation [GO:0051299]; G1/S transition of mitotic cell cycle [GO:0000082]; meiotic spindle disassembly [GO:0051229]; mitotic cell cycle [GO:0000278]; mitotic centrosome separation [GO:0007100]; mitotic nuclear membrane reassembly [GO:0007084]; mitotic spindle organization [... | axon [GO:0030424]; axonal growth cone [GO:0044295]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perikaryon [GO:0043204]; protein phosphatase type 2A complex [GO:0000159] | DEAD/H-box RNA helicase binding [GO:0017151]; metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-1 subfamily | null | SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:20392746}. Cell projection, axon {ECO:0000269|PubMed:20392746}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17218259}. Cytoplasm {ECO:0000269|PubMed:17218259}. Note=Localizes to the margins of VD neuron growth cones and to s... | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000255|RuleBase:RU004273}; CATALYTIC ACTIVITY: Reaction... | null | null | null | null | FUNCTION: Protein phosphatase which plays an essential role in early embryonic cell division (PubMed:17218259, PubMed:20392746, PubMed:21497766). Probably together with constant regulatory subunit paa-1 and regulatory subunit sur-6, positively regulates centriole duplication by preventing the degradation of sas-5 and k... | Caenorhabditis elegans |
G5EGL9 | AFF1_CAEEL | MRLWQWSIAVAICLVMVTEARLRRHHRKRRFVSSNFDEFYCGESAHAQSQFEEERESNSSKVSSVHSTQFNWGLDNTICIKLQNVVHVLKYERLEQRYPIENSYTFSVPLIDTNCKCHCYGFGTNDVCNVEKYADDRNCTTSSEFPTCYTKYHPAVEPLDCPVTSIPAKACCDIKLKPRDGRMFRAVKLQQPINDMIISHSIFANNSGKMMKVLGPDEFRINLLKGKEQFELTEYHRISVQLVASSPQQQLREGMYYFPEENHNDLREGKINEITESDLDKLGWYRRVGNDWQVATSGLLLRNAHKVVIKNCKGQVHMDQ... | null | null | regulation of egg-laying behavior [GO:0046662]; syncytium formation by plasma membrane fusion [GO:0000768] | apical plasma membrane [GO:0016324]; cell-cell contact zone [GO:0044291]; intracellular organelle [GO:0043229]; plasma membrane [GO:0005886] | null | PF14884; | 2.60.40.3980; | EFF/AFF cell fusogen family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17488621}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:21350017}. | null | null | null | null | null | FUNCTION: Required for cell fusion events during development including the fusion of anchor cells (AC), vulval A and vulval D rings, and late epidermal seam cells (PubMed:17488621). Required for amphid sheath cell fusion induced by entry into dauer stage (PubMed:21350017). {ECO:0000269|PubMed:17488621, ECO:0000269|PubM... | Caenorhabditis elegans |
G5EGM1 | MMPA_CAEEL | MFTGLHDILIILFLLVTLKIAQNVDHTKFLQKYGYLTSGDNQLSSESLSDALKNMQRMAGLEETGELDERTIQMMERPRCGHPDVEDHQKSRGKRYAPPQFKWKEKIITYGCKAVGTSTRISLDDLRRTMHQAASQWSELADVEIVESSVKNPMMVISAGRENHYPCTVRFDTKTLAHAFFPTNGQIHINDRVQFAMTNYTERMGANSLYSVVAHEMGHALGFSHSPDIDSVMFAYDTPRKWKFTSMDKYNMRSYYGAKASKKENEEEERKTENEDKRRKTEKDRGRTREHESDDIRPNECRVENPIVVQYRGEYLIFKS... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O60882}; | basement membrane disassembly [GO:0034769]; collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508] | basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270] | PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15960981}; Single-pass type I membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:15960981}. Note=Localizes to puncta on the cell surface that are often concentrated at the invasive basolateral membrane of the anchor cell. {ECO:0000269|Pu... | null | null | null | null | null | FUNCTION: Metalloprotease which, together with cadherin cdh-3 and hemicentin him-4, plays a role in anchor cell (AC) invasion during postembryonic vulval development probably by promoting the degradation of the basement membrane separating the gonad from the vulva epithelium. {ECO:0000269|PubMed:15960981}. | Caenorhabditis elegans |
G5EGM3 | TAF1_CAEEL | MNNTHHHTNGYRTEKPKNEEDLEDPYANLSDFYKNHPAARNEACSSASNGGSKSVKMEPKVEKNEEFEEYIGDPVRLEDMEPFARPSLRDDAPLSSILHPDLDGIDPRIFFKDFNPNKTLRFSRLFAQNIKHTSRAEIWWASRTFSKHQRKKEPEEPLADDVIVGAKKLKLNIIEKVPRVMLADDEEERMRRPILTDAEEMAKKNEEGTVVQPWRTGPAKIWYDMMNLPMTSQAVNYGFKLKKSPQKVSIRSGKPLNYRTPDDLPSTSSGPAPNSAPFLDKVEVIDKSCEASTSEDILLPYQVIEWENDVILDGEEVKDQ... | null | null | embryo development ending in birth or egg hatching [GO:0009792]; RNA polymerase II preinitiation complex assembly [GO:0051123]; transcription initiation at RNA polymerase II promoter [GO:0006367] | nucleus [GO:0005634]; transcription factor TFIID complex [GO:0005669] | DNA binding [GO:0003677]; histone acetyltransferase activity [GO:0004402]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II general transcription initiation factor activity [GO:0016251]; RNA polymerase II general transcription initiation factor binding [GO:0001091]; TBP-class protein binding [GO... | PF00439;PF12157;PF15288; | 1.20.920.10; | TAF1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14726532}. | null | null | null | null | null | FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similar... | Caenorhabditis elegans |
G5EGN2 | FAT6_CAEEL | MTVKTRSNIAKKIEKDGGPETQYLAVDPNEIIQLQEESKKIPYKMEIVWRNVALFAALHFAAAIGLYQLIFEAKWQTVIFTFLLYVFGGFGITAGAHRLWSHKSYKATTPMRIFLMILNNIALQNDVIEWARDHRCHHKWTDTDADPHNTTRGFFFAHMGWLLVRKHPQVKEQGAKLDMSDLLSDPVLVFQRKHYFPLVILCCFILPTIIPVYFWKETAFIAFYTAGTFRYCFTLHATWCINSAAHYFGWKPYDSSITPVENVFTTIAAVGEGGHNFHHTFPQDYRTSEYSLKYNWTRVLIDTAAALGLVYDRKTACDEI... | 1.14.19.-; 1.14.19.1 | null | innate immune response [GO:0045087]; long-chain fatty acid biosynthetic process [GO:0042759]; post-embryonic development [GO:0009791]; unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum membrane [GO:0005789] | 16:0 monogalactosyldiacylglycerol desaturase activity [GO:0009979]; iron ion binding [GO:0005506]; stearoyl-CoA 9-desaturase activity [GO:0004768] | null | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI... | null | PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis. {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}. | null | null | FUNCTION: Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols. Also acts on palmitoyl-CoA (hexadecanoy... | Caenorhabditis elegans |
G5EGP4 | VPP3_CAEEL | MGSIYRSEHMKLCQIFFQSESAYQCVAELGELGMAQFIDLNEEQNAYTRKFVNEVRRCDEMERKINFVEDEITKDLVPIPDYDEHIPAPQPKHMGEMEANLEKLEEELVQINKNCKVLKNNHVQLLEMKAVLEHVTSLLDPHSKREAAMSISEAARGEAGPISFGMKDEFDKPVKDEKELKFVTGVVKRSKAIAFERFLWRLSRAKVFAKFIQIQEQTELFSNEFEDKCVFILFFSGEQLRAKVKKICDGFQAKCYTVPENPAERTKLLLNIKVQTTDMKAVIEKTLDYRSKCIHAAATNLRKWGIMLLKLKSIFHTLNM... | null | null | nematode larval development [GO:0002119]; vacuolar acidification [GO:0007035] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]; vacuolar proton-transporting V-type ATPase, V0 domain [GO:0000220] | ATPase binding [GO:0051117]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF01496; | null | V-ATPase 116 kDa subunit family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11441002, ECO:0000269|PubMed:19741196}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the apical surface of intestinal cells (PubMed:11441002). Localizes to dot-like structures, possibly P granules, in P2 cells of 4-cell stage embryos (PubMed... | null | null | null | null | null | FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... | Caenorhabditis elegans |
G5EGP8 | CATZ1_CAEEL | MRTFVLLLALCAICILASSAYGKVRKYSNRNRYNLKGCYKQTGRVFEHKRYDRIYETEDFDSEDLPKTWDWRDANGINYASADRNQHIPQYCGSCWAFGATSALADRINIKRKNAWPQAYLSVQEVIDCSGAGTCVMGGEPGGVYKYAHEHGIPHETCNNYQARDGKCDPYNRCGSCWPGECFSIKNYTLYKVSEYGTVHGYEKMKAEIYHKGPIACGIAATKAFETYAGGIYKEVTDEDIDHIISVHGWGVDHESGVEYWIGRNSWGEPWGEHGWFKIVTSQYKNAGSKYNLKIEEDCVWADPIV | 3.4.18.1 | null | ecdysis, collagen and cuticulin-based cuticle [GO:0042395]; embryo development ending in birth or egg hatching [GO:0009792]; gonad morphogenesis [GO:0035262]; post-embryonic body morphogenesis [GO:0040032]; proteolysis involved in protein catabolic process [GO:0051603]; vulval development [GO:0040025] | collagen and cuticulin-based cuticle extracellular matrix [GO:0060102]; extracellular space [GO:0005615]; lysosome [GO:0005764]; yolk granule [GO:0042718] | cysteine-type endopeptidase activity [GO:0004197] | PF00112; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14630920, ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:16857685}. Note=In molting larvae, localizes in both the new and old cuticles, specifically at the interface where the old cuticle is being degraded before ecdysis (PubMed:14630920). Locali... | CATALYTIC ACTIVITY: Reaction=Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.; EC=3.4.18.1; Evidence={ECO:0000250|UniProtKB:Q9UBR2}; | null | null | null | null | FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed (PubMed:14630920). Probably, required for the degradation of the old cuticle (PubMed:14630920)... | Caenorhabditis elegans |
G5EGQ3 | MAX2_CAEEL | MSTSKSSKVRIRNFIGRIFSPSDKDKDRDDEMKPSSSAMDISQPYNTVHRVHVGYDGQKFSGLPQPWMDILLRDISLADQKKDPNAVVTALKFYAQSMKENEKTKFMTTNSVFTNSDDDDVDVQLTGQVTEHLRNLQCSNGSATSPSTSVSASSSSARPLTNGNNHLSTASSTDTSLSLSERNNVPSPAPVPYSESAPQLKTFTGETPKLHPRSPFPPQPPVLPQRSKTASAVATTTTNPTTSNGAPPPVPGSKGPPVPPKPSHLKIASSTVSSGCSSPQQYSSARSVGNSLSNGSVVSTTSSDGDVQLSNKENSNDKSV... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20008556}; | cell migration [GO:0016477]; gonad morphogenesis [GO:0035262]; gonadal mesoderm development [GO:0007506]; inductive cell migration [GO:0040039]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; motor neuron axon guidance [GO:0008045]; netrin-activated signaling pathway [GO:0038007]; phosphoryla... | cytoplasm [GO:0005737]; dendrite [GO:0030425]; perikaryon [GO:0043204] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267] | PF00786;PF00069; | 3.90.810.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | null | SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:17050621}. Cell projection, dendrite {ECO:0000269|PubMed:17050621}. Cytoplasm {ECO:0000269|PubMed:19023419}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20008556}; CATALYTIC... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase, which phosphorylates mlk-1. Involved in the stress response to heavy metals by activating the mlk-1/mek-1/kgb-1 pathway (PubMed:20008556). In ventral cord commissural motoneurons, required for dorsal axon guidance downstream of unc-6/netrin repulsion receptor unc-5 and probabl... | Caenorhabditis elegans |
G5EGQ6 | TEN1_CAEEL | MFQHRTTNAQGPPPNRPMPRPPAGMPMMTSSHEHDYTNDYEDPEEMARSRGEGFSNHLLIKTTPPPQPHPNFNSYEMSMSQQRRSQQHQQPMAPPLSDCWGSGVHDSGVLHKNADGAYYIPSGSLRTTSSTLSPASGQRYLDQPHTSGGAPNPTYSDASTTLLKYPLAAGTNQNRRRQQVGTMNNGDPVAGGPMALSKKKKKFDDDSDTCSRWPSKWNILLAAALLVALFVICILLFRAPNYVYTQPAPSSDATSSAAAAASRYQDLGLRALPPAISLGERVDVEFFPKSMATTELTVTKPSRIRFNATVGSGAQLVLLM... | null | null | animal organ morphogenesis [GO:0009887]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; basement membrane assembly involved in embryonic body morphogenesis [GO:2001197]; basement membrane organization [GO:0071711]; cell migration [GO:0016477]; defecation [GO:0030421]; embryo development ending in birth ... | neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF15636; | 2.10.25.10;2.120.10.30; | Tenascin family, Teneurin subfamily | PTM: Probably proteolytically processed to generate a N-terminal intracellular domain. {ECO:0000269|PubMed:15936327}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15936327}. Cell membrane {ECO:0000269|PubMed:15936327}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes in the nucleus with a punctuate pattern. | null | null | null | null | null | FUNCTION: Plays a role in the gonadal basement membrane maintenance and/or adhesion early in development. Contributes to the guidance of pharyngeal neurons. {ECO:0000269|PubMed:15936327, ECO:0000269|PubMed:18632986, ECO:0000269|PubMed:20497576}. | Caenorhabditis elegans |
G5EGS3 | KLP12_CAEEL | MADTCVQVALRIRPQGNREKLEGSRVCTSVLPNDPQVTIGGDRSFTYDHVFDMPTLQYVVYESCVEKLVDGLFDGYNATVLAYGQTGSGKTHTMGTAFDAAVTQKEEDLGVIPRAIQHTFRKIAECKAQAIEQGLLEPAFEVSVQFVELYNDDVLDLLSDDRSMSSSIRIHEDSRGEIVLHGVEQRSVFDMHGTMDILKNGALNRTVAATNMNEQSSRSHAIFTLHLKQQRVAANPLDESGEQKTGELEMEMLCAKFHFVDLAGSERMKRTGATGDRAKEGISINVGLLALGNVIAALGGANGKVSHVPYRDSKLTRLLQ... | 3.6.4.- | null | microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231] | cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225;PF00400; | 3.40.850.10;2.130.10.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:36065637}. Note=Localizes to microtubules and to the growing microtubule plus-end. {ECO:0000269|PubMed:36065637}. | null | null | null | null | null | FUNCTION: Microtubule-binding motor protein which has ATPase activity (PubMed:36065637). In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis (PubMed:36065637). Negatively regulates axonal length through inhibiting microt... | Caenorhabditis elegans |
G5EGS5 | GBF1_CAEEL | MATNGVYIVMGEANCVVALLNKARRQYQLSQVPTLEDTDPLLRNFTDLKEVLNEVADLADMNPQTYLSPFLDVIKAQNTNGPITEAALAAVAKFLNYGLIDASSIKAANAVESIAYAVVHTKFIGGKSTGSDECVLFKILQVLRSLLLSPPGILLSNEAVCDMMQSCFRIVFEQNLSLLLRKAAESTLADMTQLIFTRLPTFVEDTRHPYIRQLVNPTEKRQKRKKKRQLSVHIETKAKEPENVPTEMTKLIGEAAETAETDGAANLGYDVVLTTDPPVDTVTHPDPPIEEIIKLAEPISAGDEADSESEGGGGEEHHER... | null | null | endoplasmic reticulum organization [GO:0007029]; endosomal transport [GO:0016197]; mitochondrion organization [GO:0007005]; regulation of ARF protein signal transduction [GO:0032012]; secretion [GO:0046903] | endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi cis cisterna [GO:0000137] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF01369;PF12783; | 1.10.220.20;1.10.1000.11; | null | null | SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:23840591}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:23840591}. | null | null | null | null | null | FUNCTION: Guanine-nucleotide exchange factor (GEF) for members of the Arf family of small GTPases involved in trafficking in the early secretory pathway; its GEF activity initiates the coating of nascent vesicles via the localized generation of activated ARFs through replacement of GDP with GTP (By similarity). Also, p... | Caenorhabditis elegans |
G5EGS7 | SEL7_CAEEL | MAQPNQPTPQFQMAQIPLAAFFDNNESKTMLNSMNLRLNDMDLKLSLILELLATRLPDQRLPSIFTSPPQTVISEAPPQSFTPSATNSTSDKTSSSLKTELKTEDSDGDLDMEGEEDTEELFDNESQPSQRNQSPKETEVEDEKVLADGPFPEGAVKRAAEKAARSFQSTQPKVFAWQILRESVTDDELRNVQISLRTFHGETADHLLGRQLPKIRLVVEATMKYFKWDLLSTESQLSKAKLILSHLKNNAKVRNWTLREGRPNRVAPATPPVNVDLVWKRYLALLGPAGFTGILPNLPQNLCNGGTQSPSIPQIDPSLF... | null | null | lateral inhibition [GO:0046331]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of cell fate specification [GO:0042659]; regulation of development, heterochronic [GO:0040034]; regulation of mesodermal cell fate specificatio... | nucleus [GO:0005634] | identical protein binding [GO:0042802]; sequence-specific DNA binding [GO:0043565] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15020414}. | null | null | null | null | null | FUNCTION: Putative transcription factor (PubMed:19500563). Positive regulator of the lin-12/Notch signaling pathway (PubMed:15020414). Binds to specific DNA sequences in regulatory elements (PubMed:19500563). Involved in cell fate decisions that require cell-cell interactions, such as the anchor cell (AC) / ventral ute... | Caenorhabditis elegans |
G5EGT9 | RYK_CAEEL | MILRYLIFFAQLWALCLANVNMFISKEEMNRTFGVKAELNYIEMGNVSSYSTKFHYRVMANIDYLSFTWNAVGIVHYEVYVESDDSSVLPIVRIPLKGTVPESLQDFTVEYRCAGHRSGQFAVSLYFTFKYGNKEPLKVKLRQEKICASRDGRRGLNGGYEGHEVDDTDSIDKAFFVIICIAAAFLLIVAATLICYFKRSKKEDMIPTRLPTSFRNSLKSTKSAQPFLLSTPRDGPPTLSAISSAPCSSSSASGNSIIPSKPRNIDVRRALLQLYQDRDAFQSLPLDMEGTFGEVRYAIWRQVDDVLNGDVDDEEDTFCN... | null | null | asymmetric protein localization involved in cell fate determination [GO:0045167]; establishment of anatomical structure orientation [GO:0048560]; morphogenesis of an epithelium [GO:0002009]; polarity specification of anterior/posterior axis [GO:0009949]; polarity specification of proximal/distal axis [GO:0010085]; posi... | basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF07714;PF02019; | 1.10.510.10;2.60.40.2170; | Protein kinase superfamily, Tyr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15369677}; Single-pass type I membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:32053105}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to the basolateral cell membrane of vulval precursor cells. {ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Has no detectable kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo (By similarity). Receptor which may act as a receptor for Wnt ligand mom-2. Plays a role in controlling P7.p vulva precursor cell lineage orientation during vulva development (PubMed:15369677, PubMed:15649465).... | Caenorhabditis elegans |
G5EGU2 | EAK6_CAEEL | MTNIREDENIFMFLCEKWILINKNHIWNRINQRINIIADFDRYQRARTISEGQRTENIHRNIYGAVPYDYNLVNLTSTQRNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPKYEDFMAFYNTMKEVGVPLLAVMKNNCMSSFFKKYHHTPPTNAPIIQCSTGGARCGVFIIIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYIRTRHNQLRHL... | 3.1.3.48 | null | dauer larval development [GO:0040024]; dephosphorylation [GO:0016311] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | phosphoprotein phosphatase activity [GO:0004721] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16839187}. Cell membrane {ECO:0000269|PubMed:16839187}; Peripheral membrane protein {ECO:0000269|PubMed:16839187}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Putative phosphatase which, together with eak-4 and sdf-9, negatively regulates dauer larva formation downstream of insulin-like receptor daf-2 and in parallel of age-1, pdk-1 and akt-1. {ECO:0000269|PubMed:16839187}. | Caenorhabditis elegans |
G5EGU9 | SZY20_CAEEL | MSKENVVADSWDDADADPVKELMDKVEKVKLLQRKEEKKEAFFEKVKAEESSGVVSKLQTEEGLGPSAEEPKRVFLRRPKDGFAASENVIEASPPTSADTEEQPVTNVRSRSHHKLNQKEKQPAPTYEERQAAYQAARNRILGTEYKPDNQEIKEIKFIDRSKSPETLKMTQQNMVEHYGEELSRELMEQPAEIVPPERQYTPDFTQPPPSVSESGGVYNGPPGFQQKQPNFQPTLQQQSLHQQQYLDNQYMMQMNVQIPIQYHNQTQHQFVPHEASAISTTSQNSNGDGQNDQAIYYYQAPTQQPMNYIPYNLPNMAYP... | null | null | cell division [GO:0051301]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic chromosome segregation [GO:0045132]; negative regulation of protein localization to centrosome [GO:1904780]; positive regulation of fertilization [GO:1905516]; positive regulation of mitotic cell cycle, embryonic [GO:00... | centriole [GO:0005814]; centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634] | RNA binding [GO:0003723] | PF12752; | null | null | PTM: Phosphorylated. May be dephosphorylated by let-92. {ECO:0000269|PubMed:21497766}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27689799}. Note=Co-localizes with atx-2 in the cytoplasm. {ECO:0000269|PubMed:27689799}.; SUBCELLULAR LOCATION: [Isoform f]: Cytoplasm {ECO:0000269|PubMed:19081077}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19081077}. Cyto... | null | null | null | null | null | FUNCTION: RNA binding protein that is required for normal cell division and cytokinesis during embryonic development (PubMed:19081077, PubMed:27689799). Functions with RNA-binding protein atx-2 to ensure embryonic cell division, and to this end, plays a role in the regulation of centrosome assembly, position and size, ... | Caenorhabditis elegans |
G5EJN7 | CYPD6_PHACH | MTSTIPTPPSIPFLGHVASIEREVPLRSFRLLSEQYGEIYELNILGRKLLVVSSAKLMSDVSDDKNFYKNMSGPLLQVRNAVGDGLFTAYGEEPNWGIAHRLLMPAFGTASIRDMFPDMLDLASQLVLKWERFGPKHRIDPAEDFTRLTLDTIALCAMSYRLNSFYRDSSHPFVQSMVDFLVECNLRANRPGLLTSVMVQTNAKYEEDIKTMTELADEIIAERRRNPTDKKDLLNIMLYSKDPKTGQSLSDVNIRNNLLTFLIAGHEPTSGLLTFALYYLIKNPEAMRKAHEEVDEVLGDQQIQLTDIGKLKYIDAILRE... | 1.14.14.1; 1.6.2.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q9Y8G7}; Note=Binds 1 FAD. {ECO:0000250|UniProtKB:Q9Y8G7}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q9Y8G7}; Note=Binds 1 FMN. {ECO:0000250|UniProtKB:Q9Y8G7}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evide... | null | cytosol [GO:0005829] | aromatase activity [GO:0070330]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; NADPH-hemoprotein reductase activity [GO:0003958] | PF00667;PF00258;PF00175;PF00067; | 3.40.50.360;1.10.630.10;3.40.50.80;2.40.30.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000269|PubMed:3017... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3800 uM for nonanol {ECO:0000269|PubMed:30171007}; KM=1100 uM for decanol {ECO:0000269|PubMed:30171007}; KM=420 uM for undecanol {ECO:0000269|PubMed:30171007}; KM=350 uM for dodecanol {ECO:0000269|PubMed:30171007}; KM=120 uM for tridecanol {ECO:0000269|PubMed:30171... | null | null | null | FUNCTION: Self-sufficient cytochrome P450 monooxygenase that catalyzes the regioselective in-chain hydroxylation of fatty alcohols (C9-15) as well as fatty acids (C9-15) at the omega-1 to omega-7 or omega-1 to omega-6 positions, respectively (PubMed:30171007). Is also able to convert naphthalene to 1-naphthol and 1-nap... | Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum) |
G7CBF5 | IRTA_MYCT3 | MARGFQGVMLRGLGARDHQATVVDKEYIAPHFVRVRLVSPTLFDEVIVEPTSWLRFWFPDPDGSDTEFQRAYTITESDPETGRFAVDMVLHEPAGPASTWARTVEPGATIAVMSMGSRGFSVPEDPEDRPVGYLLIGDSASTPAINGIIEVVPHDIPIELYLEQHHDDDVLIPLAEHPRLRVHRVSRDDASSLAAALELRDWSNWYCWAGPEAGALKQVRTRLRDEFGFPKREVYAQAYWTEGRAMGSSRGETSTPAKPAAKTAPAKAAAKPAAASGAGTPEHAAAPAAATTGAPQAAPAPGAAQPRTPVRGRWRAEAGS... | 7.2.2.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:32296173}; | null | plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled lipid transmembrane transporter activity [GO:0034040]; oxidoreductase activity [GO:0016491] | PF00664;PF00005;PF08021;PF04954; | 1.20.1560.10;3.40.50.80;3.40.50.300;2.40.30.10; | ABC transporter superfamily, Siderophore-Fe(3+) uptake transporter (SIUT) (TC 3.A.1.21) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:32296173}; Multi-pass membrane protein {ECO:0000269|PubMed:32296173}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=185 uM for mycobactin {ECO:0000269|PubMed:32296173}; | null | null | null | FUNCTION: Part of the ABC transporter complex IrtAB involved in the import of iron-bound mycobactin (Fe-MBT) and carboxymycobactin (Fe-cMBT) (PubMed:32296173). Has a preference for Fe-MBT over Fe-cMBT (PubMed:32296173). Mycobactins are then reduced by the siderophore interaction domain to facilitate iron release in the... | Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile) |
G7CES0 | LPQY_MYCT3 | MDGRQVVRARRWCATAAVALMTASTVAACGSDSGEIVISYYTPANEAATFTAVAQRCNAELGGRFRIEQRSLPREADAQRLQLARRLTGNDRSLDVMALDVVWTAEFAEAGWALPLSEDPAGLAEADATTNTLPGPLETAKWNGELYAAPITTNTQLLWYRADLMDEPPATWDEMLSEAARLHAQGGPSWIAVQGKQYEGLVVWFNTLLESAGGQVLSDDGQRVTLTDTPEHRAATVKALEIIKAVATAPGADPSITQTDENTARLALEQGRAALEVNWPYVLPSLLENAIKGGVGFLPLNENPALRGSINDVGTFAPTD... | null | null | null | ATP-binding cassette (ABC) transporter complex [GO:0043190]; periplasmic space [GO:0042597] | trehalose transmembrane transporter activity [GO:0015574] | PF01547; | 3.40.190.10; | Bacterial solute-binding protein 1 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000250|UniProtKB:P9WGU9}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.thermoresistibile. Trehalose uptake is essential for virulence (By similarity). Binds de... | Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile) |
G7IYC1 | CAD2_MEDTR | MSSSNLGNVVCVTGASGYIASWLVRLLLHRGYTVKATVRDPNDPKKVDHLVKLDGAKERLQLFKANLLEEGAFDSVVQGCHGVFHTASPFYHDVKDPQAELIDPALKGTLNVLNSCAKSPSLKRVVLTSSIAAVAYNGKPRTPDVVVDETWFTDADFCAKSNLWYVVSKTLAEEAAWKFVKENNIDMVTINPAMVIGPLLQPVLNTSAAAILNLINGAQTFPNASFGWVNVKDVANAHILAYENASASGRHCLVERVAHYSEVVRILRELYPSLQLPEKCADDKPYVPIYQVSKEKAKSLGLEYTPLEVSIKETVESLKE... | 1.2.1.44 | null | phenylpropanoid biosynthetic process [GO:0009699] | cytoplasm [GO:0005737] | cinnamyl-alcohol dehydrogenase activity [GO:0045551]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; sinapyl alcohol dehydrogenase activity [GO:0052747] | PF01370; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}. | CATALYTIC ACTIVITY: Reaction=(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; PhysiologicalDirection=right-t... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.4 uM for coumaraldehyde (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:25217505}; KM=6.6 uM for coniferaldehyde (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:25217505}; KM=730 uM for sinapaldehyde (at pH 6.25 and 30 degrees Celsius) {ECO:000026... | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:25217505}. | null | null | FUNCTION: Involved in lignin biosynthesis (By similarity). Regulates the monolignol composition by catalyzing the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (By similarity). Can use coumaraldehyde and coniferaldehyde as substrates, but barely sinapaldehyde (PubMed:25217505). {ECO:0000250|UniP... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7JEE5 | CCR2_MEDTR | MPAYDNTSSVSGGDQTVCVTGAGGFIASWLVKLLLERGYTVRGTVRNPEDPKNGHLKELEGARERLTLHKVDLLDLQSIQSVVHGCHGVFHTASPVTDNPDEMLEPAVNGTKNVIIASAEAKVRRVVFTSSIGTVYMDPNTSRDVVVDESYWSDLEHCKNTKNWYCYGKTVAEQSAWDIAKENQVDLVVVNPVVVLGPLLQPTINASTIHILKYLNGAAKTYVNATQSYVHVKDVALAHLLVYETNSASGRYICCETALHRGEVVEILAKYFPEYPLPTKCSDEKNPRVKPYKFSNQKLKDLGLEFTPVKQCLYDTVRSL... | 1.2.1.-; 1.2.1.44 | null | lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699] | cytoplasm [GO:0005737] | cinnamoyl-CoA reductase activity [GO:0016621]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF01370; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily | PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000250|UniProtKB:A0A059TC02}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}. | CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44.5 uM for feruloyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=32.7 uM for sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=23.4 uM for caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|P... | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000250|UniProtKB:A0A059TC02}. | null | null | FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:20876124). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:20876124). Mediates the conversion of caffeoyl-CoA and coumaroyl-CoA to caffaldehyde and coumara... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7JFU5 | ARGI_MEDTR | MSTIARRGFHYMQRLNSANVSPALLEKAQNRVIDAALTFIRERAKFKGELMRSLGGVAATSSLLGVPLGHHSSFHEGSAFAPPRIREAIWCDSTNSTTEEGKNLRDPRVITNVGDVPIEEIRDCGVDDKRLANVISESVKLVMDEDPLRPLVLGGDHSISFPVVRAVSEKLGGAVDILHFDAHPDLYHDFEGNYYSHASPFARIMEGGYARRLVQVGIRSITNDVREQVKKYGVETHEMRTLSRDRPILENLKLGEGVKGVYVSIDVDSLDPSIAPGVSHHEPGGLLFRDILNILQNLQGDIVGGDVVEYNPQRDTYDGI... | 3.5.3.1; 3.5.3.11 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742, ECO:0000269|PubMed:32754173}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00742, ECO:0000269|PubMed:32754173}; | arginine catabolic process to ornithine [GO:0019547]; protein hexamerization [GO:0034214]; putrescine biosynthetic process from arginine, using agmatinase [GO:0033389]; urea cycle [GO:0000050] | mitochondrion [GO:0005739] | agmatinase activity [GO:0008783]; arginase activity [GO:0004053]; metal ion binding [GO:0046872] | PF00491; | 3.40.800.10; | Arginase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000305|PubMed:32754173}; CATALYTIC ACTIVITY: Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929, ChEBI:CHEBI:153... | null | PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000305}.; PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the hydrolysis of L-arginine to urea and L-ornithine (Probable). The latter can be utilized in the urea cycle or as a precursor for the synthesis of both polyamines and proline (Probable). Possesses agmatinase activity. Catalyzes the formation of putrescine from agmatine (By similarity). {ECO:000025... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7JIK2 | SUNN_MEDTR | MKNITCYLLLLCMLFTTCYSLNNDLDALLKLKKSMKGEKAKDDALKDWKFSTSASAHCSFSGVKCDEDQRVIALNVTQVPLFGHLSKEIGELNMLESLTITMDNLTGELPTELSKLTSLRILNISHNLFSGNFPGNITFGMKKLEALDAYDNNFEGPLPEEIVSLMKLKYLSFAGNFFSGTIPESYSEFQKLEILRLNYNSLTGKIPKSLSKLKMLKELQLGYENAYSGGIPPELGSIKSLRYLEISNANLTGEIPPSLGNLENLDSLFLQMNNLTGTIPPELSSMRSLMSLDLSINGLSGEIPETFSKLKNLTLINFFQ... | 2.7.11.1 | null | cell differentiation [GO:0030154]; phosphorylation [GO:0016310] | membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; receptor serine/threonine kinase binding [GO:0033612] | PF00560;PF13855;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {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:0000305}; PhysiologicalDirection=le... | null | null | null | null | FUNCTION: LRR receptor kinase involved in the regulation of root growth and root nodule organogenesis (PubMed:16240175, PubMed:16941903, PubMed:22399647). Involved in long distance nodulation signaling events (Probable) (PubMed:22399647). Involved in the autoregulation of nodulation (AON), a long distance systemic sign... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7KDA1 | PHT18_MEDTR | MATSHGVLRSLDNAKTQSYHYLAIVIAGMGFFTDAYDLFCITAVTKLIGRLYYSDPTNHSPGILPTNVNNAITGVALCGTLAGQLFFGWLGDKLGRKKVYGITLTTMVGFALLSGLSFGSTPKTVVTSLCFFRFWLGFGIGGDYPLSAVIMSEYANQKTRGSFIAAVFAMQGVGILVAGGVAMFVSKLFLLYFPAPDFETDAVLSTQPEGDFVWRIVLMFGAVPAALTYYWRMKMPETARYTALVEGDHKKAVEDMAKVLDRNILSEESNTRIAIRPLESHSYGLFSSEFLNRHGLHLLGTTSTWFLLDIAFYSLQLTQK... | null | null | arbuscular mycorrhizal association [GO:0036377]; cellular response to nitrogen levels [GO:0043562]; phosphate ion transport [GO:0006817]; response to symbiotic fungus [GO:0009610]; transmembrane transport [GO:0055085] | periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | hydrolase activity [GO:0016787]; symporter activity [GO:0015293] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Phosphate:H(+) symporter (TC 2.A.1.9) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25841038}; Multi-pass membrane protein {ECO:0000255}. Note=Present on the periarbuscular membrane in cells containing arbuscules during arbuscular mycorrhizal (AM) symbiosis with AM fungi. {ECO:0000269|PubMed:25841038}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + phosphate(in) = H(+)(out) + phosphate(out); Xref=Rhea:RHEA:29939, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q8GSG4}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29941; Evidence={ECO:0000250|UniProtKB:Q8GSG4}; | null | null | null | null | FUNCTION: Low-affinity transporter for external inorganic phosphate (Pi) that may be involved in the acquisition of phosphate released by arbuscular mycorrhizal (AM) fungi (e.g. Glomus versiforme and G.intraradices) during AM symbiosis; not required for mycorrhizal arbuscule development. {ECO:0000269|PubMed:25841038}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7KGT0 | LGB8_MEDTR | MGFTEKQESLVNSSWESFKQNLSGYSVLFYTIILEKAPAAKGMFSFLKDTTGVQDSPQLQAHAAKVFEMVRDSAVQLRATGEVILGDATLGAIHIQKGVVDPHFVVVKEALLKTIKEAAGGNWSEELSTAWEVAYDGLAASIKKSMS | null | null | null | cytoplasm [GO:0005737] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344] | PF00042; | 1.10.490.10; | Plant globin family | PTM: Nitrated in effective nodules and particularly in hypoxic conditions; this mechanism may play a protective role in the symbiosis by buffering toxic peroxynitrite NO(2)(-). Nitration level decrease during nodule senescence. {ECO:0000250|UniProtKB:P02234}.; PTM: Phosphorylation at Ser-45 disrupts the molecular envir... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29868087}. Nucleus {ECO:0000250|UniProtKB:P02240}. | null | null | null | null | null | FUNCTION: Leghemoglobin that reversibly binds oxygen O(2) through a pentacoordinated heme iron (By similarity). In root nodules, facilitates the diffusion of oxygen to the bacteroids while preventing the bacterial nitrogenase from being inactivated by buffering dioxygen, nitric oxide and carbon monoxide, and promoting ... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7L166 | RAM1_MEDTR | MINSLCGSSNSLKEKCLQPNSSNQTNTHSKKNATNSCGDLEQINVLTPQSLNLPSLKFDLDGDVEVQSPDSSMWEAFFNDHLDNDFMISSPIRNINPNSPQASTYNNCNYNYAQGMQIQSLSGCSPPRFASQIGSLNSNNQQKGKGLSPLHRVFNSPNNQYMQHVENLSLPAIEEFLEDFQGDVDHFSSTKVSSECFDMETPISTILDSLTMQNSSSYGASVNEESTLLHGGNSSSQISQESDIYHQMGSMASASLSQALQQERYQEKHQKMQAQQQSLTVPIQIGIEQEQDSGLQLVHLLLACAEAVAKGEYMLARRYL... | null | null | arbuscular mycorrhizal association [GO:0036377]; detection of phosphate ion [GO:0010247]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to nutrient [GO:0007584]; response to symbiotic fungus [GO:0009610] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF03514; | null | GRAS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23122845}. Cytoplasm {ECO:0000250|UniProtKB:A0A145P7T2}. | null | null | null | null | null | FUNCTION: Transcription factor acting as a central regulator of arbuscular mycorrhiza (AM)-related genes (e.g. AMT2;4, AMT2;5, EXO70I, STR, RAM2, LEC5, PT4, VPY, BCP1, SCP1 and RAD1) required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis and Glomus versiforme) (PubMed:23... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7LCV1 | KI106_MEDTR | MSMRLSIRTLIILAHVCLFITTTTIAQFVLDTVGEPVEGDEEYFIRPVITNKGGRSTMVSRNESCPLHVGLELTGLGRGLVVKFTPFAPHHDFDDVRVNRDLRITFQASSSCVQSTEWRLGEKDTKSGRRLIITGTDSATNGSYGNFFRIVETPLEGMYNIQWCPTEVCPSCKFECGTVDMLNENGKILLALDGGPLPLVFQKE | null | null | arbuscular mycorrhizal association [GO:0036377]; response to symbiotic fungus [GO:0009610] | apoplast [GO:0048046]; extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00197; | 2.80.10.50; | Protease inhibitor I3 (leguminous Kunitz-type inhibitor) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23662629}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:23662629}. | null | null | null | null | null | FUNCTION: Protease inhibitor that, together with SCP1, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis), probably by degrading SCP1 in the apoplast of the periarbuscular region. {ECO:0000269|PubMed:23662629}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G8BAW7 | FAS2_CANPC | MKPEIEQELSHTLLTELLAYQFASPVRWIETQDVFLKQHNTERVIEIGPSPTLAGMASRTIKAKYQSYDAALSLQRQVLCYSKDAKEIYYTPDPAEPPAAEEPKAETGKESAPAASAAAAAATQPAAAVAPPPQSAGPVESIPDEPVKASLLIHVLVAQKLKKPLDAVPMSKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEETPLEELAEQFQDTFSGSLGKTSTSLIGRLMSSKMPGGFSITNARKYLESRFGLGPGRQDSVLLTALCNEPASRLGSEGDAKSFLDTMAQKYASHAGISLSSPSAGGASSGAGAAV... | 1.1.1.100; 2.3.1.41; 2.3.1.86 | null | fatty acid biosynthetic process [GO:0006633]; mitotic nuclear membrane biogenesis [GO:0101026]; palmitic acid biosynthetic process [GO:1900535]; single-species biofilm formation on inanimate substrate [GO:0044011] | fatty acid synthase complex [GO:0005835] | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; fatty-acyl-CoA synthase activity [GO:0004321]; holo-[acyl-carrier-protein] synthase activity [GO:0008897]; magnesium ion binding [GO:00002... | PF01648;PF00106;PF18325;PF18314;PF00109;PF02801; | 3.30.70.2490;3.40.47.10;3.90.25.70;6.10.140.1410;6.10.250.1930;3.90.470.20;3.40.50.720; | Thiolase-like superfamily, Fungal fatty acid synthetase subunit alpha family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChE... | null | null | null | null | FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. {ECO:0000269|PubMed:20027295}. | Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis) |
G8GER6 | PETH1_THEFU | MPPHAARPGPAQNRRGRAMAVITPRRERSSLLSRALRFTAAAATALVTAVSLAAPAHAANPYERGPNPTDALLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAVAISPGYTGTQASVAWLGERIASHGFVVITIDTNTTLDQPDSRARQLNAALDYMINDASSAVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVRVPTLIIGADLDTIAPVLTHARPFYNSLPTSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF | 3.1.1.101; 3.1.1.74 | null | null | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | acetylesterase activity [GO:0008126]; cutinase activity [GO:0050525] | PF12146; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23604968}. Periplasm {ECO:0000269|PubMed:23604968}. | 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:23604968}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alco... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=131 uM for pNP-butanoate (at 50 degrees Celsius and pH 8) {ECO:0000269|PubMed:23604968}; Note=kcat is 178 sec(-1) for the hydrolysis of pNP-butanoate (at 50 degrees Celsius and pH 8). {ECO:0000269|PubMed:23604968}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:23604968}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius (PubMed:23604968). Optimum temperature is 65 degrees Celsius (PubMed:32269349). {ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:32269349}; | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Probable). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:23604968, PubMed:25545638). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most ab... | Thermobifida fusca (Thermomonospora fusca) |
G8H5M7 | TPS9_SOLHA | MAASSANKSRPLANFHPTVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVEAPEGSEQKLVLIDAMQRLGVAYHFHNEIETSIQNIFDAPKQNNNLHIVSLHFRLVRQQGHYMSSDVFKQFTNQDGKFKERLTNDVQGLLSLYEASYLRVRDEEILEEALAFTTTHLKSIVSNMSNNNNSLKVEVSEALTQPIRMTLPRMEARRYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVLKMTSIIDDTFDAYATFDELEPFNDAIQRWDA... | 4.2.3.-; 4.2.3.113; 4.2.3.15; 4.2.3.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (1E,4E)-germacrene B + diphosphate; Xref=Rhea:RHEA:25444, ChEBI:CHEBI:5337, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.71; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25445; Evidence={ECO:0000269|PubMed:218... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E)-germacrene B, but also smaller amounts of germacrene A and C, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into alpha-humulene, germacrene A... | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8H5M8 | TPS12_SOLHA | MAASSADKSRPLANFSPTVWGYHFLSYTPEISSQEKHEVDELKEIFRKMLVETCDNSTQKLVLIDTIQRLGVAYHFDNEIETSIQNIFDASKQNDNDDNLHIVSLRFRLVRQQGHYMSSDVFKQFTNQDGKFKETLTNDVQGLLSLYEASHLRVRDEEILEEALTFTTTHLESIVSNLSNNNKVEVSEALTQPIRMTLPRMGARKYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVIQMASFFDDTFDAYATFDELEPFNDAIQRWDI... | 4.2.3.-; 4.2.3.104; 4.2.3.106; 4.2.3.113; 4.2.3.15; 4.2.3.57 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.104; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896; Evidence={ECO:0000269|PubMed:21818683... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E,8E)-alpha-humulene and (-)-(E)-beta-caryophyllene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into beta-bisabolene, gamma-curcumene and (Z)... | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8H5M9 | TS14A_SOLHA | MNQLAMVNTTITRPLANYHSSVWGNYFLSYTPQLTETSSQEKRELEELKEKVRQMLVETPDNSTQKLVLIDTIQRLGVAYHFENHIKISIQNIFDEFEKNKNKDNDDDLCVVALRFRLVRGQRHYMSSDVFTRFTNDDGKFKETLTKDVSGLLNLYEATHLRVHGEEILEDALSFTVTHLKSMSPKLDNSLKAQVSEALFQPIHTNIPRVVARKYIRIYENIESHDDLLLKFAKLDFHILQKMHQRELSELTRWWKYLDYENKYPYARDKLVECYFWATGVYFGPQYKRARKTLTKLIVIITITDDLYDAYATYDELVPY... | 4.2.3.-; 4.2.3.15; 4.2.3.47; 4.2.3.59 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68528, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68529; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into beta-bisabolene, beta-farnesene, (E)-gamma-bisabolene, beta-acoradiene, selinene and (Z)-alpha-bisabolene (PubMed:21818683). Low or no activity w... | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8H5N0 | TPS17_SOLHA | MELCTQTVAADHEVIITRRSGSHHPTLWGDHFLAYADLRGANEGEEKQNEDLKEEVRKMLVMAPSNSLEKLELINTIQCLGLAYHFQSEIDESLSYMYTHYEEYSIGDLHAIALCFRLLRQQGYYVSCDAFKKFTNDQGNFKEELVKDVEGMLSLYEAAQFRVHGEQILDEALNFTITKLKQILPKLSNSQLAQQITNALKFPIKDGIVRVETRKYISFYQQNQNHNQVLLNFAKLDFNILQTLHKKELSDMTRWWKKMELVNTLPYARDRLVECYFWCLGTYFEPQYSVARKMLTKISFFISIIDDTYDIYGKLDELTL... | 4.2.3.-; 4.2.3.106; 4.2.3.113; 4.2.3.114; 4.2.3.15; 4.2.3.47; 4.2.3.54; 4.2.3.73; 4.2.3.81 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (+)-valencene + diphosphate; Xref=Rhea:RHEA:29511, ChEBI:CHEBI:33019, ChEBI:CHEBI:61700, ChEBI:CHEBI:175763; EC=4.2.3.73; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29512; Evidence={ECO:0000269|PubMed:21818683}... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into gamma-gurjunene, (E)-beta-farnesene and (+)-valencene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-alpha-bergamotene and (Z)-gamma-bisabol... | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8H5N1 | TS14B_SOLHA | MNQLAMVNTTITRPLANYHSSVWGNYFLSYTPQLTEISSQEKRELEELKEKVRQMLVETPDNSTQKLVLIDTIQRLGVAYHFENHIKISIQNIFDEFEKNKNKDNDDDLCVVALRFRLVRGQRHYMSSDVFTRFTNDDGKFKETLTKDVQGLLNLYEATHLRVHGEEILEEALSFTVTHLKSMSPKLDNSLKAQVSEALFQPIHTNIPRVVARKYIRIYENIESHDDLLLKFAKLDFHILQKMHQRELSELTRWWKDLDHSNKYPYARDKLVECYFWAIGVYFGPQYKRARRTLTKLIVIITITDDLYDAYATYDELVPY... | 4.2.3.-; 4.2.3.113; 4.2.3.15; 4.2.3.47; 4.2.3.59; 4.2.3.79 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:28298, ChEBI:CHEBI:33019, ChEBI:CHEBI:49239, ChEBI:CHEBI:175763; EC=4.2.3.59; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28299; Evidence={ECO:0000269|PubMed:21... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into (+)-thujopsene, beta-bisabolene, alpha-cederene, beta-acoradiene, (E)-gamma-bisabolene, (Z)-alpha-bisabolene, (Z)-beta-farnesene and (E)-beta-far... | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8JYC6 | PDF1_CAEEL | MNRFIISMIALLAVFCAVSTASPLLYRAPQYQMYDDVQFVKRSNAELINGLIGMDLGKLSAVGKRSNAELINGLLSMNLNKLSGAGRR | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; locomotion [GO:0040011]; locomotion involved in locomotory behavior [GO:0031987]; locomotor rhythm [GO:0045475]; locomotory exploration behavior... | extracellular region [GO:0005576] | null | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Probable ligand of isoforms a and b of the calcitonin receptor-like protein, pdfr-1, a G-protein coupled receptor (PubMed:18390545). May not signal through isoform c of pdfr-1 (PubMed:18390545). Involved in locomotion; more specifically mate searching behavior of males, independent of nutritional status (PubM... | Caenorhabditis elegans |
G8JZS4 | SUSB_BACTN | MKKRKILSLIAFLCISFIANAQQKLTSPDNNLVMTFQVDSKGAPTYELTYKNKVVIKPSTLGLELKKEDNTRTDFDWVDRRDLTKLDSKTNLYDGFEVKDTQTATFDETWQPVWGEEKEIRNHYNELAVTLYQPMNDRSIVIRFRLFNDGLGFRYEFPQQKSLNYFVIKEEHSQFGMNGDHIAFWIPGDYDTQEYDYTISRLSEIRGLMKEAITPNSSQTPFSQTGVQTALMMKTDDGLYINLHEAALVDYSCMHLNLDDKNMVFESWLTPDAKGDKGYMQTPCNTPWRTIIVSDDARNILASRITLNLNEPCKIADAAS... | 3.2.1.3 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:18981178}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:18981178}; | starch catabolic process [GO:0005983] | periplasmic space [GO:0042597]; plasma membrane [GO:0005886] | alpha-1,4-glucosidase activity [GO:0004558]; calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; glucan 1,4-alpha-glucosidase activity [GO:0004339] | PF14509;PF14508;PF10566; | 2.70.98.10;3.20.20.70; | Glycosyl hydrolase 97 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:8955399}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.; EC=3.2.1.3; Evidence={ECO:0000269|PubMed:18981178}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.05 mM for maltose {ECO:0000269|PubMed:18981178}; KM=0.29 mM for maltotriose {ECO:0000269|PubMed:18981178}; KM=0.64 mM for maltotetraose {ECO:0000269|PubMed:18981178}; KM=1.29 mM for maltopentaose {ECO:0000269|PubMed:18981178}; KM=2.71 mM for maltohexaose {ECO:000... | PATHWAY: Glycan degradation; starch degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:18981178}; | null | FUNCTION: Glucoamylase that hydrolyzes alpha-1,4-glucosidic linkages, alpha-1,6-, alpha-1,3- and alpha-1,2-glucosidic linkages during starch degradation. {ECO:0000269|PubMed:18981178, ECO:0000269|PubMed:8955399}. | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
G8JZS6 | SUSF_BACTN | MKKHLIYTGMFLAAIGFSACNEDFKDWADPQSNPQEESAGQLTATFTAGKDASIVMDAATADSVEIAKLSSTTAEEGSKIAVNSLTLNENHTIPFSMTEDHVFKVALAQLDSVTQEAYKSRASVVRELKISINASAVTPSGEGIQLVGNEVSITLQPATTPAVDPDGYYIVGDFTGWDGNSAQQMKKDALDENLYILEAEIESTSNFKIFPASAINGNDIDWTKALGSSVDGDDSGDNFVSWTNAGAINTALDGKIKISFDAFNYRFTVKDNSAPTELYMTGSAYNWGTPAGDPNAWKALVPVNGTKGTFWGIFYFAAND... | null | null | starch catabolic process [GO:0005983]; starch metabolic process [GO:0005982] | cell outer membrane [GO:0009279]; outer membrane [GO:0019867] | starch binding [GO:2001070] | PF17142;PF16411; | 2.60.40.3610;2.60.40.3620;2.60.40.3640; | SusF family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:22910908}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:22910908}. | null | null | PATHWAY: Glycan degradation; starch degradation. | null | null | FUNCTION: Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has lower affinity for starch compared to SusE. {ECO:0000269|PubMed:1098... | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
G8JZT0 | SUSE_BACTN | MKKISNILLAVTFALPLFTACETDNDSNPILNEPDTFTLNTPAYAANNVYDLKNAQTVELTCSQPDYGFPAATTYTVQASFEQDFIEATDESKANYTVLESTSPTAKINVDASELNNALLDLWTAVNGEQAELPTEPVAVYIRLKANITSSGKGVCFSNVIELPNVLISKSTSSLTPPKTMFIVGSMLDTDWKVWKPMAGVYGMDGQFYSMIYFDANSEFKFGTKENEYIGINDNRVTVTDKAGAGVSGSDNFVVENAGWYLFYVKAAVKGDDYQFTITFYPAEVYLFGNTTGGSWAFNDEWKFTVPATKDGNFVSPAMT... | null | null | starch catabolic process [GO:0005983] | cell outer membrane [GO:0009279]; outer membrane [GO:0019867] | starch binding [GO:2001070] | PF14292;PF16411; | 2.60.40.3610;2.60.40.3620; | SusE family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:22910908}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:22910908}. | null | null | PATHWAY: Glycan degradation; starch degradation. | null | null | FUNCTION: Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has higher affinity for starch compared to SusF. {ECO:0000269|PubMed:109... | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
G8XQX1 | OXLA_DABRR | MNVFFMFSLLFLATLGSCADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVIVGAGMSGLSAAYVLAGAGHKVTVLEASERPGGRVRTHRNVKEGWYANLGPMRVPEKHRIIREYIRKFGLKLNEFVQETENGWYFIKNIRKRVGEVKKDPGLLKYPVKPSEAGKSAGQLYQESLGKAVEELKRTNCSYILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDQLPTSMYRAIEESVHFKARVIKIQQNAEKVTVTYQTTQKNLLLETADYVIVCTTSRAARRI... | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | amino acid catabolic process [GO:0009063]; envenomation resulting in induction of edema in another organism [GO:0044398]; envenomation resulting in negative regulation of platelet aggregation in another organism [GO:0044477]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | flavin adenine dinucleotide binding [GO:0050660]; L-amino-acid oxidase activity [GO:0001716]; L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21802487}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:21802487}; CATALYTIC ACTIVITY: Reaction=H2O... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.081 mM for L-Tyr (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.142 mM for L-Phe (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.373 mM for L-Met (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0... | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:21802487). Is highly active on L-Tyr followed by L-Phe, L-Met, L-Leu, L-Trp, and weakly active on L-Ile, L-Arg, L... | Daboia russelii (Russel's viper) (Vipera russelii) |
G8XYX6 | MOT8_DANRE | MHSESDDNTAGGTPGSEDPQAEESSSPAEEFEEQERKLAPEDSTVQLIHTGCTDKRPATPPGAHPGQGFVPPEGGFGWVVVFAATWCNGSIFGIQNSFGILHMMLVKHHEKQPDQASQFKVAWVGALAMGMIFFCSPVVSMFTDHFGCRKTAVCGAFVAFIGLLTSSFATTLGLWYFTYGILFGCGSSFAFQPSLVILGHYFRQRLGLANGVVTAGSSLFSMGLPVLLKKVVEPLGLPRTFQILSIFMLVQALLALAFKPLLPSGMCPMPGMALDGGPSTPESASRWQKGLAKIRRYFNVRVFSILTYRIWAFGVATAVL... | null | null | brain development [GO:0007420]; central nervous system development [GO:0007417]; chordate embryonic development [GO:0043009]; locomotion [GO:0040011]; neuron differentiation [GO:0030182]; oligodendrocyte differentiation [GO:0048709]; optomotor response [GO:0071632]; regulation of thyroid hormone generation [GO:2000609]... | apical plasma membrane [GO:0016324] | monocarboxylic acid transmembrane transporter activity [GO:0008028]; thyroid hormone binding [GO:0070324]; thyroid hormone transmembrane transporter activity [GO:0015349] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36021}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=3,3',5-triiodo-L-thyronine(out) = 3,3',5-triiodo-L-thyronine(in); Xref=Rhea:RHEA:71811, ChEBI:CHEBI:533015; Evidence={ECO:0000269|PubMed:21952246, ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71812; Evidence={ECO:0000305|PubMed:21952246, ECO:0000305|Pub... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for T3 (at 26 degrees Celsius) {ECO:0000269|PubMed:21952246}; | null | null | null | FUNCTION: Specific thyroid hormone transmembrane transporter, that mediates both uptake and efflux of thyroid hormones across the cell membrane independently of pH or a Na(+) gradient (PubMed:21952246, PubMed:31436139). The substrate preference is 3,3-diiodothyronine (3,3'-T2) and T3 and to a lesser extentd T4 and rT3.... | Danio rerio (Zebrafish) (Brachydanio rerio) |
G9BY57 | PETH_UNKP | MDGVLWRVRTAALMAALLALAAWALVWASPSVEAQSNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDYPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELDNASHFAPNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALSDFRTNNRHCQ | 3.1.1.101; 3.1.1.74 | null | null | extracellular region [GO:0005576] | acetylesterase activity [GO:0008126]; cutinase activity [GO:0050525] | PF12695; | 3.40.50.1820; | AB hydrolase superfamily | PTM: The disulfide bond between Cys-275 and Cys-292 contributes not only to the thermodynamic stability but also to the kinetic stability of the enzyme. {ECO:0000269|PubMed:24593046}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22194294}. | CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:22194294}; CATALYTIC ACTIVITY: Reaction=(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+); Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 mM for pNP-butanoate (at 30 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:24593046}; KM=0.21 mM for pNP-butanoate (at 50 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:24593046}; KM=0.24 mM for pNP-butanoate (at 70 degrees Celsius and pH 8.0) {ECO:0000269|P... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 with pNP-butyrate as substrate. Shows 70% of the maximal activity at pH 7.0 and pH 9.5. {ECO:0000269|PubMed:22194294}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius with pNP-butanoate as substrate (PubMed:22194294, PubMed:24593046). Optimum temperature using PET as substrate is superior to 70 degrees Celsius (PubMed:22194294). Shows 70% of the maximal activity at 30 and 70 degrees Cel... | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:22194294). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters), with a preference for short-chain substrates (C4 substrate at most) (PubMed:22194294, PubMed:24593046). Cann... | Unknown prokaryotic organism |
G9FRD6 | HSDHB_CLOSR | MNFREKYGQWGIVLGATEGIGKASAFELAKRGMDVILVGRRKEALEELAKAIHEETGKEIRVLPQDLSEYDAAERLIEATKDLDMGVIEYVACLHAMGQYNKVDYAKYEQMYRVNIRTFSKLLHHYIGEFKERDRGAFITIGSLSGWTSLPFCAEYAAEKAYMMTVTEGVAYECANTNVDVMLLSAGSTITPTWLKNKPSDPKAVAAAMYPEDVIKDGFEQLGKKFTYLAGELNREKMKENNAMDRNDLIAKLGKMFDHMA | 1.1.1.201 | null | bile acid catabolic process [GO:0030573]; lipid catabolic process [GO:0016042] | null | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0047022]; ketoreductase activity [GO:0045703]; nucleotide binding [GO:0000166] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=a 7beta-hydroxysteroid + NADP(+) = a 7-oxosteroid + H(+) + NADPH; Xref=Rhea:RHEA:20233, ChEBI:CHEBI:15378, ChEBI:CHEBI:35349, ChEBI:CHEBI:47789, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.201; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:2... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.59 mM for ursocholate {ECO:0000269|PubMed:22198717}; KM=2.3 mM for 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate {ECO:0000269|PubMed:22198717}; KM=3.06 mM for ursodeoxycholate {ECO:0000269|PubMed:22198717}; KM=2.65 mM for 7-oxolithocholate {ECO:0000269|PubMed:22... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Shows a maximum of activity at pH 8.5 in the oxidation of ursocholate, and between pH 7.0 and 8.0 when tested in the reduction reaction of 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate, with a gradual drop on the alkaline side and a sharp drop on the acidic side. {ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. No activity is detected above 60 degrees Celsius. {ECO:0000269|PubMed:22198717}; | FUNCTION: 7beta-hydroxysteroid dehydrogenase that catalyzes the reduction of the 7-oxo group of 7-oxosteroids, such as 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate, 7-oxolithocholate, 7,12-dioxo-lithocholate and dehydrocholate, to the corresponding 7beta-hydroxysteroids. Is also able to catalyze the reverse oxidation... | Clostridium sardiniense (Clostridium absonum) |
G9FRD7 | HDHA_CLOSR | MKRLEGKVAIVTSSTRGIGRASAEALAKEGALVYLAARSEELANEVIADIKKQGGVAKFVYFNAREEETYTSMVEKVAEAEGRIDILVNNYGGTNVNLDKNLTAGDTDEFFRILKDNVQSVYLPAKAAIPHMEKVGGGSIVNISTIGSVVPDISRIAYCVSKSAINSLTQNIALQYARKNIRCNAVLPGLIGTRAALENMTDEFRDSFLGHVPLNRVGRPEDIANAVLYYASDDSGYVTGMIHEVAGGFALGTPQYSEYCPR | 1.1.1.- | null | bile acid catabolic process [GO:0030573]; lipid catabolic process [GO:0016042] | null | nucleotide binding [GO:0000166]; oxidoreductase activity [GO:0016491] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=cholate + NADP(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + H(+) + NADPH; Xref=Rhea:RHEA:48508, ChEBI:CHEBI:11893, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.06 mM for cholate {ECO:0000269|PubMed:22198717}; KM=0.96 mM for 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate {ECO:0000269|PubMed:22198717}; KM=0.09 mM for chenodeoxycholate {ECO:0000269|PubMed:22198717}; KM=0.13 mM for 7-oxolithocholate {ECO:0000269|PubMed:2219... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Shows a maximum of activity between pH 7.5 and 8.0 both in the oxidation reaction of cholate and in the reduction reaction of 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate. {ECO:0000269|PubMed:22198717}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. No activity is detected above 60 degrees Celsius. {ECO:0000269|PubMed:22198717}; | FUNCTION: 7alpha-hydroxysteroid dehydrogenase that catalyzes the NADP(+)-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as cholate, chenodeoxycholate, glycochenodeoxycholate and taurochenodeoxycholate, to the corresponding 7-oxosteroids (PubMed:22198717, PubMed:24810359). Is also able t... | Clostridium sardiniense (Clostridium absonum) |
G9I930 | PA2HB_MICTN | MDKMNPAHLLVLAAVCVSLLGASSIPPQALNLNQFRLMIKCTNDRVWADFVDYGCYCVARDSNTPVDDLDRCCQAQKQCYDEAVKVHGCKPLVMFYSFECRYLASDLDCSGNNTKCRNFVCNCDRTATLCILTATYNRNNHKIDPSRCQ | null | null | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; ion channel regulator activity [GO:0099106]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, K49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22094702}. | null | null | null | null | null | FUNCTION: Heterodimer: MitTx, a heteromeric complex between Kunitz- and phospholipase-A2-like proteins, potently, persistently and selectively activates rat and chicken acid-sensing ion channel ASIC1 (PubMed:22094702, PubMed:24507937). Both alternatively spliced rat isoforms ASIC1a and ASIC1b are activated, with a high... | Micrurus tener tener (Texas coral snake) |
G9M9M3 | F6H22_IPOBA | MPSTTLSTVLSDINDFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICDAAEKRGFFQIVNHGIPIEMLEKAKAATYRFFREPAEEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDEEAAQYWPPSCRDDAVEYLKSCEMVSRKLLEALMQGLNVNQIDDSKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVMANESNDRISVPVFVNPRPNDIVGPLPEV... | 1.14.11.61; 1.14.11.62 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9C899}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | coumarin biosynthetic process [GO:0009805]; phenylpropanoid biosynthetic process [GO:0009699]; response to fungus [GO:0009620]; response to molecule of fungal origin [GO:0002238] | null | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; 4-coumaroyl 2'-hydroxylase activity [GO:0102312]; metal ion binding [GO:0046872] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-dihydroxycinnamoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57868, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85008, ChEBI:CHEBI:142398; EC=1.14.11.62; Evidence={ECO:0000269|PubMed:22169019}; CATAL... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.46 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019}; KM=6.12 uM for p-Coumaroyl-CoA {ECO:0000269|PubMed:22169019}; Note=kcat is 0.35 sec(-1) with feruloyl-CoA as substrate. kcat is 0.33 sec(-1) with p-Coumaroyl-CoA as substrate. {ECO:0000269|PubMed:22169019}; | PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22169019}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:22169019}; | null | FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (PubMed:22169019). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity toward caffeoyl-CoA (PubMed:22169019). {ECO:0000269|... | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
G9M9M4 | F6H21_IPOBA | MPSTTLSTVLSDINEFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICDAAEKRGFFQIVNHGIPLEMLEKAKAATYRFFREPAEEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDEEAAQYWPPSCRDDALEYLKSCEMVSRKLLEALMQGLNVNEIDDAKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVLANETNDRISVPVFVNPKPNDIVGPLPEV... | 1.14.11.61; 1.14.11.62 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9C899}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | coumarin biosynthetic process [GO:0009805]; phenylpropanoid biosynthetic process [GO:0009699]; response to fungus [GO:0009620]; response to molecule of fungal origin [GO:0002238] | null | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; 4-coumaroyl 2'-hydroxylase activity [GO:0102312]; metal ion binding [GO:0046872] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-dihydroxycinnamoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57868, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85008, ChEBI:CHEBI:142398; EC=1.14.11.62; Evidence={ECO:0000269|PubMed:22169019}; CATAL... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.06 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019}; KM=15.25 uM for p-Coumaroyl-CoA {ECO:0000269|PubMed:22169019}; Note=kcat is 0.55 sec(-1) with feruloyl-CoA as substrate. kcat is 0.64 sec(-1) with p-Coumaroyl-CoA as substrate. {ECO:0000269|PubMed:22169019}; | PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22169019}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:22169019}; | null | FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (PubMed:22169019). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity with caffeoyl-CoA (PubMed:22169019). {ECO:0000269|Pu... | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
G9M9M5 | F6H28_IPOBA | MMPSTTLSTVLSDINEFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICNAAEKRGFFQIVNHGIPLEMLEKAKAATYRFFREPAQEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDQEAAQYWPPSCRDDALEYLKSCELVSRKLLEALMQGLNVNQIDDSKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVMANESNDRISVPVFVNPKPNDIVGPLPE... | 1.14.11.61; 1.14.11.62 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9C899}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | coumarin biosynthetic process [GO:0009805]; phenylpropanoid biosynthetic process [GO:0009699]; response to fungus [GO:0009620]; response to molecule of fungal origin [GO:0002238] | null | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; 4-coumaroyl 2'-hydroxylase activity [GO:0102312]; metal ion binding [GO:0046872] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-dihydroxycinnamoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57868, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85008, ChEBI:CHEBI:142398; EC=1.14.11.62; Evidence={ECO:0000269|PubMed:22169019}; CATAL... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.34 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019}; KM=7.92 uM for p-Coumaroyl-CoA {ECO:0000269|PubMed:22169019}; Note=kcat is 0.28 sec(-1) with feruloyl-CoA as substrate. kcat is 0.28 sec(-1) with p-Coumaroyl-CoA as substrate. {ECO:0000269|PubMed:22169019}; | PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22169019}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:22169019}; | null | FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (PubMed:22169019). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity with caffeoyl-CoA (PubMed:22169019). {ECO:0000269|Pu... | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
G9MAN7 | TPS4_SELML | MAKVLFSSFQQTGISGSLKSGQLSGVFINGTNLKSNAHAKRFRKNSTSSITIRCCASNSPTLENTKLAGAPEKRQKKKQLPYQGILHVPGDRVEELDTRETSLLVAEVKGWLMKLASGKGEISPSAYDTAWVARIASESDSSLPEFPEALEWIINSQLPDGSWGDDRHLQLYDRVLSTLSCLVTLKTWDIGHNSIAQGTKFLRENMIKLKQDDGDLLSGFEVTFPMMLHEAKQLGLDIPYETEFTRLLEISTKKKLAKIPLDKLHSAPTTLLYSLEGLQDLEIDWQKILKLQSKDGSFLSSPSSTACVYLKTKDRKSLQY... | 4.2.3.131; 5.5.1.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | 5alpha,9alpha,10beta-labda-8(20),13-dien-15-yl diphosphate biosynthetic process [GO:1901949]; 5alpha,9alpha,10beta-labda-8(20),13-dien-15-yl diphosphate catabolic process [GO:1901948]; diterpenoid biosynthetic process [GO:0016102]; gibberellin biosynthetic process [GO:0009686]; miltiradiene biosynthetic process [GO:190... | chloroplast [GO:0009507] | copalyl diphosphate synthase activity [GO:0050559]; magnesium ion binding [GO:0000287]; miltiradiene synthase activity [GO:0062205]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.50.10.160;1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene; Xref=Rhea:RHEA:33983, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635, ChEBI:CHEBI:65037; EC=4.2.3.131; Evidence={ECO:0000269|PubMed:22027823}; CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl diphosphate; Xref=Rhea... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. | null | null | FUNCTION: Bifunctional diterpene cyclase that catalyzes the successive two-step type-B (protonation-initiated cyclization) and type-A (ionization-initiated cyclization) reactions of geranylgeranyl diphosphate (GGDP) producing successively (+)-copalyl diphosphate and miltiradiene. {ECO:0000269|PubMed:22027823}. | Selaginella moellendorffii (Spikemoss) |
G9MAP1 | CLAHY_LACPN | MGALFMVKSKAIMIGAGLSNMAAAVYLIQDGHWDGKDITFYGVDMHGANDGGATTDFTNEYWNKNHPMANTTGYVARGGRMLNYRTYVDLMDLLDRIPSVTEPGMTAAEDTRDFDAKHRTYDIARLMQGGKGIINAGKLGFNNKDRTLLTKLIMMPDSEETKLDNVSIAEYFKDDPHMFQTNFWYMWETTFAFRTQSSAQELRRYMHQMIYEFTQIEHLVGVNRTRYNQFESMILPLIKYLQGQGVTFIDNKIVKDWQFKDTPMQDEITVTGLVIEDAQTGETEEVEVDEDTAVIFTNGSITDSATMGDYNTPAPENMDY... | 4.2.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:25476761}; Note=FADH2 seems to be the active cofactor and is produced through the reduction of FAD by NADH. {ECO:0000269|PubMed:25476761}; | fatty acid metabolic process [GO:0006631]; response to toxic substance [GO:0009636] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | FAD binding [GO:0071949]; oleate hydratase activity [GO:0050151] | PF06100; | 3.50.50.60; | Oleate hydratase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22093837}. Cytoplasm {ECO:0000269|PubMed:22093837}. Note=Is not strongly linked to the membrane because this enzyme is also present in the soluble cell-free extracts. {ECO:0000269|PubMed:22093837}. | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + H2O = (10S)-hydroxy-(12Z)-octadecenoate; Xref=Rhea:RHEA:75723, ChEBI:CHEBI:15377, ChEBI:CHEBI:30245, ChEBI:CHEBI:194434; Evidence={ECO:0000269|PubMed:24127592, ECO:0000269|PubMed:25476761}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75724; Evidence={ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92 uM for linoleate {ECO:0000269|PubMed:25476761}; KM=98 uM for 10-hydroxy-cis-12-octadecenoate {ECO:0000269|PubMed:25476761}; Note=kcat is 0.026 sec(-1) for the hydration of linoleate. kcat is 0.0012 sec(-1) for the dehydration of 10-hydroxy-cis-12-octadecenoate. ... | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:22093837, ECO:0000269|PubMed:24127592}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 for the hydration of linoleic acid and for the dehydration of 10-hydroxy-cis-12-octadecenoic acid (HYA).; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius for the hydration of linoleic acid and 37 degrees Celsius for the dehydration of 10-hydroxy-cis-12-octadecenoic acid (HYA). {ECO:0000269|PubMed:25476761}; | FUNCTION: Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-HY catalyze... | Lactiplantibacillus plantarum (Lactobacillus plantarum) |
H0VCJ6 | NAAA_CAVPO | MRSPGIVLLLLLLLLLPPGAAPCPADLCPAPPRVNVSLDAAPAARWLPVLRLFDPGLLRAAVARIVGDRVPKWRDVIGKLVAEMESFLPQPYTKEIRGISDFLNLSLADGFIVNLAYEASAFCTSVVAQDSRGHIYHGRNLDYPFGDLLRKMTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPYKFTVSGDERDKGWWWENMIAALFQGHSPVSWLIRTTLSESEDFEASVYKLAKTPLIADVYYIVGGTAPGEGVVVTRNRGGPADIWPLDPLNGAWFRVETNYDHWKPVPKSDDRRTPAIKALNATGQANLSLEALFQ... | 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] | 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}. | Cavia porcellus (Guinea pig) |
H0VVW3 | APOA1_CAVPO | MKAVLLVVAALFLAGSQARHFWQQDDPKTSWDVVKEFANKYVDAVKESGKGYVEQLDASSLGQQLNLRLSDNWDTLSTILTKLQADFGLATQEFWDTLEKETEWLKQIVSEDLQDVKHKVQPYLENFQKKVQEEVEHYREKVRPLGIELRDGARQKLQELQEKLTPLGEDLRDRTREHVDVLRTQLAPFSEEMRQRLAKRLEELKDSATLADYHAKASEHLKMLGEKAKPALEDLRQGLLPVLENLKASILSSIDQASKQLAAQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor sig... | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:000... | 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}... | Cavia porcellus (Guinea pig) |
H0WFA5 | BUCKY_DANRE | MEGINNNSQPMGVGQPHHPVNHTRPFFYVQPPSQPYFMYQWPMNPYGHYGFPGPALHFGRPYMAPYQFMQYPGYVIPHAPMQPIDYRRINPHYPSVASYDLRVRHHFQNAGMHRETACSEVQTDPSDSVNKLIDKIESLKACELGSDKGPNNVVSSTPDVVQGEKLTRLNEDSNLEVATKECKEDPVTRPTTYSDSAYDAESSQGRLDECVFSDVLPLDSSSVHEEEEEEEKDVNEEDEPQTVADEICSQNEMSASTTSNVFCSGVQSIADPTECHDLEKLGDEQKQDIPSADAAAVIEPLISLSEDFDLPYQILRLPCN... | null | null | morphogenesis of follicular epithelium [GO:0016333]; oocyte animal/vegetal axis specification [GO:0060832]; oocyte anterior/posterior axis specification [GO:0007314]; pole plasm assembly [GO:0007315]; spermatogenesis [GO:0007283] | cleavage furrow [GO:0032154]; cytoplasm [GO:0005737] | null | null | null | null | PTM: Symmetric dimethylarginine modification promotes interaction with tdrd6. {ECO:0000269|PubMed:30086300}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19249209, ECO:0000269|PubMed:30086300}. Cleavage furrow {ECO:0000269|PubMed:26253407}. Note=Localizes to nuage (a peri-nuclear protein-RNA aggregate that associates closely with mitochondria), the Balbiani body during oogenesis, and in the germ plasm upon fertilizatio... | null | null | null | null | null | FUNCTION: Prion-like protein required for the formation of Balbiani body (electron-dense aggregates in the oocyte) and germ plasm assembly, and for the establishment of oocyte polarity during early oogenesis (PubMed:18582455, PubMed:19249209). Mobility and aggregation properties are improved by tudor domain-containing ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
H0YL14 | TM250_HUMAN | MPVMPIPRRVRSFHGPHTTCLHAACGPVRASHLARTKYNNFDVYIKTRWLYGFIRFLLYFSCSLFTAALWGALAALFCLQYLGVRVLLRFQRKLSVLLLLLGRRRVDFRLVNELLVYGIHVTMLLVGGLGWCFMVFVDM | null | null | cilium assembly [GO:0060271]; cytoskeleton-dependent cytokinesis [GO:0061640]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of viral process [GO:0048524] | cell division site [GO:0032153]; cytoplasm [GO:0005737]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; septin complex [GO:0031105]; septin ring [GO:0005940] | GTPase activity [GO:0003924]; molecular adaptor activity [GO:0060090] | PF17685; | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:21667337}. Cytoplasm {ECO:0000269|PubMed:21667337}. Note=Upon HHV-1 infection, accumulates arround the nuclear membrane and translocates into the nucleus. | null | null | null | null | null | FUNCTION: May play a role in cell proliferation by promoting progression into S phase. {ECO:0000269|PubMed:21667337}.; FUNCTION: (Microbial infection) Promotes human herpes simplex virus 1/HHV-1 proliferation. {ECO:0000269|PubMed:21667337}. | Homo sapiens (Human) |
H0ZAB5 | GALT3_TAEGU | MALKKAPKLFKTFFHWKLWKFSIIVFVFLVFLFLLQREVGVQDFKDEAGIEPVVGKKSHVLGLVLNAMNNIKGAKPKMQIKAPIRQTKVPGERHCLPGHYTPVELKPFLDRPLQDPNAPGASGKAFKTINLNSEEQKEKQAGEEKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKRCPPLPTTSIIIVFHNEAWSTLLRTVHSVMYTSPAILLKEIILVDDASVDEYLHDKLDEYVKQFQIVKVVRQKERKGLITARLLGASVATGETLTFLDAHCECFYGWLEPLLARIAENPVAVVSPDIASIDLNTFEFSKPSPY... | 2.4.1.41 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:31932717}; | protein O-linked glycosylation via threonine [GO:0018243] | Golgi cisterna membrane [GO:0032580] | carbohydrate binding [GO:0030246]; manganese ion binding [GO:0030145]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653] | PF00535;PF00652; | 2.80.10.50; | Glycosyltransferase 2 family, GalNAc-T subfamily | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q14435}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q14435}. Note=Resides preferentially in the trans and medial parts of the Golgi stack. {ECO:0000250|UniProtKB:Q14435}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=170 uM for FGF23 NAPIPRRHTRSAEDDS peptide {ECO:0000269|PubMed:31932717}; | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:31932717). Glycosylates FGF23 (PubMed:31932717). {ECO:0000269|PubMed:31932717}. | Taeniopygia guttata (Zebra finch) (Poephila guttata) |
H1AE14 | LP9D_PHACH | MKAFFAVLAVVSAPFVLGHYTFPDFIEPSGTVTGDWVYVRETQNHYSNGPVTDVTSPEFRCYELDLQNTAGQTQTATVSAGDTVGFKANSAIYHPGYLDVMMSPASPAANSPEAGTGQTWFKIYEEKPQFENGQLVFDTTQQEVTFTIPKSLPSGQYLLRIEQIALHVASSYGGAQFYIGCAQLNVENGGNGTPGPLVSIPGVYTGYEPGILINIYNLPKNFTGYPAPGPAVWQG | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:23525113}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:23525113}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22132148}. | 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:22132148, 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 only C1 oxidation products (PubMed:22132148, PubMed:30238672). Catalysis by LPMOs requires the reduction of the active-site coppe... | Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum) |
H1UBK1 | MAP2_CAEEL | MPPANGKKGKKGGAAKAVRRIQYRPKSFKHSRFVKHAHFWSAAPEEDFDAILAEMQLADAKTAAKEATKKDAKGGKGKANGSAAATAAPEEAKQAWQAEIAAMKPIDEQFPDGKFPHGIDESPYYLKGKDGRVATDRESNEEKKALDISYEEVWQDYRRSAEAHRQVRKYVKSWIKPGMTMIEICERLETTSRRLIKEQGLEAGLAFPTGCSLNHCAAHYTPNAGDTTVLQYGDVCKIDYGIHVRGRLIDSAFTVHFDPKFDPLVEAVREATNAGIKESGIDVRLCDVGEIVEEVMTSHEVELDGKSYVVKPIRNLNGHS... | 3.4.11.18 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000255|RuleBase:RU003653}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000255|RuleBase:RU003653}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03175, ECO:00... | germ cell proliferation [GO:0036093]; proteolysis [GO:0006508] | cytoplasm [GO:0005737] | aminopeptidase activity [GO:0004177]; exopeptidase activity [GO:0008238]; initiator methionyl aminopeptidase activity [GO:0004239]; metal ion binding [GO:0046872]; metalloaminopeptidase activity [GO:0070006]; metalloexopeptidase activity [GO:0008235] | PF00557; | 3.90.230.10;1.10.10.10; | Peptidase M24A family, Methionine aminopeptidase eukaryotic type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255, ECO:0000255|HAMAP-Rule:MF_03175}. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000269|PubMed:15474045}; | null | null | null | null | FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins (PubMed:15474045). The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val) (PubMed:15474045). Required for germ cell proliferation and... | Caenorhabditis elegans |
H1VQB1 | DPCHD_COLHI | MSPAEIIRPAAKVQLMDSKAHGNNHEEIIRAPLNYLLDLPGKEVRSKLMSAFNQWLRIPEEKLEVIKRIVMLLHNASLLLDDIQDSSTLRRGLPVSHSIFGIAQTINAANYAFFLAQQEIPKLEDPRAFEVFTEELLNLHRGQGMDIYWRDASICPTEEEYFTMVSNKTGGLFRLAVRLMQLASESDRDYVPLVNVMGLIFQVRDDYLNLQSTAYTKNKGFGEDLTEGKFSFPIIHSIRSNPSNIQLSSILKQRTTDVDVKLFAVAYIESTGSFEHCRKTLAELMAQAKAIIEGMEGDSSESLSVMNQILTMLGLDGNEV... | 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]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]; terpenoid biosynthetic process [GO:0016114] | 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 | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:32286350}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B (PubMed:32286350). The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA start... | Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose fungus) |
H1ZV37 | GEOB_CASD6 | MTIDHQHIFVGGQWIAPKSTQRSNILNASTEELVGSVPKCNNEDMDRAVAAAREAMRSLAWAGLDGKGRAQHLRRFADAVERRGQQLARSVSLQNGMPINVADQLESAFVVSLLRYYASLAENLVEEEARPSPTGSTTLVRRDPVGVVGAIIPWNFPVALSIFKIAPALAAGCAVVVKPSSGTVLDSYVLAEAAAEAGLPPGVINWVPGDRGIGSHLVSHPGVDKVAFTGSTSAGRIIAEACARLLRPVTLELGGKSAAIVLEDADLDALIRSLPMSSVLNNGQACFSCTRILAPAGRYDEVVDAIAGAVSAYSVGDALD... | 1.2.1.86 | null | cellular response to organic substance [GO:0071310]; monoterpene catabolic process [GO:0043694]; monoterpenoid metabolic process [GO:0016098] | null | geranial dehydrogenase activity [GO:0034832]; NAD binding [GO:0051287] | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E)-geranial + H2O + NAD(+) = geranate + 2 H(+) + NADH; Xref=Rhea:RHEA:34351, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16980, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67260; EC=1.2.1.86; Evidence={ECO:0000269|PubMed:22286981}; PhysiologicalDirection=left-to-right; Xref=Rh... | null | PATHWAY: Terpene metabolism; monoterpene degradation. {ECO:0000269|PubMed:22286981, ECO:0000269|PubMed:24952578}. | null | null | FUNCTION: Involved in the degradation of the monoterpenes beta-myrcene and limonene (PubMed:22286981, PubMed:24952578). During anaerobic degradation of beta-myrcene, catalyzes the NAD(+)-dependent oxidation of geranial to geranic acid (PubMed:22286981). Seems to be specific for the trans-isomer geranial, since it does ... | Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen) (Alcaligenes defragrans) |
H1ZV38 | GEOA_CASD6 | MNDTQDFISAQAAVLRQVGGPLAVEPVRISMPKGDEVLIRIAGVGVCHTDLVCRDGFPVPLPIVLGHEGSGTVEAVGEQVRTLKPGDRVVLSFNSCGHCGNCHDGHPSNCLQMLPLNFGGAQRVDGGQVLDGAGHPVQSMFFGQSSFGTHAVAREINAVKVGDDLPLELLGPLGCGIQTGAGAAINSLGIGPGQSLAIFGGGGVGLSALLGARAVGADRVVVIEPNAARRALALELGASHALDPHAEGDLVAAIKAATGGGATHSLDTTGLPPVIGSAIACTLPGGTVGMVGLPAPDAPVPATLLDLLSKSVTLRPITEG... | 1.1.1.144; 1.1.1.347 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P11766}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766}; | cellular response to organic substance [GO:0071310]; monoterpene catabolic process [GO:0043694]; monoterpenoid metabolic process [GO:0016098] | null | alcohol dehydrogenase (NAD+) activity [GO:0004022]; NAD binding [GO:0051287]; perillyl-alcohol dehydrogenase activity [GO:0018457]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E)-geraniol + NAD(+) = (2E)-geranial + H(+) + NADH; Xref=Rhea:RHEA:34347, ChEBI:CHEBI:15378, ChEBI:CHEBI:16980, ChEBI:CHEBI:17447, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.347; Evidence={ECO:0000269|PubMed:22286981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34348; Eviden... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for geraniol {ECO:0000269|PubMed:22286981}; KM=7 uM for (S)-perillyl alcohol {ECO:0000269|PubMed:22286981}; KM=45 uM for nerol {ECO:0000269|PubMed:22286981}; KM=86 uM for citronellol {ECO:0000269|PubMed:22286981}; KM=21 uM for cumic alcohol {ECO:0000269|PubMed... | PATHWAY: Terpene metabolism; monoterpene degradation. {ECO:0000269|PubMed:22286981, ECO:0000269|PubMed:24952578}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4. {ECO:0000269|PubMed:22286981}; | null | FUNCTION: Involved in the degradation of the monoterpenes beta-myrcene and limonene (PubMed:22286981, PubMed:24952578). During anaerobic degradation of beta-myrcene, catalyzes the NAD(+)-dependent oxidation of geraniol to geranial (PubMed:22286981). Can also catalyze the oxidation of (S)-perillyl alcohol to perillyl al... | Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen) (Alcaligenes defragrans) |
H2AM12 | GP_SBVBH | MLLNIVLISNLACLAFALPLKEGTRGSRCFLNGELVKTVNTSKVVSECCVKDDISIIKSNAEHYKSGDRLAAVIKYYRLYQVKDWHSCNPIYDDHGSFMILDIDNTGTLIPKMHTCRVECEIALNKDTGEVILNSYRINHYRISGTMHVSGWFKNKIEIPLENTCESIEVTCGLKTLNFHACFHTHKSCTRYFKGSILPELMIESFCTNLELILLVTFILVGSVMMMILTKTYIVYVFIPIFYPFVKLYAYMYNKYFKLCKNCLLAVHPFTNCPSTCICGMIYTTTESLKLHRMCNNCSGYKALPKTRKLCKSKISNIVL... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; modulation by virus of host process [GO:0019048]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; virion membrane [GO:0055036] | null | PF03557;PF03563; | null | Nairovirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavage by host MBTPS1/S1P/SKI-1 endopeptidase yield glycoprotein N. Specific enzymatic cleavages by host furin-like protease and MBTPS1/S1P endopeptidase yield GP38. {ECO:0000250|UniProtKB:Q8JSZ3}.; PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}.... | SUBCELLULAR LOCATION: [Envelopment polyprotein]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8JSZ3}.; SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8JSZ3}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:Q... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion (By similarity). Glycoprotein N probably locks the Gn-Gc complex in a prefusion state (By similarity). Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptor... | Bovine Schmallenberg virus (isolate Bovine/BH80/Germany/2011) (SBV) |
H2B3G5 | LI601_CANLF | MKLLLLCLGLILVHAHEEENDVVKGNFDISKISGDWYSILLASDIKEKIEENGSMRVFVKDIEVLSNSSLIFTMHTKVNGKCTKISLICNKTEKDGEYDVVHDGYNLFRIIETAYEDYIIFHLNNVNQEQEFQLMELYGRKPDVSPKVKEKFVRYCQGMEIPKENILDLTQVDRCLQARQSEAAQVSSAE | null | null | null | extracellular region [GO:0005576]; extracellular space [GO:0005615] | odorant binding [GO:0005549]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23464525, ECO:0000305|PubMed:22515174}. | null | null | null | null | null | null | Canis lupus familiaris (Dog) (Canis familiaris) |
H2DF87 | RHVI1_ROSHC | MDTSTSAYAPLPGEDPLFSGHPPASLRRSWKGFAVIFASVLFLLSLVGLIIHQGPQQPPDVMPDKQDEHHHPQSTTPASETTASWEPRGKALGVSAKSNPPVSDELSYNWTNAMFSWQRTAFHFQPERNWMNDPNGPLFYKGWYHLFYQYNPDSAIWGNITWGHAVSTDLIHWLYLPIAMVADQWYDANGVWSGSATLLPDGQIVMLYTGDTVDAVQVVCLAHPANLSDPLLLDWVKYSGNPVLTPPPGILTTDFRDPTTAWTGPDGKWRITIGSKVNTTGISFVYHTEDFKTYNMSKGVLHAVPGTGMWECIDFYPVAI... | 3.2.1.26 | null | carbohydrate metabolic process [GO:0005975] | membrane [GO:0016020]; vacuolar lumen [GO:0005775] | beta-fructofuranosidase activity [GO:0004564] | PF00251;PF11837; | null | Glycosyl hydrolase 32 family | PTM: Glycosylated. {ECO:0000269|PubMed:27083698}. | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27083698}; Single-pass type II membrane protein {ECO:0000255}. Vacuole lumen {ECO:0000250|UniProtKB:Q39041}. Note=May be released into the lumen of the vacuole from the tonoplast through a proteolytic processing. {ECO:0000250|UniProtKB:Q39041}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.; EC=3.2.1.26; Evidence={ECO:0000269|PubMed:22505690}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:27083698}; | null | FUNCTION: Acidic vacuolar invertase involved in light-induced bud burst (PubMed:22505690, PubMed:27083698). {ECO:0000269|PubMed:22505690, ECO:0000269|PubMed:27083698}. | Rosa hybrid cultivar |
H2E7Q8 | POPB_GALM3 | MSSVTWAPGNYPSTRRSDHVDTYQSASKGEVPVPDPYQWLEESTDEVDKWTTAQADLAQSYLDQNADIQKLAEKFRASRNYAKFSAPTLLDDGHWYWFYNRGLQSQSVLYRSKEPALPDFSKGDDNVGDVFFDPNVLAADGSAGMVLCKFSPDGKFFAYAVSHLGGDYSTIYVRSTSSPLSQASVAQGVDGRLSDEVKWFKFSTIIWTKDSKGFLYQRYPARERHEGTRSDRNAMMCYHKVGTTQEEDIIVYQDNEHPEWIYGADTSEDGKYLYLYQFKDTSKKNLLWVAELDEDGVKSGIHWRKVVNEYAADYNIITNH... | 3.4.21.26 | null | proteolysis [GO:0006508] | cytosol [GO:0005829] | oligopeptidase activity [GO:0070012]; serine-type endopeptidase activity [GO:0004252] | PF00326;PF02897; | 3.40.50.1820;2.130.10.120; | Peptidase S9A family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000269|PubMed:28866879, ECO:0000269|PubMed:29051530}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23 uM for the full alpha-amanitin 35mer proprotein {ECO:0000269|PubMed:29051530}; KM=51 uM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=19 uM for the 25mer LWGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=8 uM for the 25mer I... | null | null | null | FUNCTION: Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-ter... | Galerina marginata (strain CBS 339.88) |
H2ELN1 | TER_NICLA | RRSGNYQPTMWDFEYIQSIHNDYAGDKYMKRFNELKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLLREHGFHISQEIFDGLSETHTKDTKGMLYLYEASFLATEGESELEQAWTEKHLREYLKNKNIDQNVAKLVHRALELPLHWRMLRLEARWFISFYKKRQDMIPLLLELAILDFNIVQAAHIQDLKYVARWWKETGLAENLPFARDRLVENFFWTIGVNFLPQYGYSRRIETKVNALVTAIDDVYDVFGTLDELQCFTDAIQRWNTDELDNLPDNMKMCYFAL... | 4.2.3.-; 4.2.3.108; 4.2.3.111; 4.2.3.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | alpha-pinene biosynthetic process [GO:0046248]; circadian rhythm [GO:0007623]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; limonene biosynthetic process [GO:0046250]; terpenoid biosynthetic process [GO:0016114] | chloroplast [GO:0009507] | 1,8-cineole synthase activity [GO:0102313]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; pinene synthase activity [GO:0050550]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol + diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.111; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552; Evidence={ECO... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21527560}. | null | null | FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent (PubMed:21527560). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-terpineol and, as minor products, sabinene, beta-myrcene, limon... | Nicotiana langsdorffii (Langsdorff's tobacco) |
H2EQR6 | DSG21_DANRE | MARRISPVVAFLLCFGLSHFFEAEARLQHSVALHRQKREWIVPPQILEENVDYTKKDFIAKIRSDKEVAHMKYLRYSLRGVGADQEPFNLFVVNPETGYVRITGILDRESISQYNLSGIALFTDGSIAENDIGLRIKVKDQNDNAPVFGVMNPGAVDELSAVGTEVMRLNCFDADEPGNPNSQIKYEIVDQQPAGQSMFTVENNRRVVVANPNLDRETVDQYVLLVKASDLNGAPGGNAATGTVTIKINDVNDNVPTLGGPYEASIEENTEKVEVMRLKVSDLHLKGTDNWEGDCYIASGNEAGYFSIHMDPKTNEAVLM... | null | null | convergent extension involved in gastrulation [GO:0060027]; desmosome assembly [GO:0002159]; epiboly involved in gastrulation with mouth forming second [GO:0055113]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156] | desmosome [GO:0030057]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509] | PF01049;PF00028; | 2.60.40.60;4.10.900.10; | null | null | SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250|UniProtKB:Q14126}. Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion (By similarity). Required for embryogenesis, specifically for progression of epiboly and normal convergence-extension movements during gastrulation (PubMed:222... | Danio rerio (Zebrafish) (Brachydanio rerio) |
H2FH31 | LEC_CREGR | MTTFLIKHKASGKFLHPYGGSSNPANNTKLVLHSDIHERMYFQFDVVDERWGYIKHVASGKIVHPYGGQANPPNETNMVLHQDRHDRALFAMDFFNDNIMHKGGKYIHPKGGSPNPPNNTETVIHGDKHAAMEFIFVSPKNKDKRVLVYA | null | null | null | null | carbohydrate binding [GO:0030246] | null | 2.80.10.50; | null | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8-10 for the hemagglutinating activity of the human erythrocytes. {ECO:0000269|PubMed:9568372}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Hemagglutinating activity of the human erythrocytes is fully maintained after heating at 50 degrees Celsius for 3 hours. The activity is partially lost after heating at 55 degrees Celsius and completely lost after heating at 65 degrees Celsius for 30 minutes. {ECO... | FUNCTION: Galactose-binding lectin (PubMed:23886951, PubMed:27010847, PubMed:28636877, PubMed:9568372). Binds both alpha and beta anomer of galactose (Gal), but has a stronger interaction with the glycans having alpha Gal at the non-reducing end and binds beta Gal weakly only in highly branched glycans. Has high affini... | Crenomytilus grayanus (Gray mussel) (Mytilus grayanus) |
H2KY84 | CMTA1_CAEEL | MNNSVTRLLFKRLLTLQLCHHFDIIPHRDQSFDCVQMQQPQNETANNFIPSIQLLWSTDPPQIRPDGTYPQAVELFPCFKDKWNTKEEILNIILAANADPKSNCVTVQSSPRPCSSSQFIYPRLDNAWYKNDGYIWKKRTNGKQNREDHLNLKISGHPHISAKYIHSAIVPTFHRRSYSVPDSDCHVLVHYLNVKTNNKIDDQAEEIARSMIENKVFISLSQLHDQLSPIFLQTLNVNQLVAEINEHLKKKGVNLPTSPLPQEPSSSTSRELERRNSCSSAFRKGLSSVALRRQPSANSEIDANHIGTMLKRFGCNGSSS... | null | null | positive chemotaxis [GO:0050918]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to oxygen levels [GO:0070482] | chromatin [GO:0000785]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; transcription coregulator activity [GO:0003712] | PF03859; | 1.20.5.190;1.25.40.20;2.60.40.10; | CAMTA family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:34499028}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:34499028). Positively modulates neuronal levels of the ubiquitous Ca2+ sensor calmodulin/cmd-1, probably by direct binding to the cmd-1 promoter, thereby regulating Ca2+ signaling, physiology, and behavior (PubMed:34499028). {ECO:0000269|PubMed:34499028}. | Caenorhabditis elegans |
H2KY86 | HELQ_CAEEL | MNRTPIRRCKSAEIEEDPFSPIPKFSRLRTPRTSREYVCPLKSTSPQSPSSSTENEPPPVSVTSPPARKRALEESTVTPIQQKIGPPVLKRSSLSKLADGFRTAAYLNNESENDDDPFGLSFRNEQVLMSKCAPAPEKRPETLTLDPSKCLPERDMEMYRKIKKLDKFYDWQQECLSDKRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISALAPFEDAFGINIEEYASNKGRFPPIKRRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKG... | 3.6.4.12 | null | DNA double-strand break processing involved in repair via single-strand annealing [GO:0010792]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; resolution of meiotic recombination intermediates [GO:00007... | chromosome [GO:0005694]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATPase binding [GO:0051117]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787]; single-stranded DNA helicase activity [GO:0017116] | PF00270;PF00271;PF20470;PF21099; | 1.10.3380.20;3.40.50.300; | Helicase family, SKI2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TDG4}. Chromosome {ECO:0000250|UniProtKB:Q8TDG4}. Note=Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:Q8TDG4}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q8TDG4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|U... | null | null | null | null | FUNCTION: Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair (PubMed:18472307, PubMed:34880204). Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated ... | Caenorhabditis elegans |
H2KYH3 | RING2_CAEEL | MDDSPGPSTSKSARDKAENAEENTSDSSSDSEVSSASEKSEESRPSSEKKKVITRVIPVRPPTRDKGHRVNLLESGNESETKSLYQRAKEGIPSYKGKPEIKLPTTSEQYYDLEEVLMNPARMEGRELTLNAYDAVRNKYNVLPGKSVCEADLQKVIGSFSCDVCQELIQGSIMTKKCGHRFCDQCILVAFMRSGNTCPTCRQNLGSKRELQQDPRFDQLIYQVVESRSIVGRMMAENREHEKDVYFGRKGYIEGGSDWNKRYGIDPNSKLKAPRPLKSAGRKKIRWFHESDEDGSVRKVMESKKGAPKEDDTNYLENDK... | 2.3.2.27 | null | negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of vulval development [GO:0040027]; nematode male tail tip morphogenesis [GO:0045138]; protein ubiquitination [GO:0016567]; regulation of cell migration [GO:0030334]; reproduction [GO:0000003] | PcG protein complex [GO:0031519]; ubiquitin ligase complex [GO:0000151] | chromatin binding [GO:0003682]; histone ubiquitin ligase activity [GO:0140852]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF13923; | 3.30.40.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q99496}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q99496}. | null | null | FUNCTION: E3 ubiquitin-protein ligase playing a central role in histone code and gene regulation (By similarity). Involved in ubiquitination of histone H2A (PubMed:19211678). Plays a role in the formation of the male-specific genital sensilla (simple sense organs) known as rays (PubMed:19211678). Required for normal mi... | Caenorhabditis elegans |
H2KYH4 | HAM2_CAEEL | MPYRAELKRPDLKGSFPCSICQKVFCHSSSLSRHRMQAHFKSYTCTTCNNEIPSNDTLRSHMYRVHNITRMFMCRCCNWAFPDKTSLHIHMQSMLKNGTPGEAAVLAKSSDVVDSTSESGSPRQSPPFSPDLLMQKRMLQVAANNNNIGSIFPTLLKSPDSKSMFPLDLSNMGPSQFLSAWLANNPINTAALNLAAQQTPSKDSIQSSNISDYDDLEVQTTEEDIKFEVESSDVSPRSVIVKTEPTFKRELEHDADIDVEGDDGEPPLKMTIDDKNIHISHDQPSPTVSDSHISGGSSSHSGESLKCFDCQVARGKLVAV... | null | null | cell fate determination [GO:0001709]; cell migration [GO:0016477]; regulation of DNA-templated transcription [GO:0006355]; regulation of neuron differentiation [GO:0045664]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565] | PF00096; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10049362}. | null | null | null | null | null | FUNCTION: Probable transcription factor that acts downstream of egl-15, to promote migration of the HSN motor neurons from the tail to the gonad primordium during HSN cell differentiation (PubMed:10049362). {ECO:0000269|PubMed:10049362}. | Caenorhabditis elegans |
H2KYJ8 | NHR66_CAEEL | MPPINEPTATTTSASSVWQGMTQLKSQVDLINIARGILSTPATTSTSCLDIQNSTPIIGSLASGKSQTPILTATMTPQIGLTGLGSLTSLPPELLLQFARLDGFNLLPAVGSPAIPSSSSCSEPSTSQASTVVSAPTLPPPSPLTSLPQKPAPLMPSGHVTTVDQQNRQQHQQQQRQQQQAQQQNSMARKYSMDTIQHHTMQHPHQLQYIPNHFMTASTDVFAAMDMSQKQSSPPGIFKIVAAKNEPSSSSNSQPGTPAMGDRRAVPACAICGTDSTGIHFGVDACAACSAFFRRTVVLNKDYSCNKGGKCTVVKDGSAG... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122] | nucleus [GO:0005634] | DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU004334}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:33259792). Binds to regulatory elements and regulates transcription of target genes, including the potassium channel accessory subunit mps-2 (PubMed:33259792). Negatively regulates transcription of mps-2, thereby modulating age-dependent memory decline (PubMed:33259792). In concer... | Caenorhabditis elegans |
H2KYQ5 | GYG1_CAEEL | MSEAWITLATNDNYAQGALVLVHSLRTAGTTRKIHCLISNEVSAPVRKQLEEHFDDVSIVDVFNSNDSDNLRLIERPDLGVTFTKLHCWRLTQYTKCVFLDADTLVLRNADELFTRPDFSAASDIGWPDSFNSGVFVYVPNNETYRQLVDFAVTHGSYDGGDQGLLNDFFSNWRDLPSEHRLPFIYNMTAGAFYTYAAAYKRYGANTKIVHFIGSVKPWHGSAAVHTGEHFQQWQKIYHAHVNHTSRTNEHAAVFPSHHHTPEHRSHSADHPKIERKDSIVREIGNFVMHVVQSVNILPSYDTDANTSDSHRNNEPHKHD... | 2.4.1.186 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P13280}; Note=Divalent metal ions. Required for self-glucosylation. Manganese is the most effective. {ECO:0000250|UniProtKB:P13280}; | glycogen biosynthetic process [GO:0005978] | cytoplasm [GO:0005737]; striated muscle dense body [GO:0055120] | glycogenin glucosyltransferase activity [GO:0008466]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity [GO:0102751] | PF01501; | null | Glycosyltransferase 8 family, Glycogenin subfamily | PTM: Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-194. {ECO:0000250|UniProtKB:P13280}. | null | CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360, Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140573; EC=2.4.1.186; Evidence={ECO:... | null | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:24982189}. | null | null | FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for gsy-1. {ECO:0000269|PubMed:24982189}. | Caenorhabditis elegans |
H2KYS3 | DAF9_CAEEL | MHLENRVLSSVLDYASKFYKRMSSLVFFSANSIQVQMNISQSSWIKCRDWMAFALSHHIIMGIYLLILRNFLPQVVPDFEWQHYFMRVFIVHIIYIIISYFIRITRYPPGPPPMAVFGNSPFVNILTPEQTFLEYREIYGPIFTLHLSQPTIILAEYKTIQEALVKNGQQTSGRSSAESFVLFTGDRLNGDGVILAMRQKWKDMRHEISRFMNKWYGAPMDELVLHHTRCLEQELAKIAETKSLIDLRDPLAGAIANVIQQITIGRNYMYQDQEFQTQLRDINAVVKEIMTAEVFFVNCYPWLRYLPEGILRKWTNYKRS... | 1.14.14.- | null | cell-cell signaling [GO:0007267]; cholesterol metabolic process [GO:0008203]; dauer larval development [GO:0040024]; organic acid metabolic process [GO:0006082]; regulation of cell migration [GO:0030334]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]; steroid hydroxylase activity [GO:0008395] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to dendrite-like structure in XXXL/R cells. {ECO:0000269|PubMed:12783794}. | CATALYTIC ACTIVITY: Reaction=5alpha-cholest-7-en-3-one + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = (25S)-Delta7-dafachronate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66620, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, Ch... | null | PATHWAY: Steroid hormone biosynthesis; dafachronic acid biosynthesis. {ECO:0000269|PubMed:16529801, ECO:0000269|PubMed:22505847}. | null | null | FUNCTION: Converts the 3-keto steroids 4-cholesten-3-one and lathosterone into the carboxylic metabolites 3-keto-4-cholestenate (Delta(4)-dafachronic acid, Delta(4)-DA) and 3-keto-7,(5a)-cholestenate (Delta(7)-dafachronic acid, Delta(7)-DA) respectively, by catalyzing successive oxidations at C-26 (PubMed:16529801, Pub... | Caenorhabditis elegans |
H2KYS8 | CPNA1_CAEEL | MVFDARLGYDPDEWEECPEPEHFLVFSGFTRYMLTFAAIAFVYYFFKLLDDKNKKESGEKEEPQTSVESVLAKAGDKLHDVKEQVQQHIPESAEELMREADQYLKEQAHSVQNNVHQFAEQAANKFPSLEVDLNLGHPIDATREKFDTVLSSVNNHLHETKNMDLSPTSRDSTQFEQIPSIAPEESAFGHDFEHVPPHLKTAAEQYYAQQHQPPPVPQHKIVQPVPISPTDQQLLHEFDIYDAPAHQRMNQISEQLGQLGQKTPAQLQQLQHAQLAHQQLQQQGVFQPIQQPSPLQIQTHPQQPYFDFSQLSPASQARYN... | null | null | positive regulation of sarcomere organization [GO:0060298]; protein ubiquitination [GO:0016567] | basal plasma membrane [GO:0009925]; M band [GO:0031430]; nucleus [GO:0005634]; striated muscle dense body [GO:0055120] | phosphatase binding [GO:0019902]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin-protein transferase activity [GO:0004842] | PF07002; | null | Copine family | null | SUBCELLULAR LOCATION: Basal cell membrane {ECO:0000269|PubMed:23283987}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:23283987}. Note=Colocalizes with unc-89, unc-112, pat-3 and pat-6 at the M-line and with alpha-actinin, unc-112, pat-3 and pat-6 in dens... | null | null | null | null | null | FUNCTION: Involved in the assembly of dense bodies and M lines during body wall muscle development. Acts by recruiting downstream of integrin-associated protein pat-6/actopaxin several dense bodies and M line components including unc-89, lim-9, scpl-1 and unc-96 to integrin-mediated attachment sites. {ECO:0000269|PubMe... | Caenorhabditis elegans |
H2KYU6 | NPL41_CAEEL | MVLEVPQTERVNDVDVFLSTQDGQIQRPKGPNCRHPVRQKCTNCLPVDPFDEEYLKEKDIKHMSFHAHVRKLLGSQGKGTTLKKPLENFRCSLKPNCDAHKPFPKGICTKCKPQVVTLNRQKFRHVDNIQIENQELVNQFLDYWRLSGHQRVGFLIGQYQPHLEVPLGIKATVAAIYEPPQHCREDGIEFLEDKNQKTIDNLLEMLGLQRVGWIFTDCWTANSAEGTVHYTRHKDSFFLSAEECITAAMLQNQHPNITEYSMDRHYGSKFVTVVASGDESMHVNFHGYQVSNQCAAMVEADILCPTLYTPELAYVRETPL... | null | null | positive regulation of protein localization to nucleus [GO:1900182]; ubiquitin-dependent protein catabolic process [GO:0006511] | nucleus [GO:0005634]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098] | metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625] | PF05021;PF05020; | 3.40.140.10; | NPL4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18728180}. Nucleus {ECO:0000269|PubMed:18728180}. Note=Localizes to the cytoplasm during mitosis. Nuclear localization upon nuclear membrane re-assembly is cdc-48-dependent. {ECO:0000269|PubMed:18728180}. | null | null | null | null | null | FUNCTION: In association with ufd-1 and ATPase cdc-48.1 and/or cdc-48.2, involved in the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:16647269, PubMed:22768338). This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfol... | Caenorhabditis elegans |
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