Datasets:
lhallee
/
exp_new_unprocessed

Dataset card Data Studio Files
xet
 Community
1
Entry
stringlengths
6
10
Sequence
stringlengths
6
35.2k
Organism
stringlengths
9
169
Function [CC]
stringlengths
24
15.3k
⌀
EC number
stringlengths
7
118
⌀
Catalytic activity
stringlengths
65
35.7k
⌀
Cofactor
stringlengths
43
1.77k
⌀
Kinetics
stringlengths
70
10.8k
⌀
Pathway
stringlengths
27
1.13k
⌀
pH dependence
stringlengths
64
855
⌀
Temperature dependence
stringlengths
70
709
⌀
Keywords
stringlengths
3
1.61k
⌀
Gene Ontology (biological process)
stringlengths
19
11.3k
⌀
Gene Ontology (cellular component)
stringlengths
17
1.47k
⌀
Gene Ontology (molecular function)
stringlengths
24
2.21k
⌀
Subcellular location [CC]
stringlengths
30
5.42k
⌀
Post-translational modification
stringlengths
16
6.52k
⌀
Domain [CC]
stringlengths
33
6.72k
⌀
InterPro
stringlengths
10
810
⌀
Gene3D
stringlengths
10
250
⌀
A0A0H3JUU7
MRQWTAIHLAKLARKASRAVGKRGTDLPGQIARKVDTDVLRKLAEQVDDIVFISGTNGKTTTSNLIGHTLKANNIQIIHNNEGANMAAGITSAFIMQSTPKTKIAVIEIDEGSIPRVLKEVTPSMMVFTNFFRDQMDRFGEIDIMVNNIAETISNKGIKLLLNADDPFVSRLKIASDTIVYYGMKAHAHEFEQSTMNESRYCPNCGRLLQYDYIHYNQIGHYHCQCGFKREQAKYEISSFDVAPFLYLNINDEKYDMKIAGDFNAYNALAAYTVLRELGLNEQTIKNGFETYTSDNGRMQYFKKERKEAMINLAKNPAGM...
Staphylococcus aureus (strain N315)
FUNCTION: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide (PubMed:22291598, PubMed:30154570). The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue (PubMed:222...
6.3.5.13
CATALYTIC ACTIVITY: Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + L-glutamate + phosph...
null
null
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:22291598}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-7.8 for isoglutaminyl synthase activity. {ECO:0000269|PubMed:22291598};
null
3D-structure;ATP-binding;Cell shape;Cell wall biogenesis/degradation;Ligase;Metal-binding;Nucleotide-binding;Peptidoglycan synthesis;Zinc
cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]
null
acid-amino acid ligase activity [GO:0016881]; ATP binding [GO:0005524]; carbon-nitrogen ligase activity on lipid II [GO:0140282]; zinc ion binding [GO:0008270]
null
null
DOMAIN: Composed of two domains: a Mur ligase middle domain containing the canonical ATP binding site and a ribbon-type zinc finger, and a C-terminal Mur ligase domain. The GatD/MurT complex has an open, boomerang-shaped conformation in which GatD is docked onto one end of MurT. Both proteins contribute to the catalyti...
IPR043703;IPR036565;IPR013221;IPR013564;
3.40.1190.10;
A0A0H3KB22
MTYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDTDFVGTDGENGGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQPLVDALHAAGFGIAIETNGSLPVLESIDWICVSPKADAPLVVTKGNELKVVIPQDNQRLADYAKLDFEYFLVQPMDGPSRDLNTKLAIDWCKRHPQWRLSMQTHKYLNIP
Burkholderia multivorans (strain ATCC 17616 / 249)
FUNCTION: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}.
4.3.99.3
CATALYTIC ACTIVITY: Reaction=6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-deazaguanine + NH4(+); Xref=Rhea:RHEA:27974, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:61032, ChEBI:CHEBI:61036; EC=4.3.99.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703};
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}; COFACT...
null
PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000305|PubMed:24362703}.
null
null
3D-structure;4Fe-4S;Iron;Iron-sulfur;Lyase;Magnesium;Metal-binding;Queuosine biosynthesis;Reference proteome;S-adenosyl-L-methionine
queuosine biosynthetic process [GO:0008616]
null
4 iron, 4 sulfur cluster binding [GO:0051539]; carbon-nitrogen lyase activity [GO:0016840]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; S-adenosyl-L-methionine binding [GO:1904047]
null
null
null
IPR024924;IPR013785;IPR030977;IPR007197;
3.20.20.70;
A0A0H3LCC3
MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKGAKEVETKEQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDPERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIGAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLTLENADLSLLGKARK...
Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000256|HAMAP-Rule:...
5.6.1.7
CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00600};
null
null
null
null
null
ATP-binding;Chaperone;Coiled coil;Cytoplasm;Isomerase;Nucleotide-binding;Reference proteome
adhesion of symbiont to host [GO:0044406]; chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activ...
capsule [GO:0042603]; cell surface [GO:0009986]; GroEL-GroES complex [GO:1990220]; host cell surface [GO:0044228]
ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; host cell surface binding [GO:0046812]; isomerase activity [GO:0016853]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}. Secreted, capsule {ECO:0000256|ARBA:ARBA00025702}. Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
null
null
IPR018370;IPR001844;IPR002423;IPR027409;IPR027413;IPR027410;
3.50.7.10;1.10.560.10;3.30.260.10;
A0A0H3LHU4
MTEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGLAFDGSSIRGFQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEPYSRDPRNIARKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGSFYEVDAISGWWNTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDKMLTNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKNTAWQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDTARHYIGGLLHHAPSLLAFT...
Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
null
6.3.1.2
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000256|ARBA:ARBA00000777, ECO:0000256|Rul...
null
null
null
null
null
ATP-binding;Cytoplasm;Ligase;Magnesium;Nucleotide-binding;Phosphoprotein;Reference proteome
glutamine biosynthetic process [GO:0006542]; nitrogen utilization [GO:0019740]; protein homooligomerization [GO:0051260]
cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]
ADP binding [GO:0043531]; ATP binding [GO:0005524]; cobalt ion binding [GO:0050897]; GDP binding [GO:0019003]; glutamine synthetase activity [GO:0004356]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU000387}.
null
null
IPR008147;IPR036651;IPR014746;IPR008146;IPR027303;IPR004809;IPR001637;IPR027302;
3.10.20.70;3.30.590.10;
A0A0H3NK84
MIPPLNRYVPALSKNELVKTVTNRDIQFTSFNGKDYPLCFLDEKTPLLFQWFERNPARFGKNDIPIINTEKNPYLNNIIKAATIEKERLIGIFVDGDFFPGQKDAFSKLEYDYENIKVIYRNDIDFSMYDKKLSEIYMENISKQESMPEEKRDCHLLQLLKKELSDIQEGNDSLIKSYLLDKGHGWFDFYRNMAMLKAGQLFLEADKVGCYDLSTNSGCIYLDADMIITEKLGGIYIPDGIAVHVERIDGRASMENGIIAVDRNNHPALLAGLEIMHTKFDADPYSDGVCNGIRKHFNYSLNEDYNSFCDFIEFKHDNII...
Salmonella typhimurium (strain SL1344)
FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:30327479, PubMed:32766249). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the...
2.4.1.-
CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP; Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322...
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:30327479};
null
null
null
null
3D-structure;Glycoprotein;Glycosyltransferase;Host cytoplasm;Manganese;Metal-binding;Secreted;Toxin;Transferase;Virulence
null
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell cytosol [GO:0044164]
manganese ion binding [GO:0030145]; protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362]; toxin activity [GO:0090729]
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9L9J3}. Host cytoplasm, host cytosol {ECO:0000305|PubMed:32432056}. Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS). {ECO:0000250|UniProtKB:Q9L9J3}.
PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins. {ECO:0000269|PubMed:32432056}.
DOMAIN: Adopts a GT-A fold and acts as an inverting enzyme that converts the alpha-configuration in the UDP-N-acetyl-alpha-D-glucosamine donor to the beta configuration in the N-linked (GlcNAc) arginine product. {ECO:0000269|PubMed:30327479, ECO:0000269|PubMed:30463645}.
null
null
A0A0H3PEK7
MRFDFFVSKRLNISRNKALELIENEEVLLNGKSFKASFDVKNFLENLKKTQDLNPEDILLTDGLKLDLLSEIYVSRAALKLKNFLEENGIEIKHKNCLDIGSSTGGFVQILLENQALKITALDVGNNQLHLSLRTNEKIILHENTDLRTFKSEEKFELITCDVSFISLINLLYYIDNLALKEIILLFKPQFEVGKNIKRDKKGVLKDDKAILKARMDFEKACAKLGWLLKNTQKSSIKGKEGNVEYFYYYIKN
Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C1920 in 23S rRNA (PubMed:24796671, PubMed:29404277). Enhances motility (PubMed:24796671, PubMed:29404277, PubMed:32134554). Enhances biofilm formation (PubMed:29404277, PubMed:32134554). Involved in the assembly of 70S ribosomes (PubMed:24796671). Involved in viru...
2.1.1.226
CATALYTIC ACTIVITY: Reaction=cytidine(1920) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1920) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43200, Rhea:RHEA-COMP:10403, Rhea:RHEA-COMP:10404, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; E...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.8 uM for 50S ribosomal subunit (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:24796671}; KM=5.8 uM for S-adenosyl-L-methionine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:24796671}; Note=kcat is 0.0048 min(-1) for 50S ribosomal subunit. kcat is...
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: High methylation activity of the 50S ribosomal subunit at 37 degrees Celsius. Loss of activity at 42 degrees Celsius. {ECO:0000269|PubMed:24796671};
Methyltransferase;RNA-binding;rRNA processing;S-adenosyl-L-methionine;Transferase;Virulence
cell motility [GO:0048870]; cellular response to antibiotic [GO:0071236]; cytosolic ribosome assembly [GO:0042256]; rRNA 2'-O-methylation [GO:0000451]; viral process [GO:0016032]
null
RNA binding [GO:0003723]; rRNA methyltransferase activity [GO:0008649]
null
null
null
IPR002877;IPR036986;IPR029063;IPR047048;
3.10.290.10;3.40.50.150;
A0A0J9UVG7
MRLLRPTPRLSSIFSSKTATSNLRFFTAMAPHNDVGAFHEALRSSKRILALCGAGLSASSGLPTFRGAGGLWRNHDATSLATLSAFKNDPGLVWLFYNYRRHMCLRAEPNPAHYALAALAEKNKDFLCLTQNVDNLSQQAGHPQDQLRTLHGSLFDIKCTNCDWIQRGNYDDPFCPALAPASVDVEPGKPFPLLDASLPLDPISPDDIPKCPQCKIGFQRPGVVWFGENLDEVMMMGITNWLLEDKVDLMLVIGTSAQVYPAAGYIDKAKRKGARIAVINPEAENEEEMYKVKPGDFAFGKDAAEYLPLLLEPVIGKLET...
Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)
FUNCTION: NAD-dependent protein-lysine deacylase that decrotonylates the PDC (pyruvate dehydrogenase complex) subunit LAT1 at 'Lys-148' to inhibit PDC activity and consequently ATP production (PubMed:34927582). Also decrotonylates histone H3 crotonylated at 'Lys-18' (H3K18cr), to repress the expression of genes involve...
2.3.1.-; 2.3.1.286
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=...
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9NXA8}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NXA8};
null
null
null
null
Chromatin regulator;Chromosome;Cytoplasm;Metal-binding;Mitochondrion;NAD;Nucleus;Reference proteome;Transferase;Transit peptide;Zinc
negative regulation of cellular respiration [GO:1901856]
chromosome [GO:0005694]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; NAD-dependent histone decrotonylase activity [GO:0160012]; NAD-dependent protein decrotonylase activity [GO:0160011]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuc...
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:34927582}. Cytoplasm, cytosol {ECO:0000269|PubMed:34927582}. Nucleus {ECO:0000269|PubMed:34927582}. Chromosome {ECO:0000269|PubMed:34927582}.
null
null
IPR029035;IPR003000;IPR026591;IPR027546;IPR026590;
3.30.1600.10;3.40.50.1220;
A0A0K0JFP3
MLGLLTITSVFRNWRNSLQRKEDYDECHMRGINNENEISGKSEKNFKLDEPPISLETVMAEFKLSNETLRRMMAHMSRNMDKGLEGGPENSTISMLPSFVPELPNGTEEGRFIAMDLGGTNLRVMLMDIKPGEELKTEQFNTRIPNWAMRGTGEQLFDYITKCLAEFLIEKGIENDGLPVGFTFSYPCDQKSLRSATLLRWTKGFETTGVVGEDVVELLEQSIARRGDIKVEVVALINDTVGTMVAAAHESGGECHIGVIIATGTNASYMEDTSKIKYGLSKAIAAYNYPEMIIDTEWGGFGDRSEADYILTQYDKIVDS...
Brugia malayi (Filarial nematode worm)
FUNCTION: Active against glucose, fructose, mannose, maltose and galactose. {ECO:0000269|PubMed:18499511}.
2.7.1.1
CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000269|PubMed:18499511}; PhysiologicalDirection=left...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.035 mM for glucose {ECO:0000269|PubMed:18499511}; KM=75 mM for fructose {ECO:0000269|PubMed:18499511}; KM=1.09 mM for ATP {ECO:0000269|PubMed:18499511};
PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000269|PubMed:18499511}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000269|PubMed:18499511}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.4. {ECO:0000269|PubMed:18499511};
null
ATP-binding;Glycolysis;Kinase;Nucleotide-binding;Reference proteome;Transferase
glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; hexose metabolic process [GO:0019318]; intracellular glucose homeostasis [GO:0001678]
cytosol [GO:0005829]; mitochondrion [GO:0005739]
ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; mannokinase activity [GO:0019158]
null
null
null
IPR043129;IPR001312;IPR022673;IPR022672;
3.30.420.40;3.40.367.20;
A0A0K0PVW1
MKSELIFLPVPAFGHLVGMVEMAKLFISRHENLSVTVLISKFFIDTGIDNYNKSLLAKPTPRLTIINLPEIDPQKYLLKPRCAIFPSLIENQKTHVRDVMSRMTQSESTRVVGLLADILFVDIFDIADEFNVPTYVYSPAGAGFLGLAFHLQTLNDDKKQDVTEFRNSDTELLVPSFANPVPAEFLPSIFLEKDGRHDVLLSLYWRCREAKGIIVNTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGEGQNSDEAAVILGWLDDQPPSSVVFLCFGSFGSFPENQVKEIAMGLERSGHRFLWSLRPCISEGETTLQLK...
Panax ginseng (Korean ginseng)
FUNCTION: Component of the dammarane-type triterpene saponins (e.g. PPT-type ginsenosides or panaxosides) biosynthetic pathway (PubMed:26032089, PubMed:27746309, PubMed:29378087). Glycosyltransferase that catalyzes the biosynthesis of ginsenoside Rh1 from protopanaxatriol (PPT) and the conversion of ginsenoside F1 to g...
2.4.1.367
CATALYTIC ACTIVITY: Reaction=(20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-ginsenoside C-K + H(+) + UDP; Xref=Rhea:RHEA:57976, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75950, ChEBI:CHEBI:77146; Evidence={ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA...
null
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305}.
null
null
Glycosyltransferase;Hydrolase;Isoprene biosynthesis;Transferase
response to molecule of fungal origin [GO:0002238]; terpenoid biosynthetic process [GO:0016114]
null
hydrolase activity [GO:0016787]; UDP-glycosyltransferase activity [GO:0008194]
null
null
null
IPR002213;IPR035595;
3.40.50.2000;
A0A0K1TQQ0
MAENSILLAVLSLLSACQQSYFALQVGKARLKYKVMPPAVSGSPEFERIFRAQQNSLEFYPVFIITLWVAGWYFNQVFATCLGLVYIYARHRYFWGYSEAPKKRITGFRLSLGVLALLAVLGAVGITNSFLDEYLDLNIAKKLRHF
Sus scrofa (Pig)
FUNCTION: Catalyzes several different glutathione-dependent reactions. Catalyzes the glutathione-dependent reduction of lipid hydroperoxides, such as 5-HPETE. Has glutathione transferase activity, toward xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB). Catalyzes also the conjugation of leukotriene...
1.11.1.-; 2.5.1.18; 4.4.1.20
CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000256|RuleB...
null
null
null
null
null
Endoplasmic reticulum;Leukotriene biosynthesis;Lipid metabolism;Lyase;Membrane;Microsome;Oxidoreductase;Proteomics identification;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix
glutathione biosynthetic process [GO:0006750]; leukotriene biosynthetic process [GO:0019370]; membrane lipid catabolic process [GO:0046466]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]
enzyme activator activity [GO:0008047]; glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; leukotriene-C4 synthase activity [GO:0004464]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369123}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369123}. Microsome membrane {ECO:0000256|RuleBase:RU369123}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369123}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membran...
null
null
IPR001446;IPR023352;IPR001129;
1.20.120.550;
A0A0K3AUJ9
MSLAPKMSKAFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVCPAGWTPGSDTIKPGVKESQEYFKKH
Caenorhabditis elegans
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:15099742). In I2 pharyngeal neurons, required for the inhibition of feeding in response to light and hydrogen peroxide (PubMed:25640076). In the intestine, plays a...
1.11.1.24
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:1...
null
null
null
null
null
Alternative splicing;Antioxidant;Cytoplasm;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome
cell redox homeostasis [GO:0045454]; cellular response to hydrogen peroxide [GO:0070301]; determination of adult lifespan [GO:0008340]; heat acclimation [GO:0010286]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of brood si...
cytoplasm [GO:0005737]; cytosol [GO:0005829]
thioredoxin peroxidase activity [GO:0008379]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19064914}.
PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. {ECO:0000250|UniProtKB:Q06830}.
null
IPR000866;IPR024706;IPR019479;IPR036249;IPR013766;
3.40.30.10;
A0A0K3AV08
MEQASVPSYVNIPPIAKTRSTSHLAPTPEHHRSVSYEDTTTASTSTDSVPEVRIRSESSQVSRESPPIRASKAFVASYEYEAQKDDELNLPLGAIITLVTVETNEDGWYRGELNGKVGLFPSNYAREVTYKDNLVEFKQDEIMLPVAVRTLSDCQIGHGATATVFKMDIKIKKELQNGRMGEAVGDQMKAALKRFNRHASNFRADVVSTDEQLEQLKREANLVNGLSHNNIVRLLGICLEDPYFGLLLELCEGSSLRNVCRNLNSDAAIPLGVLIDWATQVAEGMEYLTKQGYVHRDLKADNVLVKEEVCLCMDEEMFQY...
Caenorhabditis elegans
FUNCTION: Serine/threonine-protein kinase which, by phosphorylating and activating mek-1, plays an important role in the activation of the JNK pathway composed of mlk-1, mek-1 and kgb-1 (PubMed:15116070, PubMed:20008556). Involved in the response to environmental stress such as heavy metals (PubMed:15116070, PubMed:188...
2.7.11.25
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=2.7.11.25; Evidence={ECO:0000269|PubMed:15116070, ECO:00002...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P80192};
null
null
null
null
Alternative splicing;ATP-binding;Coiled coil;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;SH3 domain;Stress response;Transferase;Ubl conjugation
axon regeneration [GO:0031103]; defense response to Gram-negative bacterium [GO:0050829]; determination of adult lifespan [GO:0008340]; JNK cascade [GO:0007254]; MAPK cascade [GO:0000165]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of axon extension involved in regeneration [GO:0048...
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein serine kinase activity [GO:0106310]; receptor tyrosine kinase binding [GO:0030971]; scaffold...
null
PTM: May be phosphorylated on tyrosine residues by svh-2. {ECO:0000269|PubMed:22388962, ECO:0000269|PubMed:27984580}.; PTM: May be ubiquitinated and targeted for proteasomal degradation by E3 ubiquitin ligase rpm-1. {ECO:0000269|PubMed:21670305}.
null
IPR011009;IPR000719;IPR001245;IPR008271;IPR036028;IPR001452;
2.30.30.40;1.10.510.10;
A0A0K8P6T7
MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS
Piscinibacter sakaiensis (Ideonella sakaiensis)
FUNCTION: Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with MHETase to depolymerize PET (PubMed:26965627). Catalyzes the hydrolysis of PET to produce mono...
3.1.1.101
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, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701, ChEBI:CHEBI:131704; EC=3.1.1.101; Evidence={ECO:00002...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.431 mM for pNP-acetate {ECO:0000269|PubMed:30502092}; KM=0.315 mM for pNP-butanoate {ECO:0000269|PubMed:30502092}; KM=0.053 mM for pNP-hexanoate {ECO:0000269|PubMed:30502092}; KM=0.048 mM for pNP-octanoate {ECO:0000269|PubMed:30502092}; KM=2.283 mM for pNP-dodeca...
PATHWAY: Xenobiotic degradation. {ECO:0000305|PubMed:26965627}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9 for PET film hydrolysis (PubMed:26965627). Optimum pH is 9 for PET (commercial drinking bottle) hydrolysis. Optimum pH is 6.5-8.0 for BHET hydrolysis (PubMed:29603535). Optimum pH is 8.0 for the hydrolysis of pNP-esters. The enzyme is active at pH 6-10, has...
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius for PET film hydrolysis (PubMed:26965627). Optimum temperature is 30 degrees Celsius for PET (commercial drinking bottle) hydrolysis and BHET hydrolysis (PubMed:29603535). Optimum temperature is 35-45 degrees Celsius for t...
3D-structure;Disulfide bond;Hydrolase;Reference proteome;Secreted;Serine esterase;Signal
cellular response to organic substance [GO:0071310]; xenobiotic catabolic process [GO:0042178]
extracellular region [GO:0005576]
acetylesterase activity [GO:0008126]; carboxylic ester hydrolase activity [GO:0052689]
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26965627}.
null
DOMAIN: PETase retains the ancestral alpha/beta-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases. {ECO:0000269|PubMed:29666242}.
IPR029058;IPR002925;
3.40.50.1820;
A0A0K8P8E7
MQTTVTTMLLASVALAACAGGGSTPLPLPQQQPPQQEPPPPPVPLASRAACEALKDGNGDMVWPNAATVVEVAAWRDAAPATASAAALPEHCEVSGAIAKRTGIDGYPYEIKFRLRMPAEWNGRFFMEGGSGTNGSLSAATGSIGGGQIASALSRNFATIATDGGHDNAVNDNPDALGTVAFGLDPQARLDMGYNSYDQVTQAGKAAVARFYGRAADKSYFIGCSEGGREGMMLSQRFPSHYDGIVAGAPGYQLPKAGISGAWTTQSLAPAAVGLDAQGVPLINKSFSDADLHLLSQAILGTCDALDGLADGIVDNYRAC...
Piscinibacter sakaiensis (Ideonella sakaiensis)
FUNCTION: Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with PETase to depolymerize PET. Catalyzes the hydrolysis of mono(2-hydroxyethyl) terephthalate (MH...
3.1.1.102
CATALYTIC ACTIVITY: Reaction=4-[(2-hydroxyethoxy)carbonyl]benzoate + H2O = ethylene glycol + H(+) + terephthalate; Xref=Rhea:RHEA:49532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30043, ChEBI:CHEBI:30742, ChEBI:CHEBI:131704; EC=3.1.1.102; Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30979881}; Phys...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.3 uM for mono(2-hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:26965627}; Note=kcat is 31 sec(-1) for the hydrolysis of mono(2-hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius). {ECO:0000269|PubMed:26965627};
null
null
null
3D-structure;Calcium;Cell outer membrane;Disulfide bond;Hydrolase;Lipoprotein;Membrane;Metal-binding;Palmitate;Reference proteome;Serine esterase;Signal
cellular response to organic substance [GO:0071310]; xenobiotic catabolic process [GO:0042178]
cell outer membrane [GO:0009279]
carboxylic ester hydrolase activity [GO:0052689]; metal ion binding [GO:0046872]
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:26965627}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:26965627}.
null
null
IPR029058;IPR011118;
null
A0A0L7KF24
MNLTKLMKVFGYINIITNCVQSFTNRADKKRYNVFAKSFINTINTNLYTFKAVMSKTPEWIHEKSPKHNSYDIIEKRYNEEFKMTYTVYQHKKAKTQVISLGTNDPLDVEQAFAFYVKTLTHSGKGIPHILEHSVLSGSKNYNYKNSIGLLEKGTLHTHLNAYTFNDRTVYMAGSMNNKDFFNIMGVYMDSVFQPNVLENKYIFETEGWTYEVEKLKEDEKGKAEIPQMKDYKVSFNGIVYNEMKGALSSPLEDLYHEEMKYMFPDNVHSNNSGGDPKEITNLTYEEFKEFYYKNYNPKKVKVFFFSKNNPTELLNFVDQ...
Plasmodium falciparum (isolate HB3)
FUNCTION: In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains (PubMed:10542284, PubMed:12876284). In the apicoplast, degrades apicop...
3.4.24.-
null
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10542284}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q76NL8};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5 (food vacuole) (PubMed:12876284). Optimum pH is 7 (PubMed:12876284). {ECO:0000269|PubMed:12876284};
null
Apicoplast;Coiled coil;Direct protein sequencing;Hydrolase;Membrane;Metal-binding;Metalloprotease;Plastid;Protease;Reference proteome;Vacuole;Zinc
acquisition of nutrients from host [GO:0044002]; protein processing [GO:0016485]
apicoplast [GO:0020011]; chloroplast [GO:0009507]; food vacuole [GO:0020020]; mitochondrial matrix [GO:0005759]; vacuolar membrane [GO:0005774]
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10542284}; Peripheral membrane protein {ECO:0000269|PubMed:12876284}. Plastid, apicoplast {ECO:0000250|UniProtKB:Q76NL8}. Vesicle {ECO:0000269|PubMed:12876284}. Note=Localizes to the food (or digestive) vacuole, an acidic vacuole where host hemoglobin is digest...
PTM: Does not require processing for targeting to the food vacuole or maturation. {ECO:0000269|PubMed:12798513, ECO:0000269|PubMed:12876284}.
null
IPR011249;IPR011765;IPR007863;IPR013578;
3.30.830.10;
A0A0M3Q1Q3
MRRSGNYQAPVWNNDFIQSFSTDKYKDEKFLKKKEELIAQVKVLLNTKMEAVKQLELIEDLRNLGLTYYFEDEFKKILTSIYNEHKGFKNEQVGDLYFTSLAFRLLRLHGFDVSEDVFNFFKNEDGSDFKASLGENTKDVLELYEASFLIRVGEVTLEQARVFSTKILEKKVEEGIKDEKLLAWIQHSLALPLHWRIQRLEARWFLDAYKARKDMNPIIYELGKIDFHIIQETQLQEVQEVSQWWTNTNLAEKLPFVRDRIVECYFWALGLFEPHEYGYQRKMAAIIITFVTIIDDVYDVYDTLDELQLFTDAIRKWDVE...
Thymus vulgaris (Thyme)
FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (PubMed:26750479). Monoterpene synthase which catalyzes the conversion of gerany...
4.2.3.114; 4.2.3.115
CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene; Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.114; Evidence={ECO:0000269|PubMed:26750479}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560; Evidence={ECO:0000269|PubMed:26750479}; ...
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:E2E2P0}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:E2E2P0}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:E2E2P0};
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:26750479}.
null
null
3D-structure;Lyase;Magnesium;Manganese;Metal-binding
diterpenoid biosynthetic process [GO:0016102]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to UV-C [GO:0010225]
null
gamma-terpinene synthase activity [GO:0102903]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; terpene synthase activity [GO:0010333]
null
null
DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). {ECO:0000250|UniProtKB:Q9X839}.
IPR008949;IPR044814;IPR001906;IPR036965;IPR005630;IPR008930;
1.10.600.10;1.50.10.130;
A0A0N4SWI8
MDESALTLGTIDVSYLPNSSEYSIGRCKHASEEWGECGFRPPVFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDRFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKKILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATEMNLPLIFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGQKDILYRALLHGHIVELLRQQQFLEIFLEGTRSR...
Sus scrofa (Pig)
FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipids biosynthesis such as triglycerides, phosphatidic acids and lysophosphatidic acids. {ECO:0000256|ARBA:ARBA00023435}.
2.3.1.15
CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597, ChEBI:CHEBI:74544; Evidence={ECO:0000256|ARBA:ARBA00023362}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHE...
null
null
PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.; PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|PIRNR:PIRNR000437}.
null
null
Acetylation;Acyltransferase;Lipid biosynthesis;Lipid metabolism;Membrane;Mitochondrion;Phospholipid biosynthesis;Phospholipid metabolism;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix
activated T cell proliferation [GO:0050798]; activation-induced cell death of T cells [GO:0006924]; acyl-CoA metabolic process [GO:0006637]; CDP-diacylglycerol biosynthetic process [GO:0016024]; defense response to virus [GO:0051607]; fatty acid homeostasis [GO:0055089]; fatty acid metabolic process [GO:0006631]; glyce...
mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886]
glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity [GO:0102420]
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004374}.
null
null
IPR022284;IPR045520;IPR041728;IPR028354;IPR002123;
null
A0A0N9E2K8
MLTVIRRIFIIQTFIFITAEKIFHSRDHSDVLNNIHQAELITDTDTAQRFLSKYGFIKAAGSEESQLSESSGDLDFSLSLDLHEGGTTSGSSSSDLQFVSALRDFQRLSDLPVTGVFDDATKAAMNKPRCGVMDDDQELKDVTGSNSTRNHIRTSTNTSHNHEHQAPVRKKRHLSALLKNTSLQKRDVSKWTGHMAFSKSVLKWRLIGEGYSSQLSIQEQKYIFRLAFRMWSEISPLQFIEDLHSPLENIDIRLGFGTGRHLGCSQRFDGAGREFAHAWFLGDIHFDDDEHFTVPNTGSGISLLKVAVHEIGHVLGLPHI...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway. {ECO:0000269|PubMed:26429889, ECO:0000269|PubMed:26437028}.
3.4.24.-
null
null
null
null
null
null
Calcium;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Zinc
collagen catabolic process [GO:0030574]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right symmetry [GO:0007368]; embryonic heart tube left/right pattern formation [GO:0060971]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; regulation of heart looping [GO:...
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
null
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
null
IPR036375;IPR018487;IPR033739;IPR024079;IPR001818;IPR021190;IPR006026;IPR002477;IPR036365;
3.40.390.10;2.110.10.10;
A0A0N9HMN6
MEMAPTMDLEIRNGNGYGDSGEELLAAQAHIYNHIFNFISSMALKCAVELNIPEILHNHQPKAVTLSELVQALQIPQAKSACLYRLLRILVHSGFFAITKIQSEGDEEGYLPTLSSKLLLKNHPMSMSPCLLGLVNPTMVAPMHFFSDWFKRSDDMTPFEATHGASLWKYFGETPHMAEIFNEAMGCETRLAMSVVLKECKGKLEGISSLVDVGGGTGNVGRAIAEAFPNVKCTVLDLPQVVGNLKGSNNLEFVSGDMFQFIPPADVVFLKWILHDWNDEECIKILKRCKEAIPSKEEGGKLIIIDMVVNDHNKGSYEST...
Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum)
FUNCTION: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the methylation of (-)-pluviatolide to produce (-)-bursehernin (PubMed:26359402). {ECO:0000269|PubMed:26359402}.
2.1.1.323
CATALYTIC ACTIVITY: Reaction=(-)-pluviatolide + S-adenosyl-L-methionine = (-)-bursehernin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49036, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90893, ChEBI:CHEBI:90896; EC=2.1.1.323; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for (-)-pluviatolide {ECO:0000269|PubMed:26359402}; Vmax=1.7 nmol/min/mg enzyme with (-)-pluviatolide as substrate {ECO:0000269|PubMed:26359402}; Note=kcat is 0.72 sec(-1) with (-)-pluviatolide as substrate. {ECO:0000269|PubMed:26359402};
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}.
null
null
Methyltransferase;S-adenosyl-L-methionine;Transferase
aromatic compound biosynthetic process [GO:0019438]; melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]; phenylpropanoid biosynthetic process [GO:0009699]; response to wounding [GO:0009611]
null
acetylserotonin O-methyltransferase activity [GO:0017096]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]
null
null
null
IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;
3.40.50.150;1.10.10.10;
A0A0N9HTA1
MDTRADAEIKAMELIGIGVLPLAMKAIIELNVLEILSKAGPDTQLTAAQIVTDIPTTNPNAGFQLDRILRLLASHSVLSSSITKSGERVYGLTPMCKYFLPDQDGVSLAPMVVTIHDKVLLQSWHYLKDSVLKQGSLPFTEAFGMSPFEYSVSDTRFNKVFNAGMFDHSTLCMRDVLQRYKGFQGLGELVDVGGGTGGSLKMILSQYPNLKGINFDLPHVVADAPSFPGVKHIGGDMFESVPSGDAIFMKWILHDWDDGRCLTLLKNCWNALPEHGKVIIVEWILPSDAATDPTSRRVFTADLMMLAFSEGGKERTLGDY...
Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum)
FUNCTION: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the methylation of (-)-5'-demethylyatein to produce (-)-yatein (PubMed:26359402). {ECO:0000269|PubMed:26359402}.
2.1.1.330
CATALYTIC ACTIVITY: Reaction=(-)-5'-demethylyatein + S-adenosyl-L-methionine = (-)-yatein + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49040, ChEBI:CHEBI:4553, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90894; EC=2.1.1.330; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=l...
null
null
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}.
null
null
Methyltransferase;S-adenosyl-L-methionine;Transferase
aromatic compound biosynthetic process [GO:0019438]; methylation [GO:0032259]; phenylpropanoid biosynthetic process [GO:0009699]; response to wounding [GO:0009611]
null
O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]
null
null
null
IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;
3.40.50.150;1.10.10.10;
A0A0N9NCU6
MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV
Yersinia pseudotuberculosis
FUNCTION: Serine/threonine-protein acetyltransferase translocated into infected cells, which inhibits the host immune response and induces cell death by mediating acetylation of target proteins (PubMed:10489373, PubMed:12433923, PubMed:16728640, PubMed:22563435, PubMed:26810037). Inhibits the MAPK and NF-kappa-B signal...
2.3.1.-
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141025; Evidence={ECO:0000269|PubMed:16728640}; PhysiologicalDirection=left-to-righ...
COFACTOR: Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130; Evidence={ECO:0000250|UniProtKB:O68718};
null
null
null
null
Acyltransferase;Allosteric enzyme;Plasmid;Secreted;Transferase;Virulence
negative regulation of JNK cascade [GO:0046329]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of p38MAPK cascade [GO:1903753]; peptidyl-serine O-acetylation [GO:0030919]; peptidyl-threonine O-acetylation [GO:0120258]
extracellular region [GO:0005576]
O-acetyltransferase activity [GO:0016413]; toxin activity [GO:0090729]
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DUD0}. Note=Secreted via type III secretion system (T3SS). {ECO:0000250|UniProtKB:P0DUD0}.
null
null
IPR005083;
null
A0A0P0UQI8
MLSNKKSDPGSSSSSGGNGGDRAPETLAAPQAGPAGPSGPISADVKKKERASPSGEPGGPPLPHPPGPGGIDQDSAEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKERKQVIPPPAPPIEEENDSEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIINGPQHTQKVFLYIRNRTLQLWLDNPKVQLTFEATVQQLEAPYNSDAVLVHRIHSYLERHGFINFGIYKRVKPLPTKKTGKVIVIGAGVSGLAAARQLQSFGMDVTVLESRDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQV...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by me...
1.14.99.66
CATALYTIC ACTIVITY: Reaction=2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2 AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60244, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, ChEBI:CHEBI:29969, ChEBI:CHEBI:61976; EC...
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974, ECO:0000256|PIRNR:PIRNR038051, ECO:0000256|PIRSR:PIRSR038051-1};
null
null
null
null
Chromatin regulator;Coiled coil;FAD;Flavoprotein;Methyltransferase;Nucleus;Oxidoreductase;Proteomics identification;Reference proteome;Repressor;Transcription;Transcription regulation;Transferase
methylation [GO:0032259]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of hemopoiesis [GO:1903706]; regulation of retinoic acid biosynthetic process [GO:1900052]
nucleus [GO:0005634]
chromatin binding [GO:0003682]; FAD-dependent H3K4me/H3K4me3 demethylase activity [GO:0140682]; flavin adenine dinucleotide binding [GO:0050660]; histone deacetylase activity [GO:0004407]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]
SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038051}.
null
DOMAIN: The SWIRM domain may act as an anchor site for a histone tail. {ECO:0000256|PIRNR:PIRNR038051}.
IPR002937;IPR036188;IPR017366;IPR009057;IPR007526;IPR036388;
3.90.660.10;1.10.287.80;3.50.50.60;1.10.10.10;
A0A0P0VIP0
MPPRCRRLPLLFILLLAVRPLSAAAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPH...
Oryza sativa subsp. japonica (Rice)
FUNCTION: Legume-lectin receptor-like kinase required for normal pollen development and male fertility (PubMed:31833176, PubMed:32284546). Regulates pollen exine assembly and aperture development (PubMed:31833176, PubMed:32284546). Plays a critical role in annulus formation, and may participate in the formation of the ...
2.7.11.1
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:31833176}; Physiolog...
null
null
null
null
null
ATP-binding;Cell membrane;Cytoplasm;Glycoprotein;Kinase;Lectin;Membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix
defense response to bacterium [GO:0042742]; defense response to oomycetes [GO:0002229]; pollen aperture formation [GO:0062075]; pollen development [GO:0009555]; protein autophosphorylation [GO:0046777]
cytosol [GO:0005829]; plasma membrane [GO:0005886]; pollen aperture [GO:0062074]
ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; kinase activity [GO:0016301]; protein serine/threonine kinase activity [GO:0004674]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31833176, ECO:0000269|PubMed:32284546}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:32284546}. Note=During meiosis, localizes diffusely in the cytosol and plasma membrane of microspore mother cells (MMCs). During tetra...
PTM: Autophosphorylated at Thr-376; Ser-378; Thr-386; Thr-403 and Thr-657. {ECO:0000269|PubMed:31833176}.
null
IPR013320;IPR011009;IPR001220;IPR000719;IPR008271;
2.60.120.200;1.10.510.10;
A0A0P0WGX7
MASPPPFDICGDLDDDPTPPAPTPLAAPTPNGLNDRLLRLTRTHQRGPSQNPNPNPNPNPKPPPPPPPQEPEPAKVKLAGRRRLCKLSTAGDESAGDDDSIRDILDDLTTRLDSLSVDRPTARPRPHVSPLPCALHADPDPSQSQLNDGTKPSSSFVDCDDDDDDAGGAYGGFGVKEEVTRKVFKASSSFGGRGNDDKMKAKGAYAFDTVSRKTTTESKASKFFGDYDDEDDIDQDAENGKENHADDVGWEKTEDFKMEPTGTGVTRKPYNLPGRIFNMLYPHQREGLRWLWVLHCRGTGGILGDDMGLGKTMQVSAFLA...
Oryza sativa subsp. japonica (Rice)
FUNCTION: DNA helicase that acts as an essential component of the spindle assembly checkpoint (By similarity). Plays an indispensable role in the development of seed endosperm (PubMed:25327517). Is required to secure sister chromosome separation during endosperm syncytial mitosis, which involves extremely rapid free nu...
3.6.4.-
null
null
null
null
null
null
ATP-binding;Cell cycle;Cell division;Chromosome;Cytoplasm;DNA recombination;Helicase;Hydrolase;Mitosis;Nucleotide-binding;Reference proteome
cell division [GO:0051301]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; reciprocal meiotic recombination [GO:0007131]; regulation of endosperm development [GO:2000014]; regulation of mitotic sister chromatid separation [GO:0010965]; transcription-coupled nucleotide-excision repair ...
chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25327517}. Chromosome {ECO:0000269|PubMed:25327517}. Note=Localizes to the cytoplasm during interphase, but moves to the chromosome arms during mitosis. {ECO:0000269|PubMed:25327517}.
null
null
IPR014001;IPR001650;IPR027417;IPR038718;IPR049730;IPR000330;
3.40.50.300;3.40.50.10810;
A0A0P0XCU3
MEMALRPQSLLCPRSRLKVVIRPASSASGGGLAQYFLMTRRYTGSRIVRCMVSSSDCPNRKAKRTISLHTEVASSRGYAPRIAAESSIQEREHINSDEETFDTYNRLLRNESTEWKKLDTTEVDLSQDVSSSSMRKVDATDEAKLDILEDDLPRNLLNGVTMGEVDMLDEAGAEDDVFEVDLSALHNSTVGKMDAVNEVGTENDLFEVDLSALHSAAVGKVDVVDGAKAKEDLFEMDSLALHSVTMGKVDAINAAGAEGDKFEVDLSALASNNSMIEAVNVMDEAKAIEDTLEVDLSGNATSSSTYGEVKFEVDSLGNTS...
Oryza sativa subsp. japonica (Rice)
FUNCTION: Involved in starch synthesis in endosperm amyloplasts (PubMed:17297616, PubMed:17586688, PubMed:21417378, PubMed:21595523, PubMed:21730357). Plays an important role in the elongation of amylopectin B chains (PubMed:17297616, PubMed:17586688, PubMed:21417378, PubMed:21595523, PubMed:21730357). {ECO:0000269|Pub...
2.4.1.21
CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21; Evidence={ECO:0000305};
null
null
PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
null
null
Alternative splicing;Amyloplast;Chloroplast;Coiled coil;Glycosyltransferase;Plastid;Reference proteome;Starch biosynthesis;Transferase;Transit peptide
amylopectin biosynthetic process [GO:0010021]; endosperm development [GO:0009960]; starch biosynthetic process [GO:0019252]
amyloplast [GO:0009501]; chloroplast [GO:0009507]
alpha-1,4-glucan synthase activity [GO:0033201]; glycogen (starch) synthase activity [GO:0004373]; starch binding [GO:2001070]; starch synthase activity [GO:0009011]
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. Plastid, amyloplast {ECO:0000305}. Note=Amyloplast or chloroplast, soluble. {ECO:0000305}.
null
null
IPR005085;IPR001296;IPR011835;IPR013783;IPR013534;
3.40.50.2000;2.60.40.10;
A0A0R4I9Y1
MTRKRKSGKKGKPLAQKKEAQKRGGSTSSSTTQKEGAQKGDGSSSSSTTQKDGAQKRDDSTSSSSTAQKEEGQKSDGSTSSSTTNKEGAQKRDGSTSSRLQKKGPQKRKGSTSSSRAHSRSRSKSKQTSYPSQARSRSHGQHNISTTESGPLSKEAQTQTSASLLVDKDTQTETVGQASQQTQTEINGNTETAEVSQPPQLSHEDVEMEGTVQPRTKGSESDGEKEESVKRKKRKLSEIGEPAKETEDSTKLSHECEEKVGDNQKNEDTNKHYGGDSLKDLKSVTEEPKSYAAAAATGKTGKVSKEQTNQIEANQDSTME...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity. Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccha...
2.3.2.-; 2.3.2.27; 3.6.4.-
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:Q63HN8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) ...
null
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}.
null
null
Angiogenesis;ATP-binding;Cytoplasm;Hydrolase;Immunity;Lipid droplet;Lipid metabolism;Metal-binding;Multifunctional enzyme;Nucleotide-binding;Reference proteome;Transferase;Ubl conjugation pathway;Zinc;Zinc-finger
defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein K63-linked ubiquitination [GO:0070534]; regulation of lipid metabolic process [GO:0019...
cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}.
null
DOMAIN: Composed of an N-terminal stalk, a dynein-like core comprised of two catalytically active and four inactive ATPase domains, and a C-terminal E3 module. The ATPase regions do not generate movement but rather act like an intricate molecular 'switch'. {ECO:0000250|UniProtKB:E9Q555}.; DOMAIN: The RING-type zinc fin...
IPR003593;IPR027417;IPR031248;IPR046439;IPR001841;IPR013083;IPR017907;
3.40.50.300;3.30.40.10;
A0A0R4IAH0
MTSHSRPDGLPSKEQPLELLKPSGVNHIPPVDVSVALPLQVPPSAIPMDLRVDHQFALAPTDPAQREHQLQQELLALKQKQQIQRQLLIEEFQRQHEQLSRQHEAQLQEHVKHQQDLLALKHQQELLEHQRKLERHRQEQEMEKQQREQKLQLLKNKERGQESAVASTEVKMRLQEFVLNKKKALAQRSLNHCLPSDPRYWYGKTQHSSLDQSSPPQTGISTYNHPVLGMYDPKDDFPLRKTASEPNLKLRSRLKQKVSERRSSPLLRRKDGPITTAKKRSLDMAESACSSAPGSGPSSPNNSSNNITNENGIAGSISNS...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. {ECO:0000256|PIRNR:PIR...
3.5.1.98
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000256|PIRNR:PIRNR037911};
null
null
null
null
null
Chromatin regulator;Coiled coil;Hydrolase;Metal-binding;Nucleus;Proteomics identification;Reference proteome;Repressor;Transcription;Transcription regulation;Zinc
embryonic cranial skeleton morphogenesis [GO:0048701]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest cell migration [GO:0001755]; perichondral ossification [GO:0036073]; pronephros morphogenesis [GO:0072114]; regulation of neural crest formation [GO:0090299]; response to stimulus ...
histone deacetylase complex [GO:0000118]
histone deacetylase activity [GO:0004407]; metal ion binding [GO:0046872]
SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
null
null
IPR046949;IPR000286;IPR023801;IPR037138;IPR024643;IPR023696;
6.10.250.1550;3.40.800.20;
A0A0R4IBK5
MKCPKCSHEALEKAPKFCSECGHKLQSQSYETTQGTPHDKSQTPSIVPQITNAEMDETGSESKSLEIQNANVSPKRPNENTSPNPKKKKRKKRKKEKKKKSGVSEGPSSLTSDLSDISLTDKEKKMDTDQSSDSDCSSCIVEDTPTPAEPSSHLSPPENETAGPAQLSASALTTGSSKDGEESIGTTQKPVSASASKAPLGVDQQTKEEKVKCKDEGQKSLSAKAQHTPNANVDQNANVQSDANIDKDSQNVEPQKSSSVKTKPSKSTVADPKKTESEKQKSGERDNENSTQPVSSPKLKRNQTEESQKMVFGPNSAPKK...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (By similarity). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacteria...
2.3.2.-; 2.3.2.27; 3.6.4.-
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:Q63HN8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) ...
null
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}.
null
null
Angiogenesis;ATP-binding;Cytoplasm;Hydrolase;Immunity;Lipid droplet;Lipid metabolism;Metal-binding;Multifunctional enzyme;Nucleotide-binding;Reference proteome;Transferase;Ubl conjugation pathway;Zinc;Zinc-finger
blood circulation [GO:0008015]; defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein K63-linked ubiquitination [GO:0070534]; regulation of ...
cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}.
null
DOMAIN: Composed of an N-terminal stalk, a dynein-like core comprised of two catalytically active and four inactive ATPase domains, and a C-terminal E3 module. The ATPase regions do not generate movement but rather act like an intricate molecular 'switch'. {ECO:0000250|UniProtKB:E9Q555}.; DOMAIN: The RING-type zinc fin...
IPR003593;IPR027417;IPR031248;IPR046439;IPR018957;IPR001841;IPR013083;IPR017907;
3.40.50.300;3.30.40.10;
A0A0R4IKJ1
MTSENHTTIKADSALVMSPTGSTSQAAPFSPSTSKPIQELPDELIQAGWSKCWSKRENRPYYFNRFTNQSLWEMPVLGQHDVISDPLGLNAAPASGEANADAGLGNGQRKRHPSEDASQAGPNSFKRPKVEIPATPTTPTVPISPSTPGVKPWVNTTTDEKQGQASTPAPAPYRPSVVYWDLDIQTNAVIRERAPADHLPPHPEIELQRAQLTTKLRQHYHELCSQREGIEPPRESFNRWLLERKVVDKGLDPLLPSECDPVISPSMFREIMNDIPIRLSRIKYKEEARKLLFKYAEAAKKMIDSRNATPESRKVVKWNV...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs (PubMed:30467178). {ECO:0000269|PubMed:30467178}.
2.1.1.62
CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:22744, Rhea:RHEA-COMP:11518, Rhea:RHEA-COMP:11519, ...
null
null
null
null
null
3D-structure;Methyltransferase;Nucleus;Reference proteome;Transferase
mRNA methylation [GO:0080009]; positive regulation of translation [GO:0045727]
nucleus [GO:0005634]
mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity [GO:0016422]; RNA polymerase II C-terminal domain binding [GO:0099122]; S-adenosyl-L-methionine binding [GO:1904047]
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4Z3}.
null
null
IPR029048;IPR039881;IPR022035;IPR001202;IPR036020;
1.20.1270.10;2.20.70.10;
A0A0R4ILA2
MTAGVRGMACWGLCGFLFGLLRISSACPVSCFCNASRISCIDQEPGIEDFPVLMPESDMENITDIYISNQKRLFTINEDHMKFYSNLRNLTVTNTHLTYVSTMAFFNNSKLQYLNLGDNNLSTLSWMAMRNSNVSTLLLSGNPLQCACENIWIKLWLDDSERDVLQCLQEGGKAKTLSRLTLPLCEHPRVEVFPTDVSQMAGSDATVICNASGSPTPELTWTLNSSEHPPLSTSHEISKMDLQSVLTLNGLSPNDNGRKLICSAENIVGQIEATVMLNISFPPTVLELYLPERSQDWCIPFVVTGNPRPDLHWYHEGKPL...
Danio rerio (Zebrafish) (Brachydanio rerio)
null
2.7.10.1
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:0000256|ARBA:ARBA00001171, ECO...
null
null
null
null
null
ATP-binding;Developmental protein;Differentiation;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Leucine-rich repeat;Membrane;Neurogenesis;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase
cell differentiation [GO:0030154]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; lateral line development [GO:0048882]; nervous system development [GO:0007399]; neuromast primordium migration [GO:0048883]; positive regulation of neuron projection development [GO:0010976]; regulation of p...
axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synapse [GO:0045202]
ATP binding [GO:0005524]; brain-derived neurotrophic factor binding [GO:0048403]; brain-derived neurotrophic factor receptor activity [GO:0060175]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
null
null
IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR011009;IPR001611;IPR032675;IPR020777;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;IPR002011;
2.60.40.10;3.80.10.10;1.10.510.10;
A0A0R4IPY6
MMEPSFGISESQCIATVRGHEIRSGQKEPRLLSLLECSGQFKLDILSNPDAIVLSPVSQLSIPINNHFRIIREAEEALLIDIDSISKTVRIRLRGERTPELLLELQDDGQTQSFLEHVTKAKQQAERSSLPRKMEPVVPAPVKDCVPVPPQRGTSKSFSNNINNSTLANPSNTDSTRSLATDFGFEENFNHVLKVEEKKNKQNRLVAQREPPPPPIPPLPPRKGTNTSLTGPATKERPPSVQNATPVRNEFQSVDRSVSWSESPSNSTIRQAMMSSHAGSREGLLKYRLSKKEKEYVDIKNFKFFVGTWNVNGQSPDSSL...
Danio rerio (Zebrafish) (Brachydanio rerio)
null
3.1.3.36
null
null
null
null
null
null
Coiled coil;Cytoplasmic vesicle;Endosome;Hydrolase;Lipid metabolism;Proteomics identification;Reference proteome
brain development [GO:0007420]; chordate embryonic development [GO:0043009]; cilium assembly [GO:0060271]; cilium movement [GO:0003341]; cilium organization [GO:0044782]; embryonic cranial skeleton morphogenesis [GO:0048701]; endocytosis [GO:0006897]; glomerular filtration [GO:0003094]; melanosome transport [GO:0032402...
cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; membrane [GO:0016020]; phagocytic vesicle membrane [GO:0030670]
inositol phosphate phosphatase activity [GO:0052745]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]
SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00004580}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004146}. Endosome membrane {ECO:0000256|ARBA:ARBA00004608}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
null
null
IPR036691;IPR005135;IPR013783;IPR046985;IPR000300;IPR048869;IPR037793;IPR037787;IPR031995;IPR008936;IPR000198;IPR047078;
2.30.29.110;3.60.10.10;2.60.40.10;1.10.555.10;
A0A0R4IQG7
MQESEPSVCQLQPNIISVRLFKRKIGGLGFLVKQRVCKPPVIVSDLIRGGAAEECGLVQVGDIVLAVNNKPLVDMSYERALETLKNVSPESHAVLILRGPEGFTTHLETTLSSDGKTKTIRVTRPVNPAQSRPCERCSPLTPNMTKELRAIENLSSSSTPRKESRDDKPLIPLLSQDSLLREGGHAGLLLNGVEDNNDLLKEIEPVLKLIKNSKKEINGEGQRVIDRKDAEVQVERDLGVGNGQNAQLASDNDRVFDDLWRKDNMPTVLNNPYSESDKPQSYERVSPTKAVQNGSPSKCPRFMKVKNWETGALYNDTLHH...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions. {ECO:0000256|PIRNR:PIRNR000333}.
1.14.13.39
CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={...
COFACTOR: Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000256|ARBA:ARBA00001950}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|PIRNR:PIRNR000333}; Note=Binds 1 FAD. {ECO:0000256|PIRNR:PIRNR000333}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:...
null
null
null
null
Calmodulin-binding;FAD;Flavoprotein;FMN;Heme;Iron;Metal-binding;NADP;Oxidoreductase;Proteomics identification;Reference proteome;Ubl conjugation
arginine catabolic process [GO:0006527]; collateral sprouting [GO:0048668]; hematopoietic stem cell differentiation [GO:0060218]; liver development [GO:0001889]; muscle contraction [GO:0006936]; negative regulation of blood pressure [GO:0045776]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide mediated sig...
cytosol [GO:0005829]; dendritic spine [GO:0043197]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; sarcolemma [GO:0042383]
calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517]
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004468}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004468}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}.
null
null
IPR003097;IPR017927;IPR001094;IPR008254;IPR001709;IPR029039;IPR039261;IPR023173;IPR044943;IPR044940;IPR044944;IPR012144;IPR004030;IPR036119;IPR001433;IPR001478;IPR036034;IPR017938;
2.30.42.10;3.40.50.360;6.10.250.410;3.90.440.10;3.40.50.80;2.40.30.10;
A0A0R4IVA4
MTLDNLKHSAILSTLFKMADDNDLLGASEFIKDRLYFATLRSKPKSTANTHYFSTDEEFVYENFYADFGPLNLAMLYRYCCKLNKKLKSFTLTRKRIVHYTSFDQRKRANAAVLIGAYAVIYLKKTPEEAYRALISGSNASYLPFRDASFGNCTYNLTVLDCLQGIRKALQHGFLNFETFDVNEYEHYERVENGDLNWITPGKLLAFSGPHPKSKVENGYPLHAPEAYFPYFRKHNVTTIVRLNKKIYDAKRFTDAGFDHYDLFFVDGSTPSDIITRRFLHICESTSGAVAVHCKAGLGRTGTLIGCYLMKHYRFTSAEA...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. {...
3.1.3.16; 3.1.3.48
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:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVI...
null
null
null
null
null
Cell cycle;Cell division;Cell projection;Cytoplasm;Cytoskeleton;Hydrolase;Nucleus;Phosphoprotein;Protein phosphatase;Reference proteome
cell cycle [GO:0007049]; cell division [GO:0051301]; cilium assembly [GO:0060271]; dephosphorylation [GO:0016311]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of cytokinesis [GO:0032467]; regulation of exit from mitosis [GO:0007096]
centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinocilium [GO:0060091]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; spindle pole [GO:0000922]
myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, kinocil...
null
DOMAIN: Composed of two structurally equivalent A and B domains that adopt a dual specificity protein phosphatase (DSP) fold. {ECO:0000250|UniProtKB:Q9UNH5}.
IPR044506;IPR029260;IPR000340;IPR029021;IPR016130;IPR000387;IPR020422;
3.90.190.10;
A0A0R4IVA6
MAGAKPGVHALQLKPVSVNEVLKRGSKFIKWDEEANSTPSLITLRVDPNGFFLYWTGGTSMEAEILDMSHIRDTRTGKFAKTPKDQRIREMLFSGKADGNSDSRLLTVVYGNDLVNISFLNFQAVQDGYCKLWTDELFKLATNMLSQNASRNTFLLKAYTKLKLQVTQDGKIPVKNILKMFSDKKRVEMALEHCGLIFNRVDGIKPDDFTWEMFQNFLNKLSPRPEVERIFVDLGSKGKPFLSLDQLMDFINRKQRDSRLNEVLYPPLKRDQVRQLMEKYETNTSQLERDQISLMSFTKYLGGEENTVVPPERLDIIDDM...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. {ECO:0000256|PIRNR:PIRNR000956}.
3.1.4.11
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433; Evidence={ECO:0000256|ARBA:ARBA00023726}; Physiolog...
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR000956-2}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};
null
null
null
null
Calcium;Coiled coil;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Phosphoprotein;Proteomics identification;Reference proteome;Transducer
cartilage morphogenesis [GO:0060536]; embryonic viscerocranium morphogenesis [GO:0048703]; G protein-coupled receptor signaling pathway [GO:0007186]; lipid catabolic process [GO:0016042]; negative regulation of calcium ion import [GO:0090281]; negative regulation of vascular permeability [GO:0043116]; phosphatidylinosi...
cytoplasm [GO:0005737]
calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; phosphatidylinositol phospholipase C activity [GO:0004435]
null
null
null
IPR000008;IPR035892;IPR011992;IPR001192;IPR016280;IPR014815;IPR042531;IPR009535;IPR037862;IPR017946;IPR015359;IPR000909;IPR001711;
2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10;
A0A0R4IVY5
MEMSIGESLTARFEKIDAMLKDPKSEVNTDCLLDSLDALVYDLDFPALRKNKSIDDFLKRYKDTISKIRELRMKAEDYEVVKVIGRGAFGEVQLVRHKATRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSNWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDGIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKDGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNALTFPEDSDISKDAKSLICAFLT...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. {ECO:0000256|PIRNR:PIRNR037568}.
2.7.11.1
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:0000256|ARBA:ARBA00001127}; Physiol...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR037568};
null
null
null
null
ATP-binding;Cell membrane;Cell projection;Coiled coil;Cytoplasm;Cytoskeleton;Golgi apparatus;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc;Zinc-finger
actomyosin structure organization [GO:0031032]; cell development [GO:0048468]; cortical actin cytoskeleton organization [GO:0030866]; embryonic morphogenesis [GO:0048598]; epicardial cell to mesenchymal cell transition [GO:0003347]; mitotic cytokinesis [GO:0000281]; negative regulation of adherens junction organization...
bleb [GO:0032059]; centriole [GO:0005814]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; Rho-dependent protein serine/threonine kinase activity [GO:0072518]; small GTPase binding [GO:0031267]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, bleb {ECO:0000256|ARBA:ARBA00043945}. Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Membrane {ECO:0000256|ARBA:A...
null
null
IPR000961;IPR046349;IPR011009;IPR002219;IPR011993;IPR001849;IPR000719;IPR017441;IPR020684;IPR037310;IPR015008;IPR008271;
1.20.5.340;3.30.60.20;2.30.29.30;1.20.5.730;1.10.510.10;
A0A0R4IXF6
MADPAAQSSAQPRLQQAQSSGPTGSNSNPGAGSSDPARPGLSQQQWSSQKKAQVRSFPRAKKLEKLGVFSSCKANDACKCNGWKNPNPPTAARMELQQQAASLTETCRSCGHSLAEHVSHLENVSEEEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMGKPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPKERQTMYELSKMFLLCLNYWKLETPSQFRQRAQKEDAAAYKVDYTRWLCYCHVPQSNDSLPRYETCQVFGRSLLKSIFTVTRRQLLEKFRVEKDKLPPEKRTLILTHFPKFL...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferasesucc, succinyltransferase or malonyltransferase, depending on the context (By similarity). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequenc...
2.3.1.-; 2.3.1.48
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:Q92830}; ...
null
null
null
null
null
Acyltransferase;Bromodomain;Chromosome;Cytoplasm;Cytoskeleton;Nucleus;Reference proteome;Transcription;Transcription regulation;Transferase
bone morphogenesis [GO:0060349]; chromatin remodeling [GO:0006338]; epigenetic regulation of gene expression [GO:0040029]; heart development [GO:0007507]; histone succinylation [GO:0106077]; internal peptidyl-lysine acetylation [GO:0018393]; limb development [GO:0060173]; long-term memory [GO:0007616]; peptidyl-lysine ...
ATAC complex [GO:0140672]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; histone acetyltransferase complex [GO:0000123]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; histone acetyltransferase activity [GO:0004402]; histone glutaryltransferase activity [GO:0106229]; histone H3 acetyltransferase activity [GO:0010484]; histone H3K9 acetyltransferase activity [GO:0043992]; histone succinyltransferase activity [GO:0106078]; peptide-lysine-N-acetyltransfer...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92830}. Chromosome {ECO:0000250|UniProtKB:Q92830}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q92830}.
null
DOMAIN: Loop3 is required for substrate specificity and adopts different structural conformations in succinyl-CoA-bound and acetyl-CoA-bound forms. Tyr-603 has an important role in the selective binding of succinyl-CoA over acetyl-CoA. {ECO:0000250|UniProtKB:Q92830}.
IPR016181;IPR001487;IPR036427;IPR018359;IPR037800;IPR016376;IPR000182;IPR009464;
3.40.630.30;1.20.920.10;
A0A0R4IY06
MDNQQRRTDNMASGETDHLQCVEEPQPGDLIEIFRPAYQHWALYLGDGYIINLTPVDEGQATAVSSVKSVFSRKAVVRMQLLKEVVGADSYRINNKYDDDHTPLPVSEIIQRAQMLIGQEVSYDLLGSNCEHFVTLLRYGEGVSEQASRAIGAISLVTAAASAFSVLGLINTRSRNRPF
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl gro...
2.3.1.-; 3.1.1.32; 3.1.1.4
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; Physiologica...
null
null
null
null
null
Cytoplasm;Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid metabolism;Lysosome;Membrane;Mitochondrion;Reference proteome;Transferase;Transmembrane;Transmembrane helix
lens fiber cell differentiation [GO:0070306]; lipid catabolic process [GO:0016042]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; organelle disassembly [GO:1903008]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]
N-acyltransferase activity [GO:0016410]; phospholipase A1 activity [GO:0008970]; phospholipase A2 activity [GO:0004623]
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:33854238}. Mitochondrion membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO...
null
DOMAIN: The C-terminal transmembrane domain is required for the targeting of the protein to damaged organelles. {ECO:0000269|PubMed:33854238}.
IPR007053;
3.90.1720.10;
A0A0R4IZ84
MADELERVRISAAELRAQASSFNIHGDDVKDLREEGKKQRQRDSKRPDLQLYKPGVGHPNRRMDSVEGAGSDTLIQPDGFGNDPKMSDESPTSPGCSYMPGTGNEDYLNDHSKPETNHKTDGHIGGDKHKLVDENAVKIIERAGTPKSPKQSRKMRKPDRQIYQPGGRRSQGNKEVGASKELDRDRSREEEVDGKSIETPLKCEKEEKRKNRRGKNDRKKQASVETPSANKTENAVENISNKVSNLHLETVESKDRDRQDDTNQIKHSEEGRKIQTGGANRGMGEDKKKERGNGKSRPGKEKGNNQVFDKKEEGEAGGKA...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini (By similarity). Required for normal embryonic development (PubMed:19414594). {ECO:0000250|UniProtKB:Q86US8, ECO:0000269|PubMed:19414594}.; FUNCTION: Plays a role in nonsense-mediated mRNA d...
3.1.-.-
null
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q86US8};
null
null
null
null
Chromosome;Cytoplasm;Endonuclease;Hydrolase;Nonsense-mediated mRNA decay;Nuclease;Nucleus;Reference proteome;Telomere
chordate embryonic development [GO:0043009]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]
chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nucleolus [GO:0005730]; telomerase holoenzyme complex [GO:0005697]
endonuclease activity [GO:0004519]; telomerase RNA binding [GO:0070034]; telomeric DNA binding [GO:0042162]
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q86US8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q86US8}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q86US8}.
null
DOMAIN: The PINc domain confers endonuclease activity and is expected to bind the catalytic metal ion. {ECO:0000250|UniProtKB:Q86US8}.
IPR018834;IPR019458;IPR045153;IPR029060;IPR002716;IPR011990;
3.40.50.1010;1.25.40.10;
A0A0R4J8U1
MPDPAAHLPFFYGSISRAEAEEHLKLAGMADGLFLLRQCLRSLGGYVLSLVHDVRFHHFPIERQLNGTYAIAGGKAHCGPAELCQFYSQDPDGLPCNLRKPCNRPPGLEPQPGVFDCLRDAMVRDYVRQTWKLEGDALEQAIISQAPQVEKLIATTAHERMPWYHSSLTREEAERKLYSGQQTDGKFLLRPRKEQGTYALSLVYGKTVYHYLISQDKAGKYCIPEGTKFDTLWQLVEYLKLKADGLIYRLKEVCPNSSASAEAAAPTLPAHPSTFTQPHRRIDTLNSDGYTPEPARLDKPRPMPMDTSVYESPYSDPEEL...
Rattus norvegicus (Rat)
null
2.7.10.2
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000256|ARBA:ARBA00001149, ECO...
null
null
null
null
null
ATP-binding;Cytoplasm;Immunity;Kinase;Nucleotide-binding;Reference proteome;SH2 domain;Transferase;Tyrosine-protein kinase
alpha-beta T cell differentiation [GO:0046632]; beta selection [GO:0043366]; calcium-mediated signaling [GO:0019722]; cell differentiation [GO:0030154]; immune response [GO:0006955]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; negative thymic T cell selection [GO:0045060]; phosp...
cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; immunological synapse [GO:0001772]; membrane [GO:0016020]; plasma membrane [GO:0005886]; T cell receptor complex [GO:0042101]
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102]
null
null
null
IPR011009;IPR023420;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR035838;IPR008266;IPR020635;IPR012234;
3.30.505.10;1.10.510.10;
A0A0R6Y3I5
MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCQFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALEELVFGDNDRLSALVAHHFKANLLVILSDIDGYYTENPRTSTNATIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARQFLLGGSHEIGTLFYSRVSS
Leishmania donovani
FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate (PubMed:29777624). May be important for growth and survival (PubMed:29777624). {ECO:0000269|PubMed:29777624}.
2.7.2.11
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11; Evidence={ECO:0000269|PubMed:29777624}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14878; Evidence={ECO:0000269|PubMed:...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:29777624};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for L-glutamate {ECO:0000269|PubMed:29777624}; KM=0.6 mM for ATP {ECO:0000269|PubMed:29777624};
PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000269|PubMed:29777624}.
null
null
Amino-acid biosynthesis;ATP-binding;Kinase;Magnesium;Nucleotide-binding;Proline biosynthesis;Transferase
L-proline biosynthetic process [GO:0055129]; phosphorylation [GO:0016310]
cytosol [GO:0005829]
ATP binding [GO:0005524]; glutamate 5-kinase activity [GO:0004349]; identical protein binding [GO:0042802]
null
null
null
IPR036393;IPR001048;IPR041739;IPR001057;IPR011529;IPR005715;IPR019797;
3.40.1160.10;
A0A0S2UWC9
MAENGAAVQENQNVIRHQEVGHKSLLQSDALYQYILETSVYPREPESMKELRELTAKHPWNLMTTSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALAIPHDGKILAMDINRENYEIGLPVIEKAGVAHKIDFREGPALPVLDQLVEDKNNHGTYDFIFVDADKDNYINYHKRIIDLVKVGGLIGYDNTLWNGSLVAPADTPMRKYVRYYRDFILELNKALAADPRIEICMLPVGDGITLGRRIS
Petunia hybrida (Petunia)
FUNCTION: Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:26620524). Methylates caffeoyl-CoA to feruloyl-CoA, also able...
2.1.1.-; 2.1.1.104
CATALYTIC ACTIVITY: Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104; Evidence={ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|Pu...
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q40313}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000250|UniProtKB:Q40313};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=5.8 pmol/sec/mg enzyme with (E)-caffeoyl-CoA as substrate {ECO:0000269|PubMed:26620524};
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26620524}.
null
null
Cytoplasm;Lignin biosynthesis;Metal-binding;Methyltransferase;S-adenosyl-L-methionine;Transferase
circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; lignin biosynthetic process [GO:0009809]; methylation [GO:0032259]; phenylpropanoid metabolic process [GO:0009698]
cytosol [GO:0005829]
caffeoyl CoA:S-adenosyl-L-methionine O-methyltransferase activity [GO:0080076]; caffeoyl-CoA O-methyltransferase activity [GO:0042409]; metal ion binding [GO:0046872]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26620524}.
null
null
IPR029063;IPR002935;
3.40.50.150;
A0A0S2Z366
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAIS...
Homo sapiens (Human)
null
1.3.8.7
CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:6...
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974, ECO:0000256|PIRSR:PIRSR634180-3, ECO:0000256|RuleBase:RU362125};
null
PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000256|ARBA:ARBA00005198}.
null
null
Acetylation;FAD;Flavoprotein;Oxidoreductase;Transit peptide
cardiac muscle cell differentiation [GO:0055007]; carnitine metabolic process, CoA-linked [GO:0019254]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; glycogen biosynthetic process [GO:0005978]; liver development [GO:0001889]; medium-chain fatty acid catabolic process [GO:0051793]; post-embryonic ...
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
flavin adenine dinucleotide binding [GO:0050660]; medium-chain fatty acyl-CoA dehydrogenase activity [GO:0070991]
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
null
null
IPR006089;IPR006091;IPR046373;IPR036250;IPR009075;IPR013786;IPR037069;IPR009100;IPR034180;
1.10.540.10;2.40.110.10;1.20.140.10;
A0A0S2Z381
MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAIDLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYHTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFKSTLDTDYQMTKRDMGFTEE...
Homo sapiens (Human)
null
3.5.4.4
CATALYTIC ACTIVITY: Reaction=2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+); Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4; Evidence={ECO:0000256|ARBA:ARBA00034443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191; E...
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947};
null
null
null
null
Hydrolase;Nucleotide metabolism
adenosine catabolic process [GO:0006154]; allantoin metabolic process [GO:0000255]; alpha-beta T cell differentiation [GO:0046632]; amide catabolic process [GO:0043605]; AMP catabolic process [GO:0006196]; AMP salvage [GO:0044209]; B cell proliferation [GO:0042100]; calcium-mediated signaling [GO:0019722]; dAMP catabol...
anchoring junction [GO:0070161]; cytoplasmic vesicle lumen [GO:0060205]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
2'-deoxyadenosine deaminase activity [GO:0046936]; adenosine deaminase activity [GO:0004000]; zinc ion binding [GO:0008270]
SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cell membrane {ECO:0000256|ARBA:ARBA00004296}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004296}; Extracellular side {ECO:0000256|ARBA:ARBA00004296}. Cytoplasmic vesicle lumen {ECO:0000256|ARBA:ARBA00004321}.
null
null
IPR006650;IPR028893;IPR001365;IPR006330;IPR032466;
3.20.20.140;
A0A0S2Z3W3
MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLG...
Homo sapiens (Human)
null
3.2.1.52
CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine = alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6-sulfogalactosamine; Xref=Rhea:RHEA:64384, ChEBI:CHEBI:15377, ChEBI:CHEBI:152567, ChEBI:CHEBI:152568, ChEBI:CHEB...
null
null
null
null
null
Disulfide bond;Glycosidase;Hydrolase;Lysosome;Signal;Zymogen
adult walking behavior [GO:0007628]; carbohydrate metabolic process [GO:0005975]; cell morphogenesis involved in neuron differentiation [GO:0048667]; dermatan sulfate catabolic process [GO:0030209]; ganglioside catabolic process [GO:0006689]; hyaluronan catabolic process [GO:0030214]; lipid storage [GO:0019915]; lysoso...
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; membrane [GO:0016020]
beta-N-acetylhexosaminidase activity [GO:0004563]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148]
SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
null
null
IPR025705;IPR015883;IPR017853;IPR029018;IPR029019;
3.30.379.10;3.20.20.80;
A0A0S2Z4D1
MEVVDPQQLGMFTEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHKNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFCQLIDGLEYLHSQGIVHKDIKPGNLLLTTGGTLKISDLGVAEALHPFAADDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGKGSYAIPGDCGPPLSDLLKGMLEYEPAKRFSIRQIRQHSWFRKKHPPAEAPV...
Homo sapiens (Human)
null
2.7.11.1
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:0000256|ARBA:ARBA00001433}; CATALYT...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};
null
null
null
null
ATP-binding;Cell cycle;Cytoplasm;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Nucleus;Phosphoprotein;Serine/threonine-protein kinase;Transferase
axonogenesis [GO:0007409]; cell cycle [GO:0007049]; cellular response to UV-B [GO:0071493]; dendrite extension [GO:0097484]; DNA damage response [GO:0006974]; epithelial cell proliferation involved in prostate gland development [GO:0060767]; establishment of cell polarity [GO:0030010]; glucose homeostasis [GO:0042593];...
cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; protein-containing complex [GO:0032991]; Z disc [GO:0030018]
ATP binding [GO:0005524]; LRR domain binding [GO:0030275]; metal ion binding [GO:0046872]; protein kinase activator activity [GO:0030295]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
null
null
IPR011009;IPR039154;IPR000719;IPR017441;IPR008271;
1.10.510.10;
A0A0S2Z4D2
MTELPAPLSYFQNAQMSEDNHLSNTNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERES...
Homo sapiens (Human)
FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. {ECO:0000256|RuleBase:RU361148}.
3.4.23.-
null
null
null
null
null
null
Apoptosis;Cell adhesion;Cell membrane;Cell projection;Endoplasmic reticulum;Golgi apparatus;Hydrolase;Membrane;Notch signaling pathway;Phosphoprotein;Protease;Synapse;Transmembrane;Transmembrane helix
amyloid precursor protein catabolic process [GO:0042987]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; intracellular signal transduction [GO:0035556]; Notch signaling pathway [GO:0007219]; protein processing [GO:0016485]; smooth endoplasmic reticulum calcium ion homeostasis [GO:0051563]
axon [GO:0030424]; cell junction [GO:0030054]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; synapse [GO:0045202]
aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, neuron projection {ECO:0000256|ARBA:ARBA00004487}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Endo...
null
DOMAIN: The PAL motif is required for normal active site conformation. {ECO:0000256|RuleBase:RU361148}.
IPR002031;IPR001108;IPR006639;IPR042524;
1.10.472.100;
A0A0U1RPR8
MAGLQQGCHFEGQNWTAPHWKTCLPCQGPWRLTVSHLKTVSSISVLSVVFWSVLLWADSLSLLAWARETFTLGVLGPWDCDPIFAQALPSIATQLAVDQVNQDASLLPGSQLDFKVLPTGCDTPHALATFVAHKNIVAAFVGPVNPGFCSAAALLAQGWGKSLFSWACEAPEGGGDLVPTLPSAADVLLSVMRHFGWARWAIVSSHQDIWVTTAQQLATAFRTHGLPIGLVTSLGPGEKGATEVCKQLHSVHGLKIVVLCMHSALLGGLEQTTLLHCAWEEGLTDGRLVFLPYDTLLFALPYGNRSYLVLDDHGPLQEAY...
Mus musculus (Mouse)
FUNCTION: Functions as an olfactory receptor activated by urine odorants, uroguanylin and guanylin and as well by the volatile semiochemicals carbon disulfide (CS2) and carbon dioxide (CO2) (PubMed:17702944, PubMed:17724338, PubMed:20637621). Has guanylate cyclase activity upon binding of the ligand (By similarity). Ac...
4.6.1.2
CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:P51839};
null
null
null
null
null
Cell membrane;Cell projection;cGMP biosynthesis;Disulfide bond;Lyase;Membrane;Nucleotide-binding;Reference proteome;Signal;Transmembrane;Transmembrane helix
cGMP biosynthetic process [GO:0006182]; detection of carbon dioxide [GO:0003031]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; intracellular signal transduction [GO:0035556]; olfactory behavior [GO:0042048]; olfactory learning [GO:0008355]; positive regulation of cGMP-mediated si...
ciliary membrane [GO:0060170]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886]
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; guanylate cyclase activity [GO:0004383]; natriuretic peptide receptor activity [GO:0016941]; odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672]
SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:9096404}; Single-pass type I membrane protein.
null
DOMAIN: The protein kinase domain is predicted to be catalytically inactive. {ECO:0000305}.
IPR001054;IPR018297;IPR001828;IPR011009;IPR029787;IPR028082;IPR000719;IPR001245;
3.40.50.2300;6.10.250.780;3.30.70.1230;1.10.510.10;
A0A0U1RQF0
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARRVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPL...
Homo sapiens (Human)
FUNCTION: Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-ph...
1.1.1.100; 1.3.1.39; 2.3.1.38; 2.3.1.39; 2.3.1.41; 2.3.1.85; 3.1.2.14; 4.2.1.59
CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78453, ChEBI:CHEBI:78454; Evidence={ECO:0000256|ARBA:ARBA00023357}; PhysiologicalDirection=left...
null
null
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|ARBA:ARBA00005194}.
null
null
Acetylation;Fatty acid biosynthesis;Fatty acid metabolism;Hydrolase;Lipid biosynthesis;Lipid metabolism;Lyase;Multifunctional enzyme;NAD;NADP;Phosphopantetheine;Phosphoprotein;Proteomics identification;Pyridoxal phosphate;Reference proteome;S-nitrosylation;Transferase
fatty acid biosynthetic process [GO:0006633]
cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]
(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransfer...
null
null
null
IPR029058;IPR001227;IPR036736;IPR014043;IPR016035;IPR013149;IPR049391;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;IPR013217;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049552;IPR020843;IPR013968;IPR049900;IPR020806;IPR009081;IPR006162;IPR029063;IPR001031;IPR016039;
3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150;
A0A0U1ZFN5
MAGNVKKSSGAGGSGSGGSGAGGLIGLMKDAFQPHHHHHHHLSPHPPCTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTVLSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHN...
Rattus norvegicus (Rat)
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. {ECO:0000256|RuleBase:RU367001}.
2.3.2.27
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:0000256|ARBA:ARBA00000900, ECO:0000256|RuleBase:RU367001};
null
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367001}.
null
null
Calcium;Metal-binding;Proteomics identification;Reference proteome;Repeat;Transferase;Ubl conjugation pathway;Zinc;Zinc-finger
cell surface receptor signaling pathway [GO:0007166]; cellular response to hypoxia [GO:0071456]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; DNA damage response [GO:0006974]; male gonad development [GO:0008584]; mast cell deg...
axon [GO:0030424]; cilium [GO:0005929]; flotillin complex [GO:0016600]; Golgi apparatus [GO:0005794]; growth cone [GO:0030426]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; ephrin receptor binding [GO:0046875]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; phosphotyrosine residue binding [GO:0001784]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782]; receptor tyrosine kinase binding [GO:0030971]; S...
null
null
DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent S...
IPR024162;IPR014741;IPR036537;IPR003153;IPR014742;IPR024159;IPR011992;IPR036860;IPR015940;IPR009060;IPR018957;IPR001841;IPR013083;IPR017907;
1.20.930.20;1.10.8.10;1.10.238.10;3.30.505.10;3.30.40.10;
A0A0U3BRC5
MSHCTIFLYKYFPGKPRYQHCSFLHPLNHKLKSLFLPITGSRFLSNSTFSVSDSAHSHQAKPHVRNAQFDFKAYMLEKITAVNQALDAALPVREPVKIHEAMRYSLLLGGKRICPIVCLAACHLVGGDESTAMPSAAALEMIHAMSLMHDDLPCMDNDDLRRGRPSNHVVFGEGATVLAGYALIARAFEHIATATQGVGPGKILRVIGELAQLIGAEGVVGGQVVDLRCGGEGQMAIGLEQLEYIHLHKTAASVEASAVAGAVLGGASEEEIERLRKYSRSAGLLFQVVDDILDVTKSSEELGKTAGKDLAAGKTTYPKL...
Leucosceptrum canum (Hairy white-wand) (Clerodendron leucosceptrum)
FUNCTION: Involved in the biosynthesis of leucosceptrane sesterterpenoids natural products, which are playing defensive roles toward herbivorus insects (e.g. Spodoptera exigua) (PubMed:26941091). Catalyzes the condensation of isopentenyl pyrophosphate (IDP) with the allylic pyrophosphates to yield geranylfarnesyl dipho...
2.5.1.81
CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; EC=2.5.1.81; Evidence={ECO:0000269|PubMed:26941091}; Physiological...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14324}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34.89 uM for dimethylallyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=3.04 uM for isopentenyl diphosphate (in the presence of geranylgeranyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=6.28 uM for geranyl diphospha...
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30468448}.; PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:26941091}.
null
null
Chloroplast;Isoprene biosynthesis;Magnesium;Metal-binding;Plastid;Transferase;Transit peptide
response to herbivore [GO:0080027]; response to insect [GO:0009625]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; terpenoid biosynthetic process [GO:0016114]
chloroplast [GO:0009507]
farnesyltranstransferase activity [GO:0004311]; geranylfarnesyl diphosphate synthase activity [GO:0044687]; metal ion binding [GO:0046872]; transferase activity [GO:0016740]
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:26941091}.
null
null
IPR008949;IPR000092;IPR033749;
1.10.600.10;
A0A125QXJ1
MVTVGNYCEAEGPLGPAWAQNGLSPCFFFTLVPSTLMALGALALVLVLPCRRRDVPSGTEELFWAADSRVAPYALQLFLATLQVALPLAGLAGRVGTARGVRLPGYLLLASMLGSLASACGLWLLVAERRQARQSLAMGVWMKFRHSSGLLLLWTVAFAAENLALVSWNSPQWWWARADLGQQVQFGLWVLRYVISGGLFILGLWAPGLRPQSYTLRVHEADQDVERNQAQSTDRTSTWRDLGRKLRLLSSYLWPRGSPALQFIVLICLGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGT...
Mesocricetus auratus (Golden hamster)
FUNCTION: ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen. May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, in turn may parti...
7.6.2.5
CATALYTIC ACTIVITY: Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate; Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344, ChEBI:CHEBI:456216; EC=7.6.2.5; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; ...
null
null
null
null
null
ATP-binding;Cell membrane;Disulfide bond;Endoplasmic reticulum;Endosome;Glycoprotein;Golgi apparatus;Lysosome;Membrane;Mitochondrion;Mitochondrion outer membrane;Nucleotide-binding;Reference proteome;Secreted;Translocase;Transmembrane;Transmembrane helix;Transport
cellular detoxification of cadmium ion [GO:0098849]; heme metabolic process [GO:0042168]; heme transmembrane transport [GO:0035351]; porphyrin-containing compound metabolic process [GO:0006778]
early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; melanosome membrane [GO:0033162]; mitochondrial outer membrane [GO:0005741...
ABC-type heme transporter activity [GO:0015439]; ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; heme binding [GO:0020037]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}....
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NP58}.
DOMAIN: Contains two independently folding units, the N-terminal transmembrane domain (residues 1-205) and the ABC-core domain (206-842) are respectively responsible for the lysosomal targeting and the ATPase activity. {ECO:0000250|UniProtKB:Q9NP58}.
IPR003593;IPR011527;IPR036640;IPR003439;IPR017871;IPR032410;IPR027417;IPR039421;
1.20.1560.10;3.40.50.300;
A0A126GUP6
MEPHFFFTVLWMLLMGTSSTYAQEIFGYCRTPDENSGTCINLRECGYLFELLQSEEVTEQDRRFLQASQCGYRNGQVLEKHFCFTNVQICCANSRMRNQQPQWGNHPQPTQTTKPTKRSGTKLLPMAPNCGENFGDRVVGGNETTKREFPWMALIEYTKPGNVKGHHCGGSLINHRYVLTAAHCVSAIPSDWELTGVRLGEWDASTNPDCTVGKNGRRDCNEPYVDYPVEERIPHPQYPGNSRDQLNDIALLRLRDEVQYSDFILPVCLPTLASQHNNIFLGRKVVVAGWGRTETNFTSNIKLKAELDTVPTSECNQRYA...
Drosophila melanogaster (Fruit fly)
FUNCTION: Serine protease which plays an essential role in the melanization immune response by acting downstream of sp7 to activate prophenoloxidase (PPO1) (PubMed:16861233). May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A in the hemol...
3.4.21.-
null
null
null
null
null
null
Alternative splicing;Calcium;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Serine protease;Signal;Zymogen
melanization defense response [GO:0035006]; proteolysis [GO:0006508]; response to fungus [GO:0009620]; Toll receptor ligand protein activation cascade [GO:0160032]
null
endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; serine hydrolase activity [GO:0017171]; serine-type endopeptidase activity [GO:0004252]
null
null
DOMAIN: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure. {ECO:0000255|PROSITE-ProRule:PRU01236}.
IPR022700;IPR038565;IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;IPR033116;
3.30.1640.30;2.40.10.10;
A0A126GV13
MAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLASGRKLTIGSKRPVNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGPSGSGASTPVVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLS...
Drosophila melanogaster (Fruit fly)
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Inv...
5.6.1.1
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000256|ARBA:ARBA00036378, ECO:0000256|HAMAP-Rule:MF_03021};
null
null
null
null
null
ATP-binding;Cell cycle;Cell division;Chromosome;Cytoplasm;Cytoskeleton;Developmental protein;Differentiation;Hydrolase;Isomerase;Lipid droplet;Membrane;Microtubule;Mitosis;Neurogenesis;Nucleotide-binding;Reference proteome
adult locomotory behavior [GO:0008344]; cell differentiation [GO:0030154]; cell division [GO:0051301]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; nervous system development [GO:0007399]; positive regulation of microtubule de...
centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; spindle [GO:0005819]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
SUBCELLULAR LOCATION: Membrane {ECO:0000256|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000256|HAMAP-...
null
null
IPR003593;IPR041569;IPR003959;IPR003960;IPR007330;IPR036181;IPR027417;IPR015415;IPR017179;
1.10.8.60;3.40.50.300;1.20.58.80;
A0A139WFS2
MVIAKKITINNRFDGMPKPSDFKTIEEELPPLKPGEFLAEAVFLSVDPYMRAYAHNIPLGATMVGSQVAKIIESRNDKYPVGKHVVGKFDWRSHTISSGLPTVIQGAGNAPAPYLVPDLGNLPMSYLLGVLGMPGSTAYFGFLDICKPKNGEVVAVSGAAGAVGSIVGQIAKIEGCKVVGITGSEDKGRFLVDGLGFDGFVNYKTDDVAKKLDQLVPEGIDCYFDNVAGEISSTVIGHMRDYGFVGPFRPTTMMWKTRPENYLYQERSGEAFQQILKWLQAGRMKYHETITKGFDNMVAAFIEMLQGKNLGKAIVKVAKS...
Tribolium castaneum (Red flour beetle)
null
1.3.1.48; 1.3.1.74
CATALYTIC ACTIVITY: Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974, ChEBI:CHEBI:133975; Evidence={ECO:0000256|ARBA:ARBA00023...
null
null
null
null
null
Fatty acid metabolism;Hydroxylation;Lipid metabolism;Oxidoreductase;Prostaglandin metabolism;Reference proteome
prostaglandin metabolic process [GO:0006693]
cytoplasm [GO:0005737]
13-prostaglandin reductase activity [GO:0036132]; 15-oxoprostaglandin 13-oxidase activity [GO:0047522]; 2-alkenal reductase [NAD(P)+] activity [GO:0032440]
null
null
null
IPR013149;IPR041694;IPR011032;IPR045010;IPR036291;IPR020843;IPR014190;
3.90.180.10;3.40.50.720;
A0A140LIF8
MEEAVESPEVKEFEYFSDAVFIPKDGNTLSVGVIKRIETAVKEGEVVKVVSIVKEIIQNVSRNKIKIAVTGDSGNGMSSFINALRLIGHEEKDSAPTGVVRTTQKPTCYFSSHFPYVELWDLPGLGATAQSVESYLEEMQISIYDLIIIVASEQFSLNHVKLAITMQRMRKRFYVVWTKLDRDLSTSTFPEPQLLQSIQRNIRDSLQKEKVKEHPMFLVSVFKPESHDFPKLRETLQKDLPVIKYHGLVETLYQVCEKTVNERVESIKKSIDEDNLHTEFGISDPGNAIEIRKAFQKTFGLDDISLHLVALEMKNKHFNT...
Mus musculus (Mouse)
FUNCTION: Immunity-related GTPase that plays important roles in innate immunity and inflammatory response (PubMed:17641048, PubMed:33124745, PubMed:33124769, PubMed:34078740, PubMed:34338548). Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes...
3.6.5.-
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:34078740}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:34078740}...
null
null
null
null
null
Cytoplasm;Cytoplasmic vesicle;Golgi apparatus;GTP-binding;Hydrolase;Immunity;Innate immunity;Membrane;Nucleotide-binding;Reference proteome;Ubl conjugation
cellular response to interferon-beta [GO:0035458]; defense response [GO:0006952]; defense response to protozoan [GO:0042832]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]; negative regulation of non-canonical inflammasome complex assembly [GO:0160076]; protein targeting to vacu...
cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; vacuolar membrane [GO:0005774]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:34078740}. Golgi apparatus membrane {ECO:0000269|PubMed:34078740}. Cytoplasm, cytosol {ECO:0000269|PubMed:34078740}. Note=Localizes to parasitophorous vacuole membranes. {ECO:0000269|PubMed:34078740}.
PTM: Ubiquitinated; polyubiquitinated in the cytosol, promoting Gbp1 recruitment to the T.gondii parasitophorous vacuole membranes. {ECO:0000269|PubMed:34078740}.
null
IPR030385;IPR007743;IPR027417;
3.40.50.300;
A0A140T892
MLVLERCDLELEANGRDHHTADLCRERLVVRRGQPFWLTLHFEGRNYEASVDSLTFCAVTGPDPSEEAGTKALFRLSDATEEGAWAAVAADQRDSTLSLHLSTPANAPVGHYRLSLEASTGYQGSSFMLGQFTLLFNSWCPADAVYLDSDEERQEYVLTQQGFIYQGSAKFIKNIPWNFGQFEEGILDICLMLLDVNPKFLRNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGRWDNNYADGISPMSWIGSVDILRRWKRDGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEFGEI...
Bos taurus (Bovine)
null
2.3.2.13; 3.5.1.44
CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline + L-glutaminyl-[protein] = 5-(R)-noradrenalinyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66560, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17054, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011, ChEBI:CHEBI:72587, ChEBI:CHEBI:167178; Evidence={ECO:0000256|ARBA:ARBA00036051}; Physiolog...
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR000459-2}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000459-2};
null
null
null
null
Acyltransferase;Calcium;Cell membrane;Chromosome;Extracellular matrix;GTP-binding;Hydrolase;Membrane;Metal-binding;Mitochondrion;Nucleotide-binding;Nucleus;Protease;Proteomics identification;Reference proteome;Secreted;Transferase
proteolysis [GO:0006508]
chromosome [GO:0005694]; collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
GTP binding [GO:0005525]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; protein-glutamine gamma-glutamyltransferase activity [GO:0003810]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Chromosome {ECO:0000256|ARBA:ARBA00004286}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted, extracellular s...
null
null
IPR013783;IPR014756;IPR038765;IPR002931;IPR036985;IPR023608;IPR013808;IPR008958;IPR036238;IPR001102;
2.60.40.10;3.90.260.10;
A0A140T8D4
MIWEVTVLLSLVLGTGAVPLEDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIVHRNGIPDEQIIVMMYDDIANSEDNPTPGIVINRPNGSDVYQGVLKDYTGEDVTPKNFLAVLRGDAEAVKGVGSGKVLKSGPRDHVFVYFTDHGATGILVFPNEDLHVKDLNETIRYMYEHKMYQKMVFYIEACESGSMMNHLPPDINVYATTAANPRESSYACYYDEQRSTFLGDWYSVNWMEDSDVEDLTKETLHKQYQLVKSHTNTSHVMQYGNKSISAMKLMQFQGLKHQASSPISLPAVSRLDLTPSPEVPLSIMKRKLM...
Bos taurus (Bovine)
null
3.4.22.34
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.; EC=3.4.22.34; Evidence={ECO:0000256|ARBA:ARBA00000810};
null
null
null
null
null
Hydrolase;Protease;Reference proteome;Signal;Thiol protease;Zymogen
antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; associative learning [GO:0008306]; cellular response to amyloid-beta [GO:1904646]; cellular response to calcium ion [GO:0071277]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; dendritic spine organizat...
apical part of cell [GO:0045177]; extracellular region [GO:0005576]; late endosome [GO:0005770]; lysosomal lumen [GO:0043202]; perinuclear region of cytoplasm [GO:0048471]
cysteine-type endopeptidase activity [GO:0004197]; endopeptidase activator activity [GO:0061133]
null
null
null
IPR043577;IPR048501;IPR046427;IPR001096;
1.10.132.130;3.40.50.1460;
A0A140TAB8
MKSGSGGGSPTSLWGLVFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGFLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTIDWSLILDAVSNNYIVGNKPPKECGDLCPGTLEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSVCGKRACTENNECCHPECLGSCHTPDDNTTCVACRHYYYKGVCVPACPPGTYRFEGWRCVDRDFCANIPNAESSDSDGFVIHDGECMQECPSGFIRNSTQSMY...
Rattus norvegicus (Rat)
null
2.7.10.1
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:0000256|ARBA:ARBA00001171, ECO...
null
null
null
null
null
ATP-binding;Cleavage on pair of basic residues;Glycoprotein;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase
amyloid-beta clearance [GO:0097242]; cellular response to amyloid-beta [GO:1904646]; cellular response to glucose stimulus [GO:0071333]; immune response [GO:0006955]; negative regulation of apoptotic process [GO:0043066]; negative regulation of MAPK cascade [GO:0043409]; phosphorylation [GO:0016310]; positive regulatio...
alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; axon [GO:0030424]; insulin receptor complex [GO:0005899]; intracellular membrane-bounded organelle [GO:0043231]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; insulin binding [GO:0043559]; insulin receptor activity [GO:0005009]; insulin receptor binding [GO:0005158]; insulin receptor substrate binding [GO:0043560]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor receptor activity ...
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
null
null
IPR003961;IPR036116;IPR006211;IPR006212;IPR009030;IPR013783;IPR011009;IPR000719;IPR017441;IPR000494;IPR036941;IPR001245;IPR008266;IPR020635;IPR016246;IPR002011;
2.60.40.10;3.80.20.20;1.10.510.10;
A0A140TAU9
MWELLAFLLLAIAYFFRPKVKCPGAKYPKSLPYLPLVGSLPFLPRHGHPHVNFFKLQKKYGPIYSLRMGTKTTVMVGHYQLAKEVLIKKGKEFSGRPQVATLNILSDNQKGVAFADHGAPWQLHRKLVRAAFALFKDGNQKLEKIICHETSLLCDLLATQNGQTIDLSSPLFLAVTNVICWICFNSSYMKGDPALETMQNYHKGILETLEKDNVVDIFPALKIFPNKSLEKMRHCVNIRNELLSKIFEKHKENFNSDSITSMLDLLIQAKKNSDNNNTGPDQDSKLLSDKHILATIGDIFGAGVETTTSVVKWIVAFLLH...
Equus caballus (Horse)
null
1.14.14.19; 1.14.14.32
CATALYTIC ACTIVITY: Reaction=16alpha,17alpha-dihydroxypregnenolone + O2 + reduced [NADPH--hemoprotein reductase] = 3beta,16alpha-dihydroxy-androst-5-en-17-one + acetate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53224, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CH...
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|ARBA:ARBA00001971, ECO:0000256|PIRSR:PIRSR602401-1};
null
PATHWAY: Hormone biosynthesis. {ECO:0000256|ARBA:ARBA00004972}.; PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis. {ECO:0000256|ARBA:ARBA00043954}.; PATHWAY: Steroid hormone biosynthesis. {ECO:0000256|ARBA:ARBA00025710}.
null
null
Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Signal;Steroidogenesis
hormone biosynthetic process [GO:0042446]; progesterone metabolic process [GO:0042448]; steroid biosynthetic process [GO:0006694]
endoplasmic reticulum membrane [GO:0005789]
17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid 17-alpha-monooxygenase activity [GO:0004508]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}. Membrane {ECO:0000256|ARBA:ARBA00004370}. Microsome membrane {ECO:0000256|ARBA:ARBA00004524}.
null
null
IPR001128;IPR017972;IPR002401;IPR036396;
1.10.630.10;
A0A140VJG8
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
Homo sapiens (Human)
FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. {ECO:0000256|ARBA:ARBA00003256}.
2.1.1.6
CATALYTIC ACTIVITY: Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53092, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:89268; Evidence={ECO:0000256|ARBA:ARBA00001894}; Phys...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRNR:PIRNR037177, ECO:0000256|PIRSR:PIRSR037177-3}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRNR:PIRNR037177, ECO:0000256|PIRSR:PIRSR037177-3};
null
null
null
null
Catecholamine metabolism;Magnesium;Metal-binding;Methyltransferase;Neurotransmitter degradation;S-adenosyl-L-methionine;Transferase
artery development [GO:0060840]; behavioral fear response [GO:0001662]; cellular response to cocaine [GO:0071314]; cellular response to phosphate starvation [GO:0016036]; cerebellar cortex morphogenesis [GO:0021696]; cholesterol efflux [GO:0033344]; detection of temperature stimulus involved in sensory perception of pa...
axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; synapse [GO:0045202]; vesicle [GO:0031982]
catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; magnesium ion binding [GO:0000287]; orcinol O-methyltransferase activity [GO:0102938]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004228}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004228}; Extracellular side {ECO:0000256|ARBA:ARBA00004228}.
null
null
IPR017128;IPR029063;IPR002935;
3.40.50.150;
A0A140VJL2
MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLPWDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYDFYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIFHTPFCKMVQKSLARLMFNDF...
Homo sapiens (Human)
FUNCTION: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. {ECO:0000256|RuleBase:RU364071}.; FUNCTION: Catalyzes the first irreversible step in ketogenesis, condensing acetyl-CoA to acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate. {ECO:00002...
2.3.3.10
CATALYTIC ACTIVITY: Reaction=acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+); Xref=Rhea:RHEA:10188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43074, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.10; Evidence={ECO:0000256|ARBA:ARBA00001222}; PhysiologicalDi...
null
null
PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3. {ECO:0000256|ARBA:ARBA00005218, ECO:0000256|RuleBase:RU364071}.
null
null
Acetylation;Cholesterol biosynthesis;Cholesterol metabolism;Lipid biosynthesis;Lipid metabolism;Mitochondrion;Phosphoprotein;Steroid biosynthesis;Steroid metabolism;Sterol biosynthesis;Sterol metabolism;Transferase;Transit peptide
acetyl-CoA metabolic process [GO:0006084]; adipose tissue development [GO:0060612]; cellular response to amino acid stimulus [GO:0071230]; cellular response to fatty acid [GO:0071398]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to insulin stimulus [GO:0032869]; cellular response to lip...
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
hydroxymethylglutaryl-CoA synthase activity [GO:0004421]
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
null
null
IPR000590;IPR013746;IPR013528;IPR010122;IPR016039;
3.40.47.10;
A0A140VJL3
MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA
Homo sapiens (Human)
FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway. {ECO:0000256|ARBA:ARBA00025301}.
2.4.2.8
CATALYTIC ACTIVITY: Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8; Evidence={ECO:0000256|RuleBase:RU364099};
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|RuleBase:RU364099};
null
PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1. {ECO:0000256|ARBA:ARBA00004669, ECO:0000256|RuleBase:RU364099}.
null
null
Cytoplasm;Glycosyltransferase;Magnesium;Metal-binding;Nucleotide-binding;Purine salvage;Transferase
adenine metabolic process [GO:0046083]; AMP salvage [GO:0044209]; central nervous system neuron development [GO:0021954]; cerebral cortex neuron differentiation [GO:0021895]; dendrite morphogenesis [GO:0048813]; dopamine metabolic process [GO:0042417]; dopaminergic neuron differentiation [GO:0071542]; GMP salvage [GO:0...
cytosol [GO:0005829]
guanine phosphoribosyltransferase activity [GO:0052657]; hypoxanthine phosphoribosyltransferase activity [GO:0004422]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364099}.
null
null
IPR005904;IPR000836;IPR029057;
3.40.50.2020;
A0A140VK13
MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDTIRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMYLSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNPAKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKARHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWAELRQKLMSSGNEESLRKVDS...
Homo sapiens (Human)
null
2.3.1.21
CATALYTIC ACTIVITY: Reaction=(5Z)-tetradecenoyl-CoA + (R)-carnitine = CoA + O-(5Z)-tetradecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44852, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:84649, ChEBI:CHEBI:84650; Evidence={ECO:0000256|ARBA:ARBA00035780}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + (R)-carnitine =...
null
null
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000256|ARBA:ARBA00005005}.
null
null
Acyltransferase;Fatty acid metabolism;Lipid metabolism;Membrane;Mitochondrion;Mitochondrion inner membrane;Transferase;Transport
fatty acid beta-oxidation [GO:0006635]; in utero embryonic development [GO:0001701]; positive regulation of cold-induced thermogenesis [GO:0120162]
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
carnitine O-palmitoyltransferase activity [GO:0004095]
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
null
null
IPR000542;IPR042572;IPR023213;IPR039551;IPR042231;
1.20.1280.180;3.30.559.10;1.10.275.20;3.30.559.70;
A0A142ZC57
MKYTDFLAHPDEIIPTIRMMYADYRLKNMEIKDPSVRFCYNMLNRVSRSFAMVIQQLPVELRDATCVFYLILRALDTVEDDMAIPKEVKIPMLRTFHEHLSDRSWKIKCGYGPYVDLMDNYPLVTDVYLRFDEGTKAVIKDITRRMGNGMADFIDLDEVLTIPQYDLYCHYVAGLCGIGMCKLFVDSGLEKEDLVAEEDLANQMGLFLQKNNIVRDYLEDINELPAPRMFWPKEIWGNYAKQLDEFKDPKNLDKAMLCLNHMVTDALRHCEVGLRSLSLLHNPNILRAVLIPQVMGVRTLTLVYNNPEVFRGVVKMRRGE...
Botryococcus braunii (Green alga)
FUNCTION: Converts the C20 geranylgeranyl diphosphate (GGPP) to the C40 lycopaoctaene, the first committed intermediate in the production of lycopadiene (PubMed:27050299, PubMed:28813599). Converts farnesyl diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in eukaryotes (PubMed:27050299, PubMed:28813...
2.5.1.148; 2.5.1.21
CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000269|PubMed:27050299}; CATALYTIC ACTIVITY:...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P37268};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for geranylgeranyl diphosphate {ECO:0000269|PubMed:27050299}; KM=0.13 mM for farnesyl diphosphate {ECO:0000269|PubMed:27050299}; KM=0.11 mM for phytil diphosphate {ECO:0000269|PubMed:27050299};
null
null
null
Magnesium;Membrane;Metal-binding;NAD;NADP;Transferase;Transmembrane;Transmembrane helix
cholesterol biosynthetic process [GO:0006695]; ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate metabolic process [GO:0045338]; sterol biosynthetic process [GO:0016126]
endoplasmic reticulum membrane [GO:0005789]
farnesyl-diphosphate farnesyltransferase activity [GO:0004310]; farnesyltranstransferase activity [GO:0004311]; metal ion binding [GO:0046872]; squalene synthase activity [GO:0051996]
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
null
null
IPR008949;IPR002060;IPR006449;IPR019845;IPR044844;IPR033904;
1.10.600.10;
A0A143RHU3
MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVEQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEEMMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFPEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEV...
Felis catus (Cat) (Felis silvestris catus)
null
2.7.11.1
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:0000256|ARBA:ARBA00001433}; CATALYT...
null
null
null
null
null
ATP-binding;Carbohydrate metabolism;Glucose metabolism;Glycogen biosynthesis;Kinase;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Sugar transport;Transferase;Transport
activation-induced cell death of T cells [GO:0006924]; apoptotic mitochondrial changes [GO:0008637]; behavioral response to pain [GO:0048266]; canonical NF-kappaB signal transduction [GO:0007249]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to cadmium ion [GO:0071276]; cellular res...
cell-cell junction [GO:0005911]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; spindle [GO:0005819]; vesicle [GO:0031982]
14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; nitric-oxide synthase regulator activity [GO:0030235]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; potassium channel activator activity [GO:00991...
null
null
null
IPR000961;IPR034676;IPR011009;IPR011993;IPR001849;IPR039026;IPR017892;IPR000719;IPR017441;IPR008271;
2.30.29.30;1.10.510.10;
A0A143ZZK9
MSSQNNNKQGGQDINNKKDSDDIKPSVSKEDLINSLKNDELNKNTTMDQNDMKKNENMNIKKNEVLNNSNNVEDGDNENSKFMNKSKEGLNNINGEKNDDNNSIVKVEESPKSIGYNYYASESIENLCKEFGLESINTGLNSEQVKINRDKYGENFIEKDEVVPVWLIFLSQYCSPVVLLLLVAAVASLALNEVVEGVAIISIVTLNACLATYMEKSSGDAIGKLAEMASPQCTVLRNGQKVVIPSREVVVGDVVLINTGDSISADLRLFDVIELKTNESLLTGESEDIKKTIVADNLSTPFATNLCFATTSVTSGSGKG...
Plasmodium falciparum (isolate 3D7)
FUNCTION: Sodium-exporting ATPase (PubMed:23414762, PubMed:29986883, PubMed:31311978, PubMed:36180431). Required for the extrusion of Na(+) from the intraerythrocytic parasites to maintain a low cytosolic concentration of Na(+) (PubMed:23414762, PubMed:25322084, PubMed:25453091, PubMed:29555632, PubMed:36180431). {ECO:...
7.2.2.3
CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:29986883, ECO:0000269|P...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for ATP (in the presence of 150-153 mM of Na(+)) {ECO:0000269|PubMed:29986883}; KM=16.1 mM for Na(+) {ECO:0000269|PubMed:29986883};
null
null
null
ATP-binding;Cell membrane;Hydrolase;Ion transport;Membrane;Nucleotide-binding;Reference proteome;Sodium;Sodium transport;Translocase;Transmembrane;Transmembrane helix;Transport
calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; manganese ion transport [GO:0006828]
endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
ABC-type sodium transporter activity [GO:0140679]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type calcium transporter activity [GO:0005388]; P-type sodium transporter activity [GO:0008554]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20813948, ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:29986883, ECO:0000269|PubMed:8813672}; Multi-pass membrane protein {ECO:0000255}.
null
null
IPR006068;IPR004014;IPR023299;IPR018303;IPR023298;IPR008250;IPR036412;IPR023214;IPR001757;IPR044492;
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
A0A144A134
MKNLDINTFDNIEDIPLGSSEQDPYDFFTLSDRNVMNSDMKKNIVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEMFIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPPTFNEVRHILNLAQILSLEEGLDLLTFDADETLYPDGHDFNDEVLASYISCLLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMGGESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVIKDFGLCAQIQRKEKSIGLVPNKIPSLN...
Plasmodium falciparum (isolate 3D7)
FUNCTION: Specifically, catalyzes the dephosphorylation of inosine monophosphate (IMP) into inosine (PubMed:32591529). By dephosphorylating IMP, plays a role in the purine salvage pathway (PubMed:32591529). Does not have phosphotransferase activity with IMP as phosphate donor and adenosine as phosphate acceptor (PubMed...
3.1.3.99
CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000269|PubMed:32591529};
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32591529};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 mM for IMP (at pH 5, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=66 mM for IMP (at pH 8, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=6.8 mM for IMP (at pH 8, 25 degrees Celsius and in the ...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5. {ECO:0000269|PubMed:32591529};
null
3D-structure;Allosteric enzyme;ATP-binding;Cytoplasm;Hydrolase;Magnesium;Metal-binding;Nucleotide metabolism;Nucleotide-binding;Reference proteome
IMP catabolic process [GO:0006204]; inosine salvage [GO:0006190]; nicotinamide riboside biosynthetic process [GO:0071590]; nicotinic acid riboside biosynthetic process [GO:0071592]
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; IMP 5'-nucleotidase activity [GO:0050483]; magnesium ion binding [GO:0000287]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32591529}.
null
null
IPR036412;IPR023214;IPR009453;
3.40.50.1000;
A0A144A2H0
MQLNFLLFVFIFLMVFHLNIFNKGKRQNLVSAYLNHFKKSYFSGVTSGSDCVNKSEVSSDNNNNNNNNNNKIAHNFFSKKYQRNFENNNLSENQENNKNIIYSGSNIFKNIYNTEMMSNNNTVDVNMMDNNPAARLEELRTIMKKNKIDVYILINSDEHNSEIINEKDKKIVKITNYSGADGILIVTKDKPILYVNALYELQAMNELDQNLFTLRISRIDNRDEIFETISSLEFNTIAFDGKNTSVVFYEKLRKALLNAYPKKKIVEKIIYNNNFDDVNKKDDENVLNFLVLEKSLVEIKDYPVNNKTLYIHDRKYNGAC...
Plasmodium falciparum (isolate 3D7)
FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides (PubMed:17895246, PubMed:19574214, PubMed:27462122). In the food vacuole, involved in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides (PubMed:17895246, PubMed:19574214). In the cytop...
3.4.11.9
CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214, ECO:0000269|PubMed:27462122};
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19574214}; Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000269|PubMed:27462122};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.51 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=0.86 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 5.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=1.4 mM for human hemogl...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 (PubMed:19574214). Active at pH 5.5-7.5 (PubMed:19574214). {ECO:0000269|PubMed:19574214};
null
3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome;Signal;Vacuole
hemoglobin catabolic process [GO:0042540]; proteolysis [GO:0006508]
cytoplasm [GO:0005737]; food vacuole [GO:0020020]; vacuolar lumen [GO:0005775]
manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]
SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. Cytoplasm {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. Note=Localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:1...
PTM: The N-terminus may be proteolytically cleaved to generate a 73-kDa mature form. {ECO:0000269|PubMed:19574214}.
null
IPR029149;IPR036005;IPR000587;IPR000994;IPR033740;IPR032416;IPR001131;
3.90.230.10;3.40.350.10;
A0A163UT06
MNIKHNYISYFQMNGIQIPGISNPEAIIPITGEKKSYKLVLDFNDGAISIIEARYLDSKLHREIQDLSDNDVTILGTEISDGAYDENLDIHCDKCNKFYRPYCRLHPLFKIPDRVLKRDESSNLSFSQQTLPILFRIEESKLPNAGLGVIAEVFIPVGMVFGPYKGRRCQKKTDFYKDGYAWLIKSGDKRFYIDGSDAERSNWLRYINSPRFEDEQNMLAFQTNGKIFYRVIKPIRINQELLVWYGSSYGNEFVESENGNKYKKPAKNPFICVGAQR
Caenorhabditis elegans
FUNCTION: Histone methyltransferase that specifically mono- and di-methylates 'Lys-4' of histone H3 in vitro (PubMed:24685137). Does not tri-methylate 'Lys-4' of histone H3 in vitro (PubMed:24685137). Promotes spermatid development and fertility by positively regulating the transcription of spermatocyte-specific genes ...
2.1.1.-; 2.1.1.364
CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:...
null
null
null
null
null
Alternative splicing;Methyltransferase;Nucleus;Reference proteome;S-adenosyl-L-methionine;Transferase
methylation [GO:0032259]; oligodendrocyte development [GO:0014003]; regulation of DNA-templated transcription [GO:0006355]
nucleus [GO:0005634]
histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 monomethyltransferase activity [GO:0140945]
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29702639}. Note=In males and hermaphrodites, localizes to foci in the nucleus of spermatocytes, which express the mono- and di-methyl states of 'Lys-4' of histone H3 (PubMed:29702639). These foci are stable nuclear structures with slow diffusion and liquid-like properti...
null
null
IPR044417;IPR001214;IPR046341;
2.170.270.10;
A0A166U5H3
MAGMKTSPSQDEEACVLAIQLATSTVLPMILKSAIELDILNTISKAGPGNYLSPSDLASKLLMSNPHAPIMLERILRVLATYKVLGCKPSELSDGEVEWLYCWTPVCKFLSNNEDGASIAPLLLVHQDQVPMKSWYHLTDAILDGGTAFNKAYGMNIFDYASQDPQFNKVFNRSMAGHSTITMKKILETYNGFEGLKSIVDVGGGSGATLNMIISKYPTIKGINFDLPHVVGDSPIHPGVEHVGGDMFASVPKGDAIFLKWIFHSWSDEDCLRILKNCYEALADNKKVIVAEFIIPEVPGGSDDATKSVVHLDAVMLAYV...
Kitagawia praeruptora (Peucedanum praeruptorum)
FUNCTION: O-methyltransferase involved in the biosynthesis of furocoumarins natural products such as bergapten, a photosensitizer used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses (PubMed:27252733, PubMed:30934718, PubMed:31666994). Cat...
2.1.1.69
CATALYTIC ACTIVITY: Reaction=bergaptol + S-adenosyl-L-methionine = bergapten + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11808, ChEBI:CHEBI:18293, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77728; EC=2.1.1.69; Evidence={ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}; Physi...
null
null
PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.; PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.
null
null
3D-structure;Cytoplasm;Methyltransferase;S-adenosyl-L-methionine;Transferase
aromatic compound biosynthetic process [GO:0019438]; coumarin biosynthetic process [GO:0009805]; methylation [GO:0032259]; response to jasmonic acid [GO:0009753]
cytoplasm [GO:0005737]
5-hydroxyfuranocoumarin 5-O-methyltransferase activity [GO:0030752]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27252733}.
null
null
IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;
3.40.50.150;1.10.10.10;
A0A172J1V3
MTENNRAGAVPLSSILLQMITGYWVTQSLYVAAKLGIADLVADAPKPIEELAAKTGAKAPLLKRVLRTIASIGVFTETEPGIFGITPLAALLRSGTPDSMRPQAIMHGEEQYRAWADVLHNVQTGETAFEKEFGTSYFGYLAKHPEADRVFNEAQAGYTKQVAHAVVDAYDFSPFKTVIDIGAGYGPLLSAILRSQPEARGILFDQPHVAQAAGKRLAEAGVGDRCGTVGGDFFVEVPADGDVYILSLLLHDWDDQRSIEILRNCRRAMPAHGKLLIVELVLPEGEEPFFGKWLDLHMLVLLGAQERTADEFKTLFAASG...
Lysobacter antibioticus
FUNCTION: Involved in the biosynthesis of phenazine natural products including myxin, an N(5),N(10)-dioxide phenazine antiobiotic, which has antimicrobial activity. O-methyltransferase, which converts iodinin (1,6-dihydroxyphenazine N(5),N(10)-dioxide) to myxin (1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide). Catalyz...
2.1.1.-
CATALYTIC ACTIVITY: Reaction=1,6-dihydroxyphenazine + S-adenosyl-L-methionine = 1-hydroxy-6-methoxyphenazine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72523, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192365, ChEBI:CHEBI:192366; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDir...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.6 uM for 6-hydroxy-1-methoxyphenazine N(5)-oxide (at pH 7.8 and at room temperature) {ECO:0000269|PubMed:29510028}; Vmax=2.9 umol/min/mg enzyme with 6-hydroxy-1-methoxyphenazine N(5)-oxide as substrate (at pH 7.8 and at room temperature) {ECO:0000269|PubMed:2951...
null
null
null
3D-structure;Methyltransferase;S-adenosyl-L-methionine;Transferase
methylation [GO:0032259]; phenazine biosynthetic process [GO:0002047]
null
identical protein binding [GO:0042802]; O-methyltransferase activity [GO:0008171]; protein homodimerization activity [GO:0042803]; S-adenosyl-L-methionine binding [GO:1904047]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]
null
null
DOMAIN: Contains an N-terminal dimerization domain. The C-terminal region contains the S-adenosyl-L-methionine binding site. {ECO:0000305|PubMed:29510028}.
IPR031725;IPR016461;IPR001077;IPR029063;IPR036388;IPR036390;
3.40.50.150;1.10.10.10;
A0A193AU77
MGSESLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNIGEEPSPIGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKEVIPRMIKKNEEQNRPVSCLINNPFIPWVSDVAESLGLPSAMLWVQSCACFAAYYHYYHGLVPFPSESAMEIDVQLPCMPLLKHDEVPSFLYPTTPYPFLRRAIMGQYKNLDKPFCVLMDTFQELEHEIIEYMSKICPIKTVGPLFKNPKAPNANVRGDFMKADDCISWLDSKPPASVVYVSFGSVVYLKQDQWDEIAFGLLNSGLNFLWVMKPPHKDSGYQ...
Punica granatum (Pomegranate)
FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinna...
2.4.1.120; 2.4.1.136; 2.4.1.170; 2.4.1.177; 2.4.1.194; 2.4.1.81
CATALYTIC ACTIVITY: Reaction=3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP; Xref=Rhea:RHEA:15249, ChEBI:CHEBI:15834, ChEBI:CHEBI:16918, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=3,4-dihydroxybenzoate + UDP...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.98 mM for gallic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.17 mM for 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=4.44 mM for 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsi...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:27227328};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity remains fairly constant between 20-55 degrees Celsius. Active even at 0 degrees Celsius. {ECO:0000269|PubMed:27227328};
Cytoplasm;Glycosyltransferase;Reference proteome;Transferase
3,4-dihydroxybenzoate metabolic process [GO:0046278]; cinnamic acid ester metabolic process [GO:0009801]; ferulate metabolic process [GO:0033494]
cytoplasm [GO:0005737]
4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity [GO:0047250]; cinnamate beta-D-glucosyltransferase activity [GO:0050412]; flavone 7-O-beta-glucosyltransferase activity [GO:0047891]; gallate 1-beta-glucosyltransferase activity [GO:0047913]; isoflavone 7-O-glucosyltransferase activity [GO:0050004]; quercetin 3-...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27227328}.
null
null
IPR002213;IPR035595;
3.40.50.2000;
A0A193AUF6
MGSESSLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNISDQPAPVGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKVLIPQMIQKNAEQGRPVSCLINNPFIPWVSDVAETLGLPSAMLWVQSCACFLAYYHYYHGLVPFPSENAMEIDVQLPSMPLLKHDEVPSFLYPTTPYPFLRRAILGQYKNLEKPFCILMDTFQELEHEIIEYTSKICPIKTVGPLFKNPKAPNTTVKGDFMKADDCIGWLDSKPASSVVYVSFGSVVYLKQDQWDEIAYGLLNSGVNFLWVMKPPHKDSGY...
Punica granatum (Pomegranate)
FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinna...
2.4.1.120; 2.4.1.136; 2.4.1.170; 2.4.1.177; 2.4.1.194; 2.4.1.81
CATALYTIC ACTIVITY: Reaction=3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP; Xref=Rhea:RHEA:15249, ChEBI:CHEBI:15834, ChEBI:CHEBI:16918, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=3,4-dihydroxybenzoate + UDP...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.89 mM for gallic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.19 mM for 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=2.46 mM for 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsi...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:27227328};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity remains fairly constant between 20-55 degrees Celsius. Active even at 0 degrees Celsius. {ECO:0000269|PubMed:27227328};
Cytoplasm;Glycosyltransferase;Reference proteome;Transferase
3,4-dihydroxybenzoate metabolic process [GO:0046278]; cinnamic acid ester metabolic process [GO:0009801]; ferulate metabolic process [GO:0033494]
cytoplasm [GO:0005737]
4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity [GO:0047250]; cinnamate beta-D-glucosyltransferase activity [GO:0050412]; flavone 7-O-beta-glucosyltransferase activity [GO:0047891]; gallate 1-beta-glucosyltransferase activity [GO:0047913]; isoflavone 7-O-glucosyltransferase activity [GO:0050004]; quercetin 3-...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27227328}.
null
null
IPR002213;IPR035595;
3.40.50.2000;
A0A193KX02
MVSPAIALAFLPLLLTLIIRYRYYFVLLYRAVLTRWVRDCLSGISREERAFQYILTHATPGDSQSILDTFDTWCSKVEFISNIGPKKGKILDRLLQENCPITVLELGTHCGYSTVRMARSLPIGARIYSVEMDQRNAQVAEKIIRLAGFDDDMVELIQRPSDEVIPRLREDLGVERLDLVLMDHWKRCYLPDLHLLEDSGLIGQGSIILADNVIFPGAPNFLRYARRCGLYEVRVHRATLEYMRGIPDGMAELTYIGIK
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (By similarity). Required for auditory function. Component of the hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for t...
2.1.1.6
CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000250|UniProtKB:P21964};
null
null
null
null
null
Catecholamine metabolism;Cell membrane;Deafness;Endoplasmic reticulum;Golgi apparatus;Hearing;Membrane;Methyltransferase;Neurotransmitter degradation;Reference proteome;S-adenosyl-L-methionine;Transferase
auditory behavior [GO:0031223]; catecholamine catabolic process [GO:0042424]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; developmental process [GO:0032502]; dopamine metabolic process [GO:0042417]; endocytosis [GO:0006897]; hair cell differentiation [GO:0035315]; inner ear receptor ce...
basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]
catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; orcinol O-methyltransferase activity [GO:0102938]
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:28534737}. Golgi apparatus {ECO:0000269|PubMed:28534737}. Basolateral cell membrane {ECO:0000269|PubMed:28534737}. Note=Enriched in an apical membrane compartment above the nucleus in the hair cells. Not detectable in the hair bundle. May be present at low...
null
null
IPR029063;IPR002935;
3.40.50.150;
A0A1B0GTW7
MLLLLLLLLLLPPLVLRVAASRCLHDETQKSVSLLRPPFSQLPSKSRSSSLTLPSSRDPQPLRIQSCYLGDHISDGAWDPEGEGMRGGSRALAAVREATQRIQAVLAVQGPLLLSRDPAQYCHAVWGDPDSPNYHRCSLLNPGYKGESCLGAKIPDTHLRGYALWPEQGPPQLVQPDGPGVQNTDFLLYVRVAHTSKCHQETVSLCCPGWSTAAQSQLTAALTSWAQRRGFVMLPRLCLKLLGSSNLPTLASQSIRITGPSVIAYAACCQLDSEDRPLAGTIVYCAQHLTSPSLSHSDIVMATLHELLHALGFSGQLFKK...
Homo sapiens (Human)
FUNCTION: Putative metalloproteinase that plays a role in left-right patterning process. {ECO:0000250|UniProtKB:A0A1D5NSK0}.
3.4.24.-
null
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08148}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148};
null
null
null
null
Alternative splicing;Disease variant;Glycoprotein;Heterotaxy;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc
cell adhesion [GO:0007155]; establishment of left/right asymmetry [GO:0061966]; proteolysis [GO:0006508]
cytoplasm [GO:0005737]; membrane [GO:0016020]
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
null
null
IPR001577;
3.10.170.20;3.90.132.10;
A0A1B0GWR2
MTATTRGSPVGGNDNQGQAPDGQSQPPLQQNQTSSPDSSNENSPATPPDEQGQGDAPPQIEDEEPAFPHTDLAKLDDMINRPRWVVPVLPKGELEVLLEAAIDLSKKGLDVKSEACQRFFRDGLTISFTKILTDEAVSGWKFEIHRCIINNTHRLVELCVAKLAQDWFPLLELLAMALNPHCKFHIYNGTRPCESVSSSVQLPEDELFARSPDPRSPKGWLVDLLNKFGTLNGFQILHDRFINGSALNVQIIAALIKPFGQCYEFLTLHTVKKYFLPIIEMVPQFLENLTDEELKKEAKNEAKNDALSMIIKSLKSLASR...
Rattus norvegicus (Rat)
null
3.4.19.12
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
null
null
null
null
null
Hydrolase;Protease;Proteomics identification;Reference proteome;Thiol protease;Ubl conjugation pathway
axon extension [GO:0048675]; BMP signaling pathway [GO:0030509]; cell migration [GO:0016477]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cerebellar cortex structural organization [GO:0021698]; cilium assembly [GO:0060271]; cytosolic ciliogenesis [GO:0061824]; hippocampus development [GO...
apical part of cell [GO:0045177]; centrosome [GO:0005813]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; nucleus [GO:0005634]
co-SMAD binding [GO:0070410]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; deubiquitinase activity [GO:0101005]; K11-linked deubiquitinase activity [GO:0180017]; K48-linked deubiquitinase activity [GO:1990380]; K63-linked deubiquitinase activity [GO:0061578]; mo...
null
null
null
IPR016024;IPR021905;IPR038765;IPR001394;IPR018200;IPR028889;
3.90.70.10;
A0A1B1FHP3
MAGKSAEEEHPIKAYGWAVKDRTTGILSPFKFSRRATGDDDVRIKILYCGICHTDLASIKNEYEFLSYPLVPGMEIVGIATEVGKDVTKVKVGEKVALSAYLGCCGKCYSCVNELENYCPEVIIGYGTPYHDGTICYGGLSNETVANQSFVLRFPERLSPAGGAPLLSAGITSFSAMRNSGIDKPGLHVGVVGLGGLGHLAVKFAKAFGLKVTVISTTPSKKDDAINGLGADGFLLSRDDEQMKAAIGTLDAIIDTLAVVHPIAPLLDLLRSQGKFLLLGAPSQSLELPPIPLLSGGKSIIGSAAGNVKQTQEMLDFAAE...
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts precondylocarpine acetate to dihydroprecondylocarpine acetate. {ECO:0000269|PubMed:2...
1.1.1.-
CATALYTIC ACTIVITY: Reaction=dihydroprecondylocarpine acetate + NADP(+) = H(+) + NADPH + precondylocarpine acetate; Xref=Rhea:RHEA:58576, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142769, ChEBI:CHEBI:142770; Evidence={ECO:0000269|PubMed:29724909}; PhysiologicalDirection=right-to-left; Xref=Rh...
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00327}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00327};
null
PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29724909}.
null
null
3D-structure;Alkaloid metabolism;Cytoplasm;Glycoprotein;Metal-binding;NAD;Oxidoreductase;Zinc
alcohol metabolic process [GO:0006066]; alkaloid biosynthetic process [GO:0009821]; lignin biosynthetic process [GO:0009809]
cytosol [GO:0005829]
alcohol dehydrogenase (NADP+) activity [GO:0008106]; cinnamyl-alcohol dehydrogenase activity [GO:0045551]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}.
null
null
IPR013149;IPR013154;IPR047109;IPR011032;IPR036291;IPR020843;
3.90.180.10;3.40.50.720;
A0A1B1J8Z2
MIIKLLVALIHYLHETMAVQSIITTPLLVILMSLRSYAFTEPSLHRQQPPSKGGVRAAYWPAWSDFSTSSIDTNYFTHIYYAFVQPAPESFNLEITESYKKWAPKYDGIHNIRPRVTTLLSIGGGGNNATLFSEMASSKQNRASFINSTIHVARKHEFNGLDLDWEWPGDEKDMSNLALLLKEWYKALVVEANTSRKSRLLLTSAVYFNSTISLIGNGPRSYPVRAIRKYLDWASPMCFDYNGAWANETGFNAALYDPNSNISTKYGIGSWIGSGVPAEKLVMGLPLYGRAWELKDPNDHGVGAKAVGPAVDTDGSMDYD...
Lotus japonicus (Lotus corniculatus var. japonicus)
FUNCTION: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5 (PubMed:27383628). Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules (PubMed:27383628). Has the capacity...
3.2.1.14
CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000269|PubMed:27383628};
null
null
PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305}.
null
null
Carbohydrate metabolism;Chitin degradation;Glycoprotein;Glycosidase;Hydrolase;Nodulation;Plant defense;Polysaccharide degradation;Signal
chitin catabolic process [GO:0006032]; defense response to fungus [GO:0050832]; nodulation [GO:0009877]; polysaccharide catabolic process [GO:0000272]
extracellular region [GO:0005576]
chitin binding [GO:0008061]; chitinase activity [GO:0004568]
null
null
null
IPR011583;IPR029070;IPR001223;IPR001579;IPR017853;
3.10.50.10;3.20.20.80;
A0A1C7D1B7
MKKLSRTISGVTPVAVMTKPLPCPGKCIYCPTFAATPQSYTPESPAVLRAKSCEYQAYKQVALRLRIIQDMGHPTDKVELIIMGGTFLSADITYQYGFIKDCYDALNGVVAGSLEEAKTINETAQHRCVGLCIETRPDICGKAEIQRMIDFGTTRVELGVQMLDDDIYKLVERGHRVSDVAEATCLLREYGLKVHYHWMPGLPGSSPEKDLALSRMVFEDPRFCPDGLKLYPTMVVEGTILEQWWKEGRYTPYPNGTMTGLIADIKALVPPYVRISRVLRDIPAVFISAGLKDSLRDGVRQILESRHQKCRCIRCREYGH...
Dehalococcoides mccartyi (strain CBDB1)
FUNCTION: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:27455459). The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adeno...
2.3.1.311
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:5...
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:27455459}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q02908};
null
PATHWAY: tRNA modification. {ECO:0000269|PubMed:27455459}.
null
null
3D-structure;4Fe-4S;Acyltransferase;Iron;Iron-sulfur;Metal-binding;RNA-binding;S-adenosyl-L-methionine;Transferase;tRNA processing;tRNA-binding;Zinc
tRNA acetylation [GO:0051391]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble uridine modification [GO:0002098]
cytoplasm [GO:0005737]; elongator holoenzyme complex [GO:0033588]
4 iron, 4 sulfur cluster binding [GO:0051539]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; S-adenosyl-L-methionine binding [GO:1904047]; tRNA binding [GO:0000049]; tRNA uridine(34) acetyltransferase activity [GO:0106261]
null
null
null
IPR016181;IPR039661;IPR034687;IPR006638;IPR032432;IPR007197;
3.40.630.30;
A0A1D5NSK0
MSFLLCIGILLLPWFPCVCGKCIFDQIQRSVNVVSPPTAQYASAYRFKTQRSKRHIMPMDNLQPIRIKIWIPSESPALSDWEREKLMSAVGEAVSEVSSLLSVKRVKDRLLLNRDVNKYCKFIWRNSSTLNHMKCGRAHENYRFESCLGVIIPDEHLDGCSVYPNPEHPVPTVLRPRGPGVPDADFLLYVFTHNTEKCRAESSVLAYTAHCQTGSDGRPLAGTMVICRETLKKERYTYQHFVKVTTVIHELFHVLGFSKELLSNWKDFGVDCWSHGQVTSTDQTGQVRLYSPTVIRAMQKHFNSTHTDLGAPLENKDAAL...
Danio rerio (Zebrafish) (Brachydanio rerio)
FUNCTION: Plays an essential role for patterning the left-right axis. Requires solely on the left side, downstream of the leftward flow, but upstream of dand5, a nodal inhibitor involved in left-right patterning. {ECO:0000269|PubMed:34903892}.
3.4.24.-
null
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08148}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148};
null
null
null
null
Developmental protein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc
cell adhesion [GO:0007155]; determination of heart left/right asymmetry [GO:0061371]; establishment of left/right asymmetry [GO:0061966]; proteolysis [GO:0006508]
cytoplasm [GO:0005737]; membrane [GO:0016020]
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
null
null
IPR001577;
3.10.170.20;3.90.132.10;2.30.34.10;
A0A1D5NSP9
MVKAKVWILKKHFEGFPKESNFELKEVDLPELQDGDVLVEAIYFSLDPYMRSLSKMFLKEGDVQYGTQLAKVLKSKDPEFPEGCYVVADCGWRTHTVTKAKGPRGPILTRIVSEWPTDIPMSLALGSLGMPGLTALYGLEEVCKIQPGQTVLVSAAAGTVGTVVGQICKIKGCKVVGSAGGDDKVAYLKELGFDQAFNYKTVPSLEEALKNASPEGYDCYFESVGGPMFTAALKNMKPGGRIAVCGAIATYNDTTPQMCPYPHHEIIVRSLTIQGFMVTNYKEKDEESVKRLLTWMKEGKLKTKEMVTVGFDKLPIAFMK...
Danio rerio (Zebrafish) (Brachydanio rerio)
null
1.3.1.48; 1.3.1.74
CATALYTIC ACTIVITY: Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate + NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974, ChEBI:CHEBI:133975; Evidence={ECO:0000256|ARBA:ARBA00023...
null
null
null
null
null
Fatty acid metabolism;Hydroxylation;Lipid metabolism;Oxidoreductase;Prostaglandin metabolism;Reference proteome
prostaglandin metabolic process [GO:0006693]
cytoplasm [GO:0005737]
13-prostaglandin reductase activity [GO:0036132]; 15-oxoprostaglandin 13-oxidase activity [GO:0047522]; 2-alkenal reductase [NAD(P)+] activity [GO:0032440]
null
null
null
IPR013149;IPR041694;IPR011032;IPR045010;IPR036291;IPR020843;IPR014190;
3.90.180.10;3.40.50.720;
A0A1D5NZL7
MAGAQPGVHALQLKPVCVSDTLKKGIKFVKWDDDSTVVTPIILRTDPQGFFFYWTDQNKETELLDISLVKDARCGKHARAPKDPKLRELLDAGNVGSRLENRMITVVYGPDLVNISYLNLVAFQEDIAKEWSDEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACNLPSSRNDSIPQDDFTPDVYRVFLNNLCPRPEIDHIFSEFGAKSKPYLTVDQMMEFINLKQRDPRLNEILYPPLKQEQVQQLIEKYEPNSNLAKKGQISVDGFMRYLSGEENGVVPPEKLDLNEDMS...
Gallus gallus (Chicken)
FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. {ECO:0000256|PIRNR:PIRNR000956}.
3.1.4.11
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433; Evidence={ECO:0000256|ARBA:ARBA00023726}; Physiolog...
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR000956-2}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};
null
null
null
null
Calcium;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Phosphoprotein;Proteomics identification;Reference proteome;Transducer
activation of meiosis involved in egg activation [GO:0060466]; cerebral cortex development [GO:0021987]; fat cell differentiation [GO:0045444]; G protein-coupled receptor signaling pathway [GO:0007186]; G2/M transition of mitotic cell cycle [GO:0000086]; glutamate receptor signaling pathway [GO:0007215]; insulin-like g...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; nuclear speck [GO:0016607]; postsynaptic cytosol [GO:0099524]
calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; GTPase activator activity [GO:0005096]; lamin binding [GO:0005521]; phosphatidylinositol phospholipase C activity [GO:0004435]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
null
null
null
IPR000008;IPR035892;IPR011992;IPR001192;IPR016280;IPR028400;IPR014815;IPR042531;IPR009535;IPR037862;IPR017946;IPR015359;IPR000909;IPR001711;
2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10;
A0A1D5NZW4
MFDRTRLPFVALDVVCVVLAGLPLGVLNLAKIKPYQRGFFCNDDSIKYPFHDSTITSTVLYTVGFTLPILSIILGETLSVFYNHLHSNSFVRNNYIATIYKAIGTFIFGAAASQSLTDIAKYSIGRLRPHFLAVCQPDWTQINCSLGYIENIPCQGDKAKINEGRLSFYSGHSSFSMYCMLFLALYLQARMKGDWARLVRPTIQFGLIAASIYVGLSRVSDYKHHWSDVLTGLIQGALVAILIVVYVSDFFKVRGCTFQPKEDSHTTLHETPTNGNHFGSNHQP
Gallus gallus (Chicken)
null
3.1.3.106; 3.1.3.4; 3.6.1.75
CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937, ChEBI:CHEBI:84973; Evidence={ECO:0000256|ARBA:ARBA00000974}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885; Ev...
null
null
PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000256|ARBA:ARBA00005074}.; PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
null
null
Cell membrane;Hydrolase;Lipid metabolism;Membrane;Reference proteome
phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]
apical plasma membrane [GO:0016324]; caveola [GO:0005901]; plasma membrane [GO:0005886]
lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatidate phosphatase activity [GO:0008195]
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane raft {ECO:0000256|ARBA:ARBA00004314}; Multi-pass membrane protein ...
null
null
IPR036938;IPR000326;IPR043216;
1.20.144.10;
A0A1D5PHB6
MSYEQRRDWGRGRGRGGDGGSSAASSGGGGHGGRGGGRGRHPSHLKGREIGLWYARKQGQKSKETDRQQRAVVRMDERREEQIVQLLNAVQPRAEKEQEAMSWWSGDEEGHVPEQPPKVKPGAEKAEKAPVKRRPILQKTFLDQDVEYLFEKNDQDADLDEQLKEDLRKKKSDPRYIEMQRFREKLPSYGMRQELVNLINNNRVTVISGETGCGKTTQVTQFILDDYIERGKGSTCRIVCTQPRRISAISVAERVAAERAEACGNGKSTGYQIRLQSRLPRKQGSILYCTTGIVLQWLQSDKHLSSISHVVLDEIHERNL...
Gallus gallus (Chicken)
null
3.6.4.13
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=3.6.4.13; Evidence={ECO:0000256|ARBA:ARBA00001556};
null
null
null
null
null
ATP-binding;Helicase;Hydrolase;Nucleotide-binding;Proteomics identification;Reference proteome;RNA-binding
3'-UTR-mediated mRNA destabilization [GO:0061158]; cellular response to arsenite ion [GO:1903843]; cellular response to heat [GO:0034605]; cellular response to UV [GO:0034644]; G-quadruplex DNA unwinding [GO:0044806]; negative regulation of translation [GO:0017148]; ossification [GO:0001503]; positive regulation of can...
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]
ATP binding [GO:0005524]; DNA helicase activity [GO:0003678]; double-stranded RNA binding [GO:0003725]; G-quadruplex DNA binding [GO:0051880]; G-quadruplex RNA binding [GO:0002151]; histone deacetylase binding [GO:0042826]; hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; mRNA 3'-UTR AU-rich region ...
null
null
null
IPR011709;IPR011545;IPR002464;IPR048333;IPR007502;IPR014001;IPR001650;IPR027417;
1.20.120.1080;3.40.50.300;
A0A1D5PIQ5
MSQERPKFYRQELNKTVWEVPERYQNLSPVGSGAYGSVCSAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPAKSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGPELLKKISSESARNYIQSLSYMPKMNFENVFIGANPLAVDLLEKMLVLDTDKRITAAEALAHAYFAQYHDPDDEPVA...
Gallus gallus (Chicken)
null
2.7.11.24
null
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};
null
null
null
null
Proteomics identification;Reference proteome;Stress response
angiogenesis [GO:0001525]; bone development [GO:0060348]; cartilage condensation [GO:0001502]; cell morphogenesis [GO:0000902]; cellular response to ionizing radiation [GO:0071479]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to UV-B [G...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle pole [GO:0000922]
ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; mitogen-activated protein kinase p38 binding [GO:0048273]; NFAT protein binding [GO:0051525]; protein phosphatase binding [GO:0019903]; protein serine/threonine kinase activity [GO:0004674]
null
null
null
IPR011009;IPR003527;IPR038784;IPR008352;IPR000719;IPR017441;
1.10.510.10;
A0A1D5PLJ8
MPSAINAAVAQQTAAGSVPSTTSTTTEGTGGGTGGIYSAIISRNQPIIKVKEKTYEELHKKCLEENILYEDPDFPPNETSLFYSQKVPIKFEWKRPREICENPRFIIGGANRTDICQGELGDCWFLAAIACLTLNKKLLCRVIPHDQSFIQNYAGIFHFQFWRYGDWVDVIIDDCLPTYNNQLVFTKSSQRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVTEFYEIKDAPKDIYKIMKHAIARGSLMASSIDDNLGFSYGAAPRSDIGELIARMVKNLENAQMTYSTVDYQGTDERPAWTIMPMQYETRMS...
Gallus gallus (Chicken)
FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000256|RuleBase:RU367132}.
3.4.22.54
CATALYTIC ACTIVITY: Reaction=Broad endopeptidase activity.; EC=3.4.22.54; Evidence={ECO:0000256|ARBA:ARBA00023702, ECO:0000256|RuleBase:RU367132};
null
null
null
null
null
Calcium;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Repeat;Thiol protease
calcium-dependent self proteolysis [GO:1990092]; cellular response to calcium ion [GO:0071277]; cellular response to salt stress [GO:0071472]; G1 to G0 transition involved in cell differentiation [GO:0070315]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; ligase regulator activity [GO:0055103]; molecular adaptor activity [GO:0060090]; sodium ion binding [GO:0031402]; structural constituent of muscle [GO:0008307]; titin binding [GO:0031432]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU367132}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
null
null
IPR033883;IPR022684;IPR022682;IPR022683;IPR036213;IPR029531;IPR011992;IPR018247;IPR002048;IPR038765;IPR000169;IPR001300;
2.60.120.380;3.90.70.10;1.10.238.10;
A0A1D5PNE8
MELSEVRCLSDSDELYTINRTPPGSSRPQRLLWQTAVRHITEQRFIQEHSSSSGGSSSVGGKGFSSEETCCPNHHPHHHHHHFRRQSAGRSLGSERHNNGGTKVFPERTSSNGDLGFLPLDCAPSNSDFFLNWGYTYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRKSEVVMNILDVLTKLTLLFLHLTLASAPMDPIKGILLGFFTGIEVVICALVVVRKDTTSYTYLQYSGVVTWVAMATQILAAGLGCGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLVTSVLQLIMQLVIPRLAVTSLNQIAAQAVLFMCMN...
Gallus gallus (Chicken)
FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. {ECO:0000256|PIRNR:PIRNR039050}.
4.6.1.1
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000256|ARBA:ARBA00001593, ECO:0000256|PIRNR:PIRNR039050};
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR039050}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};
null
null
null
null
ATP-binding;cAMP biosynthesis;Lyase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Reference proteome
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP biosynthetic process [GO:0006171]; cellular response to glucagon stimulus [GO:0071377]; cellular response to morphine [GO:0071315]; glucose mediated signaling pathway [GO:0010255]; intracellular signal transduction [GO:0035556]...
apical plasma membrane [GO:0016324]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body membrane [GO:0032809]; postsynaptic density [GO:0014069]; ...
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; metal ion binding [GO:0046872]
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
null
null
IPR001054;IPR018297;IPR032628;IPR030672;IPR009398;IPR029787;
3.30.70.1230;
A0A1D5PPP7
MSGAERRPAAGRVQLDSKPTPTTTADGNQNITEVDAFDKRQTFDPAVQYKMNHQRRGVALIFNHEHFFWHLRLPDRRGTLADRNNLKRSLTDLGFEVRIFDDLKAEDVLKKVFEASRDDYSNADCFVCVFLSHGENDHVYAYDAQIKIETITNMFRGDKCQSLVGKPKIFIIQACRGDKHDDPVLVQDSVDSKDETTVNQTEVDAAGVYTLPAGADFIMCYSVAQGYFSHRETVNGSWYIQDLCEALGKHGSSLEFTELLTVVNRKVSHRKVDICRDINAIGKKQIPCFASMLTKKLYFHPKSK
Gallus gallus (Chicken)
FUNCTION: Cysteine protease that plays essential roles in programmed cell death, development and innate immunity (PubMed:11953316). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein lamin-A/LMNA thereby inducing nuclear shrinkage and fragme...
3.4.22.59
CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59; Evidence={ECO:0000250|UniProtKB:P55212};
null
null
null
null
null
Apoptosis;Autocatalytic cleavage;Cytoplasm;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Zymogen
activation of innate immune response [GO:0002218]; apoptotic chromosome condensation [GO:0030263]; apoptotic DNA fragmentation [GO:0006309]; apoptotic nuclear changes [GO:0030262]; apoptotic process [GO:0006915]; hepatocyte apoptotic process [GO:0097284]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:...
cytoplasm [GO:0005737]; nucleus [GO:0005634]
cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type peptidase activity [GO:0008234]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}.
null
DOMAIN: The N-terminal disordered prodomain is required to prevent self-activation. {ECO:0000250|UniProtKB:P55212}.; DOMAIN: The Tri-arginine exosite is required to recruit substrates for hydrolysis. {ECO:0000250|UniProtKB:P55212}.; DOMAIN: Undergoes helix-strand structural transitions upon substrate-binding: the 130's...
IPR029030;IPR033139;IPR011600;IPR002138;IPR001309;IPR015917;
3.40.50.1460;
A0A1D5PRR9
MSGGRQRTLPEAWRRAAGPALQAGRDADGNDDDDDELLAAAAAELDPDPNPNVDPNPGPGPEAAAGGFCAAAGALWIYPTNRPERPYQLRMARAALFANTLLCLPTGLGKTFVAAVVMYNFYRWFPSGKVLFLAPTKALVAQQMEACAQLMGIPGRDMAEMTGGTQALSRRELWASRRVFFLTPQIMVNDLSRGTCPAVEVKCLVVDEAHKALGNHAYCQVVKELSRYTTQFRVLALTATPGSDTKAVQQVVSNLLIAQIELCSEDSPEIQPYSHERQVEKIVVPLGEELGGIQRAYIHVLETFAGRLIKLGVLARRDVP...
Gallus gallus (Chicken)
FUNCTION: DNA-dependent ATPase component of the Fanconi anemia (FA) core complex (By similarity). Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal break...
3.6.4.13
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=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q8IYD8};
null
null
null
null
null
3D-structure;ATP-binding;DNA damage;DNA repair;DNA-binding;Helicase;Hydrolase;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome
double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; interstrand cross-link repair [GO:0036297]
nucleus [GO:0005634]
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; four-way junction DNA binding [GO:0000400]; four-way junction helicase activity [GO:0009378]; nuclease activity [GO:0004518]; RNA helicase activity [GO:0003724]
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19465393}.
PTM: Phosphorylated; hyperphosphorylated in response to genotoxic stress. {ECO:0000269|PubMed:19465393}.
null
IPR011545;IPR006166;IPR031879;IPR039686;IPR044749;IPR014001;IPR001650;IPR027417;IPR011335;IPR010994;IPR047418;
3.40.50.10130;1.10.150.20;1.20.1320.20;3.40.50.300;
A0A1D5PUY5
MAEPPAAPGPEGEEGPVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIRADIEKDVLTVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIKCSLNPEWNETFRFQLKEADKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKSGVDGWFKLLSQEEGEYFNVPVPPEGEEGNEELRQKFERAKIGTGSKAADEKT...
Gallus gallus (Chicken)
null
2.7.11.13
CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|PIRNR:PIRNR000550};
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR000550-4}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000256|PIRSR:PIRSR000550-4};
null
null
null
null
Adaptive immunity;ATP-binding;Calcium;Cytoplasm;Immunity;Kinase;Metal-binding;Nucleotide-binding;Nucleus;Phosphoprotein;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc;Zinc-finger
adaptive immune response [GO:0002250]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; calcium ion transport [GO:0006816]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to carbohydrate stimulus [GO:0071322]; intracellular calcium ion homeostasis [GO:0006874]; in...
nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; presynaptic cytosol [GO:0099523]; spectrin [GO:0008091]
ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone H3T6 kinase activity [GO:0035403]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coa...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
null
null
IPR000961;IPR046349;IPR000008;IPR035892;IPR034664;IPR020454;IPR011009;IPR002219;IPR017892;IPR000719;IPR017441;IPR014375;IPR008271;
3.30.60.20;2.60.40.150;1.10.510.10;
A0A1D5PZB7
MLCPWQFAFKPHAVKNQSSEEKDINNNVEKDVKVHSFVKDDAKLHSLSKKQMKMSPIITSAEKHPQNGIKASNQISRCPRHVKVRNMENGSSLLDTLHLTAKEVINCRTRACQGALMTPKGLVRSTRDGPVPPAELLPQAVDFVKQYYSSFKELKIEEHLARLETVTKEIETTGTYHLTKDELIFAAKQAWRNAPRCIGRIQWSNLQVFDARDCKTAKEMFEYICRHIQYATNNGNIRSAITIFPQRTDGKHDFRVWNSQLIRYAGYQMPDGSVIGDPASVEFTKLCIELGWKPKYGRFDVVPLILQANGQDPEIFEYPP...
Gallus gallus (Chicken)
FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions. {ECO:0000256|PIRNR:PIRNR000333}.
1.14.13.39
CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={...
COFACTOR: Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000256|ARBA:ARBA00001950}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|PIRNR:PIRNR000333}; Note=Binds 1 FAD. {ECO:0000256|PIRNR:PIRNR000333}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:...
null
null
null
null
Calmodulin-binding;FAD;Flavoprotein;FMN;Heme;Iron;Metal-binding;NADP;Oxidoreductase;Reference proteome
arginine catabolic process [GO:0006527]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to type II interferon [GO:0071346]; cellular response to xenobiotic stimulus [GO:0071466]; circadian rhythm [GO:0007623]; defense response to bacterium [GO:0042742]; inflammatory response [GO:0006954]; negat...
cortical cytoskeleton [GO:0030863]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]
arginine binding [GO:0034618]; calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517]; protein homodimerization activity [GO:0042803]; t...
null
null
null
IPR003097;IPR017927;IPR001094;IPR008254;IPR001709;IPR029039;IPR039261;IPR023173;IPR044943;IPR044940;IPR044944;IPR012144;IPR004030;IPR036119;IPR001433;IPR017938;
3.40.50.360;6.10.250.410;3.90.440.10;3.40.50.80;2.40.30.10;
A0A1D5PZJ5
MRKKQKTAWKEILKWEKEVTGTKPKMSTTRKILLILGFLSTLAAIALITVAVTQNQPLPKNIKYGIVLDAGSSHTNLYVYEWPAEKENDTGVVQQVEVCKVEGPGISGYSQTTEKAGPSLVQCLRQAEGVIPLKQHQETPVYLGATAGMRLLRLENKDAAEKVLSSVEKTLRSAPFNFQGARIISGQEEGAYGWITINYLLGNFKQSGWKKFLHSLKSVSETSGALDLGGASTQITFVPDEISSESPQNLLYFRLYGKDYRVYTHSFLCYGKDQALQQKLARDLQSTENSSLFDPCFHQGYQRTISVSNFFKNPCTSVEK...
Gallus gallus (Chicken)
null
3.6.1.5
CATALYTIC ACTIVITY: Reaction=2 H2O + ITP = 2 H(+) + IMP + 2 phosphate; Xref=Rhea:RHEA:77735, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; Evidence={ECO:0000256|ARBA:ARBA00043682}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77736; Evidence={ECO:0000256|ARBA:ARB...
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00001913};
null
null
null
null
ATP-binding;Calcium;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Nucleotide-binding;Proteomics identification;Reference proteome;Transmembrane;Transmembrane helix
nucleoside diphosphate catabolic process [GO:0009134]
plasma membrane [GO:0005886]
GDP phosphatase activity [GO:0004382]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134]
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
null
null
IPR000407;
3.30.420.40;3.30.420.150;
A0A1D5Q1K7
ADGATALQPGRESETLSQKKRKNEKDREERETEKRKRQSKAKKEEETAAFFPCDAFLCEIESREESLAVSPRLECSGAISAHCSLRLLGSSNSPASASRVAGITGAHCNFQSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEAILNKPGLKYKPAVNQIECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPWAKPEDPSLLED...
Macaca mulatta (Rhesus macaque)
null
1.1.1.21; 1.1.1.300
CATALYTIC ACTIVITY: Reaction=(E)-hex-2-en-1-ol + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:58424, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:141205; Evidence={ECO:0000256|ARBA:ARBA00035762}; CATALYTIC ACTIVITY: Reaction=(E,E)-2,4-hexadien-1-ol + NADP(+) = (E,E)...
null
null
null
null
null
Acetylation;NADP;Reference proteome
cellular hyperosmotic salinity response [GO:0071475]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; epithelial cell maturation [GO:0002070]; fructose biosynthetic process [GO:0046370]; L-ascorbic acid biosynthetic process [GO:0019853]; metanephric collecting duct development [...
cytosol [GO:0005829]; nucleoplasm [GO:0005654]
alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; glyceraldehyde oxidoreductase activity [GO:0043795]; L-glucuronate reductase activity [GO:0047939]; retinal dehydrogenase activity [GO:0001758]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
null
null
IPR020471;IPR018170;IPR023210;IPR036812;
3.20.20.100;
A0A1D5Q1P0
MESALPAAGFLYWVGAGTVAYLALRISYSLFTALRVWGVGNEAGVGPGLGEWAVVTGGTDGIGKSYAEELAKRGMKVVLISRSQDKLDQVSSEIKEKFKVETRTIVVDFTLEDIYDKIKTGLAGLEIGILVNNVGMSYEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMFPVPLLTIYSATKTFVDFFSQCLHEEYRSKGIFVQSVLPYFVATKLAKIRKPTLDKPTPETFVKSAIKTVGLQSRTNGYLIHVLMGWIISNLPSWIYLKIAMNMNKATRAHYLKKIKKN
Macaca mulatta (Rhesus macaque)
FUNCTION: Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducin...
1.1.1.330; 1.1.1.62
CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + H(+) + NADPH = (3R)-hydroxy-(7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + NADP(+); Xref=Rhea:RHEA:39323, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73852, ChEBI:CHEBI:76415; Evidence={ECO:0000256|ARBA:ARBA00036946}; CATALYTIC ...
null
null
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|ARBA:ARBA00005194}.; PATHWAY: Steroid biosynthesis; estrogen biosynthesis. {ECO:0000256|ARBA:ARBA00037929}.
null
null
Lipid biosynthesis;Lipid metabolism;Membrane;Oxidoreductase;Reference proteome;Steroid biosynthesis;Transmembrane;Transmembrane helix
extracellular matrix organization [GO:0030198]; fatty acid elongation, saturated fatty acid [GO:0019367]; positive regulation of cell-substrate adhesion [GO:0010811]; steroid biosynthetic process [GO:0006694]
endoplasmic reticulum [GO:0005783]; extracellular matrix [GO:0031012]; fatty acid elongase complex [GO:0009923]
collagen binding [GO:0005518]; fibronectin binding [GO:0001968]; heparin binding [GO:0008201]; oxidoreductase activity [GO:0016491]; very-long-chain 3-oxoacyl-CoA reductase activity [GO:0141040]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
null
null
IPR036291;IPR020904;IPR002347;
3.40.50.720;
A0A1D5Q1X3
MAKERGLISPSDFAQLQKYMESSSVALSSVLLRCAHDWEREEREMGRCARSRLSTHLRCTWTACSSSQRRGVKSDSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIYLEVDNVPRHLSLALFQSFKTDHCLNEANVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEWVRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKSRKDIGV...
Macaca mulatta (Rhesus macaque)
null
2.7.1.107
CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023371}; PhysiologicalDirection=l...
null
null
PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000256|ARBA:ARBA00005175}.
null
null
Acetylation;ATP-binding;Calcium;Kinase;Lipid metabolism;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Repeat;Transferase;Zinc;Zinc-finger
diacylglycerol metabolic process [GO:0046339]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; phosphatidic acid biosynthetic process [GO:0006654]; platelet activation [GO:0030168]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]
cytosol [GO:0005829]; plasma membrane [GO:0005886]
alkylglycerol kinase activity [GO:0047649]; ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; calcium ion binding [GO:0005509]; phospholipid binding [GO:0005543]; protein kinase activity [GO:0004672]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
null
null
IPR017438;IPR046349;IPR047469;IPR029477;IPR037607;IPR038199;IPR000756;IPR001206;IPR011992;IPR018247;IPR002048;IPR011009;IPR016064;IPR002219;IPR000719;IPR017441;IPR008271;
2.60.200.40;3.30.60.20;1.10.238.110;1.10.238.10;1.10.510.10;
A0A1D5Q2Y8
SLSPGGMEGVACKILLLLLPLLLLLEPQVSQGLVITPPGPELILNVSSTFVLTCSGSAPVVWERMSQELPQEMAKAQDNTFSSVLTLTNLTGLDTGEYFCTYNDSRGLEPDERKRLYIFVPDPTMGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDIALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWMYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLG...
Macaca mulatta (Rhesus macaque)
FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in...
2.7.10.1
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:0000256|ARBA:ARBA00001171, ECO...
null
null
null
null
null
ATP-binding;Cell membrane;Chemotaxis;Cytoplasmic vesicle;Developmental protein;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Lysosome;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kin...
angiogenesis [GO:0001525]; cell chemotaxis [GO:0060326]; phosphorylation [GO:0016310]; positive regulation of phosphate metabolic process [GO:0045937]; positive regulation of protein modification process [GO:0031401]; positive regulation of response to stimulus [GO:0048584]; positive regulation of smooth muscle cell mi...
cytoplasmic vesicle [GO:0031410]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; platelet-derived growth factor beta-receptor activity [GO:0005019]; platelet-derived growth factor binding [GO:0048407]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR500948}; Single-pass type I membrane protein {ECO:0000256|PIRNR:PIRNR500948}. Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR500948}. Lysosome lumen {ECO:0000256|PIRNR:PIRNR500948}. Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}; Single-p...
null
null
IPR007110;IPR036179;IPR013783;IPR003599;IPR003598;IPR013151;IPR011009;IPR027288;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;IPR001824;
2.60.40.10;1.10.510.10;
A0A1D5Q330
MAWRCPRMGRVPLAWCLALCGWVCMAPRGTQAEESPFVGNPGNITGARGLTGTLRCQLQVQGEPPEVHWLRDGQILELADSTQTQVPLGEDEQDDWIVVSQLRIASLQLSDAGQYQCLVFLGHQNFVSQPGYVGLEGLPYFLEEPEDRTVAANTHFNLSCQAQGPPEPVDLLWLQDAVPLATAPGHGPQRNLHVPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQQPRNLHLVSRQPTELEVAWTPGLSGIYPLTHCTLQAMLSDNEVGIQAGEPDPPEEPLTLQASVPPHQLRLGSLHPHTPYYIRVACTSSQGPSSW...
Macaca mulatta (Rhesus macaque)
null
2.7.10.1
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:0000256|ARBA:ARBA00001171};
null
null
null
null
null
ATP-binding;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase
blood vessel remodeling [GO:0001974]; cell maturation [GO:0048469]; cell migration [GO:0016477]; cellular response to extracellular stimulus [GO:0031668]; cellular response to interferon-alpha [GO:0035457]; cellular response to lipopolysaccharide [GO:0071222]; dendritic cell differentiation [GO:0097028]; erythrocyte ho...
actin cytoskeleton [GO:0015629]; cell surface [GO:0009986]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphatidylserine binding [GO:0001786]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; virus receptor activity [GO:0001618]
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
null
null
IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR003599;IPR011009;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;
2.60.40.10;1.10.510.10;
A0A1D5Q518
MGMWASLDALWEIPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSEIEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEERNSEEIKAKVKNK...
Macaca mulatta (Rhesus macaque)
FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated proteins. {ECO:0000256|RuleBase:RU366005}.
3.4.24.84
CATALYTIC ACTIVITY: Reaction=Hydrolyzes the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids with aliphatic side chains and P3' is any C-terminal residue.; EC=3.4.24.84; Evidence={ECO:0000256|ARBA:ARBA00044456, ECO:0000256|RuleBase:RU366005};
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR627057-2, ECO:0000256|RuleBase:RU366005}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR627057-2, ECO:0000256|RuleBase:RU366005};
null
null
null
null
Endoplasmic reticulum;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc
adult walking behavior [GO:0007628]; bone mineralization [GO:0030282]; CAAX-box protein processing [GO:0071586]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; CAMKK-AMPK signaling cascade [GO:0061762]; cardiac conduction [GO:0061337]; cardiac muscle cell development [GO:0055013]; cardiac ventricle develo...
endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; protein-containing complex [GO:0032991]
double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU366005}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU366005}.
null
null
IPR027057;IPR001915;IPR032456;
3.30.2010.10;
A0A1D5Q874
MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSSSGSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASGSGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRKSEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHTYLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTSLLQVILQVVIPRLAVISINQ...
Macaca mulatta (Rhesus macaque)
FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. {ECO:0000256|PIRNR:PIRNR039050}.
4.6.1.1
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000256|ARBA:ARBA00001593, ECO:0000256|PIRNR:PIRNR039050};
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRNR:PIRNR039050}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};
null
null
null
null
ATP-binding;cAMP biosynthesis;Lyase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Reference proteome;Transmembrane;Transmembrane helix
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP biosynthetic process [GO:0006171]; cellular response to glucagon stimulus [GO:0071377]; cellular response to morphine [GO:0071315]; glucose mediated signaling pathway [GO:0010255]; intracellular signal transduction [GO:0035556]...
apical plasma membrane [GO:0016324]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body membrane [GO:0032809]; postsynaptic density [GO:0014069]; ...
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; metal ion binding [GO:0046872]
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
null
null
IPR001054;IPR018297;IPR032628;IPR030672;IPR009398;IPR029787;
3.30.70.1230;
A0A1D5Q9I1
MGCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPLQGDPRQQGLKDKACRSLAVGFHLTPTYSLPGPAFLVPRPVTPGFLPIPARFSLMPLVFTDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMG...
Macaca mulatta (Rhesus macaque)
null
2.7.10.2
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000256|ARBA:ARBA00001149, ECO...
null
null
null
null
null
ATP-binding;Cell membrane;Cytoplasm;Kinase;Lipoprotein;Membrane;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;SH2 domain;SH3 domain;Transferase;Tyrosine-protein kinase
B cell receptor signaling pathway [GO:0050853]; Fc-gamma receptor signaling pathway [GO:0038094]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; intracellular zinc ion homeostasis [GO:0006882]; phosphorylation [GO:0016310]; positive regulation of heterotypic cell-cell adhesion [GO:...
cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; immunological synapse [GO:0001772]; membrane raft [GO:0045121]; pericentriolar material [GO:0000242]
ATP binding [GO:0005524]; ATPase binding [GO:0051117]; CD4 receptor binding [GO:0042609]; CD8 receptor binding [GO:0042610]; identical protein binding [GO:0042802]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol 3-kinase binding [GO:0043548]; phospholipase activator activity [...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic sid...
null
null
IPR011009;IPR035850;IPR035749;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR036028;IPR001452;IPR008266;IPR020635;
3.30.505.10;2.30.30.40;1.10.510.10;