Datasets:
lhallee
/
exp_new_unprocessed

Dataset card Data Studio Files
xet
 Community
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Sequence
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35.2k
Organism
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169
Function [CC]
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15.3k
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EC number
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118
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Catalytic activity
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Cofactor
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1.77k
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Kinetics
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10.8k
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Pathway
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pH dependence
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855
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Temperature dependence
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709
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Keywords
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Gene Ontology (biological process)
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11.3k
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Gene Ontology (cellular component)
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Gene Ontology (molecular function)
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2.21k
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Subcellular location [CC]
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Post-translational modification
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Domain [CC]
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InterPro
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810
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Gene3D
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250
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A0A009IHW8
MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQKKKIDIDNKLLKEKQNLIKEEILERKKLEVLTKKQQKDEIEHQKKLKREIDAIKASTQYITDVSISSYNNTIPETEPEYDLFISHASEDKEDFVRPLAETLQQLGVNVWYDEFTLKVGDSLRQKIDSGLRNSKYGTVVLSTDFIKKDWTNYELDGLVAREMNGHKMILPIWHKITKNDVLDYSPNLADKVALNTSVNSIEEIAHQLADVILNR
Acinetobacter baumannii (strain 1295743)
FUNCTION: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922). In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed 2'cADPR (v-cADPR) (PubMed:29395922, PubMed:36048923). Cleaves NADP(+), but does not cyclize the prod...
3.2.2.-; 3.2.2.6
CATALYTIC ACTIVITY: Reaction=NAD(+) = 2'cADPR + H(+) + nicotinamide; Xref=Rhea:RHEA:75299, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:194248; Evidence={ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75300; Evidence={ECO:0000269|PubMed:36048923}; CATALYTIC AC...
null
null
null
null
null
3D-structure;Coiled coil;Hydrolase;NAD
NAD catabolic process [GO:0019677]; signal transduction [GO:0007165]
null
NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135]
null
null
DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity (Probable). The TIR domain alone is active and produces cADPR (residues 134-267) (PubMed:36048923). {ECO:0000255|PROSITE-ProRule:PRU00204, ECO:0000269|PubMed:36048923, ECO:0000305|PubMed:3...
IPR000157;IPR035897;
3.40.50.10140;
A0A023I7E1
MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEA...
Rhizomucor miehei
FUNCTION: Cleaves internal linkages in 1,3-beta-glucan. {ECO:0000269|PubMed:34801773}.
3.2.1.39
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:34801773};
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:34801773};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:34801773};
3D-structure;Carbohydrate metabolism;Cell wall;Cell wall biogenesis/degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal
cell wall organization [GO:0071555]; polysaccharide catabolic process [GO:0000272]
cell surface [GO:0009986]; extracellular region [GO:0005576]
glucan endo-1,3-beta-D-glucosidase activity [GO:0042973]; glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group [GO:0052861]; glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group [GO:0052862]
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250|UniProtKB:P53753}.
null
null
IPR005200;IPR040720;IPR040451;
1.10.287.1170;1.20.5.420;
A0A024B7W1
MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGC...
Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV)
FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface ...
2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13
CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:C...
null
null
null
null
null
3D-structure;4Fe-4S;Acetylation;Activation of host autophagy by virus;ATP-binding;Capsid protein;Clathrin-mediated endocytosis of virus by host;Cleavage on pair of basic residues;Disulfide bond;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;Glycoprotein;GTP-binding;Hel...
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; negative regulation of innate immune response [GO:0045824]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT ca...
centrosome [GO:0005813]; extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; mRNA (nucleoside-2'-O-)-methyltransferas...
SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000269|PubMed:36594413}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}...
PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m...
DOMAIN: [Small envelope protein M]: The transmembrane domain contains an endoplasmic reticulum retention signal. {ECO:0000250|UniProtKB:P17763}.; DOMAIN: [Envelope protein E]: The transmembrane domain contains an endoplasmic reticulum retention signal. {ECO:0000250|UniProtKB:P17763}.; DOMAIN: [Capsid protein C]: The di...
IPR043502;IPR000069;IPR038302;IPR013755;IPR001122;IPR037172;IPR011492;IPR027287;IPR026470;IPR038345;IPR011998;IPR001157;IPR000752;IPR000487;IPR001850;IPR000404;IPR001528;IPR046811;IPR002535;IPR038688;IPR047530;IPR000208;IPR000336;IPR014412;IPR036253;IPR038055;IPR013756;IPR014001;IPR001650;IPR014756;IPR026490;IPR049486;...
1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10;
A0A024R6A3
MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAEST...
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-beta formation [GO:0034205]; apoptotic signaling pathway [GO:0097190]; autophagosome assembly [GO:0000045]; blood vessel development [GO:0001568]; brain morphogenesis [GO:0048854]; Cajal-Retzius cell differentiation [GO:0021870]; cell adhesion [GO:0007155]; cell fate specification [GO:0001708]; cerebellum devel...
cell cortex [GO:0005938]; cell junction [GO:0030054]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; dendritic shaft [GO:0043198]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:00...
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;
A0A024SC78
MRSLAILTTLLAGHAFAYPKPAPQSVNRRDWPSINEFLSELAKVMPIGDTITAACDLISDGEDAAASLFGISETENDPCGDVTVLFARGTCDPGNVGVLVGPWFFDSLQTALGSRTLGVKGVPYPASVQDFLSGSVQNGINMANQIKSVLQSCPNTKLVLGGYSQGSMVVHNAASNLDAATMSKISAVVLFGDPYYGKPVANFDAAKTLVVCHDGDNICQGGDIILLPHLTYAEDADTAAAFVVPLVS
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:25219509). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:25219509). {ECO:0000269|PubMed:25219509}.
3.1.1.74
CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:25219509};
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-7. {ECO:0000269|PubMed:25219509};
null
3D-structure;Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal
null
extracellular region [GO:0005576]
cutinase activity [GO:0050525]
SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361263}.
PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}.
DOMAIN: In contract to classical cutinases, possesses a lid formed by two N-terminal helices which covers its active site (PubMed:25219509). The lid opens in the presence of surfactants to uncover the catalytic crevice, allowing enzyme activity and inhibition (PubMed:25219509). {ECO:0000269|PubMed:25219509}.
IPR029058;IPR000675;IPR043580;IPR043579;IPR011150;
3.40.50.1820;
A0A044RE18
MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAF...
Onchocerca volvulus
FUNCTION: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. {ECO:0000269|PubMed:12855702}.
3.4.21.75
CATALYTIC ACTIVITY: Reaction=Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.; EC=3.4.21.75; Evidence={ECO:0000269|P...
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12855702}; Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Active from pH 7.0 to 8.5. {ECO:0000269|PubMed:12855702};
null
Autocatalytic cleavage;Calcium;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen
dibasic protein processing [GO:0090472]; zymogen activation [GO:0031638]
extracellular region [GO:0005576]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12855702}.
PTM: N-glycosylated. {ECO:0000269|PubMed:12855702}.; PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is probably autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound as a potent autoinhibitor. Probably following transport to the trans Golgi, a se...
null
IPR008979;IPR034182;IPR002884;IPR000209;IPR036852;IPR023827;IPR022398;IPR023828;IPR015500;IPR032815;IPR038466;
2.60.120.260;3.30.70.850;3.40.50.200;
A0A059AF78
MESCNCVEPQWPADELLMKYQYLSDFFIALAYFSIPLELIYFVKKSAVFPYRWVLVQFGAFIVLCGATHLINLWTFAIHSRTVAYVMTIAKVLTAAVSCITALMLVHIIPDLLSVKTRELFLKNKAAELDREMGLIRTQEETGRHCALWMPTRSGLELQLSYTLRQQQNPVGYTVPIHLPVINRVFSSNRALKISPNSPVARIRPLAGKYIPGEVVAVRVPLLHLSNFQINDWPELSTKRYALMVLMLPSDSARQWHVHELELVEVVADQVAVALSHAAILEESMRARDLLMEQNVALDLARREAETAIRARNDFLAVMN...
Eucalyptus grandis (Flooded gum)
null
2.7.13.3
null
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000256|PIRSR:PIRSR026389-2}; Note=Binds 1 copper ion per dimer. {ECO:0000256|PIRSR:PIRSR026389-2};
null
null
null
null
ATP-binding;Copper;Disulfide bond;Endoplasmic reticulum;Ethylene signaling pathway;Kinase;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Receptor;Transferase;Transmembrane;Transmembrane helix
cell division [GO:0051301]; cytokinin metabolic process [GO:0009690]; defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; detection of ethylene stimulus [GO:0009727]; hydrogen peroxide biosynthetic process [GO:0050665]; negative regulation of ethylene-activated ...
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
ATP binding [GO:0005524]; ethylene binding [GO:0051740]; ethylene receptor activity [GO:0038199]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphorelay sensor kinase activity [GO:0000155]
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
IPR011006;IPR014525;IPR003018;IPR029016;IPR003594;IPR036890;IPR005467;IPR003661;IPR036097;IPR004358;IPR001789;
1.10.287.130;3.30.450.40;3.40.50.2300;3.30.565.10;
A0A059TC02
MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPI...
Petunia hybrida (Petunia)
FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:24985707, PubMed:25217505). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed...
1.2.1.44
CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; Ph...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=208.6 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:25217505}; KM=307.6 uM for feruloyl-CoA {ECO:0000269|PubMed:25217505}; KM=270.3 uM for sinapoyl-CoA {ECO:0000269|PubMed:25217505}; Vmax=1235.7 nmol/sec/mg enzyme with p-coumaroyl-CoA as substrate {ECO:0000269|PubMed:...
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:25217505};
null
3D-structure;Cytoplasm;Disulfide bond;Lignin biosynthesis;NADP;Nucleotide-binding;Oxidoreductase;Phenylpropanoid metabolism
circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699]
cytoplasm [GO:0005737]
cinnamoyl-CoA reductase activity [GO:0016621]; nucleotide binding [GO:0000166]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24985707}.
PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000269|PubMed:25217505}.
null
IPR001509;IPR036291;
3.40.50.720;
A0A060WBM3
MEAFNHKLNTYIDSWMGPRDERVQGWLLLDNYPPTFALTLMYLLIVWLGPKYMRHRQPVSCQGLLVLYNLALTLLSFYMFYEMVSAVWQGGYNFYCQDTHSAGETDTKIINVLWWYYFSKVIEFMDTFFFILRKNNHQITFLHIYHHASMLNIWWFVMNWVPCGHSYFGASLNSFIHVLMYSYYGLSAVPAIRPYLWWKRYITQGQLIQFFLTMSQTICAVIWPCGFPRGWLFFQIFYMASLIALFSNFYIQTYKKHRVSQKKAYHQNGSVDSLNGHANGVTPTETITHRKVRAD
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that...
2.3.1.199
CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(13Z)-eicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39679, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:75121, ChEBI:CHEBI:76559; Evidence={ECO:0000256|ARBA:ARBA00001296}; PhysiologicalDirection=left...
null
null
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03205}.
null
null
Cell projection;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Lipid biosynthesis;Lipid metabolism;Membrane;Reference proteome;Transferase;Transmembrane;Transmembrane helix
fatty acid elongation [GO:0030497]; fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO...
dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]
fatty acid elongase activity [GO:0009922]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=...
null
null
IPR002076;IPR033677;
null
A0A060XQE7
MEEIVVAGISGRLPESNNLEEFWENLFNGVDMVTEDDRRWKPGLYGLPKRNGKLKDISRFDAAFFGVHPKQAHTMDPQLRLMLEIAYEAIVDGGLNPTELRGSRTGVYIGVSGSEAGEAFSRDPEELLGYSMTGCQRAMFANRLSYFFDFNGPSTAIDTACSSSLLALENAFNAIRHGHCDAALVGGVNLLLKPNTSVQFMKLGMLSPEGTCKSFDSSGNGYCRSEAAVAVLLTRRSMAKRVYATVLNAGNNTDGYKEQGVTFPSGEMQQRLVRSLYQEVNITPDQVEYIEAHGTGTKVGDPQEVNGIVSVFCHSKRDPL...
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
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;NAD;Phosphopantetheine;Phosphoprotein;Pyridoxal phosphate;Reference proteome;S-nitrosylation;Transferase
cellular response to insulin stimulus [GO:0032869]; fatty acid biosynthetic process [GO:0006633]
cytoplasm [GO:0005737]
(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;IPR049391;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;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;
A0A061AE05
MLTPRDENNEGDAMPMLKKPRYSSLSGQSTNITYQEHTISREERAAAVGRHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENVKFIEVHVSTTLEVCEQRDPKPSELYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLPEQIPDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDLKHKVAFVGEKSD...
Caenorhabditis elegans
FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway (PubMed:16497669). The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group fro...
2.7.1.25; 2.7.7.4
CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|PubMed:16497669}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate...
null
null
PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000303|PubMed:16497669}.
null
null
Alternative splicing;ATP-binding;Developmental protein;Kinase;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;Nucleus;Reference proteome;Transferase
3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103]
nucleus [GO:0005634]
adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; sulfate adenylyltransferase (ATP) activity [GO:0004781]
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16497669}.
null
null
IPR002891;IPR025980;IPR027417;IPR015947;IPR014729;IPR024951;IPR002650;
3.40.50.620;3.40.50.300;3.10.400.10;
A0A061I403
MPMASVIAVAEPKWISVWGRFLWLTLLSMALGSLLALLLPLGAVEEQCLAVLRSFHLLRSKLDRTQHVVTKCTSPSTELSVTSGDVGLLTVKTKTSPAGKLEAKAALNQALEMKRQGKREKAHKLFLHALKMDPGFVDALNEFGIFSEEEKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTIDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPH...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (PubMed:27918543). The side chain of Glu-231 determines which of the two ...
2.7.7.108; 3.1.4.-
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+). {ECO:0000250|UniProtKB:Q9BVA6};
null
null
null
null
ATP-binding;Endoplasmic reticulum;Glycoprotein;Hydrolase;Magnesium;Manganese;Membrane;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Reference proteome;Repeat;Signal-anchor;TPR repeat;Transferase;Transmembrane;Transmembrane helix;Unfolded protein response
protein adenylylation [GO:0018117]; protein deadenylylation [GO:0044602]; regulation of IRE1-mediated unfolded protein response [GO:1903894]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986]
endoplasmic reticulum membrane [GO:0005789]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}.
PTM: Auto-AMPylated in vitro. {ECO:0000250|UniProtKB:Q9BVA6}.
DOMAIN: The fido domain mediates the adenylyltransferase activity. {ECO:0000250|UniProtKB:Q9BVA6}.
IPR003812;IPR036597;IPR040198;IPR011990;
1.10.3290.10;1.25.40.10;
A0A061IKA1
MESKALLLVALGVWLQSLTASQGGVAAADGGRDFTDIESKFALRTPDDTAEDNCHLIPGIAESVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNVGYEINKV...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipopr...
3.1.1.34
CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000256|ARBA:ARBA00000652}; PhysiologicalDirection=left-t...
null
null
null
null
null
Calcium;Cell membrane;Chylomicron;Disulfide bond;Extracellular matrix;Glycoprotein;Heparin-binding;Hydrolase;Lipid degradation;Lipid metabolism;Lipoprotein;Membrane;Metal-binding;Nitration;Secreted;Signal;VLDL
fatty acid biosynthetic process [GO:0006633]; response to glucose [GO:0009749]; triglyceride catabolic process [GO:0019433]; very-low-density lipoprotein particle remodeling [GO:0034372]
chylomicron [GO:0042627]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361]
1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; apolipoprotein binding [GO:0034185]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; metal ion binding [GO:0046872]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362020}; Peripheral membrane protein {ECO:0000256|RuleBase:RU362020}; Extracellular side {ECO:0000256|RuleBase:RU362020}. Secreted {ECO:0000256|RuleBase:RU362020}. Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|...
PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000256|RuleBase:RU362020}.
null
IPR029058;IPR013818;IPR016272;IPR033906;IPR002330;IPR001024;IPR036392;IPR000734;
3.40.50.1820;2.60.60.20;
A0A067XGX8
MALTATATTRGGSALPNSCLQTPKFQSLQKPTFISSFPTNKKTKPRTKHISAVQSPPSTTKWNLESWKTKPAFQLPDYPDKVELESVLKTLSTYPPIVFAGEARNLEEKLGEAALGNAFLLQGGDCAESFKEFSANNIRDTFRVMLQMGVVLMFGGQMPVIKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNVNGDAFDEKSRIPDPHRMVRAYTQSVATLNLLRAFASGGYAAMQRVNQWNLDFTDQSEQGDRYRELAHRVDEAMGFMTAAGLTVDHTIMTTTDFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMI...
Petunia hybrida (Petunia)
FUNCTION: Involved in the production of volatile organic compounds (VOCs) (PubMed:24815009). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). {ECO:000...
2.5.1.54
CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512};
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}.
null
null
Amino-acid biosynthesis;Aromatic amino acid biosynthesis;Chloroplast;Manganese;Metal-binding;Plastid;Transferase;Transit peptide
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]
chloroplast [GO:0009507]
3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; metal ion binding [GO:0046872]
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}.
null
null
IPR013785;IPR002480;
3.20.20.70;
A0A067XH53
MALSTNSTTSSLLPKTPLVQQPLLKNASLPTTTKAIRFIQPISAIHSSDSSKNTPIVSAKPSSPPAATSTAAATAVTKQEWSIDSWKTKKALQLPEYPNQEELKNVLKTIEDFPPIVFAGEARHLEEKLGEAAMGRAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVIKVGRMAGQFAKPRSDNFEEKNGVKLPSYRGDNVNGDAFDLKSRTPDPQRLIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELANRVDEALGFMNAAGLTTDHPIMTTTEFWTSHECLLLPYEQS...
Petunia hybrida (Petunia)
FUNCTION: Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:24815009). Catalyz...
2.5.1.54
CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512};
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}.
null
null
Amino-acid biosynthesis;Aromatic amino acid biosynthesis;Chloroplast;Manganese;Metal-binding;Plastid;Transferase;Transit peptide
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; green leaf volatile biosynthetic process [GO:0010597]
chloroplast [GO:0009507]
3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; metal ion binding [GO:0046872]
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}.
null
null
IPR013785;IPR002480;
3.20.20.70;
A0A067XR63
MNAEGGNLHREFEITWGDGRARIHNNGGLLTLSLDRASGSGFRSKNEYLFGRIEIQIKLVAGNSAGTVATYYLSSEGPTHDEIDFEFLGNSSGEPYTLHTNVFSQGKGNREQQFFLWFDPTMDFHTYTILWNPQRIIFYVDETPIREFKNLERHGIPFPRSQAMRVYSSMWNADDWATRGGLVKTDWTKAPFTASYRSYKADACVWSGEASSCGSQDSNPSDKWWMTEELNATRMKRLRWVQKKYMVYNYCVDKMRFPEGLAPECNIS
Diospyros kaki (Kaki persimmon) (Diospyros chinensis)
FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall assembly and synthesis in fast growing tissues and in the maintenance of firmness in mature fruits. {ECO:0000269|PubMed:27242828}.
2.4.1.207
CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:...
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5-6. Activity decreases sharply when the pH is lowered from 5 to 4. {ECO:0000269|PubMed:27242828};
null
Cell wall biogenesis/degradation;Cytoplasm;Disulfide bond;Fruit ripening;Glycoprotein;Glycosidase;Glycosyltransferase;Hydrolase;Transferase
cell wall assembly [GO:0070726]; fruit ripening [GO:0009835]; xyloglucan metabolic process [GO:0010411]
apoplast [GO:0048046]; cytoplasm [GO:0005737]
hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; xyloglucan:xyloglucosyl transferase activity [GO:0016762]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27242828}. Note=Dispersed throughout the cell. {ECO:0000269|PubMed:27242828}.
PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}.
null
IPR044791;IPR008264;IPR013320;IPR000757;IPR008263;IPR010713;IPR016455;
2.60.120.200;
A0A067YMX8
MAASPYSIFAVQLLLLASWMLSSSSSNFNQDFNIAWGGGRARILNNGELVTLSLDKASGSGFRSKNLYLFGKIDMQLKLVPGNSAGTVTTYYLSSEGSVRDEIDFEFLGNLTGEPYTLHTNVYSHGKGEREQQFRLWFDPAADFHTYSILWNSKTIVFYVDQTPVREFKNMESIGVPYLRQPMRLFSSIWNADEWATRGGLIKTDWTQAPFTTSYRNFRADNACVWAAKASSCGLAAGGNAWLSVELDAKSRGRLRWVRRNQMIYDYCVDGKRFPRGVPPECKLNLHI
Diospyros kaki (Kaki persimmon) (Diospyros chinensis)
FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Overexpression in Arabidopsis transgenic plants causes accelerated dark-induced leaf senescence and higher lipid peroxidation of the leaf cells. Overexpression in tr...
2.4.1.207
CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:...
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6. Activity decreases sharply when the pH is lowered from 5 to 4. {ECO:0000269|PubMed:27966647};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 30-40 degrees Celsius. {ECO:0000269|PubMed:27966647};
Apoplast;Cell wall;Cell wall biogenesis/degradation;Disulfide bond;Fruit ripening;Glycoprotein;Glycosidase;Glycosyltransferase;Hydrolase;Secreted;Signal;Transferase
cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; cellular response to gibberellin stimulus [GO:0071370]; fruit ripening [GO:0009835]; response to abscisic acid [GO:0009737]; xyloglucan catabolic process [GO:2000899]
apoplast [GO:0048046]
hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; polysaccharide binding [GO:0030247]; xyloglucan:xyloglucosyl transferase activity [GO:0016762]
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27966647}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}.
PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}.
null
IPR044791;IPR013320;IPR000757;IPR008263;IPR010713;IPR016455;
2.60.120.200;
A0A068C605
MERLDKTINSYLDVWLGPRDPRVKGWLLLENYTPTFIFSVLYLLIVWLGPKYMRNKQPFSCRGILVVYNLGLTLLSLYMFYELVTGVWEGGYNFFCQDTHSGGEADMKIIRVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHATMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSAVPAMRPYLWWKKYITQGQLTQFVLTIFQTSCGVVWPCAFPQGWLYFQISYMISLIILFTNFYIQTYNKKASSRRKEYQNGSAATVNGYTNSFSSLENNVKQRKQRKD
Anas platyrhynchos (Mallard) (Anas boschas)
FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that...
2.3.1.199
CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(13Z)-eicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39679, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:75121, ChEBI:CHEBI:76559; Evidence={ECO:0000256|ARBA:ARBA00001296}; PhysiologicalDirection=left...
null
null
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03205}.
null
null
Cell projection;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Lipid biosynthesis;Lipid metabolism;Membrane;Transferase;Transmembrane;Transmembrane helix
fatty acid elongation [GO:0030497]; fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO...
dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]
fatty acid elongase activity [GO:0009922]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=...
null
null
IPR002076;IPR033677;
null
A0A072TFB1
MKKLLAALALAVVAVPVWAATQTVTLSVPGMTCAACPITVKHALSQVTGVEKTDVRFEQREAVVTFDDGKTSVQALTKATADAGYPSPVCLAASCRRWAVRAASRDRQSGRHHWSGLPEPVRRVVHPHPATGLRRRRAVRQCGRLAQASAVAPYRARPDRAAAGAGSRVCDARLWRAQRLAALSRSRHYGGDIALGPVLPGPTQRSKAMMTLKIDGMTCASCAEHVRQALEKVPGVRSAAVSYSKALADLTVDEGVSHDTLTAAVTTAGYHARVADVPPHSAGLPGKTPGSAETGGKRSGGDSALRVAVIGSGGAAMAAA...
Medicago truncatula (Barrel medic) (Medicago tribuloides)
FUNCTION: Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase. {ECO:0000256|ARBA:ARBA00025326}.
1.16.1.1; 4.99.1.2
CATALYTIC ACTIVITY: Reaction=H(+) + Hg + NADP(+) = Hg(2+) + NADPH; Xref=Rhea:RHEA:23856, ChEBI:CHEBI:15378, ChEBI:CHEBI:16170, ChEBI:CHEBI:16793, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.1; Evidence={ECO:0000256|ARBA:ARBA00000896}; CATALYTIC ACTIVITY: Reaction=an alkylmercury + H(+) = an alkane + Hg(2+); Xref=Rh...
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974};
null
null
null
null
Copper;FAD;Flavoprotein;Lyase;Mercuric resistance;Mercury;Metal-binding;NADP;Oxidoreductase;Periplasm;Redox-active center;Reference proteome;Signal
organomercury catabolic process [GO:0046413]
null
alkylmercury lyase activity [GO:0018836]; copper ion binding [GO:0005507]; flavin adenine dinucleotide binding [GO:0050660]; mercury (II) reductase activity [GO:0016152]; mercury ion binding [GO:0045340]; mercury ion transmembrane transporter activity [GO:0015097]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955];...
SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
null
null
IPR036188;IPR023753;IPR016156;IPR017969;IPR006122;IPR006121;IPR036163;IPR004927;IPR024259;IPR021179;IPR011795;IPR004099;IPR012999;IPR036390;
3.30.390.30;3.30.450.410;3.30.70.100;3.50.50.60;
A0A072ULZ1
MEENKKTVDGSVDFTEEQEALVVKSWNAMKNNSCDLSLKFFTKILEIAPPAKQMFSFLKDSNVPLEQNPKLKPHAMSVFLMTCESAVQLRKAGKVRVRESNLKKLGATHFKTGVQDEHFEVTKQALLETIEEAIPEMWSLAMKNAWAEAHDQLANAIKVEMKEAHDQMDNANLIINMEENTGSCFTEEQEALVVKSWNAIKYNSGDLSLKFFKKILEIAPPAKQLFSFLKDSNVPLEHNPKLKPHAMSVFLMTCESAVQLRKAGKVTVRESNLKKLGATHFKTGVKDEHFEVTKQALLETIKEALPEMWSPAMENAWGEA...
Medicago truncatula (Barrel medic) (Medicago tribuloides)
FUNCTION: Phytoglobin that regulates the fine tuning of nitric oxide (NO) concentration in the cytosol in response to sudden changes in O(2) availability, and performs both symbiotic and nonsymbiotic functions (PubMed:33329665). Exhibits NO dioxygenase activity in the presence of O(2) but nitrite reductase (NiR) activi...
1.7.2.-
CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:00002...
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:33329665}; Note=Binds 2 heme groups per subunit. {ECO:0000269|PubMed:33329665};
null
null
null
null
Alternative splicing;Cytoplasm;Heme;Iron;Metal-binding;Nodulation;Nucleus;Oxidoreductase;Oxygen transport;Reference proteome;Repeat;Transport
response to ammonium ion [GO:0060359]; response to hypoxia [GO:0001666]; response to nitrate [GO:0010167]; response to nitric oxide [GO:0071731]; response to symbiotic bacterium [GO:0009609]
null
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}.
null
null
IPR000971;IPR009050;IPR012292;IPR001032;IPR019824;
1.10.490.10;
A0A072UR65
MANILNLKHLLTLALILLALATKSSTSSSSSITRVKGIYWLENPFFPPTTVDTSLFTHIFYSFLTPNNITYKLEISSSQILSLNTFTKTFKTKSPPAATLFSIGGAGSNSSLLAFIASDPPACAAFINSTIDVARTFGFDGIDLDWEFPKNTKEMNDLGEMLFQWRKAISDEGATTGRPPLLLTAAVYFAVNFSIYGEPRMYPVNSINENLDWVNVMSYELRGPRSNKTGAPSGTFDPKSNVSVVSGLLSWIHSGVVPEKLVMGMPLYGKSWKLRDPNVHGIGAPSVGSGPGVNGLMAYFQVLDFNRQKSAKVEYDVDTA...
Medicago truncatula (Barrel medic) (Medicago tribuloides)
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
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.5 mM for (GlcNAc)6 {ECO:0000269|PubMed:27383628}; KM=8.6 mM for (GlcNAc)5 {ECO:0000269|PubMed:27383628};
PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305}.
null
null
Carbohydrate metabolism;Chitin degradation;Glycoprotein;Glycosidase;Hydrolase;Plant defense;Polysaccharide degradation;Reference proteome;Signal
chitin catabolic process [GO:0006032]; defense response to fungus [GO:0050832]; 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;
A0A072VDF2
MPAATAAAAAESSSVSGETICVTGAGGFIASWMVKLLLEKGYTVRGTLRNPDDPKNGHLKKLEGAKERLTLVKVDLLDLNSVKEAVNGCHGVFHTASPVTDNPEEMVEPAVNGAKNVIIAGAEAKVRRVVFTSSIGAVYMDPNRSVDVEVDESCWSDLEFCKKTKNWYCYGKAVAEAAAWDVAKEKGVDLVVVNPVLVLGPLLQPTINASTIHILKYLTGSAKTYANATQAYVHVRDVALAHILVYEKPSASGRYLCAETSLHRGELVEILAKYFPEYPIPTKCSDEKNPRVKPHIFSNKKLKDLGLEFTPVSECLYETV...
Medicago truncatula (Barrel medic) (Medicago tribuloides)
FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:20876124). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:20876124). Mediates the conversion of feruloyl-CoA to coniferylaldehyde (PubMed:20876124). Also ...
1.2.1.-; 1.2.1.44
CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=54.5 uM for feruloyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=7.2 uM for sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=161 uM for caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|Pub...
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000250|UniProtKB:A0A059TC02}.
null
null
Cytoplasm;Disulfide bond;NADP;Oxidoreductase;Reference proteome
lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699]
cytoplasm [GO:0005737]
cinnamoyl-CoA reductase activity [GO:0016621]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}.
PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000250|UniProtKB:A0A059TC02}.
null
IPR001509;IPR036291;
3.40.50.720;
A0A075D5I4
MAEKQQAVAEFYDNSTGAWEVFFGDHLHDGFYDPGTTATIAGSRAAVVRMIDEALRFANISDDPAKKPKTMLDVGCGIGGTCLHVAKKYGIQCKGITISSEQVKCAQGFAEEQGLEKKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPIVIVSYAHRNLSPSEGSLKPEEKKVLKKICDNIVLSWVCSSADYVRWLTPLPVEDIKAADWTQNITPFYPLLMKEAFTWKGFTSLLMKGGWSAIKVVLAVRMMAKAADDGVLKFVAVTCRKSK
Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with l...
2.1.1.-
CATALYTIC ACTIVITY: Reaction=picrinine + S-adenosyl-L-methionine = ervincine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70505, ChEBI:CHEBI:194555; Evidence={ECO:0000269|PubMed:26848097}; PhysiologicalDirection=left-to-right; Xref=Rhea:R...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for picrinine {ECO:0000269|PubMed:26848097}; KM=9.3 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:26848097}; Vmax=126.1 pmol/sec/mg enzyme with picrinine as substrate {ECO:0000269|PubMed:26848097}; Vmax=97.2 pmol/sec/mg enzyme with S-adenosyl-L-methionin...
PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:26848097};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. {ECO:0000269|PubMed:26848097};
Alkaloid metabolism;Membrane;Methyltransferase;S-adenosyl-L-methionine;Transferase;Vacuole
alkaloid biosynthetic process [GO:0009821]; methylation [GO:0032259]; vindoline biosynthetic process [GO:1900985]
plant-type vacuole membrane [GO:0009705]
N-methyltransferase activity [GO:0008170]
SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:35166361}.
null
null
IPR025714;IPR025774;IPR029063;
3.40.50.150;
A0A075D657
MYTCSIIIYILTFWQLSKIKKQVAAAEKQVMTVTEKQEAVAEFYDKSTDAWEVFFGEHLHDGFYEPGTTATIPGSKVAVVRMIDELLRFAGISDDPEKKPKTMLDVGCGLGGTCLHVAKKYDIKCTGITISPEQVKCAQDLAATQGLESKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPVVIAGYAARNLSPSEESLKPEEKMVLEKICDHIVLSWLCSTGDYVKWLTPLPVQDIKVWDLTQNITPFYPLCIKEAFTWKSFTSLLKMGGWSAIKVVFAVKMMAMAAEEGLLKFAAVTCRK...
Vinca minor (Common periwinkle)
FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with l...
2.1.1.-
CATALYTIC ACTIVITY: Reaction=picrinine + S-adenosyl-L-methionine = ervincine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70505, ChEBI:CHEBI:194555; Evidence={ECO:0000269|PubMed:26848097}; PhysiologicalDirection=left-to-right; Xref=Rhea:R...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.1 uM for picrinine {ECO:0000269|PubMed:26848097}; KM=15.8 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:26848097}; Vmax=100.8 pmol/sec/mg enzyme with picrinine as substrate {ECO:0000269|PubMed:26848097}; Vmax=135 pmol/sec/mg enzyme with S-adenosyl-L-methion...
PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:26848097};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. {ECO:0000269|PubMed:26848097};
Alkaloid metabolism;Cytoplasm;Methyltransferase;S-adenosyl-L-methionine;Transferase
alkaloid biosynthetic process [GO:0009821]; methylation [GO:0032259]; vindoline biosynthetic process [GO:1900985]
cytosol [GO:0005829]
N-methyltransferase activity [GO:0008170]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35166361}.
null
null
IPR013216;IPR025774;IPR029063;
3.40.50.150;
A0A075FBG7
MSITFNLKIAPFSGPGIQRSKETFPATEIQITASTKSTMTTKCSFNASTDFMGKLREKVGGKADKPPVVIHPVDISSNLCMIDTLQSLGVDRYFQSEINTLLEHTYRLWKEKKKNIIFKDVSCCAIAFRLLREKGYQVSSDKLAPFADYRIRDVATILELYRASQARLYEDEHTLEKLHDWSSNLLKQHLLNGSIPDHKLHKQVEYFLKNYHGILDRVAVRRSLDLYNINHHHRIPDVADGFPKEDFLEYSMQDFNICQAQQQEELHQLQRWYADCRLDTLNYGRDVVRIANFLTSAIFGEPEFSDARLAFAKHIILVTR...
Marrubium vulgare (White horehound)
FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to 9,13(R)-epoxy-labd-14-e...
4.2.3.131; 4.2.3.189; 4.2.3.190
CATALYTIC ACTIVITY: Reaction=peregrinol diphosphate = (13R)-9,13-epoxylabd-14-ene + diphosphate; Xref=Rhea:RHEA:54512, ChEBI:CHEBI:33019, ChEBI:CHEBI:138232, ChEBI:CHEBI:138233; EC=4.2.3.189; Evidence={ECO:0000269|PubMed:24990389}; CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene; Xref=...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q40577}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:24990389}.
null
null
Chloroplast;Lyase;Magnesium;Metal-binding;Plastid;Transit peptide
gibberellin biosynthetic process [GO:0009686]; miltiradiene biosynthetic process [GO:1901946]
chloroplast [GO:0009507]
9,13-epoxylabda-14-ene synthase activity [GO:0106239]; magnesium ion binding [GO:0000287]; manoyl oxide synthase activity [GO:0062206]; miltiradiene synthase activity [GO:0062205]; terpene synthase activity [GO:0010333]
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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:G8GJ94}.
IPR008949;IPR001906;IPR036965;IPR005630;IPR008930;
1.10.600.10;1.50.10.130;
A0A075TMP0
MASTTPSTYKQAVFKEQGAGLTLEEVALTLPKRDEILVKVEACGVCHSDHFAQTNLMGGGFPLVPGHEIIGRVAAVGEGETVWKEGDRIGGAWHGGHDGTCGACKKGFFQMCDNEQVNGISRNGGYAEYCIIRREAAVHIPDHVNAAKYAPMLCAGVTVFNAMRHMKIPPGELVAIQGLGGLGHLALQYANKFGYRVVALSRDSTKEEFARKLGAHEYIDTSREDPVAALQKLGGASLIVSTAPVPEIINPLIQGLGVMGKLLILSIVGGIEVHTGLLVGKGKSIWSWPSGHATDSEDAIAFADLHGIDCLIEEFPLDKC...
Penicillium expansum (Blue mold rot fungus)
FUNCTION: Alcohol dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatD catalyzes the conversion...
1.1.1.-
CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + neopatulin = (E)-ascladiol + NADP(+); Xref=Rhea:RHEA:62224, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145111, ChEBI:CHEBI:145112; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62225; Evidence={ECO:00002...
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q96533}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96533};
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
null
null
Cytoplasm;Metal-binding;NAD;NADP;Oxidoreductase;Reference proteome;Zinc
patulin biosynthetic process [GO:0140723]
cytosol [GO:0005829]
alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase (NADP+) activity [GO:0008106]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
null
null
IPR013149;IPR013154;IPR011032;IPR036291;IPR020843;
3.90.180.10;3.40.50.720;
A0A075TMP8
MDILQLAPTHLLAILLSSTSALFLITYLLRAGHRPSDLPNGPPTVPLFGNELQVPKSDAHFQFSRWAKEYGGFFTLKRYNNTTIVISDQKLIKTLLDKKSNIYSHRPASLVSHLITQSDHLLVMQYGERWRMLRKTIHQYFMEPRCERDHWKVQEAEAKQMLHDYLTMPEDHMLHPKRYSNSITNSLVFGIRTKTVHDEYMKKLFYLMDKWSLVQELGATPPVDSFALLRYVPQWMLGNWRNRAVEVGDLMQSLYQTVLDQVKERRQRGIQRDSFMDRVLDTLKQTPLSENELRFLGGVLMEGGSDTSSSLILTIIQAMT...
Penicillium expansum (Blue mold rot fungus)
FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatI catalyzes the co...
1.-.-.-
CATALYTIC ACTIVITY: Reaction=3-hydroxybenzyl alcohol + O2 + reduced [NADPH--hemoprotein reductase] = gentisyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:62212, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:5325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI...
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
null
null
Endoplasmic reticulum;Glycoprotein;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix
patulin biosynthetic process [GO:0140723]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}.
null
null
IPR001128;IPR002401;IPR036396;
1.10.630.10;
A0A075TR33
MRLHQSPPRLLVCILSVLQVSAGLSSNCRCMPGDSCWPSLNDWARFNTSIGGRLVDTQPLGQPCHDPFYTASECNELKQQWTHPELHDASSSSIMSAAVANETCDAFTPRSKPCTLGAMVRYAVNASSPDDFVQTIRFSQERNIRLVIRNTGHDYAGKSTGAGALSIWTHSLKEIDFLNYTSAHYTGPAVRMTAGIQGTDINPAAHKKGLVIVGGECATVGPVGGFTQGGGHSALSSRFGLAADQVLEWEVVDGMGRLLTASPTQNPDLYWALSGGGGGTFGVVYAVTVKTFPDFAVTGVVLQFENIDPSSNRFFEAVGH...
Penicillium expansum (Blue mold rot fungus)
FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatO acts with patJ in th...
1.-.-.-
null
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
null
null
FAD;Flavoprotein;Glycoprotein;Oxidoreductase;Reference proteome;Signal;Vacuole
patulin biosynthetic process [GO:0140723]
fungal-type vacuole lumen [GO:0000328]; vacuole [GO:0005773]
FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218]
SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}.
null
null
IPR012951;IPR016166;IPR036318;IPR016169;IPR006094;
3.30.465.10;
A0A075TR41
MAPFVPYHYSAGQSTIVKFGGLLTTEFLEPPPGRCFLFRQTYRHTIEGSIPENLRKLINSPDRPKGPPPHFHQFQTEYFRVENGVLGISVDGVVRRITPEDGEISVKAGSVHNFFIHPDSPENMTVYLSASDSGNDYQLDRVFFENWYGYWHDALLHDGGIDWIQFLAIQDGGDAYTPAPAWVPFRRQVGYWTCVIVGRWIGGLLGYKPFFREYTTDWDFAVAKMKGSFFQRHLVHAAFEEEKSWTKQAELEPKGKPENAEFEPWTEDMSPAPLSLGPVAYEQGLFHGVQPGSVNGSNGHSTGVESKLEQLGSRAQRRVV...
Penicillium expansum (Blue mold rot fungus)
FUNCTION: Probable oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatJ acts with patO in the ...
1.-.-.-
null
null
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
null
null
Cytoplasmic vesicle;Oxidoreductase;Reference proteome;Vacuole
patulin biosynthetic process [GO:0140723]
cytoplasmic vesicle lumen [GO:0060205]; fungal-type vacuole lumen [GO:0000328]; vacuole [GO:0005773]
oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218]
SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:30680886}.
null
null
IPR014710;IPR011051;
2.60.120.10;
A0A075TRC0
MHSVSPSTYPSGGTSPAPADTPGTEYSEYEFSNDVAVVGMACRVAGGNHNPELLWQSLLSQKSAVGEIPEMRWEPYYRRDPRNAKELKKTTSRGYFLDRLEDFDCQFFGISPKEAEQMDPQQRVSLEVASEALEDAGIPAKSLSGSDTAVFWGVNSDDYSKLVLEDLPNVEAWMGIGTAYCGVPNRISYHLNLMGPSTAVDAACASSLVAVHHGVQAIRLGESQVAIVGGVNALCGPGLTRVLDKAGAISSDGSCKSFDDDAHGYARGEGAGALVLKSLHRALLDHDNVLAVIKGSAVAQDGKTNGIMAPNAKAQQLAAR...
Penicillium expansum (Blue mold rot fungus)
FUNCTION: 6-methylsalicylic acid synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886, PubMed:35339702). Pa...
2.3.1.165
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 3 CO2 + 4 CoA + H2O + NADP(+); Xref=Rhea:RHEA:12240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:36658, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; ...
null
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
null
null
Cytoplasm;Multifunctional enzyme;NADP;Phosphopantetheine;Phosphoprotein;Reference proteome;Transferase
fatty acid biosynthetic process [GO:0006633]; patulin biosynthetic process [GO:0140723]
cytosol [GO:0005829]
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; 6-methylsalicylic acid synthase activity [GO:0050641]; fatty acid synthase activity [GO:0004312]; phosphopantetheine binding [GO:0031177]; polyketide synthase activity [GO:0016218]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
null
DOMAIN: Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a produ...
IPR001227;IPR036736;IPR014043;IPR016035;IPR018201;IPR014031;IPR014030;IPR016036;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049552;IPR013968;IPR049900;IPR020806;IPR009081;IPR006162;IPR016039;
3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.40.50.720;3.10.129.110;
A0A075TRK9
MRLTSGIFHAAIAVAAVGAVLPEGPSSSKTHRNEYARRMLGSSFGIPKNQTFDYLVIGGGTAGLTIATRLAEQGVGSVAVIEAGGFYELNNGNLSQIPAQDAFYVGTDLDDWQPGIDWGFHTTPQAGAYDRVSHYARGKCLGGSSARNYMAYQRGTKAAHQRWADTVGDSSYTWEQFLPFFEKSLHFTPANDALRGANASVVSDPSVLGNGDGPLSVTYPHYAQAFATWAKHAFIEIGLQIRSGFQSGALLGQSYGLYTINATTMHRESSETSFLRKGLADPNLTVFQSALAKRIRFQDKRAVGVDVETMGRAYTLSARK...
Penicillium expansum (Blue mold rot fungus)
FUNCTION: Patulin synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatE catalyzes the last step of th...
1.1.-.-
CATALYTIC ACTIVITY: Reaction=(E)-ascladiol + A = AH2 + patulin; Xref=Rhea:RHEA:62228, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:74926, ChEBI:CHEBI:145112; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62229; Evidence={ECO:0000269|PubMed:30680886};
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:E4QP00};
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
null
null
3D-structure;Cell wall;Cytoplasm;FAD;Flavoprotein;Glycoprotein;Oxidoreductase;Reference proteome;Secreted;Signal;Vacuole
patulin biosynthetic process [GO:0140723]
cell cortex [GO:0005938]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; vacuole [GO:0005773]
flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on CH-OH group of donors [GO:0016614]; polyketide synthase activity [GO:0016218]
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:30680886}. Vacuole {ECO:0000269|PubMed:30680886}. Secreted {ECO:0000269|PubMed:30680886}. Secreted, cell wall {ECO:0000269|PubMed:30680886}.
null
null
IPR036188;IPR012132;IPR000172;IPR007867;
3.50.50.60;3.30.560.10;
A0A075TRL5
MEPFLLLLLVLLPAIVLVRYAFTYGHRTSTMPIGPPTLPFIGNIHQITKKYTHIKFTEWAAQYGGLYMLKIGNGNMAVITDRRLVKEVLDRKSGIYSHRPHSFVSHDLITKGNHLLVMHYGDQWRTFRRLVHQHLMETMVENHHTKIVNAEAIQLVRDYMIDPEHHMAHPKRYSNSITNSIVFGIRTANREGANMRRLYKLMEEWSEVMETGATPPVDLFPWLKLLPQWLFNNYIDRAKAIGVQMETLYVDILNKVIKRREDGHNNGTFMDKVLDSQEKHNLPWHQLAFIGGVLMEGGSDTSSSLTLAIVQALIQNPDVQ...
Penicillium expansum (Blue mold rot fungus)
FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatH catalyzes the co...
1.-.-.-
CATALYTIC ACTIVITY: Reaction=3-methylphenol + O2 + reduced [NADPH--hemoprotein reductase] = 3-hydroxybenzyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:62208, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17069, ChEBI:...
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
null
null
Endoplasmic reticulum;Glycoprotein;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix
patulin biosynthetic process [GO:0140723]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}.
null
null
IPR001128;IPR002401;IPR036396;
1.10.630.10;
A0A075TXZ1
MAKIDVHHHFYPPAMRQALDRAGGDPSGWYIPPWTLELDQDITRQMKVTTTILSVTAPGPGIEPDVTKAAALARSCNESAAAIRDAKPQQYGFFASVPSLFDTAAVLKEIEYACTTLRADGVTLFTRYGKGSNYLGHAAFRPIWADLSRRGAVVFIHPTHPVDTQLINTWLPQPMFDYPHETGRAAMDLLTSGILQDYPGCKIILSHAGGTLPYLIHRAATMLPLMPRTLGLSTEELVEAARTFYFDTAISSNPVTLKALFEFAAPGHVLFGSDFPNAPHDAILRFTNFLEAYELPEETKRQVDSGAALELFPRLKGILD...
Penicillium expansum (Blue mold rot fungus)
FUNCTION: 6-methylsalicylic acid decarboxylase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatG catalyzes...
4.1.1.52
CATALYTIC ACTIVITY: Reaction=6-methylsalicylate + H(+) = 3-methylphenol + CO2; Xref=Rhea:RHEA:23112, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17231, ChEBI:CHEBI:36658; EC=4.1.1.52; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23113; Evidence={ECO:0000269|PubMed:3...
null
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
null
null
Cytoplasm;Decarboxylase;Hydrolase;Lyase;Metal-binding;Reference proteome;Zinc
patulin biosynthetic process [GO:0140723]
cytosol [GO:0005829]
6-methylsalicylate decarboxylase activity [GO:0047596]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; polyketide synthase activity [GO:0016218]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
null
null
IPR032465;IPR006680;IPR032466;
3.20.20.140;
A0A076FFM5
MPFPMEVLQASSLSFPLLRRHSRNNLINKFRNPTLPRIDIPRQNIDLKTFAATTPTVACPPSDPEIIPEKKEDKFDWYENWYPVATVCDLDKRRPHGRKVIGIDVVVWWDRKENAWKVFDDTCPHRLAPLSEGRIDQWGRLQCVYHGWCFDGVGACKFIPQAPHDGPPVETSKKACVKGVYPSCVRNGIVWFWPNSDPKYKDIYLTNKPHYIPELDDPSFTCTTITREVPYGYEILAENLMDPSHVPYAHYGILELEKVKESSKRDREGGHEMEISVGTIDVNGFSAKHVSADYYFVPPYVYYGRITPNAATKTKDATLP...
Ocimum basilicum (Sweet basil)
FUNCTION: Rieske-type, PAO-family oxygenase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proli...
1.14.15.-
CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] + salvigenin = 8-hydroxysalvigenin + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:73455, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:C...
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for salvigenin {ECO:0000269|PubMed:25139498}; Vmax=60.3 pmol/sec/mg enzyme with salvigenin as substrate {ECO:0000269|PubMed:25139498};
PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.
null
null
2Fe-2S;Chloroplast;Cytoplasm;Iron;Iron-sulfur;Membrane;Metal-binding;Oxidoreductase;Plastid;Transit peptide;Transmembrane;Transmembrane helix
flavonoid metabolic process [GO:0009812]
chloroplast [GO:0009507]; chloroplast membrane [GO:0031969]; cytoplasm [GO:0005737]
2 iron, 2 sulfur cluster binding [GO:0051537]; chlorophyllide a oxygenase [overall] activity [GO:0010277]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497]
SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:25139498}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:25139498}.
null
null
IPR013626;IPR017941;IPR036922;
2.102.10.10;
A0A078CGE6
MARQMTSSQFHKSKTLDNKYMLGDEIGKGAYGRVYIGLDLENGDFVAIKQVSLENIVQEDLNTIMQEIDLLKNLNHKNIVKYLGSLKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADVNTHSVVGTPYWMAPEVIEMSGVCAASDIWSVGCTVIELLTCVPPYYDLQPMPALFRIVQDDSPPIPDSLSPDITDFLRQCFKKDSRQRPDAKTLLSHPWIRNSRRALQSSLRHSGTIRYMKGADSSSEKDGEGSQDIAESVSAEKV...
Brassica napus (Rape)
FUNCTION: Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells (PubMed:11489177). Required for the normal functioning of the plasma membrane in developing pollen. Involved in the regulation of cell expansion and embryo develo...
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:11489177}; CATALYTIC...
null
null
null
null
null
ATP-binding;Cell cycle;Cell division;Cell membrane;Cytoplasm;Cytoskeleton;Kinase;Membrane;Nucleotide-binding;Nucleus;Phosphoprotein;Repeat;Serine/threonine-protein kinase;Transferase
cell cycle [GO:0007049]; cell division [GO:0051301]; MAPK cascade [GO:0000165]; protein autophosphorylation [GO:0046777]; regulation of cell division [GO:0051302]
cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8T2I8}. Nucleus, nucleolus {ECO:0000269|PubMed:15292395}. Cell membrane {ECO:0000250|UniProtKB:Q9LJD8}. Note=Accumulates in the nucleolus during interphase (PubMed:15292395). Localized to the plasma membrane in developi...
PTM: Autophosphorylated. {ECO:0000269|PubMed:11489177}.
null
IPR011989;IPR016024;IPR011009;IPR000719;IPR017441;IPR001245;IPR008271;
1.25.10.10;1.10.510.10;
A0A087QH05
LQCYCHLCTKDNFTCVTDGLCFTSVTRTADKVIHNSMCIAEIDLIPRDRPFVCAPSARDGVITLPHCCDKDHCNKIELPIPTPGKPASNLGPVELAAVIAGPVCFVCISLMLILYLCHNRTVIHHRVPSEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIAD...
Aptenodytes forsteri (Emperor penguin)
null
2.7.11.30
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence={ECO:0000256|ARBA:AR...
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
Apoptosis;ATP-binding;Cell junction;Differentiation;Growth regulation;Isopeptide bond;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Serine/threonine-protein kinase;Signal;Tight junction;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation
activin receptor signaling pathway [GO:0032924]; apoptotic process [GO:0006915]; cardiac epithelial to mesenchymal transition [GO:0060317]; endothelial cell activation [GO:0042118]; heart development [GO:0007507]; intracellular signal transduction [GO:0035556]; mesenchymal cell differentiation [GO:0048762]; nervous sys...
activin receptor complex [GO:0048179]; bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; membrane [GO:0016020]; membrane raft [GO:0045121]
activin binding [GO:0048185]; activin receptor activity, type I [GO:0016361]; ATP binding [GO:0005524]; SMAD binding [GO:0046332]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type I [GO:0005025]
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Membrane {ECO:0000256|ARBA...
null
null
IPR000472;IPR003605;IPR011009;IPR000719;IPR017441;IPR008271;IPR045860;IPR000333;
2.10.60.10;1.10.510.10;
A0A087X1C5
MGLEALVPLAMIVAIFLLLVDLMHRHQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREAMVTRGEDTADRPPAPIYQVLGFGPRSQGVILSRYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFADQAGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLPHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAKKEKAKGSPESSFNDENLRIVVGNLFLAGMVTTSTTLAWGLLL...
Homo sapiens (Human)
FUNCTION: May be responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It may be involved in the metabolism of codeine to morphine (PubMed:15051713). However, another study could not confirm it (PubMed:18838503). {ECO:0000269|PubMed:15051713, ECO:0000269|PubMed:18838503}.
1.14.14.1
CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57...
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413;
null
null
null
null
Cytoplasm;Glycoprotein;Heme;Iron;Membrane;Metal-binding;Mitochondrion;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix
arachidonic acid metabolic process [GO:0019369]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]
cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]
aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000305|PubMed:15051713}. Mitochondrion {ECO:0000269|PubMed:18838503}.
null
null
IPR001128;IPR017972;IPR002401;IPR008069;IPR036396;
1.10.630.10;
A0A087X296
MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTGKKQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGV...
Homo sapiens (Human)
null
1.14.99.1
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000256|ARBA:ARBA00000144}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000256|ARBA:ARBA00000144}; CATALYT...
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|ARBA:ARBA00001970};
null
PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000256|ARBA:ARBA00004702}.
null
null
Dioxygenase;EGF-like domain;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Metal-binding;Microsome;Oxidoreductase;Peroxidase;Prostaglandin biosynthesis;Prostaglandin metabolism;Proteomics identification;Reference proteome;Signal
cyclooxygenase pathway [GO:0019371]; response to oxidative stress [GO:0006979]
endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; neuron projection [GO:0043005]
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}.
null
null
IPR000742;IPR019791;IPR010255;IPR037120;
1.10.640.10;2.10.25.10;
A0A089QRB9
MRTATATSVAVIGMACRLPGGIDSPQRLWEALLRGDDLVGEIPADRWDANVYYDPEPGVPGRSVSRWGAFLDDVGGFDCDFFGLTEREATAIDPQHRLLLEVSWEAIEHAGVDPATLAESQTGVFVGLTHGDYELLSADCGAAEGPYGFTGTSNSFASGRVAYTLGLHGPAVTVDTACSSGLTAVHQACRSLDDGESDLALAGGVVVTLEPRKSVSGSLQGMLSPTGRCHAFDEAADGFVSGEGCVVLLLKRLPDAVRDGDRVLAIVRGTAANQDGRTVNIAAPSAQAQIAVYQQALAAAGVEASTVGMVEAHGTGTPVG...
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
FUNCTION: Polyketide synthase involved in the biosynthesis of methyl-branched fatty acids such as mycolipanoic, mycolipenic (phthienoic) and mycolipodienoic acids required for the synthesis of a major class of polyacylated trehaloses. Catalyzes the elongation of CoA esters of long-chain fatty acids by incorporation of ...
2.3.1.252
CATALYTIC ACTIVITY: Reaction=3 (S)-methylmalonyl-CoA + a long-chain fatty acyl-CoA + 9 H(+) + holo-[mycolipanoate synthase] + 6 NADPH = 3 CO2 + 4 CoA + 3 H2O + long-chain mycolipanoyl-[mycolipanoate synthase] + 6 NADP(+); Xref=Rhea:RHEA:50344, Rhea:RHEA-COMP:12617, Rhea:RHEA-COMP:12618, ChEBI:CHEBI:15377, ChEBI:CHEBI:1...
null
null
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305|PubMed:12207710}.
null
null
Acyltransferase;Cell membrane;Direct protein sequencing;Lipoprotein;Membrane;Multifunctional enzyme;NADP;Palmitate;Phosphopantetheine;Phosphoprotein;Reference proteome;Signal;Transferase
DIM/DIP cell wall layer assembly [GO:0071770]; methyl-branched fatty acid biosynthetic process [GO:1902321]; secondary metabolite biosynthetic process [GO:0044550]
plasma membrane [GO:0005886]; polyketide synthase complex [GO:0034081]
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
null
null
IPR001227;IPR036736;IPR014043;IPR016035;IPR013149;IPR013154;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049551;IPR049552;IPR020843;IPR013968;IPR049900;IPR020806;IPR009081;IPR016039;
3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;
A0A090N8E9
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHRKCNYSFHATPNTYKRKNTETAL...
Homo sapiens (Human)
null
2.1.1.356
CATALYTIC ACTIVITY: Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEB...
null
null
null
null
null
Biological rhythms;Chromatin regulator;Methyltransferase;Nucleus;Repressor;S-adenosyl-L-methionine;Transcription;Transcription regulation;Transferase
B cell differentiation [GO:0030183]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to trichostatin A [GO:0035984]; cerebellar cortex development [GO:0021695]; facultative heterochromatin formation [GO:0140718]; G1 to G0 transition [...
chromatin silencing complex [GO:0005677]; ESC/E(Z) complex [GO:0035098]; nucleoplasm [GO:0005654]; pericentric heterochromatin [GO:0005721]; pronucleus [GO:0045120]; synapse [GO:0045202]
chromatin DNA binding [GO:0031490]; histone H3K27 trimethyltransferase activity [GO:0140951]; lncRNA binding [GO:0106222]; primary miRNA binding [GO:0070878]; ribonucleoprotein complex binding [GO:0043021]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promot...
SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
null
null
IPR026489;IPR045318;IPR048358;IPR021654;IPR044439;IPR041343;IPR041355;IPR001005;IPR001214;IPR046341;IPR033467;
1.20.58.1880;2.170.270.10;
A0A093GWH1
MLRLSTLLRRTRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKAIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAREGFEKISKGANPVEIRRGVMLAVDAVITELKKLSKPVTTPEEIAQVATISANGDQEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLISEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIAT...
Struthio camelus australis
FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondria...
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|ARBA:ARBA00034033};
null
null
null
null
null
ATP-binding;Chaperone;Nucleotide-binding;Reference proteome
apoptotic mitochondrial changes [GO:0008637]; B cell proliferation [GO:0042100]; biological process involved in interaction with symbiont [GO:0051702]; cellular response to interleukin-7 [GO:0098761]; chaperone cofactor-dependent protein refolding [GO:0051085]; isotype switching to IgG isotypes [GO:0048291]; mitochondr...
cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; coated vesicle [GO:0030135]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; GroEL-GroES complex [GO:1990220]; lipopolysaccharide receptor complex [GO:0046696]; migrasome [GO:0140494]; mitochondrial inner membrane [GO:0005743]; mitochondrial ...
apolipoprotein A-I binding [GO:0034186]; ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; double-stranded RNA binding [GO:0003725]; high-density lipoprotein particle binding [GO:0008035]; lipopolysaccharide binding [GO:0001530]; p53 binding [GO:0002039]; protein-folding chaperone binding ...
null
null
null
IPR018370;IPR001844;IPR002423;IPR027409;IPR027413;IPR027410;
3.50.7.10;1.10.560.10;3.30.260.10;
A0A093HNK4
MPTPNISTSAAKGFRRAVSELDSKQAEAIMSPRFIGRRQSLIEDARKEREAAAAATDAAESTETIVFEEKDGRAMLNLFFTLKGAKTSPLSRALKVFETFEAKIHHLETRLSRKPREGTTELEYFVRCEVHSSDLNTFISSIKRVTEEVRTTKEDKFHWFPRKICELDKCHHLVTKFDPDLDLDHPGYSDQVYRQRRKTIAEIAFHYKHGDPIPHVEYTAEETTTWKEVYSTLKSLYPTHACKEYLEAFNLLEKYCGYSENNIPQLEEVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEP...
Struthio camelus australis
null
1.14.16.2
null
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|ARBA:ARBA00001954, ECO:0000256|PIRSR:PIRSR601273-2};
null
PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. {ECO:0000256|ARBA:ARBA00004700}.
null
null
Catecholamine biosynthesis;Cell projection;Cytoplasm;Iron;Metal-binding;Monooxygenase;Neurotransmitter biosynthesis;Oxidoreductase;Phosphoprotein;Reference proteome
courtship behavior [GO:0007619]; dopamine biosynthetic process from tyrosine [GO:0006585]; eating behavior [GO:0042755]; embryonic camera-type eye morphogenesis [GO:0048596]; epinephrine biosynthetic process [GO:0042418]; eye photoreceptor cell development [GO:0042462]; grooming behavior [GO:0007625]; heart development...
axon [GO:0030424]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; melanosome membrane [GO:0033162]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; smooth endoplasmic reticulum [GO:0005790]; synapse [GO:0045202]
enzyme binding [GO:0019899]; iron ion binding [GO:0005506]; tyrosine 3-monooxygenase activity [GO:0004511]
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
null
null
IPR045865;IPR001273;IPR018301;IPR036951;IPR036329;IPR019774;IPR041903;IPR049321;IPR005962;IPR019773;IPR021164;
3.30.70.260;1.10.800.10;
A0A095AMW7
MNTTGYDILRNPFLNKGTAFSEAERQQLGLTGTLPSQIQTIEEQAEQAYKQFQAKSPLLEKRIFLMNLFNENVTLFYHLMDQHVSEFMPIVYDPVVAESIEQYNEIYTNPQNAAFLSVDRPEDVENALKNAAAGRDIKLVVVTDAEGILGMGDWGVNGVDIAVGKLMVYTAAAGIDPATVLPVSIDAGTNNKELLHNPLYLGNKHERIAGEQYLEFIDKFVTAEQNLFPESLLHWEDFGRSNAQVILDKYKESIATFNDDIQGTGMIVLAGIFGALNISKQKLVDQKFVTFGAGTAGMGIVNQIFSELKQAGLSDDEARN...
Leuconostoc mesenteroides
FUNCTION: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate. {ECO:0000269|PubMed:16345941}.
4.1.1.101
CATALYTIC ACTIVITY: Reaction=(S)-malate + H(+) = (S)-lactate + CO2; Xref=Rhea:RHEA:46276, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:16651; EC=4.1.1.101; Evidence={ECO:0000269|PubMed:16345941};
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16345941}; COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:16345941};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.043 mM for NAD {ECO:0000269|PubMed:16345941}; KM=16.7 mM for (S)-malate {ECO:0000269|PubMed:16345941};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.35. {ECO:0000269|PubMed:16345941};
null
Lyase;Manganese;Metal-binding;NAD
malate metabolic process [GO:0006108]; malolactic fermentation [GO:0043464]; pyruvate metabolic process [GO:0006090]
cytosol [GO:0005829]
carboxy-lyase activity [GO:0016831]; malate dehydrogenase (decarboxylating) (NAD+) activity [GO:0004471]; malolactic enzyme activity [GO:0043883]; manganese ion binding [GO:0030145]; NAD binding [GO:0051287]
null
null
null
IPR046346;IPR015884;IPR012301;IPR037062;IPR012302;IPR001891;IPR048182;IPR036291;
3.40.50.10380;3.40.50.720;
A0A095C6S0
MSFDAVVIGSGVIGLSIARELDNRGLKVAMVARDLAEDSLSVGFASPWAGCNWYSFAEGGTPAAEWDAITFSKLAKLAEDHPDLCEKIPFCSVWDLPKSDSESEPWFKDLVFEYKKLKSTPGQHLAGGKKFGYSFKSYVLHAPNYIRHLSSEIRARGIPIHRYRLSSIDEAYNLPGIGKVSLVVNASGLGAKSLIGVEDEKVYSGRGQTVLVRAPGFKACIMHTEGFYADLDESGREITPPPPAYIIPRPGPEGHVVLGGVYQKDNWSTLPDLKEAERILKDCYNLAPELAGPNGKSWKDIEIISHNVGLRPAREGEPRL...
Cryptococcus deuterogattii (strain R265) (Cryptococcus gattii VGII (strain R265))
FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:26132227). Enables the organism to utilize D-amino acids as a source of nutrients (PubMed:26132227). Enables the organism to utilize D-alanine, D-cysteine, D-histidine, D-leucine, D-methionine, D-phenylalanine, D-pro...
1.4.3.3
CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-ri...
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P80324};
null
null
null
null
FAD;Flavoprotein;Oxidoreductase;Peroxisome
aspartate catabolic process [GO:0006533]; cellular detoxification [GO:1990748]; D-amino acid catabolic process [GO:0019478]; nitrogen utilization [GO:0019740]
peroxisomal matrix [GO:0005782]
D-amino-acid oxidase activity [GO:0003884]; D-aspartate oxidase activity [GO:0008445]; FAD binding [GO:0071949]
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P80324}.
null
null
IPR006181;IPR023209;IPR006076;
3.30.9.10;3.40.50.720;
A0A096MJC6
MWASCCNWFCLDGQPEETPPPQGARTQAYSNPGYSSFPSPTGSEPSCKACGVHFASTTRKQQTCLDCKKNFCMTCSSQEGNGPRLCLLCLRFRATAFQREELMKMKVKDLRDYLSLHDISTEMCREKEELVFLVLGQQPVISEADRTRAPTLPQAFPEQQAFLTQPQSSTVPPTSPGLPSSPAQVTSVLAQDQETQQAIGHVSQDHEEPIFLESTARVPPEDETQSVDSEDSFVPGRRASLSDLTHLEDIEGLTVRQLKEILARNFVNYKGCCEKWELMERVTRLYKDQKGLQHLVSGNEDQNGGAVPSGLEENLCKICM...
Rattus norvegicus (Rat)
null
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};
null
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906}.
null
null
Apoptosis;Cytoplasm;Metal-binding;Proteomics identification;Reference proteome;Repeat;Zinc;Zinc-finger
apoptotic process [GO:0006915]; chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; DNA strand invasion [GO:0042148]; double-strand break repair via homologous recombination [GO:0000724]; interstrand cross-link repair [GO:0036297]; negative regulation of extrinsic apoptotic signaling pathway via dea...
centrosome [GO:0005813]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; replication fork [GO:0005657]
ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent DNA damage sensor activity [GO:0140664]; gamma-tubulin binding [GO:0043015]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697]; ubiquitin protein ligase activity [GO:0061630]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
null
null
IPR049320;IPR036361;IPR011011;IPR001841;IPR013083;
1.10.720.140;3.30.40.10;
A0A096MJU6
MSEAYLRCWIFSWKSVWVRPCQGLHFKTRLLQGSLLYTALDSYSTVQAAPKCNSGSVKFQGLAETSGIMKMDMEDADMTLWTEAEFEEKCTYIVNDHPWDSSADGGTSVQAEASLPRNLLFKYAANNSKEVIGVVSKEYIPKGTRFGPLIGEVYTNDTVPKNANRKYFWRIYSREEFHHFIDGFNEEKSNWMRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERLHYPYPGELTVMNLTQTESNPKQYSSEKNELYPKSVPKREYSVKEILKLDSNPSKRKDSYRSNISPYTSEKDMDGFRKNG...
Rattus norvegicus (Rat)
FUNCTION: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress...
2.1.1.-
null
null
null
null
null
null
DNA-binding;Methyltransferase;Nucleus;Reference proteome;Transferase
aorta development [GO:0035904]; artery morphogenesis [GO:0048844]; cardiac septum development [GO:0003279]; cell fate commitment [GO:0045165]; coronary vasculature development [GO:0060976]; embryonic placenta development [GO:0001892]; eye photoreceptor cell development [GO:0042462]; gene expression [GO:0010467]; germ c...
cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone deacetylase binding [GO:0042826]; histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; promoter-speci...
SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR013212}. Cytoplasm {ECO:0000256|PIRNR:PIRNR013212}.
null
null
IPR016608;IPR044413;IPR001214;IPR046341;IPR036236;IPR013087;
3.30.160.60;2.170.270.10;
A0A096MPL2
MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAIS...
Papio anubis (Olive baboon)
FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle pr...
3.5.1.98
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:35899, ChEBI:CHEBI:137954; Evidence={ECO:0000256|ARBA:ARBA00029357}; PhysiologicalDirection=l...
null
null
null
null
null
Chromatin regulator;Hydrolase;Metal-binding;Nucleus;Reference proteome;Repressor;Transcription;Transcription regulation
cellular response to fluid shear stress [GO:0071498]; circadian regulation of gene expression [GO:0032922]; cornified envelope assembly [GO:1903575]; DNA repair-dependent chromatin remodeling [GO:0140861]; establishment of mitotic spindle orientation [GO:0000132]; establishment of skin barrier [GO:0061436]; in utero em...
cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitotic spindle [GO:0072686]; plasma membrane [GO:0005886]; Rpd3L-Expanded complex [GO:0070210]; transcription repressor complex [GO:0017053]
chromatin DNA binding [GO:0031490]; cyclin binding [GO:0030332]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; histone decrotonylase activity [GO:0160009]; metal ion binding [GO:0046872]; NF-kappaB binding [GO:0051059]; protein de-2-hydroxyisobutyrylase activity [GO:0160010]; tran...
SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037913}.
null
null
IPR000286;IPR003084;IPR023801;IPR037138;IPR023696;
3.40.800.20;
A0A096MZD4
MTSSLQRPWRVPWLPWTILLVGTAAASQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDETIIIALASVSVLTVLIVALCFGYRMLTGDRKQGLHSMNMMEAAASEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERVTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELP...
Papio anubis (Olive baboon)
null
2.7.11.30
null
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;Kinase;Magnesium;Manganese;Membrane;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix
anterior/posterior pattern specification [GO:0009952]; aortic valve development [GO:0003176]; atrial septum morphogenesis [GO:0060413]; blood vessel remodeling [GO:0001974]; cellular response to starvation [GO:0009267]; chondrocyte development [GO:0002063]; endocardial cushion development [GO:0003197]; endochondral bon...
adherens junction [GO:0005912]; axon [GO:0030424]; caveola [GO:0005901]; cell body [GO:0044297]; cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; dendrite [GO:0030425]; nucleoplasm [GO:0005654]; postsynaptic density [GO:0014069]; receptor complex [GO:0043235]
activin receptor activity, type II [GO:0016362]; ATP binding [GO:0005524]; BMP binding [GO:0036122]; BMP receptor activity [GO:0098821]; cadherin binding [GO:0045296]; protein tyrosine kinase binding [GO:1990782]; transforming growth factor beta receptor activity [GO:0005024]
null
null
null
IPR000472;IPR011009;IPR000719;IPR017441;IPR045860;IPR000333;
2.10.60.10;1.10.510.10;
A0A096NTX9
MADVFPANDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISP...
Papio anubis (Olive baboon)
null
2.7.11.13
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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000946}; CATALY...
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
Acetylation;ATP-binding;Calcium;Cytoplasm;Kinase;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc;Zinc-finger
desmosome assembly [GO:0002159]; negative regulation of glial cell apoptotic process [GO:0034351]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of angiotensin-activated signaling pathway [GO:0110063]; positive regulation of blood vessel endothelial cell migration [...
ciliary basal body [GO:0036064]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; calcium,diacylglycerol-dependent serine/threonine kinase activity [GO:0004698]; enzyme binding [GO:0019899]; histone H3T6 kinase activity [GO:0035403]; protein serine kinase activity [GO:0106310]; zinc ion binding [GO:0008270]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004318}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004318}.
null
null
IPR000961;IPR046349;IPR000008;IPR035892;IPR034663;IPR020454;IPR011009;IPR002219;IPR017892;IPR000719;IPR017441;IPR014375;IPR008271;
3.30.60.20;2.60.40.150;1.10.510.10;
A0A096P8D3
MTRVERGRVLARAIERAVAHRASARRWTTTTRTPAWMVTGWMGGRGVDRSTAMTRFERCGSTASSKITAAPMVYVRGEEMTAYVMDLIRSRWIEPRVDVGGWETFDLRAKNRDDTEDRVLRDVIEAGKRIKAIFKEPTVTPTADQVKRLGLRKSWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVLFERHAVGGEYSAGYKNVGKGKLTTTFTPSEGPDAGKTVVVDEREIVDEEAAVVTYHNPYDNVHDLARFFFGRCLEAKVTPYVVTKKTVFKWQEPFWQIMRTVFDEEFKAQFVAAGVMKEGEELVHLLSDA...
Ostreococcus tauri
FUNCTION: Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (Probable). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production (Probable). {ECO:0000305|PubMed:25724193}.
1.1.1.41
CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH; Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41; Evidence={ECO:0000269|PubMed:25724193}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23633; Ev...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25724193, ECO:0000269|Ref.4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25724193}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000269|Ref.4};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=226 uM for NAD(+) with Mg(2+) as cofactor {ECO:0000269|PubMed:25724193}; KM=265 uM for NAD(+) with Mn(2+) as cofactor {ECO:0000269|PubMed:25724193};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 with Mn(2+) as cofactor and 8.5 with Mg(2+) as cofactor. {ECO:0000269|PubMed:25724193};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:25724193};
3D-structure;Magnesium;Manganese;Metal-binding;Mitochondrion;NAD;Oxidoreductase;Reference proteome;Transit peptide;Tricarboxylic acid cycle
isocitrate metabolic process [GO:0006102]; NAD metabolic process [GO:0019674]; NADP metabolic process [GO:0006739]; tricarboxylic acid cycle [GO:0006099]
cytosol [GO:0005829]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]
isocitrate dehydrogenase (NAD+) activity [GO:0004449]; isocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
null
null
IPR004790;IPR024084;
3.40.718.10;
A0A0A0MPX5
MAISPTATELLLASFAFCLVFWVVRAWQPRVPKGLKSPPGPWGWPLLGHVLTLGKNPHLVLARLSQRYGDVLQIRIGSTPVLVLSGLDTIRQALVQQGDDFKGRPNLYSFSLVTDGHSMSFSPDSGPVWAARRRLAQSALNTFSIASDPASSSSCYLEDHVSKEAEALLSRLQEQMAEVGSFDPHSQVVLSVANVIGAMCFGQHFPQDSEEKLSLIHSSNIFVENASSGNPVDFFPILQYIPTPGLQRFKAFNQKLVQFLQKIIQEHYQDFDENNIQDITGALLKHCKKGSRANGGRIPHEKIVSLINDIFGAGFDTVTT...
Felis catus (Cat) (Felis silvestris catus)
FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. {ECO:0000256|RuleBase:RU368045}.
1.14.14.1
CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231; EC=4.2.1.152; Evidence={ECO:0000256|ARBA:ARBA00001395}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:3...
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|ARBA:ARBA00001971, ECO:0000256|PIRSR:PIRSR602401-1, ECO:0000256|RuleBase:RU368045};
null
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000256|ARBA:ARBA00004891}.; PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
null
null
Endoplasmic reticulum;Heme;Iron;Lipid metabolism;Lyase;Membrane;Metal-binding;Microsome;Monooxygenase;Oxidoreductase;Reference proteome;Signal
alkaloid metabolic process [GO:0009820]; cellular respiration [GO:0045333]; cellular response to cadmium ion [GO:0071276]; dibenzo-p-dioxin metabolic process [GO:0018894]; estrogen metabolic process [GO:0008210]; hormone biosynthetic process [GO:0042446]; hydrogen peroxide biosynthetic process [GO:0050665]; lung develo...
endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; aromatase activity [GO:0070330]; caffeine oxidase activity [GO:0034875]; demethylase activity [GO:0032451]; enzyme binding [GO:0019899]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activity [GO:0101021]; heme binding [GO:002003...
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368045}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368045}. Microsome membrane {ECO:0000256|RuleBase:RU368045}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368045}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membran...
null
null
IPR001128;IPR017972;IPR002401;IPR008066;IPR036396;
1.10.630.10;
A0A0A0MPX9
MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQQTLKNALRLQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPYVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATQRTQCNTTQGNEVTSILRWAKDSGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNVRDIEVIMGGGRKYMFPKNRTDVEYEMDEKARGTRLDGLNLVDIWKSFKPRHKHSHYVWNRTELLTLDPYGVDYLLGLFEPGDMQYELNRNSTTDPSLSEMVEIAIKIL...
Felis catus (Cat) (Felis silvestris catus)
null
3.1.3.1
CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437; Evidence={ECO:0000256|ARBA:ARBA000...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
null
null
null
null
Calcium;Cell membrane;Disulfide bond;Glycoprotein;GPI-anchor;Hydrolase;Lipoprotein;Magnesium;Membrane;Metal-binding;Phosphoprotein;Reference proteome;Signal;Zinc
bone mineralization [GO:0030282]; calcium ion homeostasis [GO:0055074]; cellular homeostasis [GO:0019725]; cellular response to organic cyclic compound [GO:0071407]; dephosphorylation [GO:0016311]; developmental process involved in reproduction [GO:0003006]; endochondral ossification [GO:0001958]; futile creatine cycle...
extracellular matrix [GO:0031012]; extracellular membrane-bounded organelle [GO:0065010]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
ADP phosphatase activity [GO:0043262]; alkaline phosphatase activity [GO:0004035]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; inorganic diphosphate phosphatase activity [GO:0004427]; phosphoamidase activity [GO:0050187]; phosphoethanolamine phosphatase activity [GO:0052732]; pyridoxal phosp...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Extracellular vesicle membrane {ECO:0000256|ARBA:ARBA00037828}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00037828}. Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor {ECO...
null
null
IPR001952;IPR018299;IPR017850;
3.40.720.10;
A0A0A0MPZ5
MVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGKPITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDHFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKAAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN...
Felis catus (Cat) (Felis silvestris catus)
null
1.2.1.12
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000256|ARBA:ARBA00001810,...
null
null
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869, ECO:0000256|RuleBase:RU361160}.
null
null
ADP-ribosylation;Apoptosis;Cytoplasm;Cytoskeleton;Glycolysis;Methylation;NAD;Nucleotide-binding;Nucleus;Oxidoreductase;Reference proteome;S-nitrosylation;Transferase;Translation regulation
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; apoptotic process [GO:0006915]; cellular response to type II interferon [GO:0071346]; defense response to fungus [GO:0050832]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; killing by host of symbiont cells ...
cytoskeleton [GO:0005856]; cytosol [GO:0005829]; GAIT complex [GO:0097452]; lipid droplet [GO:0005811]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:1990904]
aspartic-type endopeptidase inhibitor activity [GO:0019828]; disordered domain specific binding [GO:0097718]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosyl...
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
null
null
IPR020831;IPR020830;IPR020829;IPR020828;IPR006424;IPR036291;
3.40.50.720;
A0A0A0MQ23
AAPALDLGRPAMRHRGLGLAALLALLAALAPRSSAAPEPALWPMPLSVKTSPRLLHLSRDNFSIGYGPSSTAGPTCSLLQEAFRRYHEYIFGFDKRQRRPAKPNSAIELQQLLVTVVLDSECDLFPNITSDESYTLLVKEPVAFLKANRVWGVLRGLETFSQLIYQDSYGTFTVNESDIIDSPRFPHRGILIDTARHFLPVKSILKTLDAMAFNKFNVLHWHIVDDQSFPYQSVTFPELSNKGSYSLSHVYTPNDVHTVIEYARLRGIRVIPEFDSPGHTQSWGKGQKDLLTPCYNEHKQSGTFGPINPILNSTYNFLSQ...
Felis catus (Cat) (Felis silvestris catus)
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;Reference proteome;Signal
astrocyte cell migration [GO:0043615]; chondroitin sulfate catabolic process [GO:0030207]; dermatan sulfate catabolic process [GO:0030209]; ganglioside catabolic process [GO:0006689]; glycosaminoglycan metabolic process [GO:0030203]; hyaluronan catabolic process [GO:0030214]; intracellular calcium ion homeostasis [GO:0...
acrosomal vesicle [GO:0001669]; azurophil granule [GO:0042582]; beta-N-acetylhexosaminidase complex [GO:1905379]; cortical granule [GO:0060473]; extracellular space [GO:0005615]; lysosome [GO:0005764]; membrane [GO:0016020]
acetylglucosaminyltransferase activity [GO:0008375]; beta-N-acetylhexosaminidase activity [GO:0004563]; identical protein binding [GO:0042802]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148]
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000256|ARBA:ARBA00037865}. Lysosome {ECO:0000256|ARBA:ARBA00004371}.
null
null
IPR025705;IPR015883;IPR017853;IPR029018;IPR029019;
3.30.379.10;3.20.20.80;
A0A0A1C3I2
MDVRRRLPPKLRRPLPITESSHHHRKTPFPADVDRSPSPTPKASDALPLPLYLTNGIFFTLFFSVAYYLLHRWRDKIRSSTPLHIVTLSELAAIVSLIASFIYLLGFFGIDFVQSFVSRADVDVDIDVEPDILEADRRPCSKLMDQPPPPPVVMSSEEDEEIVKSVVSGKTPSYSLESKLGDCYRAASIRREAVQRTTGRSLLGLPLDGFDYESILGQCCEMPIGYVQIPVGIAGPLLLNGCEYVVPMATTEGCLVASTNRGCKAIYACGGATGILLKDGMTRAPVVRFSTAKRASDLKFFLEDPLNFDTLAVVFNKSSR...
Panax ginseng (Korean ginseng)
FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:24569845, PubMed:29378087). Promotes triterpenes accumulation in r...
1.1.1.34
CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003};
null
null
PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000305}.
null
null
Chloroplast;Endoplasmic reticulum;Glycoprotein;Isoprene biosynthesis;Membrane;NADP;Oxidoreductase;Peroxisome;Plastid;Transmembrane;Transmembrane helix
coenzyme A metabolic process [GO:0015936]; response to absence of light [GO:0009646]; response to jasmonic acid [GO:0009753]; saponin biosynthetic process [GO:0016135]; sterol biosynthetic process [GO:0016126]; triterpenoid biosynthetic process [GO:0016104]
chloroplast membrane [GO:0031969]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778]
hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:00002...
null
null
IPR002202;IPR023074;IPR023076;IPR004554;IPR023282;IPR009023;IPR009029;
1.10.3270.10;3.30.70.420;
A0A0A1C930
MDVRRRPVKSLSSAKTATAGEPPKSQQQHPKASDALPLPLYLTNGLFFTMFFSVMYFLLHRWREKIRNSTPLHVVTLSELAALVLLMASVIYLLGFFGIGFVRSVIRPSPDAWDILEDDNAINEEDSRREPCAEAIDCSLPPKPKIVHMVPQKALNPKSAFADMMVEQPALAIAPLTEEDEEIVKSVVTGKIPSYSLESKLGDCKKAASIRREALQRITGKSLAGLPLDGFDYKSILGQCCEMPVGYVQIPVGIAGPLLLNETEYSVPMATTEGCLVASTNRGCKAIYASGGATSVLLRDGMTRAPVVRFSTVKRAAELK...
Panax ginseng (Korean ginseng)
FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:24569845, PubMed:29378087). {ECO:0000250|UniProtKB:P14891, ECO:000...
1.1.1.34
CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003};
null
null
PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000305}.
null
null
Chloroplast;Endoplasmic reticulum;Glycoprotein;Isoprene biosynthesis;Membrane;NADP;Oxidoreductase;Peroxisome;Plastid;Transmembrane;Transmembrane helix
coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; response to jasmonic acid [GO:0009753]; saponin biosynthetic process [GO:0016135]; triterpenoid biosynthetic process [GO:0016104]
chloroplast membrane [GO:0031969]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778]
hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane pro...
null
null
IPR002202;IPR023074;IPR023076;IPR004554;IPR023282;IPR009023;IPR009029;
1.10.3270.10;3.30.70.420;
A0A0A1H8I4
MFPRLPTLALGALLLASTPLLAAQPVTTLTVLSSGGIMGTIREVAPAYEKATGVKLDIAAAPSMGDTPQAIPNRLARNEPADVVLMVGSALDKLVASGQVAKDSRVDLGQSFIAMAVRQGAPKPDISNMDAFKQTLEKAQSVAYSDSASGVYLSRILFPRMQLDKSFMAKARMIPAEPVGAVVARGEAQLGFQQLSELKAVPGIDIVGLIPDQAQKMTLYSGAMVSKSQHPEAARALLQYLASKDAAKAIEDSGLKPVPAQP
Pseudomonas sp
FUNCTION: Involved in assimilation of trans-aconitic acid. Preference for cis-aconitic acid is 14-fold higher than for trans-aconitic acid. Not active on intermediates of tricarboxylic acid (TCA) cycle including citric acid, succinic acid, fumaric acid, and 2-oxoglutaric acid or on other dicarboxilic acids including it...
5.3.3.7
CATALYTIC ACTIVITY: Reaction=trans-aconitate = cis-aconitate; Xref=Rhea:RHEA:17265, ChEBI:CHEBI:15708, ChEBI:CHEBI:16383; EC=5.3.3.7; Evidence={ECO:0000269|PubMed:26293748};
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.9 mM for cis-aconitic acid {ECO:0000269|PubMed:26293748}; KM=80 mM for trans-aconitic acid {ECO:0000269|PubMed:26293748}; Note=kcat and kcat/KM are 4500 sec(-1) and 760 sec(-1) mM(-1), respectively for cis-aconitic acid. kcat and kcat/KM are 15000 sec(-1) and 190...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:26293748};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:26293748};
Direct protein sequencing;Isomerase;Signal
cellular response to calcium ion [GO:0071277]; cellular response to iron ion [GO:0071281]; cellular response to magnesium ion [GO:0071286]; cellular response to manganese ion [GO:0071287]; cellular response to nickel ion [GO:0071289]; cellular response to silver ion [GO:0071292]; response to DDT [GO:0046680]; response ...
outer membrane-bounded periplasmic space [GO:0030288]
aconitate delta-isomerase activity [GO:0047614]
null
null
null
null
3.40.190.10;
A0A0A1HA03
MMGDLTTSFPATTLTTNDQPHVVVCSGAGMGHLTPFLNLASALSSAPYNCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSALSPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPEHIFTSFTISNAKYFSLSKGILVNTFDSFEPETLSALNSGDTLSDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELR...
Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum)
FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin (PubMed:25142187). No activity with flavanones, flavones or flavonols (PubMed:25142187). Exhibits C-glycosylation activity toward 2...
2.4.1.360
CATALYTIC ACTIVITY: Reaction=a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-oxodihydrochalcone + H(+) + UDP; Xref=Rhea:RHEA:51504, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:142482, ChEBI:CHEBI:142483; EC=2.4.1.360; Evidence={...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 uM for 2-hydroxynaringenin {ECO:0000269|PubMed:25142187}; KM=40 uM for 2-hydroxypinocembrin {ECO:0000269|PubMed:25142187}; KM=36.5 uM for 2-phenyl-2',4',6'-trihydroxyactophenone {ECO:0000269|PubMed:25142187}; KM=3.73 uM for phloretin {ECO:0000269|PubMed:3269916...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:25142187};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-50 degrees Celsius. {ECO:0000269|PubMed:25142187};
3D-structure;Direct protein sequencing;Glycosyltransferase;Transferase
null
null
UDP-glucosyltransferase activity [GO:0035251]
null
null
null
IPR002213;IPR035595;
3.40.50.2000;
A0A0A6ZFY4
MDNQNGRISIALLPFLAHGHISPFFELAKQLAKRNCNVFLCSTPINLSSIKDKDSSASIKLVELHLPSSPDLPPHYHTTNGLPSHLMLPLRNAFETAGPTFSEILKTLNPDLLIYDFNPSWAPEIASSHNIPAVYFLTTAAASSSIGLHAFKNPGEKYPFPDFYDNSNITPEPPSADNMKLLHDFIACFERSCDIILIKSFRELEGKYIDLLSTLSDKTLVPVGPLVQDPMGHNEDPKTEQIINWLDKRAESTVVFVCFGSEYFLSNEELEEVAIGLEISTVNFIWAVRLIEGEKKGILPEGFVQRVGDRGLVVEGWAPQ...
Panax ginseng (Korean ginseng)
FUNCTION: Component of the dammarane-type triterpene saponins (e.g. PPD-type ginsenosides or panaxosides) biosynthetic pathway (PubMed:25320211, PubMed:25769286, PubMed:27746309, PubMed:29378087). Glycosyltransferase that catalyzes the conversion of ginsenoside Rh2 to ginsenoside Rg3 (PubMed:25320211, PubMed:25769286, ...
2.4.1.365
CATALYTIC ACTIVITY: Reaction=(20S)-ginsenoside F2 + UDP-alpha-D-glucose = (20S)-ginsenoside Rd + H(+) + UDP; Xref=Rhea:RHEA:58004, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:67988, ChEBI:CHEBI:77145; EC=2.4.1.365; Evidence={ECO:0000269|PubMed:25320211}; PhysiologicalDirection=left-to-right; Xr...
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=149 uM for ginsenoside Rh2 (at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:25769286}; KM=311 uM for ginsenoside Rh2 (at pH 7 and 35 degrees Celsius) {ECO:0000269|PubMed:25320211}; KM=188 uM for ginsenoside F2 (at pH 7 and 35 degrees Celsius) {ECO:0000269|PubMe...
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305}.
null
null
Glycosyltransferase;Isoprene biosynthesis;Transferase
response to molecule of fungal origin [GO:0002238]; saponin biosynthetic process [GO:0016135]; terpene biosynthetic process [GO:0046246]; terpenoid biosynthetic process [GO:0016114]
null
UDP-glycosyltransferase activity [GO:0008194]
null
null
null
IPR002213;IPR035595;
3.40.50.2000;
A0A0A7EPL0
MVIPATSRFGFRAEFNTKEFQASCISLANEIDAAIGRNEVPGNIQELALILNNVCRRKCDDYQTRAVVMALMISVKSACQLGWFPERETQELLAIIDLMWNGFSCPENVTSCVNSPVTLISQVIERFYPCVKLGHILVSFEAKPESKMMMKDFHISKKMPHSPKQKVGLFVVRTEDISRSNCIVHPQGVSFLLNGKGIDKRVNISMESGPQLPTNVTALLNLGANLLQAIGCFGGSYLIAIAFMDVIPLPNKPLLKDYVHPEVVGSNSDCDIIEGPSRISLSCPISRTRIKLPVKGHVCKHLQCFDFWNYVNMNTRRPSW...
Arabidopsis thaliana (Mouse-ear cress)
FUNCTION: Together with MOM1 and PIAL2, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation (PubMed:27113777). E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates (Pub...
2.3.2.-
null
null
null
PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:25415977}.
null
null
Alternative splicing;Ligase;Metal-binding;Nucleus;Reference proteome;Repeat;Transferase;Ubl conjugation pathway;Zinc;Zinc-finger
positive regulation of sulfur metabolic process [GO:0051176]; protein sumoylation [GO:0016925]; regulation of gene silencing by regulatory ncRNA [GO:0060966]; response to abscisic acid [GO:0009737]; response to osmotic stress [GO:0006970]; response to salt stress [GO:0009651]
nucleus [GO:0005634]
ligase activity [GO:0016874]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; zinc ion binding [GO:0008270]
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
IPR004181;IPR013083;
3.30.40.10;
A0A0B4J2F2
MVIMSEFSADPAGQGQGQQKPLRVGFYDIERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDSSNLEKIYREVQLMKLLNHPHIIKLYQVMETKDMLYIVTEFAKNGEMFDYLTSNGHLSENEARKKFWQILSAVEYCHDHHIVHRDLKTENLLLDGNMDIKLADFGFGNFYKSGEPLSTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPFFMSQDCESLIRRMLVVDPARRITIAQIRQHRWMRAEPCLPGPACPAFSAHSYTSNLGDYDEQALGIMQTLGVDRQ...
Homo sapiens (Human)
FUNCTION: Probable serine/threonine-protein kinase. {ECO:0000250|UniProtKB:P57059}.
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:0000250|UniProtKB:P57059}; CATALYTI...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
null
null
null
null
ATP-binding;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase
intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
null
null
null
IPR011009;IPR000719;IPR017441;IPR008271;IPR017090;IPR034672;IPR015940;
1.10.510.10;
A0A0B4JCQ5
MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSGEAFFVEECLEDEDEELPANLATSPIPNSFLASRDKANDTMEDISGVVTDKNASEELLLPLPLPRRNSIDFSKEEPKEAVVEGSKFENQVSDYTQRRHTDNTLERRNLSEKLKEFTTQKIRQEWAEHEELFQGEKKPADSDSLDNQSKASNEAETEKAIPAVIEDTEKEKDQIKPDVNLTTVTTSEATKEVSKSKTKKRRKKSQMKKNAQRKNSSSSSLGSAGGGDLPSAETPSLGVSNID...
Drosophila melanogaster (Fruit fly)
null
3.1.3.4
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000256|ARBA:ARBA00001180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:2743...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};
null
null
null
null
Hydrolase;Proteomics identification;Reference proteome
cellular response to insulin stimulus [GO:0032869]; fatty acid catabolic process [GO:0009062]; imaginal disc-derived wing vein specification [GO:0007474]; lipid homeostasis [GO:0055088]; negative regulation of BMP signaling pathway [GO:0030514]; positive regulation of transcription by RNA polymerase II [GO:0045944]; re...
cytoplasm [GO:0005737]; female germline ring canal inner rim [GO:0035183]; nucleus [GO:0005634]
phosphatidate phosphatase activity [GO:0008195]; transcription coactivator activity [GO:0003713]
null
null
null
IPR036412;IPR026058;IPR031703;IPR007651;IPR013209;IPR031315;
null
A0A0B4JCS1
MKLGDSGEAFFVEECLEDEDEELPANLATSPIPNSFLASRDKANDTMEDISGVVTDKNASEELLLPLPLPRRNSIDFSKEEPKEAVVEGSKFENQVSDYTQRRHTDNTLERRNLSEKLKEFTTQKIRQEWAEHEELFQGEKKPADSDSLDNQSKASNEAETEKAIPAVIEDTEKEKDQIKPDVNLTTVTTSEATKEVSKSKTKKRRKKSQMKKNAQRKNSSSSSLGSAGGGDLPSAETPSLGVSNIDEGDAPISSATNNNNTSSSNDEQLSAPLVTARTGDDSPLSEIPHTPTSNPRLDLDIHFFSDTEITTPVGGGGAG...
Drosophila melanogaster (Fruit fly)
null
3.1.3.4
null
null
null
null
null
null
Hydrolase;Proteomics identification;Reference proteome
cellular response to insulin stimulus [GO:0032869]; fatty acid catabolic process [GO:0009062]; imaginal disc-derived wing vein specification [GO:0007474]; lipid homeostasis [GO:0055088]; negative regulation of BMP signaling pathway [GO:0030514]; positive regulation of transcription by RNA polymerase II [GO:0045944]; re...
cytoplasm [GO:0005737]; female germline ring canal inner rim [GO:0035183]; nucleus [GO:0005634]
phosphatidate phosphatase activity [GO:0008195]; transcription coactivator activity [GO:0003713]
null
null
null
IPR036412;IPR026058;IPR031703;IPR013209;IPR031315;
null
A0A0B4JCU7
MTNCQSSVFIVVGTLFSIMAAAQSAPVSTTTQAEIYLSQFGYLPASARNPASSGLHDQRTWVSAIEEFQSFAGLNITGELDAETMKLMSLPRCGVRDRVGTGDSRSKRYALQGSRWRVKNLTYKISKYPKRLKRVDVDAEIGRAFAVWSEDTDLTFTRKTSGPVHIEIKFVESEHGDGDAFDGQGGTLAHAFFPVFGGDAHFDDAELWTIGSPRGTNLFQVAAHEFGHSLGLSHSDQSSALMAPFYRGFEPVFKLDEDDKAAIQSLYGRKTNQLRPTNVYPATTQRPYSPPKVPLDDSICKDSKVDTLFNSAQGETYAFK...
Drosophila melanogaster (Fruit fly)
null
3.4.24.-
null
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-2}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR...
null
null
null
null
Calcium;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Zinc
adult fat body development [GO:0007505]; basement membrane disassembly [GO:0034769]; basement membrane organization [GO:0071711]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; collagen catabolic process [GO:0030574]; dorsal trunk growth, open tracheal system [GO:0035001]; extracellular matri...
dendrite [GO:0030425]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
null
null
null
IPR000585;IPR036375;IPR018487;IPR018486;IPR033739;IPR024079;IPR001818;IPR021190;IPR006026;IPR002477;IPR036365;
3.40.390.10;2.110.10.10;
A0A0B4JD00
MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSGEAFFVEECLEDEDEELPANLATSPIPNSFLASRDKANDTMEDISGVVTDKNASEELLLPLPLPRRNSIDFSKEEPKEAVVEGSKFENQVSDYTQRRHTDNTLERRNLSEKLKEFTTQKIRQEWAEHEELFQGEKKPADSDSLDNQSKASNEAETEKAIPAVIEDTEKEKDQIKPDVNLTTVTTSEATKEVSKSKTKKRRKKSQMKKNAQRKNSSSSSLGSAGGGDLPSAETPSLGVSNID...
Drosophila melanogaster (Fruit fly)
null
3.1.3.4
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000256|ARBA:ARBA00001180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:2743...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};
null
null
null
null
Hydrolase;Proteomics identification;Reference proteome
cellular response to insulin stimulus [GO:0032869]; fatty acid catabolic process [GO:0009062]; imaginal disc-derived wing vein specification [GO:0007474]; lipid homeostasis [GO:0055088]; negative regulation of BMP signaling pathway [GO:0030514]; positive regulation of transcription by RNA polymerase II [GO:0045944]; re...
cytoplasm [GO:0005737]; female germline ring canal inner rim [GO:0035183]; nucleus [GO:0005634]
phosphatidate phosphatase activity [GO:0008195]; transcription coactivator activity [GO:0003713]
null
null
null
IPR036412;IPR026058;IPR031703;IPR007651;IPR013209;IPR031315;
null
A0A0B4JD27
MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSGEAFFVEECLEDEDEELPANLATSPIPNSFLASRDKANDTMEDISGVVTDKNASEELLLPLPLPRRNSIDFSKEEPKEAVVEGSKFENQVSDYTQRRHTDNTLERRNLSEKLKEFTTQKIRQEWAEHEELFQGEKKPADSDSLDNQSKASNEAETEKAIPAVIEDTEKEKDQIKPDVNLTTVTTSEATKEVSKSKTKKRRKKSQMKKNAQRKNSSSSSLGSAGGGDLPSAETPSLGVSNID...
Drosophila melanogaster (Fruit fly)
null
3.1.3.4
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000256|ARBA:ARBA00001180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:2743...
null
null
null
null
null
Hydrolase;Proteomics identification;Reference proteome
cellular response to insulin stimulus [GO:0032869]; fatty acid catabolic process [GO:0009062]; imaginal disc-derived wing vein specification [GO:0007474]; lipid homeostasis [GO:0055088]; negative regulation of BMP signaling pathway [GO:0030514]; positive regulation of transcription by RNA polymerase II [GO:0045944]; re...
cytoplasm [GO:0005737]; female germline ring canal inner rim [GO:0035183]; nucleus [GO:0005634]
phosphatidate phosphatase activity [GO:0008195]; transcription coactivator activity [GO:0003713]
null
null
null
IPR036412;IPR026058;IPR007651;IPR013209;IPR031315;
null
A0A0B4JD31
MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSGEAFFVEECLEDEDEELPANLATSPIPNSFLASRDKANDTMEDISGVVTDKNASEELLLPLPLPRRNSIDFSKEEPKEAVVEGSKFENQVSDYTQRRHTDNTLERRNLSEKLKEFTTQKIRQEWAEHEELFQGEKKPADSDSLDNQSKASNEAETEKAIPAVIEDTEKEKDQIKPDVNLTTVTTSEATKEVSKSKTKKRRKKSQMKKNAQRKNSSSSSLGSAGGGDLPSAETPSLGVSNID...
Drosophila melanogaster (Fruit fly)
null
3.1.3.4
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000256|ARBA:ARBA00001180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:2743...
null
null
null
null
null
Hydrolase;Proteomics identification;Reference proteome
cellular response to insulin stimulus [GO:0032869]; fatty acid catabolic process [GO:0009062]; imaginal disc-derived wing vein specification [GO:0007474]; lipid homeostasis [GO:0055088]; negative regulation of BMP signaling pathway [GO:0030514]; positive regulation of transcription by RNA polymerase II [GO:0045944]; re...
cytoplasm [GO:0005737]; female germline ring canal inner rim [GO:0035183]; nucleus [GO:0005634]
phosphatidate phosphatase activity [GO:0008195]; transcription coactivator activity [GO:0003713]
null
null
null
IPR036412;IPR026058;IPR007651;IPR013209;IPR031315;
null
A0A0B4JD53
MTNCQSSVFIVVGTLFSIMAAAQSAPVSTTTQAEIYLSQFGYLPASARNPASSGLHDQRTWVSAIEEFQSFAGLNITGELDAETMKLMSLPRCGVRDRVGTGDSRSKRYALQGSRWRVKNLTYKISKYPKRLKRVDVDAEIGRAFAVWSEDTDLTFTRKTSGPVHIEIKFVESEHGDGDAFDGQGGTLAHAFFPVFGGDAHFDDAELWTIGSPRGTNLFQVAAHEFGHSLGLSHSDQSSALMAPFYRGFEPVFKLDEDDKAAIQSLYGRKTNQLRPTNVYPATTQRPYSPPKVPLDDSICKDSKVDTLFNSAQGETYAFK...
Drosophila melanogaster (Fruit fly)
null
3.4.24.-
null
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-2}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR...
null
null
null
null
Calcium;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Zinc
adult fat body development [GO:0007505]; basement membrane disassembly [GO:0034769]; basement membrane organization [GO:0071711]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; collagen catabolic process [GO:0030574]; dorsal trunk growth, open tracheal system [GO:0035001]; extracellular matri...
dendrite [GO:0030425]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
null
null
null
IPR000585;IPR036375;IPR018487;IPR018486;IPR033739;IPR024079;IPR001818;IPR021190;IPR006026;IPR002477;IPR036365;
3.40.390.10;2.110.10.10;
A0A0B4JD64
MRDVTASRSGEICLQVKHPQAEFRRIPTTRTYTSLLVLPAIRGNSSSSSLAARSCILTRPEDCTALIGGHVRLSVRYEPFPGTKVIWYKACHPIVESSNVTIRTTSQQSTLYITDISADDSGKYTVEVMNDYGVEAAAASVAVEGPPEPPSGQPSVSLGPDRVAVAWCGPPYDGGCMITGFIIEMQTIGDENCDEDSWQQVTRVVDSLAYTVKNLQPERQYRFRVRAENIHGRSAPGQASELVQITNTPQRSTSSDASDRFGQATVSVQSGGDFKSRFEIIEELGKGRFGIVYKVQERGQPEQLLAAKVIKCIKSQDRQK...
Drosophila melanogaster (Fruit fly)
null
2.7.11.17; 2.7.11.18
null
null
null
null
null
null
ATP-binding;Immunoglobulin domain;Nucleotide-binding;Reference proteome;Repeat;Transferase
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; protein phosphorylation [GO:0006468]
null
ATP binding [GO:0005524]; calmodulin-dependent protein kinase activity [GO:0004683]; myosin light chain kinase activity [GO:0004687]; structural constituent of cytoskeleton [GO:0005200]
null
null
null
IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR011009;IPR000719;IPR017441;IPR008271;
2.60.40.10;1.10.510.10;
A0A0B4JD82
MGNGCSKCCQCNEHKQLNGTLSSASSVYRKRSRGEIPIENSDRFRITATSNAVQLAVEHVQREDAGHYTLFARTKRQDVVRRHVELIVEDRSTGDDPPVFVRRLPDLSVKVGTRTRLLTEIRSSTDLKLTWYRNDRRVCANDRITEVNEGTFHYLEISPVTLDDGGQWMLMAENFGGRNSCLGTLNVLVPKAYKTPEFVEELRAVLTEQGTVSLECKVVGVPTPHLRWFKDSKEIKAGDIFALTANADDPTSLGTYTCEARNCMGVTYSSSKVHVVGRGSREGSLKPADSVASNAPPPIFTNELRDMSLLIGETIILGCQ...
Drosophila melanogaster (Fruit fly)
null
2.7.11.17; 2.7.11.18
null
null
null
null
null
null
ATP-binding;Coiled coil;Immunoglobulin domain;Nucleotide-binding;Proteomics identification;Reference proteome;Repeat;Transferase
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; protein phosphorylation [GO:0006468]
null
ATP binding [GO:0005524]; calmodulin-dependent protein kinase activity [GO:0004683]; myosin light chain kinase activity [GO:0004687]; structural constituent of cytoskeleton [GO:0005200]
null
null
null
IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR003598;IPR013106;IPR011009;IPR000719;IPR017441;IPR008271;
2.60.40.10;1.10.510.10;
A0A0B4JDA7
MTNCQSSVFIVVGTLFSIMAAAQSAPVSTTTQAEIYLSQFGYLPASARNPASSGLHDQRTWVSAIEEFQSFAGLNITGELDAETMKLMSLPRCGVRDRVGTGDSRSKRYALQGSRWRVKNLTYKISKYPKRLKRVDVDAEIGRAFAVWSEDTDLTFTRKTSGPVHIEIKFVESEHGDGDAFDGQGGTLAHAFFPVFGGDAHFDDAELWTIGSPRGTNLFQVAAHEFGHSLGLSHSDQSSALMAPFYRGFEPVFKLDEDDKAAIQSLYGRKTNQLRPTNVYPATTQRPYSPPKVPLDDSICKDSKVDTLFNSAQGETYAFK...
Drosophila melanogaster (Fruit fly)
null
3.4.24.-
null
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-2}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR...
null
null
null
null
Calcium;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Zinc
adult fat body development [GO:0007505]; basement membrane disassembly [GO:0034769]; basement membrane organization [GO:0071711]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; collagen catabolic process [GO:0030574]; dorsal trunk growth, open tracheal system [GO:0035001]; extracellular matri...
dendrite [GO:0030425]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
null
null
null
IPR000585;IPR036375;IPR018487;IPR018486;IPR033739;IPR024079;IPR001818;IPR021190;IPR006026;IPR002477;IPR036365;
3.40.390.10;2.110.10.10;
A0A0B4K692
MQTVIQNPNWWRRRNKLEKSLLVSLGIMFVVLATGFGLWIGKVLRTSPPSNPQATALHGDSTTINQVPTGTASKGKSGDSGDVCLTQECIHTASTVLRKMKPEVEPCDNFYEFACGTYLEEENIPDDKVSISTFSVISDKLQEQLKDIITAERPETEPKHFRLPNLLYKACMNKTLIETLGPEPITRVAERLGGWPLIKGDSWNADDSWTWQEQVKKFRTAGFSMDYIIDFSIGVDLQNSTKRLIDLDQSSLALSREYLVKGFNETLVTAYYKYMVDIAVLFGANRDLAKTELLLSLEFEMALANISWPNEKRRNSSELY...
Drosophila melanogaster (Fruit fly)
FUNCTION: Metalloendoprotease which cleaves peptides such as tachykinin peptide TK-2 at the amino side of hydrophobic residues (PubMed:15554877, PubMed:17157960). Functions in female fertility, embryogenesis and memory formation (PubMed:24395329, PubMed:27629706). Required in females for normal patterns of egg laying, ...
3.4.24.11
CATALYTIC ACTIVITY: Reaction=Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11; Evidence={ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960};
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08473}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08473};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5 at 35 degrees Celsius. {ECO:0000269|PubMed:17157960};
null
Alternative splicing;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal-anchor;Transmembrane;Transmembrane helix;Zinc
protein processing [GO:0016485]; proteolysis [GO:0006508]; sperm competition [GO:0046692]
extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]
endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960}. Note=A secreted form exists that is probably produced by proteolytic cleavage (Probable). In embryos, adult Malpighian tubules and testes, detected ...
PTM: N-glycosylated. {ECO:0000269|PubMed:17157960}.; PTM: The soluble form is probably produced by proteolytic cleavage. {ECO:0000305|PubMed:15554877, ECO:0000305|PubMed:17157960}.
null
IPR024079;IPR000718;IPR018497;IPR042089;IPR008753;
3.40.390.10;1.10.1380.10;
A0A0B4K697
MQRRERQASGGGPQTTTAGPSAGNVANATTALAGGKSSSNNMYSTRQSVSTTTGVLMVGPNFRVGKKIGCGNFGELRLGRRMCCFGGGVGGRNGRGTTDNGGAGKNLYNNEHVAIKMEPMKSKAPQLHLEYRFYKLLGSHADNAPDGIPRIYHLGTCGGRYNAMVLELLGLSLEDLFNICARKFSLKTVLMIAKQLLHRIEYVHSRHLIYRDVKPENFLIGRTSTKREKIIHIIDFGLAKEYIDLDTNRHIPYREHKSLTGTARYMSINTHMGREQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRA...
Drosophila melanogaster (Fruit fly)
null
2.7.11.1
null
null
null
null
null
null
Proteomics identification;Reference proteome;Transferase;Wnt signaling pathway
endocytosis [GO:0006897]; glial cell migration [GO:0008347]; negative regulation of actin nucleation [GO:0051126]; olfactory learning [GO:0008355]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; protein phosphorylation [GO:0006468]; regulation of endocytic recycling [GO:2001135]; signal transducti...
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sperm individualization complex [GO:0070864]
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]
null
null
null
IPR022247;IPR011009;IPR000719;IPR008271;
1.10.510.10;
A0A0B4K7C4
MQRRERQASGGGPQTTTAGPSAGNVANATTALAGGKSSSNNMYSTRQSVSTTTGVLMVGPNFRVGKKIGCGNFGELRLGRRMCCFGGGVGGRNGRGTTDNGKNLYNNEHVAIKMEPMKSKAPQLHLEYRFYKLLGSHADNAPDGIPRIYHLGTCGGRYNAMVLELLGLSLEDLFNICARKFSLKTVLMIAKQLLHRIEYVHSRHLIYRDVKPENFLIGRTSTKREKIIHIIDFGLAKEYIDLDTNRHIPYREHKSLTGTARYMSINTHMGREQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI...
Drosophila melanogaster (Fruit fly)
null
2.7.11.1
null
null
null
null
null
null
Proteomics identification;Reference proteome;Transferase;Wnt signaling pathway
endocytosis [GO:0006897]; glial cell migration [GO:0008347]; negative regulation of actin nucleation [GO:0051126]; olfactory learning [GO:0008355]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; protein phosphorylation [GO:0006468]; regulation of endocytic recycling [GO:2001135]; signal transducti...
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sperm individualization complex [GO:0070864]
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]
null
null
null
IPR022247;IPR011009;IPR000719;IPR008271;
1.10.510.10;
A0A0B4K7C5
MSKSNLVISCLLLVAISNSLVRAQDLKVEVISTPEVCEQKSKNGDSLTMHYTGTLQADGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQGAGNVIPPKATLLFDVELINIGNAPPTTNVFKEIDDNADKQLSREEVIVYVSEYLKKQMTAVEGQDSEELKNMLAENDKLVEEIFQHEDKDKNGFISHDEFSGPKHDEL
Drosophila melanogaster (Fruit fly)
null
5.2.1.8
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|PROSITE-ProRule:PRU00277};
null
null
null
null
null
Calcium;Isomerase;Proteomics identification;Reference proteome;Rotamase;Signal
chaeta development [GO:0022416]; imaginal disc development [GO:0007444]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; muscle cell cellular homeostasis [GO:0046716]; positive regulation of Notch signaling pathway [GO:0045747]
endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]
calcium ion binding [GO:0005509]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]
null
null
null
IPR011992;IPR018247;IPR002048;IPR046357;IPR001179;
3.10.50.40;1.10.238.10;
A0A0B4K7H5
MTNCQSSVFIVVGTLFSIMAAAQSAPVSTTTQAEIYLSQFGYLPASARNPASSGLHDQRTWVSAIEEFQSFAGLNITGELDAETMKLMSLPRCGVRDRVGTGDSRSKRYALQGSRWRVKNLTYKISKYPKRLKRVDVDAEIGRAFAVWSEDTDLTFTRKTSGPVHIEIKFVESEHGDGDAFDGQGGTLAHAFFPVFGGDAHFDDAELWTIGSPRGTNLFQVAAHEFGHSLGLSHSDQSSALMAPFYRGFEPVFKLDEDDKAAIQSLYGRKTNQLRPTNVYPATTQRPYSPPKVPLDDSICKDSKVDTLFNSAQGETYAFK...
Drosophila melanogaster (Fruit fly)
null
3.4.24.-
null
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-2}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR...
null
null
null
null
Calcium;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Zinc
adult fat body development [GO:0007505]; basement membrane disassembly [GO:0034769]; basement membrane organization [GO:0071711]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; collagen catabolic process [GO:0030574]; dorsal trunk growth, open tracheal system [GO:0035001]; extracellular matri...
dendrite [GO:0030425]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
null
null
null
IPR000585;IPR036375;IPR018487;IPR018486;IPR033739;IPR024079;IPR001818;IPR021190;IPR006026;IPR002477;IPR036365;
3.40.390.10;2.110.10.10;
A0A0B4K7J2
MFTTRKEVDAHVHKMLGKLQPGRERDIKGLAVARLYMKVQEYPKAIEYLNGYLRVRDDAVGHNMIATCYSRLNPPDVTEALQHYQRSIQIDPRQSEVVIDACELLVKENNASITECARYWLDQANSLDLSGNKQVFNLRMRVNLADSNGERDDTSGGDGEQNTLEILMYKELQARPQDVNIRIQLLRSYVEKMKIDQAFNYALKTELESKNCTSQSNEWYEQIWMVLFKIEMAKDVKKNWRFWHFALHTLDRLVQLSLEGSGLADSSKQLFRLDQYLFKFSTSIERSGDAPQRDLHQACIDHFTGQLLLHAVTLIFKREV...
Drosophila melanogaster (Fruit fly)
FUNCTION: E3 SUMO-protein ligase (By similarity). Component of the nuclear pore complex (NPC), a complex required for trafficking across the nuclear envelope (PubMed:17682050). Required for nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner, but a...
2.3.2.-
null
null
null
null
null
null
Alternative splicing;Isopeptide bond;Metal-binding;mRNA transport;Nuclear pore complex;Nucleus;Phosphoprotein;Protein transport;Reference proteome;Repeat;TPR repeat;Transferase;Translocation;Transport;Ubl conjugation pathway;Zinc;Zinc-finger
germ cell development [GO:0007281]; juvenile hormone mediated signaling pathway [GO:0035626]; mRNA transport [GO:0051028]; NLS-bearing protein import into nucleus [GO:0006607]; nuclear pore complex assembly [GO:0051292]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expr...
annulate lamellae [GO:0005642]; cytoplasm [GO:0005737]; nuclear pore [GO:0005643]
GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; SUMO transferase activity [GO:0019789]
SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Note=Localizes to annulate lamellae, stacked membrane sheets of the endoplasmic reticulum. Localizes to granules which travel from nurse cells into the ooplasm through ring canals connecting the cytoplasm of the two cell types. {ECO:000...
null
DOMAIN: Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conserva...
IPR011993;IPR000156;IPR045255;IPR011990;IPR001876;IPR036443;
2.30.29.30;1.25.40.10;4.10.1060.10;
A0A0B4K7J3
MESNIYLVFLLTFLLYNNARAEISDHLREDIPDLDMELSSASSAHLNGKELPAVPQNSVQTHPRRHIKSKRRMKRRYKCYSCEPPCRDPYEFTHTCQNAIQCWKSRTRDADGQVQESRGCSTSPDQLPMICSQNSLKINGPSKRNTGKFVNVVCCAGDYCNEGDFPELLPFDSNDVTVITADTSSISKMLVAVLGPFLVIALLGAVTIFFIRRSHRKRLAASRTKQDPEAYLVNDELLRATSAGDSTLREYLQHSVTSGSGSGLPLLVQRTLAKQVTLIECIGRGKYGEVWRGHWHGESIAVKIFFSRDEESWKRETEIY...
Drosophila melanogaster (Fruit fly)
null
2.7.11.30
null
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;Kinase;Membrane;Nucleotide-binding;Receptor;Reference proteome;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix
anterior/posterior pattern specification, imaginal disc [GO:0007448]; BMP signaling pathway [GO:0030509]; cellular response to growth factor stimulus [GO:0071363]; defense response to Gram-negative bacterium [GO:0050829]; dorsal/ventral pattern formation [GO:0009953]; follicle cell of egg chamber development [GO:003070...
BMP receptor complex [GO:0070724]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; BMP binding [GO:0036122]; BMP receptor activity [GO:0098821]; I-SMAD binding [GO:0070411]; SMAD binding [GO:0046332]; transforming growth factor beta receptor activity, type I [GO:0005025]; transmembrane receptor protein serine/threonine kinase activity [GO:0004675]
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
null
null
IPR000472;IPR003605;IPR011009;IPR000719;IPR017441;IPR001245;IPR008271;IPR045860;IPR000333;
2.10.60.10;1.10.510.10;
A0A0B4K7Q3
MGGFLDKPKTAKHNDEGEGNKLLFGVSSMQGWRSEMEDAYYARAGLGDALPDWSFFAVFDGHAGCKVSEHCAKHLLESIISTEEFIGGDHVKGIRTGFLRIDEVMRELPEFTRESEKCGGTTAVCAFVGLTQVYIANCGDSRAVLCRQGVPVFATQDHKPILPEEKERIYNAGGSVMIKRVNGTLAVSRALGDYDFKNVKEKGQCEQLVSPEPEIFCQSRQDSDEFLVLACDGIWDVMSNEDVCSFIHSRMRVTSNLVSIANQVVDTCLHKGSRDNMSIIIIAFPGAPKPTEEAIEAEHRLEKQIEKITRERELAEWANC...
Drosophila melanogaster (Fruit fly)
null
3.1.3.16
null
null
null
null
null
null
Coiled coil;Cytoplasm;Hydrolase;Lipoprotein;Membrane;Metal-binding;Myristate;Phosphoprotein;Protein phosphatase;Proteomics identification;Reference proteome
determination of adult lifespan [GO:0008340]; dorsal closure [GO:0007391]; imaginal disc fusion, thorax closure [GO:0046529]; mitotic cell cycle [GO:0000278]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of JN...
cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]
magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
null
null
IPR015655;IPR000222;IPR012911;IPR036457;IPR001932;
3.60.40.10;
A0A0B4KF46
MAGNSAAAGGDIDESLYSRQLYVLGHDAMRRMANSDILLSGLGGLGLEIAKNVILGGVKSITLHDTATCGLHDLSSQFYLTEADIGKNRAEASCAQLAELNNYVRTVSHTGPLTEEFLRKFRVVVLTNSDGEEQQRIAKFAHENGIALIIAETRGLFAKVFCDFGESFTIYDQDGTQPISTMIASITHDAQGVVTCLDETRHGFNDGDYVTFSEVQGMQELNGCQPLKITVLGPYTFSIGDTSKFGEYKSGGVATQVKMPKTISFKPLAQATEEPEFLISDFAKLDSPATLHVAFNALSCYRKAHNGALPRPWNEEDANS...
Drosophila melanogaster (Fruit fly)
null
6.2.1.45
CATALYTIC ACTIVITY: Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
null
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906}.
null
null
ATP-binding;Ligase;Nucleotide-binding;Proteomics identification;Reference proteome;Ubl conjugation pathway
autophagy [GO:0006914]; DNA damage response [GO:0006974]; follicle cell of egg chamber development [GO:0030707]; larval midgut cell programmed cell death [GO:0035096]; lipid storage [GO:0019915]; mushroom body development [GO:0016319]; neuron remodeling [GO:0016322]; protein polyubiquitination [GO:0000209]; protein ubi...
cytoplasm [GO:0005737]; dendrite [GO:0030425]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; ubiquitin activating enzyme activity [GO:0004839]
null
null
null
IPR032420;IPR032418;IPR042302;IPR045886;IPR000594;IPR018965;IPR042449;IPR038252;IPR019572;IPR042063;IPR035985;IPR018075;IPR018074;IPR033127;IPR000011;
3.40.50.720;2.40.30.180;3.50.50.80;3.40.50.12550;1.10.10.2660;3.10.290.60;
A0A0B4KF69
MNKADVNRRVLAIQAKKKRHKNRKRGKQNGTNPQEQSNSSQNQNPKPSSNPIPEPNRSSENLQAPDNANNSHLNAPSSAAFSKATATATASTSSGGSAGTPDQYQPPKKTQAKAKPNTQKEHQQQPPRSSSNESYESETFSDNEDQELMEDYCKGGYHPVNIGDLFHDRYHVIRKLGWGHFSTVWLCWDLQAMGYVAIKIVKSAPHFAETARDEIKILKTVRETDPSNPRRHKTVQMLDDFKITGVNGTHICMVFEVLGDNLLKLIRKSNYRGIPLANVKTITRQVLEGLDYLHTCCKIIHTDIKPENVLLCVDEPHVRS...
Drosophila melanogaster (Fruit fly)
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;Kinase;Nucleotide-binding;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase
intracellular signal transduction [GO:0035556]; oocyte karyosome formation [GO:0030717]; peptidyl-serine phosphorylation [GO:0018105]; regulation of mRNA processing [GO:0050684]; spindle assembly involved in female meiosis [GO:0007056]; spliceosomal complex assembly [GO:0000245]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
null
null
null
IPR011009;IPR000719;IPR017441;IPR008271;
1.10.510.10;
A0A0B4KF84
MGNGCSKCCQCNEHKQLNGTLSSASSVYRKRSRGEIPIENSDRFRITATSNAVQLAVEHVQREDAGHYTLFARTKRQDVVRRHVELIVEDRSTGDDPPVFVRRLPDLSVKVGTRTRLLTEIRSSTDLKLTWYRNDRRVCANDRITEVNEGTFHYLEISPVTLDDGGQWMLMAENFGGRNSCLGTLNVLVPKAYKTPEFVEELRAVLTEQGTVSLECKVVGVPTPHLRWFKDSKEIKAGDIFALTANADDPTSLGTYTCEARNCMGVTYSSSKVHVVGRGSREGSLKPADSVASNAPPPIFTNELRDMSLLIGETIILGCQ...
Drosophila melanogaster (Fruit fly)
null
2.7.11.17; 2.7.11.18
null
null
null
null
null
null
ATP-binding;Coiled coil;Immunoglobulin domain;Nucleotide-binding;Proteomics identification;Reference proteome;Repeat;Transferase
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; protein phosphorylation [GO:0006468]
null
ATP binding [GO:0005524]; calmodulin-dependent protein kinase activity [GO:0004683]; myosin light chain kinase activity [GO:0004687]; structural constituent of cytoskeleton [GO:0005200]
null
null
null
IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR003598;IPR013106;IPR011009;IPR000719;IPR017441;IPR008271;
2.60.40.10;1.10.510.10;
A0A0B4KFE4
MDSFWVQSAIGAIKAIAFVYDIITLPVYLVLQKPWKRRQDSRRVKAKPINQKMLVDESKYAPDDIEAKIVRNDDNELTYRTTDPPRDVHVKMLQENIDTLEKVFNYVAKTYTSKRCLGTRQILSEEDEVQQNGRVFKKYNLGDYKWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLPKFKTLLDKCPLVKTIIYIEDQLQKTETTGFKEGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKG...
Drosophila melanogaster (Fruit fly)
null
6.2.1.3
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000256|ARBA:ARBA00024484}; Physiological...
null
null
null
null
null
Fatty acid metabolism;Ligase;Lipid metabolism;Proteomics identification;Reference proteome
axon guidance [GO:0007411]; fatty acid biosynthetic process [GO:0006633]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; long-chain fatty-acyl-CoA metabolic process [GO:0035336]; nervous system development [GO:0007399]; neuron differentiation [GO:00301...
axon [GO:0030424]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; lipid droplet [GO:0005811]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]
long-chain fatty acid-CoA ligase activity [GO:0004467]; palmitoyl-CoA ligase activity [GO:0090433]
null
null
null
IPR045851;IPR020845;IPR000873;IPR042099;
3.30.300.30;3.40.50.12780;
A0A0B4KFL3
MSITQHLEKLTHSSALIGTNLCLSFLATMTTTCSDRQLLRGGKQKTTTCVGMTVMAKTTFEEICENAKLARDMALTGNYDSACIYYEGLQGLLARQLKATADPLRKGKWSMINQQISQEHAKIKAIQRTLQDISLDLQSTKFAHKLRHQLSEESTTSKDPSAWFKPDPDIWTPPPKDPDVWGPPKPPPTTQAVGRRAAPNNRRTTPATQNSRPSSTIPQSTARNGPASTRNSRNSTSATAPSGGARTTNGRAGGRKLSTSNTNEARDDDSTAAGNNGGAAGDGENGDPQAAQEEERKFQPNNHIEAELVDILERDILQKD...
Drosophila melanogaster (Fruit fly)
FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. {ECO:0000256|HAMAP-Rule:MF_03023}.
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|HAMAP-Rule:MF_03023};
null
null
null
null
null
ATP-binding;Cell cycle;Cell division;Cytoplasm;Cytoskeleton;Hydrolase;Isomerase;Microtubule;Mitosis;Nucleotide-binding;Reference proteome
cell division [GO:0051301]; cytoplasmic microtubule organization [GO:0031122]; dendrite development [GO:0016358]; microtubule depolymerization [GO:0007019]; microtubule severing [GO:0051013]; mitotic sister chromatid segregation [GO:0000070]; negative regulation of cell migration [GO:0030336]; regulation of synaptic as...
cell cortex [GO:0005938]; cell leading edge [GO:0031252]; centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasmic microtubule [GO:0005881]; microtubule cytoskeleton [GO:0015630]; spindle pole [GO:0000922]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]; myosin binding [GO:0017022]
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03023}. Note=Predo...
null
null
IPR003593;IPR041569;IPR003959;IPR003960;IPR028596;IPR048611;IPR048612;IPR027417;IPR015415;
1.10.8.60;3.40.50.300;1.20.58.80;
A0A0B4KFR5
MASDKIKVAVRVRPFNRREIELDTKCIVEMEKQQTILQNPPPLEKIERKQPKTFAFDHCFYSLNPEDENFASQETVFDCVGRGILDNAFQGYNACIFAYGQTGSGKSYTMMGTQESKGIIPRLCDQLFSAIANKSTPELMYKVEVSYMEIYNEKVHDLLDPKPNKQSLKVREHNVMGPYVDGLSQLAVTSYQDIDNLMTEGNKSRTVAATNMNAESSRSHAVFSVVLTQILTDQATGVSGEKVSRMSLVDLAGSERAVKTGAVGDRLKEGSNINKSLTTLGLVISKLADQSNGKKSGNDKFVPYRDSVLTWLLKDNLGGN...
Drosophila melanogaster (Fruit fly)
null
3.6.1.3
null
null
null
null
null
null
ATP-binding;Coiled coil;Cytoplasm;Cytoskeleton;Hydrolase;Microtubule;Motor protein;Nucleotide-binding;Proteomics identification;Reference proteome
cytoskeleton-dependent intracellular transport [GO:0030705]; establishment of spindle orientation [GO:0051294]; microtubule-based movement [GO:0007018]; regulation of olfactory learning [GO:0090328]; regulation of synapse structure or activity [GO:0050803]
early endosome [GO:0005769]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule plus-end [GO:0035371]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; protein homodimerization activity [GO:0042803]
null
null
null
IPR036859;IPR000938;IPR000253;IPR022164;IPR022140;IPR032405;IPR019821;IPR001752;IPR036961;IPR027417;IPR008984;
2.60.200.20;6.10.250.2520;2.30.30.190;3.40.850.10;
A0A0B4KG24
MEKQQTILQNPPPLEKIERKQPKTFAFDHCFYSLNPEDENFASQETVFDCVGRGILDNAFQGYNACIFAYGQTGSGKSYTMMGTQESKGIIPRLCDQLFSAIANKSTPELMYKVEVSYMEIYNEKVHDLLDPKPNKQSLKVREHNVMGPYVDGLSQLAVTSYQDIDNLMTEGNKSRTVAATNMNAESSRSHAVFSVVLTQILTDQATGVSGEKVSRMSLVDLAGSERAVKTGAVGDRLKEGSNINKSLTTLGLVISKLADQSNGKKSGNDKFVPYRDSVLTWLLKDNLGGNSRTVMVATISPSADNYEETLSTLRYADRA...
Drosophila melanogaster (Fruit fly)
null
3.6.1.3
null
null
null
null
null
null
ATP-binding;Coiled coil;Cytoplasm;Cytoskeleton;Hydrolase;Microtubule;Motor protein;Nucleotide-binding;Proteomics identification;Reference proteome
cytoskeleton-dependent intracellular transport [GO:0030705]; establishment of spindle orientation [GO:0051294]; microtubule-based movement [GO:0007018]
early endosome [GO:0005769]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule plus-end [GO:0035371]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; protein homodimerization activity [GO:0042803]
null
null
null
IPR036859;IPR000938;IPR000253;IPR022164;IPR022140;IPR032405;IPR019821;IPR001752;IPR036961;IPR027417;IPR008984;
2.60.200.20;6.10.250.2520;2.30.30.190;3.40.850.10;
A0A0B4KG35
MERSPAANAAEPPGEDGVPEAGHRPPPRITFSENSSSLIRCIPNERATFFVKIDCSEEDEPELLPFKFEWSRGEIPIENSDRFRITATSNAVQLAVEHVQREDAGHYTLFARTKRQDVVRRHVELIVEDRSTGDDPPVFVRRLPDLSVKVGTRTRLLTEIRSSTDLKLTWYRNDRRVCANDRITEVNEGTFHYLEISPVTLDDGGQWMLMAENFGGRNSCLGTLNVLVPKAYKTPEFVEELRAVLTEQGTVSLECKVVGVPTPHLRWFKDSKEIKAGDIFALTANADDPTSLGTYTCEARNCMGVTYSSSKVHVVGRGSR...
Drosophila melanogaster (Fruit fly)
null
2.7.11.17; 2.7.11.18
null
null
null
null
null
null
ATP-binding;Coiled coil;Immunoglobulin domain;Nucleotide-binding;Proteomics identification;Reference proteome;Repeat;Transferase
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; negative regulation of hippo signaling [GO:0035331]; protein phosphorylation [GO:0006468]
lateral cell cortex [GO:0097575]
ATP binding [GO:0005524]; calmodulin-dependent protein kinase activity [GO:0004683]; cytoskeletal motor activator activity [GO:0140660]; myosin light chain kinase activity [GO:0004687]; protein serine/threonine kinase activity [GO:0004674]; structural constituent of cytoskeleton [GO:0005200]
null
null
null
IPR003961;IPR036116;IPR007110;IPR036179;IPR013783;IPR013098;IPR003599;IPR003598;IPR013106;IPR011009;IPR000719;IPR017441;IPR008271;
2.60.40.10;1.10.510.10;
A0A0B4KG59
MSKYDLLYLTAQLTLVCCLIGIHGSILPGSHGIIECEHFDEKMCNTTQQCETRIEHCKMEADKFPSCYVLWSVNETTGILRIKMKGCFTDMHECNQTECVTSAEPRQGNIHFCCCKGSRCNSNQKYIKSTTEATTQVPKEKTQDGSNLIYIYIGTSVFSVLMVIVGMGLLLYRRRKQAHFNEIPTHEAEITNSSPLLSNRPIQLLEQKASGRFGDVWQAKLNNQDVAVKIFRMQEKESWTTEHDIYKLPRMRHPNILEFLGVEKHMDKPEYWLISTYQHNGSLCDYLKSHTISWPELCRIAESMANGLAHLHEEIPASKT...
Drosophila melanogaster (Fruit fly)
null
2.7.11.30
CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence={ECO:0000256|R...
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|RuleBase:RU361271}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|RuleBase:RU361271};
null
null
null
null
ATP-binding;Kinase;Magnesium;Manganese;Membrane;Metal-binding;Nucleotide-binding;Proteomics identification;Receptor;Reference proteome;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix
activin receptor signaling pathway [GO:0032924]; axon guidance [GO:0007411]; BMP signaling pathway [GO:0030509]; cellular response to glucose stimulus [GO:0071333]; cellular response to growth factor stimulus [GO:0071363]; dorsal closure [GO:0007391]; dorsal/ventral pattern formation [GO:0009953]; germ-line stem cell d...
activin receptor complex [GO:0048179]; basolateral plasma membrane [GO:0016323]; BMP receptor complex [GO:0070724]; plasma membrane [GO:0005886]
activin binding [GO:0048185]; activin receptor activity [GO:0017002]; activin receptor activity, type II [GO:0016362]; ATP binding [GO:0005524]; BMP receptor activity [GO:0098821]; metal ion binding [GO:0046872]; SMAD binding [GO:0046332]; transforming growth factor beta binding [GO:0050431]; transforming growth factor...
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}.
null
null
IPR000472;IPR011009;IPR000719;IPR008271;IPR045860;IPR000333;
2.10.60.10;1.10.510.10;
A0A0B4KG66
MTTPVPRRTKDMMALGLDSDSEDDFNTPYRPRQAAAGERKQQPVASFQVQTRGKENEPHPLPINMLPRRVSELTMMDSDSDEEDIKSNHNLNCAILNDSFVLSPSQELTNSNSNITTRRTPSAAPLKQSDSNLSFLGRFNDMGINCSSQGSPVANSEKQVAKKTAPTLQAAPSATERRPLQETETPLRNELPSTSKTKPDADFITPQVRTIGSTLAGKSRSAVSNDFRAQKVLFQTPMTVSRAAPVASDSISFSLCDTITESPDIPEPPKKAEPPKSQHPSKKSLDHVFRESDKDNVPDKVDNVEPKELVSIPAVAVPPE...
Drosophila melanogaster (Fruit fly)
null
2.7.11.-; 2.7.12.1
null
null
null
null
null
null
ATP-binding;Kinase;Nucleotide-binding;Reference proteome;Transferase
achiasmate meiosis I [GO:0000705]; chromosome segregation [GO:0007059]; distributive segregation [GO:0032837]; female meiosis chromosome segregation [GO:0016321]; female meiotic nuclear division [GO:0007143]; male germ-line stem cell asymmetric division [GO:0048133]; meiotic cell cycle [GO:0051321]; meiotic metaphase I...
centrosome [GO:0005813]; kinetochore [GO:0000776]; nucleus [GO:0005634]; outer kinetochore [GO:0000940]
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]
null
null
null
IPR011009;IPR027084;IPR000719;IPR017441;IPR008271;
1.10.510.10;
A0A0B4KGS4
MSFTKWFKKKGGDGGSISEIGAPTNFQRHFHVSRNQETGDLEGLPAPWVRLMNSQITRDEQDKNPDAAYHAVKYYNYSIKKKENEVFKPFITEDVIHEESKEIENYVNYKNKHKSQDPEKSDDDGSSTATETESSSGCGSSAGNSNSSSINDSSQQSTVPLDALEEVFKELKTNLEHRETLKAAPQEPPPVPPKKSPHTIPPKPQIKPKPRVTQKFSRTSDIRRDEDSDNQHKINTDTIIIKPAVGAQDAGADDNPDETILRRSKEKRAQKTDAEIYVELRAICNSDDPRERYKTTQEVGKGASGIVFIAADLQNESQVA...
Drosophila melanogaster (Fruit fly)
null
2.7.11.1
null
null
null
null
null
null
ATP-binding;Nucleotide-binding;Proteomics identification;Reference proteome;Transferase
actin filament organization [GO:0007015]; border follicle cell migration [GO:0007298]; cell projection organization [GO:0030030]; intracellular signal transduction [GO:0035556]; myoblast fusion [GO:0007520]; positive regulation of synapse assembly [GO:0051965]; regulation of axonogenesis [GO:0050770]; regulation of MAP...
cytoplasm [GO:0005737]; ruffle [GO:0001726]
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]
null
null
null
IPR000095;IPR036936;IPR011009;IPR033923;IPR000719;IPR017441;IPR008271;
3.90.810.10;1.10.510.10;
A0A0B4KGX7
MENADATSQSDVHIDYKTPKKTHSLIDSEQLLDKINILTTKPENHSQNAKLPTIKDFVIIKPISRGAFGKVFLGYKNNDSKRLFAIKVMRKSEMINKNMVSQVITERNALALSRSQFCVSLFYSLQSLSYVYLVMEYMVGGDLKSLLAMFGYFDEPTARFYVAEMVMALQYLHQHGIVHRDIKPDNMLLSSSGHVKLTDFGLSKIDMRRDLEISDLINCSPNLNARTPGQLLSLTSHLSFGSEKKLNDFGSVSSGQNNGMGSVATGTSHLLQAINKHSLIMELSDSEGDTSLNDAEKTSDSKISGVSPFFSAEEANESIT...
Drosophila melanogaster (Fruit fly)
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;Kinase;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase
chromosome condensation [GO:0030261]; female meiosis I [GO:0007144]; female meiotic nuclear division [GO:0007143]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; phosphorylation [GO:0016310]; regulation of meiotic nuclear division [GO:0040020]; regulation of mitotic cell cycle [GO:0007...
cytoplasm [GO:0005737]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]
14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
null
null
null
IPR000961;IPR011009;IPR000719;IPR008271;
1.10.510.10;
A0A0B4KH16
MSDSDEDAREEVRQIKHGELRTAVISGDERTVRVLLAALGTERQIIVNMAPSGANTLLFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDHFPELIQQPTVERWLPLHAACINGHIKLLELLISYSYPDYLYQTYRDEEGQWEWRLPFDANAHDVTGQTSLYIASILGNKQLVGVLLKWQLHCRRTLGDSASSVSTPITPTRKRISFGIQAIMSKLHISGESEGPDDLASQESTECQRCPINVNLLCGAARETALLAAVRGGHLDVVQSLLQHGANPNIVAKPVEDHNDPKCCEEIYGLSNV...
Drosophila melanogaster (Fruit fly)
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};
null
null
null
null
ANK repeat;ATP-binding;Differentiation;GTP-binding;Kinase;Leucine-rich repeat;Nucleotide-binding;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase
autophagy [GO:0006914]; axo-dendritic transport [GO:0008088]; cell differentiation [GO:0030154]; establishment of Golgi localization [GO:0051683]; locomotion [GO:0040011]; lysosome localization [GO:0032418]; negative regulation of dendrite morphogenesis [GO:0050774]; peptidyl-serine phosphorylation [GO:0018105]; regula...
cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic branch point [GO:1990033]; dendritic shaft [GO:0043198]; Golgi stack [GO:0005795]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]
ATP binding [GO:0005524]; GTP binding [GO:0005525]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]
null
null
null
IPR002110;IPR036770;IPR032171;IPR011009;IPR001611;IPR003591;IPR032675;IPR027417;IPR000719;IPR017441;IPR011047;IPR020859;IPR008271;
1.25.40.20;3.40.50.300;3.80.10.10;3.30.70.1390;1.10.510.10;
A0A0B4KH77
MEGGYVNEEDSDAIMGVESPAIISFTNPKLQIPLMASAIYAPTTITTNTTSTAGTPTSAKNASASASASASASLSSPAGPSAAGSASTSSAPAGGGPWQGLVAKLRNFKLDDTKNIRKRFHFDYISKDRFLGGQLKTKNGQKYVFNGPPSGVYVSKACLIIAAFITVLALLFTIAITYFVTRQGLNPKEVTPPSCITADHPDVNATPIQTAGWVSMNSPPPLQAATPTPMASPTPTNTPTVTTTLAMPASSEKPEIRMVDPKVGDIPVVEPAAGEVEDNTTKPINRPLKLYEGWRPLHYSLLIEPSVATSISNGSLTIEI...
Drosophila melanogaster (Fruit fly)
null
3.4.11.-
null
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR634016-3}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
null
null
null
null
Aminopeptidase;Glycoprotein;GPI-anchor;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc
cell dedifferentiation [GO:0043697]; germ-line stem-cell niche homeostasis [GO:0060250]; male germ-line stem cell population maintenance [GO:0036098]; peptide catabolic process [GO:0043171]; protein processing [GO:0016485]; proteolysis [GO:0006508]; somatic stem cell population maintenance [GO:0035019]
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
aminopeptidase activity [GO:0004177]; metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270]
SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
null
null
IPR045357;IPR042097;IPR024571;IPR034016;IPR001930;IPR014782;IPR027268;
1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730;
A0A0B4KHH7
MSAFIEETKSLLPRIAFIACGCFSPPTPMHLRMFEIAKDHFEMQGTHRVVGGIISPTHDSYGKKGLASALDRCAMVKLATQSSNWIRLSDWEVHQNQWMRTQAVLQHHQNYINNHINSGGGGGDDGENTHLPGWLPRGLHDSRDPVHLKLLCGADLLESFAVPGLWAEADIEDIVANHGLVVITRAGSNPGKFIFDSDILTKYQSNITLITNWVPNEVSSTLIRRLLGRGQSVKYLLDDLVLEYIKRQRLFNFKSKYITDAVRPNHLLFNHAYTDNNKNANSYSIGDQLEQDMDESDTPSPQLQHTPTSRVFCCGEVPLR...
Drosophila melanogaster (Fruit fly)
null
2.7.7.1; 2.7.7.18
CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18; Evidence={ECO:0000256|RuleBase:RU362021}; CATALYTIC ACTIVITY: Reaction=ATP + beta-n...
null
null
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1. {ECO:0000256|ARBA:ARBA00004658, ECO:0000256|RuleBase:RU362021}.; PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. {ECO:0000256|ARBA:ARBA00005019}.
null
null
ATP-binding;NAD;Nucleotide-binding;Nucleotidyltransferase;Proteomics identification;Pyridine nucleotide biosynthesis;Reference proteome;Transferase
dendritic spine maintenance [GO:0097062]; NAD biosynthetic process [GO:0009435]; photoreceptor cell maintenance [GO:0045494]
cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]
ATP binding [GO:0005524]; nicotinamide-nucleotide adenylyltransferase activity [GO:0000309]; nicotinate-nucleotide adenylyltransferase activity [GO:0004515]; unfolded protein binding [GO:0051082]
null
null
null
IPR004821;IPR005248;IPR045094;IPR014729;
3.40.50.620;
A0A0B4KHL4
MQRRERQASGGGPQTTTAGPSAGNVANATTALAGGKSSSNNMYSTRQSVSTTTGVLMVGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKMEPMKSKAPQLHLEYRFYKLLGSHADNAPDGIPRIYHLGTCGGRYNAMVLELLGLSLEDLFNICARKFSLKTVLMIAKQLLHRIEYVHSRHLIYRDVKPENFLIGRTSTKREKIIHIIDFGLAKEYIDLDTNRHIPYREHKSLTGTARYMSINTHMGREQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCDGHPEEFATYLRYVRRLD...
Drosophila melanogaster (Fruit fly)
null
2.7.11.1
null
null
null
null
null
null
ATP-binding;Nucleotide-binding;Proteomics identification;Reference proteome;Transferase;Wnt signaling pathway
endocytosis [GO:0006897]; glial cell migration [GO:0008347]; negative regulation of actin nucleation [GO:0051126]; olfactory learning [GO:0008355]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of smoothened signaling pathway [GO:0045880]; protein phosphorylation [GO:0006468];...
cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sperm individualization complex [GO:0070864]
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]
null
null
null
IPR022247;IPR011009;IPR000719;IPR017441;IPR008271;
1.10.510.10;
A0A0B4KHT3
MSDSDEARAQGDIGAMEVGAQKLFSNSHPPQKQLVQPLDHPTPTKRQIKTNATHSPNATFLNKCNSCRASWAPTCAVRHKTAWINDHKNVAIDFPQFNAREEVRQIKHGELRTAVISGDERTVRVLLAALGTERQIIVNMAPSGANTLLFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDHFPELIQQPTVERWLPLHAACINGHIKLLELLISYSYPDYLYQTYRDEEGQWEWRLPFDANAHDVTGQTSLYIASILGNKQLVGVLLKWQLHCRRTLGDSASSVSTPITPTRKRISFGIQA...
Drosophila melanogaster (Fruit fly)
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};
null
null
null
null
ANK repeat;ATP-binding;Differentiation;GTP-binding;Kinase;Leucine-rich repeat;Nucleotide-binding;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase
autophagy [GO:0006914]; axo-dendritic transport [GO:0008088]; cell differentiation [GO:0030154]; establishment of Golgi localization [GO:0051683]; locomotion [GO:0040011]; lysosome localization [GO:0032418]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of neuron apoptotic process [GO:...
cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic branch point [GO:1990033]; dendritic shaft [GO:0043198]; Golgi stack [GO:0005795]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; subsynaptic reticulum [GO:0071212]; terminal bouton [GO:0043195]
ATP binding [GO:0005524]; GTP binding [GO:0005525]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]
null
null
null
IPR002110;IPR036770;IPR032171;IPR011009;IPR001611;IPR003591;IPR032675;IPR027417;IPR000719;IPR017441;IPR011047;IPR020859;IPR008271;
1.25.40.20;3.40.50.300;3.80.10.10;3.30.70.1390;1.10.510.10;
A0A0B4KHX7
MADEKAKESFRERQAQELEVIKSIFGCDVEDLRPQANPSLWKPTDIRIQLTPLRDSSNGLETYVCTKLHVTCPSKYPKLPPKISLEESKGMSDQLLEALRNQLQAQSQELRGEVMIYELAQTVQAFLLEHNKPPKGSFYDQMLQDKQKRDQELQDIQRQRESLQRQTLIDEVERRKEMFKTEAKRRGEPRRSMSESNPRHPSSSESSENSSPYYRGHIYPSKCLDHRNTETLYFHKMGRQIQRGCCVGEGHSQRGCIAYTGIDMHCGQLLYITEWNIKYSQLEQPCIGGGKCHWSSESKCMGSHRVDEVMASIEKQVSSL...
Drosophila melanogaster (Fruit fly)
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;Kinase;Nucleotide-binding;Proteomics identification;Reference proteome;Serine/threonine-protein kinase;Transferase
DNA damage checkpoint signaling [GO:0000077]; negative regulation of cytoplasmic translational initiation in response to stress [GO:1990625]; positive regulation of cell size [GO:0045793]; protein phosphorylation [GO:0006468]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein serine kinase activity [GO:0106310]
null
null
null
IPR045864;IPR016255;IPR011009;IPR000719;IPR017441;IPR006575;IPR008271;IPR016135;
1.10.510.10;3.10.110.10;
A0A0B4KI27
MVKLIASLLLLAVVAQAYGDFKCALSKQESKSFVRELQREREEHQLKEKQNLSHEGQDQECKGSLAVPEITKDWVDMKDACIKGMRNQIQEEINASYQYLAMGAYFSRDTVNRPGFAEHFFKAAKEEREHGSKLVEYLSMRGQLTEGVSDLINVPTVAKQEWTDGAAALSDALDLEIKVTKSIRKLIQTCENKPYNHYHLVDYLTGVYLEEQLHGQRELAGKLTTLKKMMDTNGELGEFLFDKTL
Drosophila melanogaster (Fruit fly)
FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. {ECO:0000256|RuleBase:RU361145}.
1.16.3.1
CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000256|RuleBase:RU361145};
null
null
null
null
null
Iron;Iron storage;Metal-binding;Oxidoreductase;Proteomics identification;Reference proteome;Secreted;Signal
detoxification of iron ion [GO:1990461]; intracellular iron ion homeostasis [GO:0006879]; intracellular sequestering of iron ion [GO:0006880]; iron ion import across plasma membrane [GO:0098711]; response to fungus [GO:0009620]
extracellular region [GO:0005576]; fusome [GO:0045169]; Golgi apparatus [GO:0005794]; intracellular ferritin complex [GO:0008043]
ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; ferroxidase activity [GO:0004322]
null
null
null
IPR001519;IPR012347;IPR009040;IPR009078;IPR008331;
1.20.1260.10;
A0A0B4LEJ6
MLGFSLWGEAVKRGFFCDDSSLRHPYRDSTMPSWILYLMCGALPLTVMLVVEFFRGQDKRLHSPFPKSTMCSGYHLCHLELPTWLVECYHRMGIFIFGLGVEQLSTNIAKYSIGRLRPHFYTLCQPVMKDGTTCSDPINAARYIEEFTCAAVDITSKQLKDMRLSFPSGHASFACYSMLYLVIYLHRRMQWKQLRMLCHLLQFLLLMFAWYTALTRVSDYKHHWSDVLAGSGIGLTYAVVVTSTMW
Drosophila melanogaster (Fruit fly)
null
3.1.3.-; 3.1.3.4
null
null
null
null
null
null
Hydrolase;Membrane;Reference proteome;Transmembrane;Transmembrane helix
ectopic germ cell programmed cell death [GO:0035234]; germ cell development [GO:0007281]; germ cell migration [GO:0008354]; germ cell repulsion [GO:0035233]; phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; pole cell development [GO:0007277]; pole cell migration [GO:0007280]; si...
apical part of cell [GO:0045177]; plasma membrane [GO:0005886]
lipid phosphatase activity [GO:0042577]; lipid transporter activity [GO:0005319]; phosphatidate phosphatase activity [GO:0008195]
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
null
null
IPR036938;IPR000326;IPR043216;
1.20.144.10;
A0A0B4LFB8
MLRIYQNTYRRTARKAVVYSTKVACCNHSTLCGITSHPRRAQDSGSSSSNGRHRGHEEFLLAGNPARGWQMPPPSRGYGMLVVRILRGALKLRYIVLGGAIGGGVSLSKKYEEWKDGLPNFKWLEDAMPQGERWSQFSRNLIEVGSLVKNAIEVAKDDLKAKTTVAALGITSDESRKKYEKLQSQVETLQTEIMNVQIKYQKELEKMEKENRELRQQYLILKTNKKTTAKKIKKSLIDMYSEVLDELSGYDTGYTMADHLPRVVVVGDQSSGKTSVLESIAKARIFPRGSGEMMTRAPVKVTLAEGPYHVAQFRDSDREY...
Drosophila melanogaster (Fruit fly)
null
3.6.5.5
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; EC=3.6.5.5; Evidence={ECO:0000256|ARBA:ARBA00001837};
null
null
null
null
null
Apoptosis;Coiled coil;Lipid-binding;Membrane;Mitochondrion;Mitochondrion inner membrane;Proteomics identification;Reference proteome;Transit peptide;Transmembrane;Transmembrane helix
apoptotic process [GO:0006915]; compound eye morphogenesis [GO:0001745]; mitochondrial fusion [GO:0008053]; mitochondrion organization [GO:0007005]; positive regulation of mitochondrial fusion [GO:0010636]
cytoplasm [GO:0005737]; microtubule [GO:0005874]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; lipid binding [GO:0008289]; microtubule binding [GO:0008017]
SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
null
null
IPR022812;IPR001401;IPR045063;IPR030381;IPR045817;IPR027417;
3.40.50.300;