ID A0A1X7VVZ4_AMPQE Unreviewed; 505 AA.
AC A0A1X7VVZ4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Non-specific protein-tyrosine kinase {ECO:0008006|Google:ProtNLM};
GN Name=100635378 {ECO:0000313|EnsemblMetazoa:Aqu2.1.44044_001};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.44044_001, ECO:0000313|Proteomes:UP000007879};
RN [1] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20686567; DOI=10.1038/nature09201;
RA Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The Amphimedon queenslandica genome and the evolution of animal
RT complexity.";
RL Nature 466:720-726(2010).
RN [2] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT evolution of animal complexity.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.44044_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
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DR RefSeq; XP_011410277.2; XM_011411975.2.
DR AlphaFoldDB; A0A1X7VVZ4; -.
DR STRING; 400682.A0A1X7VVZ4; -.
DR EnsemblMetazoa; Aqu2.1.44044_001; Aqu2.1.44044_001; Aqu2.1.44044.
DR GeneID; 100635378; -.
DR KEGG; aqu:100635378; -.
DR eggNOG; KOG0196; Eukaryota.
DR InParanoid; A0A1X7VVZ4; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000007879; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR CDD; cd00821; PH; 1.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF600; PDGF-AND VEGF-RECEPTOR RELATED, ISOFORM J; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00233; PH; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000007879}.
FT DOMAIN 15..112
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 241..502
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 505 AA; 57337 MW; A6FE0C87A967915A CRC64;
MASASGCMAP GNSTIRSMQG SLKMYKKRKW KTYFFKVTGS TYFHYFPQSN HNKAKKEVFL
TKVKGVTIPL SPPKGGEYVF EVRFTKDKPW VLSALTNEER HKWIETIYPQ YKPPESFVPT
DLPGDNGRGR DCSIQSLVLH TKAVVDTVPV FYKYERKANT DVVTKSSEFN EEEQKKYIEL
SMHSQVTNDD LDADSDGYFV MSSPQLSDSV VQTSIKNQRS TSLSQQTTTV EQHHIIPSSC
LSNETIIGQG NFGQVCVADY LPLVGSSSIQ VAVKMLFDRN SQDSVLKEFN VMASTMHPNI
VRLYGLVVDS TAMGLRIVME YLPYGDLKTY LKVSAKKPVR TLVKYMIDVS MGMHYIAQKG
LIHRDLAARN VLVGERETCK ISDFSLIKEL PADTSTYQSF TSVPLPIRWM SPEALVHKEF
SEASDIWSYG VLQWEMFNPD ETPYQSMEDA QVVMYVMNGK RLSPPRECPY HISTIMESCW
DSDPRKRPSF LKLTSLLTHT NMAFN
//
