ID A0A1X7TNW2_AMPQE Unreviewed; 1147 AA.
AC A0A1X7TNW2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.16392_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:Aqu2.1.16392_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=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001149,
CC ECO:0000256|RuleBase:RU362096};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR AlphaFoldDB; A0A1X7TNW2; -.
DR STRING; 400682.A0A1X7TNW2; -.
DR EnsemblMetazoa; Aqu2.1.16392_001; Aqu2.1.16392_001; Aqu2.1.16392.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; A0A1X7TNW2; -.
DR Proteomes; UP000007879; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0031349; P:positive regulation of defense response; IEA:UniProt.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IEA:UniProt.
DR GO; GO:0032103; P:positive regulation of response to external stimulus; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01670; Death; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR24418:SF294; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362096};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362096};
KW Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|RuleBase:RU362096}.
FT DOMAIN 34..108
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT DOMAIN 710..773
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 783..872
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 893..1147
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT COILED 518..545
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1147 AA; 131656 MW; AAA8B5B8FA708969 CRC64;
MASSKLPRML PVVLDIGNLN EIVQILKQYR FPEAKWFEFG LNLGLLYPTL EAIDANHRGN
TSRCLMECLS KWLSKADENV YPPTWQTLAS ALRKLEAKAV AENIEKTMAS QLLQHYSSRI
SGATLSEESI DLLHTEGLIS EETLREVKSC GYTLTDDVMR EIYTTVAYDH NKLKSFVRIL
LTTGTVSIAN DLMRDCEEIF YMAESSPDEI TFVTEGSPGD VSSIEPISVE ESNDRPKEFE
FQVSEDYNYQ FDKMRGNFGT FYFKVTRLVS HTIRVNQLED FIEFLDDCYP ELNPDLTSAA
TVKDVMKVIK TKCNVINIAP VEVAVSFNSE VETEAKPLVA DYNAAVTEFC HTFKLQFLLD
KKLSTSDFLI CETIEFVLDW DPAEHLLNDI RRLMEKAFKG LSRRIIVKSM YKGNSIIIIC
GAPTHLMNAL QLRARDNLTV LQEKFALMRL KIGHCTVYDR TIRNKELKIV TEETEMCEEE
SVKMNLYHND KENLLASQVA QLLTLKQKQE FINSSMQASD FKSKIKQIER EKAASTKKRM
LLSENEHLQS TLRIRISRKE VLQDNKKEIG KLQESISSIS VQMLKMRPSD NKEVKSTQTV
LSFSGSICVA QDDYSETTIS FKKGELLQLS TNGHEVQSLE TGQKSAVPMK YIGYSRVELL
YLFQFVMTTG TGLSLLPGHF QLDDEEKAEY FILKITKDRT LLQSLRESIT KYKLFKASYN
FEAQTSDNLT LKKGEVVKVV KYHEDDERWW YMHSLHTDEE GYVPINYITP IEGKCSLMSY
KYIYYHTVSR DEAEERLSQA NTQSGTFLIR ESISGMNTLS VKDEVTIRHY HIYIENNKYY
MNPRVKFVSL NDLVHHYMMK ADGLTCSLTV PIPKQVNIPI AMNKELEINE LDIEFEQCIN
AGQFGETWKG NCKGKGPVII KTNIATNITQ ETFIKEAYVL LKLYHKNIIS LYGVCTEDYP
FYIVTEPMNE NLKDYLTTNN PTPAELVDIA IQVTDGMIYL GEQDYIHCDL RAINILLGDR
NTVKIANFHL AQHLNSNKYW IVKEGTTLAF KWTAPECHTS KQLSIKSDVW SFGILLWELA
TKGKIPYPGM TNAQVQESVS RGYHMPIPQD CTEPFKQLMI NCWKRSEDKR PSFKKILVYL
SHTHDTE
//
