ID A0A1X7TN49_AMPQE Unreviewed; 1163 AA.
AC A0A1X7TN49;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:Aqu2.1.16391_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:Aqu2.1.16391_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; A0A1X7TN49; -.
DR STRING; 400682.A0A1X7TN49; -.
DR EnsemblMetazoa; Aqu2.1.16391_001; Aqu2.1.16391_001; Aqu2.1.16391.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; A0A1X7TN49; -.
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; PR00401; SH2DOMAIN.
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 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 51..125
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT DOMAIN 722..784
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 794..883
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 904..1163
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 1163 AA; 134411 MW; 6D131E442E5AE3F3 CRC64;
MEGGKRKENR REWKKEKRNE RRKKCVFTLS LDISKLNEIV QILKQYRFPE AKWFEFGLNL
GLLYPTLEAI DANHRGNTSR CLMECLSKWL SKADENVYPP TWQTLASALR KLEAKAVAEN
IEKTMVDPAS QLLQHYSSRI SGATLSEESV DLLHTEGLIS EETLREVKSY GYTLTDDAMR
EIYTAVAYDH NKLKSFASIL LRSTGTASIA NDLMRDSEDI FYRAENFPDE DITFVQAEDS
PFENCEEHNV STIKLSVEES KVILKEFEFQ ISENYNYHFE KMRGNFGSFY FKVTRLASLT
IRVNQLEDFI EFVDDCYPEL GPNLTSAATV KDVMKVIRTK CNVINIAPVE VAVSFNSEVE
TEAKPMVADY NAAVNEFCHN FKLQFFLDKK LSTSDFLICE TIEFVLDWDP AEHLLNDIRR
LMEKAFQGLS RRIIVKSMHK GNSIIIICGA PTHLMNALQL RARDNLTVLQ EEFALMRLKI
GHFKVYDRTI RNKELKIFAE EIEMCEGELA KINFYHNNKE SLLASQAVQL IPLKQKKEFI
SSSMQASDFK SKVKQIEREK AANTKRQILL RETEHLQSTL RIRISRKEVL QDNEKEIGEL
QENKEVKSTQ TVLSSNRYIC EAQDDYNYPA ISFKKGELLQ LSTNGHEVQS LETGQKSAVP
MKYIGYSRVE LLYLFQFAMT TRTGLSLLPG HFQLDDEEKA EYFILKIAYD STLLQSLRKL
VTKNKLFVAN YNFEGLSPHD LTLKEGEVLE VVKYDDDDGW WYMHSLDTDS KGYVPINYIA
PIKGKYSPMY YKYIYYHTVS RDEAEERLSQ ADTQAGTFLI RESISGPNTL SVKDGVTIRH
YHISIENNQY YINPRVKFDS LNDLVQHYMT EADSLPCSLT VPIPKQANTP IAKNKELEIN
KSHIKFEQCI NAGQFGETWK GDWKDKGPVI IKTNIATDIT QETLLVEAGI LQKLHHKNII
SLYGVCTESY PFYIVTEPMN ENLKYYLNKT LITPAELVDI AIQVTEGMIY LGEQDYIHCD
LRAENILVYI NIGDHNTVKI ANFHLIQHLN GKKYWTVKED TKVVLRWTAP EFFTLNRLSI
KSDVWSFGIL LWELATKGKE PYPDMATEEV KEAVSKGYHM PIPRDCPEPF KQLMPNCWKN
HEYKRPNFNN IIDILLKYKI SYL
//
