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Database: UniProt
Entry: A0A096LTJ9_POEFO
LinkDB: A0A096LTJ9_POEFO
Original site: A0A096LTJ9_POEFO 
ID   A0A096LTJ9_POEFO        Unreviewed;       544 AA.
AC   A0A096LTJ9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   Name=SRC {ECO:0000313|Ensembl:ENSPFOP00000022490.1};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000022490.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000022490.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   EMBL; AYCK01002358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007546916.1; XM_007546854.2.
DR   AlphaFoldDB; A0A096LTJ9; -.
DR   Ensembl; ENSPFOT00000021964.1; ENSPFOP00000022490.1; ENSPFOG00000013135.2.
DR   GeneID; 103134564; -.
DR   GeneTree; ENSGT00940000158250; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   CDD; cd05071; PTKc_Src; 1.
DR   CDD; cd10365; SH2_Src_Src; 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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
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   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418:SF53; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC; 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   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000028760};
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          92..153
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          159..256
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          278..531
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         306
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   544 AA;  60946 MW;  1507C84CA266B40A CRC64;
     MGAGKSKPKE PGQRSMSLDG TIGTGSDSGH FHHLGPSQQT QTPNRSPAVG TGRPRYQGQH
     QHAPTNTPEL SLFGGVDHTG TVTSPQRGPL SGGVTTFVAL YDYESRTVSD LTFRKGDRLQ
     IVNNTEGDWW LARSLTTGES GYIPSNYVAP SDSIQAEEWY FGKITRRDSE RLLLNPQNRR
     GTFLVRESET TKGAYCLSVL DYDNTKGLNV KHYKIRKLDS GGFYITSRTQ FTSLQQLVFH
     YRKHSDGLCH ALTDVCPVAK PQTQGLARDA WEIPRESLRL DVKLGQGCFG EVWMGTWNGT
     TRVAIKTLKP GTMSPEAFLQ EAQVMKKLRH EKLVQLYAVV SEEPIYIVTE YMSQGSLLDF
     LKGDAGKMLR LPQLVDMAAQ IAAGMAYVER MNYVHRDLRA ANILVGDNLV CKVADFGLAR
     LIEDNEYTAR QGAKFPIKWT APEAALYGRF TIKSDVWSFG VLLTELATKG RVPYPGMVNR
     EVLDQVERGY RMPCPAECPT SLHDLMLSCW RKDPEERPTF EYLQGFLEDY FTSTEPQYQP
     GENL
//
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