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Database: UniProt
Entry: A0A3B4B4C0_9GOBI
LinkDB: A0A3B4B4C0_9GOBI
Original site: A0A3B4B4C0_9GOBI 
ID   A0A3B4B4C0_9GOBI        Unreviewed;       506 AA.
AC   A0A3B4B4C0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000023449.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000023449.1}
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   AlphaFoldDB; A0A3B4B4C0; -.
DR   STRING; 409849.ENSPMGP00000023449; -.
DR   Ensembl; ENSPMGT00000024982.1; ENSPMGP00000023449.1; ENSPMGG00000018966.1.
DR   Proteomes; UP000261520; Unplaced.
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; cd00173; SH2; 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:SF265; PROTEIN-TYROSINE KINASE 6; 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|PROSITE-ProRule:PRU10141,
KW   ECO:0000256|RuleBase:RU362096};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; 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          60..124
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          130..222
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          244..500
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          22..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         272
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   506 AA;  57941 MW;  2470A57FB2F23D2F CRC64;
     MDECIHRCCP CLVTLWNRIR GEKPHDGPGS HRDSGGSDTS APRVIPTPDK TTQRSSRDTS
     SEAIYVAMWP FEARSEDEMS FDKGDLFDVL SRNGDWWKAR RIDKNGRVLG TGIVPSNYLE
     RAETEAKEVW YFGTMNRFEA QGHLMSSENQ SGAFLIRQSD RESVGYVLSV RSDTRVKHFK
     VIKDNSNQFH IEPSTHFPTL IDLVEHYKNY NLTNAGLLGK PCKRKKPKPT EMDLKEWELP
     KSEFTLEEEL GSGYFSDVYK GRWKSHISVA IKIIKNSELN HQEFIREVEI LKRLRHRHLI
     SLFAVCTESP PYYIVTELME KGSLLEFLRG PEGQHQDTVT LVDMGAQVAD GMSYLEENNC
     IHRDLAARNV LVGEGHICKV ADFGLGRLIK EPFYVSEEKK IPYKWTAPEA ISHGKFSSKS
     DVWSFGVLLY EIITCGGNPY PGQTLSIQEV FEEVSRGYRM PRPSKCPEFL YKIMMDCWNA
     EPASRPTFRS IKDKLCNSKY SKVYCS
//
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