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Database: UniProt
Entry: A0A3B5AK26_9TELE
LinkDB: A0A3B5AK26_9TELE
Original site: A0A3B5AK26_9TELE 
ID   A0A3B5AK26_9TELE        Unreviewed;       637 AA.
AC   A0A3B5AK26;
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};
GN   Name=BTK {ECO:0000313|Ensembl:ENSSPAP00000013862.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000013862.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000013862.1}
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR   AlphaFoldDB; A0A3B5AK26; -.
DR   STRING; 144197.ENSSPAP00000013862; -.
DR   Ensembl; ENSSPAT00000014095.1; ENSSPAP00000013862.1; ENSSPAG00000010436.1.
DR   GeneTree; ENSGT00940000158469; -.
DR   Proteomes; UP000261400; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01238; PH_Btk; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; 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; 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   InterPro; IPR001562; Znf_Btk_motif.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF92; TYROSINE-PROTEIN KINASE BTK; 1.
DR   Pfam; PF00779; BTK; 1.
DR   Pfam; PF00169; PH; 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; SM00107; BTK; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS51113; ZF_BTK; 1.
PE   3: Inferred from homology;
KW   Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW   ECO:0000256|RuleBase:RU362096}; Immunity {ECO:0000256|ARBA:ARBA00023130};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   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}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00432}.
FT   DOMAIN          4..118
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          192..252
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          259..355
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          379..633
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          159..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..189
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         407
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   637 AA;  73713 MW;  AB044087C0183230 CRC64;
     MSENILEEIF IKRSQQKKKT SPLNYKERWF ILTQEKIAYY DFDSDKQKRK SLRGSVDIEK
     IKCVETVQPE PNTPQERMYR GLKQCFSLVI YDEGPLYIFA KTEEIRAQWI KKLKELVRFN
     KDLMQKYHPC FWVDGAWLCC QQEVKQAMGC KVLDRFTSKE SRRRGSRKPL PPTPTEPGRP
     LPPQPAEPQG PTVGMTVIAE YNYPPMTAQD LELRKDEEYT ILEICDANWW RARDKHGQEG
     YIPSNYVVEA DNGLEKYDWY CKNMNRSQAE QLLKSENKDG GFLVRESSKA GKYTVSLHTK
     GGGETSGSCK HYNICTTPKG QFYLAEKHNF NTIAELINYH QHNAAGMVCR LKHIVSNRAR
     PPSTAGLGYG VWEIDPRYLT FIKELGTGQF GVVKYGKWQG KHDVAIKMIK EGSMSEDDFI
     EEAKIMMKLR HENLVQLYGV CTKQRPIYIV TEFLSNGCLL TYLKEGLTQH PTAVQLLEMC
     KDVSEGMAYL ESQQYIHRDL AARNCLVDGN GTVKVTDFGL SRYVLDDEYK SSAGSKFPVR
     WSPPEVLLYC KFSSKSDIWA YGVLMWEVYS LGKLPYERLN NTEMVEQVSR GLRLYRPQLA
     NEKVYSIMLN CWQDKAEERP TFQELVLTVQ DLLYELQ
//
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