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Database: UniProt
Entry: A0A0N4TS37_BRUPA
LinkDB: A0A0N4TS37_BRUPA
Original site: A0A0N4TS37_BRUPA 
ID   A0A0N4TS37_BRUPA        Unreviewed;       384 AA.
AC   A0A0N4TS37;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   ORFNames=BPAG_LOCUS11456 {ECO:0000313|EMBL:VDN92642.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001149401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0001149401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN92642.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UZAD01013231; VDN92642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4TS37; -.
DR   STRING; 6280.A0A0N4TS37; -.
DR   WBParaSite; BPAG_0001149401-mRNA-1; BPAG_0001149401-mRNA-1; BPAG_0001149401.
DR   Proteomes; UP000038020; Unplaced.
DR   Proteomes; UP000278627; 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; cd00192; PTKc; 1.
DR   CDD; cd10361; SH2_Fps_family; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR035849; Fes/Fps/Fer_SH2.
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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF418; TYROSINE-PROTEIN KINASE FER; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PIRSF; PIRSF000654; Integrin-linked_kinase; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 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.
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   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW   ECO:0000256|RuleBase:RU362096};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278627};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
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          9..105
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          113..376
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   384 AA;  44178 MW;  C79D006B7E68E062 CRC64;
     MNENQTEKYY HGYLTVDDIQ PLLKNDGDFL IRKTNYKDIT TLSLDVCTNK GIKHFIINQD
     KKGEIYIEKN KKKSIAELIE WHLSTKTPIT ERSQIVLKKG ITRPSWLLKK EQIKMIKKLG
     EGAFGEVYCG EYKDANDHVH LAAIKTMHDK ASRRARFSFL KEARIMRKFD HPNIVRIFGI
     VADEAPLLIL MELCEGGSTL SFLRKNRGMI VPQLKMRFIT ETASGLKYLE QKNCIHRDIA
     ARNCLLTRNF HIKLSDFGMS DEKTPIQDKS LDKVPIKWLA PETMQNRIYS TKTDVWSYGI
     MIEMYSEGYE PYPSLSNIQT RAKIIIQNYR MDMPQSTPPA VATLVSKCWA KNPIDRPSFA
     KIYDELKNLS ADNPDITLSS GEGD
//
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