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Database: UniProt
Entry: A0A0N5BS11_STREA
LinkDB: A0A0N5BS11_STREA
Original site: A0A0N5BS11_STREA 
ID   A0A0N5BS11_STREA        Unreviewed;       449 AA.
AC   A0A0N5BS11;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000865700.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0000865700.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-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; A0A0N5BS11; -.
DR   STRING; 174720.A0A0N5BS11; -.
DR   WBParaSite; SPAL_0000865700.1; SPAL_0000865700.1; SPAL_0000865700.
DR   Proteomes; UP000046392; 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; 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:SF425; TYROSINE-PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
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   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          38..141
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          153..414
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          427..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   449 AA;  51589 MW;  9B2E8760A24E1D86 CRC64;
     MVKQNKTSNT NKSFEEKNGT IIVSINDPVI NELIKQPYYH GFLPREDINK MLKKCGDFLV
     RLSEPVPGKE RAYILSVRIK PQKGSVTITR CLNHFVIKKT PDNRYQISKA AFKSVVELIN
     HYSESKKSVS CGNDILLKNP VGKQPWEFCH SQIKVTKKLG EGAFAEVHLG TYDENLSGRT
     KNVAIKLAKL EKLTKDQIKE IMKEARLMRK FDHPNVVRLF GIAAGQEPLM LIMELCTNGA
     LDKYLQKNTL DIDRKMNMCC GAAFGIEYLH SLKIIHRDIA ARNCLYGGDG QVKISDFGMS
     VEGTQYKMDP KCRVPVKWCS PETIVSKVYY TESDVYAYGI MVWEIFNNGT EPYSSFSNYE
     FIIKVIKEDY RMSFPDEMPK NFKECILKRC WEKNPKERAS MSEVVECLQR ETGICRYEAQ
     KEQLIDDIES KSTHEQRPNN TVDKTFELS
//
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