ID G7YWB9_CLOSI Unreviewed; 605 AA.
AC G7YWB9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN ORFNames=CLF_112394 {ECO:0000313|EMBL:GAA57249.1};
OS Clonorchis sinensis (Chinese liver fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA57249.1, ECO:0000313|Proteomes:UP000008909};
RN [1] {ECO:0000313|EMBL:GAA57249.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Henan {ECO:0000313|EMBL:GAA57249.1};
RX PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA Yu X.;
RT "The draft genome of the carcinogenic human liver fluke Clonorchis
RT sinensis.";
RL Genome Biol. 12:R107-R107(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Henan;
RA Wang X., Huang Y., Chen W., Liu H., Guo L., Chen Y., Luo F., Zhou W.,
RA Sun J., Mao Q., Liang P., Zhou C., Tian Y., Men J., Lv X., Huang L.,
RA Zhou J., Hu Y., Li R., Zhang F., Lei H., Li X., Hu X., Liang C., Xu J.,
RA Wu Z., Yu X.;
RT "The genome and transcriptome sequence of Clonorchis sinensis provide
RT insights into the carcinogenic liver fluke.";
RL Submitted (OCT-2011) 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; DF144618; GAA57249.1; -; Genomic_DNA.
DR AlphaFoldDB; G7YWB9; -.
DR Proteomes; UP000008909; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd05034; PTKc_Src_like; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF447; TYROSINE-PROTEIN KINASE SRC64B; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096};
KW Reference proteome {ECO:0000313|Proteomes:UP000008909};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|RuleBase:RU362096}.
FT TRANSMEM 15..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..161
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 186..441
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 549..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 605 AA; 68480 MW; 1A99DB8998461893 CRC64;
MNIFQSNEAY TYSEFLVFSL FALWGQVTGP GFSYLIITII IVRCYLKMKV YILAVIRQSP
TSWYFRSISR KDSERLLLLK GNIRGTFLIR ASETTTGALS LSVRDTESQR GETVKHYKIK
QLSDTGQVCI TTKQVFSDLK ALVTHYSVNA DGLCCCLTRP CPRPPPLPTD LSRSTRDHWE
IPRSSLVLLE QLGAGQFGEV WKGRWNGSMD VAIKTLKPGT MSKEDFLKEA RIMKRLHHPK
LVRLYAVVTA DPIYIVTELM SLGSLLHYLR DGPGRNLELK LLIDMVAQIA SGMAHLEKER
YIHRDLAARN VLVSENNTVK VADFGLARII DTASETYTAK QGAQFPIKWT APEAALLGRF
TVKSDVWSFG IVIYEIITHG QTPYPSMNNT QTLQQVESGY RMPRPPSCPD PVYQVMLRTW
DTIPDKRPTF DSLCTYFEDY FSNAERTYKP TDQKQYQHNQ KDDDTVEWTA AVVSIGNHPN
SKRRASQRSQ CIGQDKQSAK EGIRLLLGNA TKRSACFYIA REPTLDGVRL ACTFQSHLRE
NLPLTQPCRK LEDQTAGPTQ LRTDEASSYG DETFASQLPS SASRSTTAGR LETNWEWENT
NRGLH
//
