ID A0A158RA69_TAEAS Unreviewed; 946 AA.
AC A0A158RA69;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-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=TASK_LOCUS8579 {ECO:0000313|EMBL:VDK40587.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000857801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000857801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK40587.1, ECO:0000313|Proteomes:UP000282613}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYRS01018832; VDK40587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158RA69; -.
DR STRING; 60517.A0A158RA69; -.
DR WBParaSite; TASK_0000857801-mRNA-1; TASK_0000857801-mRNA-1; TASK_0000857801.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; 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 Gene3D; 3.30.505.10; SH2 domain; 2.
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:SF421; INACTIVE TYROSINE-PROTEIN KINASE WSCK-RELATED; 1.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
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; 2.
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:UP000282613};
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 28..120
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 216..306
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 654..919
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 946 AA; 104225 MW; 9A74FE0199492FC4 CRC64;
MARPGVGGGN SGRQSGESAG IPPHSVGYFH GKITRDQAEA ALFAHKALEG LFLLRESVHQ
NYAISICHGG RVHHYNIEKQ PDGSYQIRRK FPGPVELVKH HAVHLDGFLT LARFPLDRPT
GESPIVLQGV RSDELEEKLK LKAMEMGLKD IMNVVSIDPD VGSMLISSML GSVSKPDENR
IMGVKKGPSV TEALAGPMRD HLRYLVLRDL HFLQPWYHDC IRRRESERRL EENGGGNGSF
LVRYRKEDGA YVLSLMYEKE PRHYKIEQHL NRLSIEGGQY FETLIEMIDH YHFRQDGLLC
KLRKVVAAPD FIRTKQDSAS ISSESLEGSP SSLKKTDSSI NNSRNASHSL PSLASCPVNS
AASDNLGGGS PVPRKFCDGV MHASNDLISF NDWPNVTSLL ANQNANNNAT TNNNSNIGGG
GKLPQNSVNV KRMSAVPVGK FSRPTLPSLQ SVNLGCGDGF VHTPFTPVST EATPTPRPGT
VTSSPTSPFS RVRLKSTFTS TSVGTTVTTA TTPKTRGCLA VIVANAGRAP DFILFILPDP
SSSLVSINVE ALPPPPPHIL NPFIQRTASQ TSVGPQPCHH APDVSTFCNS ACCQQKHQLQ
QQQQKAEAIV VEKVEKEEVS STKPSSSVLP AIEEAQKIYD SLPYNTLFLQ PDSIRLMERL
GGGNFGQVVK AIYKTPQGQE VEVAVKTLRE SQIASTGEQT ILSEAKTMTQ LKHRHIVRLI
GVCKAQHFML VLELAPLGPI NKYLKKHPDT PVWVLSELMH QVAQGMAYLE ACKLVHRDLA
ARNVLLVTQR FAKVSDFGMS KALNFGNDYY RAASAGKWPL KWYAPECIYY FRFDSKSDVW
SYGITLWEVF SYGERPYKDM KGAQILAMLD QGLRLSRPVR CPEAIYSVMQ QCWNAEGVRR
PTFAELVLTM SRLAKGPLFP NNFSSCNENE RGASVSGESA GAFAFF
//