ID A0A0V1GUR0_9BILA Unreviewed; 894 AA.
AC A0A0V1GUR0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
DE Flags: Fragment;
GN Name=V-FPS {ECO:0000313|EMBL:KRZ01968.1};
GN ORFNames=T11_5925 {ECO:0000313|EMBL:KRZ01968.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ01968.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ01968.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ01968.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ01968.1}.
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DR EMBL; JYDP01000250; KRZ01968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1GUR0; -.
DR STRING; 268475.A0A0V1GUR0; -.
DR Proteomes; UP000055024; 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; cd10361; SH2_Fps_family; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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:SF294; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 2.
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:UP000055024};
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 89..184
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 197..456
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 527..618
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 635..894
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 894
FT /evidence="ECO:0000313|EMBL:KRZ01968.1"
SQ SEQUENCE 894 AA; 102937 MW; C0C3317EF35CF5B7 CRC64;
MKDQKNNNEE EYVRCRYDKG DEDTYYEAEN HFNVDNPWTP ETSIYENQPS ETGAVDEITE
NDCSDLTVYR TKRNPIREFY QKVLCNERFF HGYLPLQDAR ELLKYKPRGH FVVHTTNECG
FLNPVVLSVK HYSEVVHHVL NVGVMGKCFT TNRMFDSVSH IIAHYVQSGE YIDDRINFRL
ITAANFCDWQ IRTENVLTIK QDIGKGCFSN VSFGFHVDKG KFIEAAIKCP KEVAEVDTVG
MMYTEHRLLQ QLDCPYIIKP FGITVFAEIP MMVMEYANGG SLENYLKKNT VKIKRKMKFC
LQIASALQYL KRKELIHRDI AARNCLVFKG SDKITAKLSD FNLCKEIYEE EERSPCISLR
WSAPESLGDN LWSYESDLWM FGVLMWEIFT NALYPHNKDS FENTEEFRSY LMEGNTLEML
PEIPAAIQTI ILQLHSINPA KRGNVATVLK ELKALLSIDD TCLLLRIQSN MDKPVARVKP
MRKDQPAQTE VVDALTGNGC SHLTPCRSKA HNQMREFYRK QLANESYFHG YMTEKDAREI
LKYKPNGWFL VHTTNERGVL KPVVLSVKYN GEVVHHVLNV GLLGKCFGRI RVFDSVPEMI
AHHMQSGEFI DDKIKFQLTT AANFSDWQIK TEKAVIIRED IAQGSFSNVS FGFYIHNSKY
NEAAIKCPID VPWVDTVGMM YTEHRLLQQL DCPYIVKPFG ITVFTEVPMM VMEYASGGSL
DNCLKRSSFK VNRKIEFCFQ IASALQYLKR KKLIHRDIAA RNCLLFRGFE KLTVKLSDFN
LCKAESEVEK DLPSIPLHWS APESLGASLW SYESDLWMFG VLMWEIFTNA LHPHDNVDIE
DTEEFCTYLM EGNTLEMLPE IPAAIQTIIL QLHSINPAKR GNVATVLKEL KALL
//
