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Database: UniProt
Entry: A0A0V1L4T2_9BILA
LinkDB: A0A0V1L4T2_9BILA
Original site: A0A0V1L4T2_9BILA 
ID   A0A0V1L4T2_9BILA        Unreviewed;       478 AA.
AC   A0A0V1L4T2;
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=CSK {ECO:0000313|EMBL:KRZ54527.1};
GN   ORFNames=T02_8095 {ECO:0000313|EMBL:KRZ54527.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ54527.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ54527.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ54527.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-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:KRZ54527.1}.
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DR   EMBL; JYDW01000136; KRZ54527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1L4T2; -.
DR   STRING; 6335.A0A0V1L4T2; -.
DR   Proteomes; UP000054721; 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; cd09937; SH2_csk_like; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR035027; Csk-like_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:SF440; 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   Reference proteome {ECO:0000313|Proteomes:UP000054721};
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          91..195
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          220..473
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         478
FT                   /evidence="ECO:0000313|EMBL:KRZ54527.1"
SQ   SEQUENCE   478 AA;  54266 MW;  52F2D5F56161183E CRC64;
     LKFSIINLPA WKCSSRTMID VEPVSTSSDW PSVAKLVRLY LDYCTKVENV PTVDNKNTAC
     SVPRDPVNRL LPVVKSVKTM HSGEETSDSP WFHGSISREE TNRLLTHKPD GTFLIRESTN
     YPGDFTLCIA FNGKVEHYRL MQCLLDKFVN KSNIIFHQNN MLTCDHEGFF QSLQLLVAHY
     TRGADGLCHK LVEALLVDDG DQRRLTKLNE SNWIVRKEHL QLLDVIGHGE FGDVMGGLFK
     GKKVAVKVMK RGNHVIESLL QEASMMMTLK HQNLVELLGV VLNDGTDVYL VTEFMPNGSL
     LDYVRSRGRQ MVTQSQQLNF AFDICCGMVY LEKKNLVHRD LAARNILLSE DMVAKVADFG
     LAKSVDSIDA EDANCRFPIK WTAPEALCHN KFTGKSDVWS FGILLWEIYS FGRVPYPRIP
     VQEVVRYIKN GYRMEPPEGC PSDIAELMSQ TWTIKAECRP NFQQILKALQ LMLQKLNG
//
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