ID A0A0V0ZNU6_9BILA Unreviewed; 1142 AA.
AC A0A0V0ZNU6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:KRY14219.1};
GN ORFNames=T12_2953 {ECO:0000313|EMBL:KRY14219.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY14219.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY14219.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY14219.1};
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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:KRY14219.1}.
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DR EMBL; JYDQ01000121; KRY14219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZNU6; -.
DR Proteomes; UP000054783; 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; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
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; PF06602; Myotub-related; 2.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 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:UP000054783};
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..180
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 205..458
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 638..1021
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 1068..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY14219.1"
SQ SEQUENCE 1142 AA; 130280 MW; 13E371C7423F7CD9 CRC64;
LKFSIINLPA WKCSSRTMID VEPVSTSSDW PSVAKLVRLY LDYCTKVENV PTVDNKNTAC
SVPRDPVNRL LPVVKRVKTM HSGEETSDSP WFHGSISREE TNRLLTHKPD GTFLIRESTN
YPGDFTLCIA FNGKVEHYRI FHQNNMLTCD HEGFFQSLQL LVAHYTRGAD GLCHKLVEAL
LVDDGDQRRL TKLNESNWIV RKEHLQLLDV IGHGEFGDVM GGLFKGKKVA VKVMKRGNHV
IESLLQEASM MMTLKHQNLV ELLGVVLNDG TDVYLVTEFM PNGSLLDYVR SRGRQMVTQS
QQLNFAFDIC CGMVYLEKKN LVHRDLAARN ILLSEDMVAK VADFGLAKSV DSIDAEDANC
RFPIKWTAPE ALCHNKFTGK SDVWSFGILL WEIYSFGRVP YPRIPVQEVV RYIKNGYRME
PPEGCPSDIA ELMSQTWTIK AECRPNFQQI LKALQLMLQN IQRGMNSLNS SRAESFKSYV
EQEEDSSNGN PSLNLISGEQ EVTTPCENVI LYFPFSDSRQ GIIGNVHCTF FRLIFLPATE
MNNQRSYFRT QRIFGNSNFE TALLNVYRLE HSSNADPKKF RHLVNFLSFA DDIHTLKIYC
KFVNCLLQYS FPMSLENLPC FHLRHPTNWK RKLKKCSFDC REDWQCELQR CGTGGGHSWR
ITQINENNRL IRSYSCCFVV PSSWYDNMIE TSVSNWKERR VPFWCWSHLN GSSLVRTSSM
TTDTEVTRKQ WLLFEAAVGE SHAKKKQPVV IDVSLSVRDV ANAYDALRKI CSIDNSTEFW
AIDSRWYSEV ESTGWLFLVQ KCLSQVHCCV ETISIFGSSV ILREKLNQDG CCVIASLVQI
CCDPFYRTID GFEMLIRKEW LAFAHPFASR LHGLTSAGRS DEELAPFFLL FLDCVFQLLV
QYPTDFQFTE HYLIAMWDLC LTGLVVSFST NCLRDRIDHH HFDDHTDYWT EFYHDDYRQF
FKNSCYLFAK SRLAENYSSS LSAGSSSAGI LSPSSSPSLS SSSTLLPESQ PFVLNFWQMA
FLRWSAPAQV ANGGDIQLTL HVNSLNAHLL KLLQEKIRLE IGANTTTRSD ATSGTFLATT
TTSNRNDDKA GSDSSLSCAD LSNLRITSAF PFTYETLPIP DYLYILPIRQ QPKASRHTGK
QQ
//
