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Database: UniProt
Entry: A0A0R3X1V5_HYDTA
LinkDB: A0A0R3X1V5_HYDTA
Original site: A0A0R3X1V5_HYDTA 
ID   A0A0R3X1V5_HYDTA        Unreviewed;       532 AA.
AC   A0A0R3X1V5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   ORFNames=TTAC_LOCUS7205 {ECO:0000313|EMBL:VDM31547.1};
OS   Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX   NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000722001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TTAC_0000722001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM31547.1, ECO:0000313|Proteomes:UP000274429}
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|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; UYWX01020353; VDM31547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3X1V5; -.
DR   STRING; 6205.A0A0R3X1V5; -.
DR   WBParaSite; TTAC_0000722001-mRNA-1; TTAC_0000722001-mRNA-1; TTAC_0000722001.
DR   Proteomes; UP000046396; Unplaced.
DR   Proteomes; UP000274429; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00173; SH2; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR24418:SF294; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362096};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362096};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274429};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
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          69..132
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          126..234
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          254..511
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          13..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  60263 MW;  3C244F076C2F036D CRC64;
     MVYGSMGHFL RKLKRKKSGD RAAEGGYVPP KPAHPWQRRR RQEEKLDNEK KEQVTLTKIN
     PWFQLCSNLQ NQTAMALFSF SGDIQNGELE ALEGDSLTIE SVDRSDVWWQ AVNKRTGKSG
     FIPYNYVTEE IGVKDVIDAW QETDRRESEA KLSMPGLSNG TYILRPSSNP LRIALSVLCL
     VGTTKIIKHF SVRYDQTLSG YSITPGKKFA HLKDLTDYYK VSHNGNAPLL SSSMPHSPPV
     IQSRSSRIPL EKVELKTHIA RGGRFGSVYK AVYTVSGKQN VVAKKISSHI GRDAIVARAE
     ACHKLQNRAI VHFLGFCEAP KSGLMLLLWE YMPGDASKWL YGTNFLVTVA FPRILDGMDY
     LESVETFHGE LTTSNVFLSS ELCAKIGNFG FNGRFSESRS NALDFVMTQA VRWAAPESLD
     TSHFYDIRCD VWSFGIVMFE VFTFGLTPYK DMDVEEVVDR VRAGYRLPNP SSLGFYCEDV
     MYETMRNCWY ADSTDRPTFH ELWFVFEDHL VKDGGAYAEL KSAPSTYDPP YF
//
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