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Database: UniProt
Entry: A0A068YHF8_ECHMU
LinkDB: A0A068YHF8_ECHMU
Original site: A0A068YHF8_ECHMU 
ID   A0A068YHF8_ECHMU        Unreviewed;       723 AA.
AC   A0A068YHF8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 53.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   ORFNames=EmuJ_000932000 {ECO:0000313|EMBL:CDS41651.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS41651.1};
RN   [1] {ECO:0000313|EMBL:CDS41651.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA   Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA   Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA   De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA   Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA   Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA   Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA   Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA   Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA   Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA   Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA   Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA   Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT   "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL   Nature 496:57-63(2013).
RN   [2] {ECO:0000313|EMBL:CDS41651.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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}.
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DR   EMBL; LN902846; CDS41651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068YHF8; -.
DR   STRING; 6211.A0A068YHF8; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   OMA; PGHNTRR; -.
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; cd11845; SH3_Src_like; 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; 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; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF447; TYROSINE-PROTEIN KINASE SRC64B; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-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.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; 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          209..270
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          276..374
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          399..654
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          142..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         427
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   723 AA;  80449 MW;  B0ACC6EF3E218C88 CRC64;
     MGNCGTHSSA VDEVEEAKRY PELSLEQLDH LSLDLQNNLV KYGTKYLGQC KPSLHGAATD
     PSFDQISNAD MPCDAPSARS TTPSSGIRPK IYVKCPSLDE SRAHLSSSPI SYGGGGSISS
     ERRHQLEQRP NSVSHLLRYG LNHVNNNSSN HSPSANSCCL PNEQRNPRPS PTVKQTQHCV
     SSNTEKYSQK LTPKPVHQKY LVHHSLGKNS SKYFVAIFDY KARCEGDLTV HKGDAVVMLD
     RSDTDWWLVE NATSHQHGYV PSAYLAEENS IEVFEWYFRE ISRKDSERLL VQQGNPTGTF
     LVRPSETTRG GLSLSVRDYD PSVGAVVCHF KIKHHPPSGG ICITSTLVFP NLVDLINHYT
     SHADGLCCRL TQPYPRPPPF LSDLSRRTKD DWEIPRSSLV LQERLGAGQF GEVWRGEWKG
     ATPVAIKTLK EGTMTKEDFL KEARIMKTLS HPHLVRLFAV VTTEPIYIVT ELMPNGSLLA
     FLRSDVDKTL GLKELVDFMS QIATGMAYLE EKCLVHRDLA ARNVLVGDNN IVKIADFGLT
     RAIDTTTEAY TAKQGAKFPI KWTAPEAAYR GQFTIKSDVW SFGVVMYEII THGQEPFPSM
     STMETLDQVN NGYRMPCPQN CPAAIYEVML HTWDATPDLR PTFVLLCDFF ETFVVADPHP
     IEPEVATIDS RTGALASEPC KRRPGHDQLS CLPPIIRGLS GILAGSLSPA LCWRDLLIIM
     VLK
//
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