ID A0A087VXK3_ECHMU Unreviewed; 798 AA.
AC A0A087VXK3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Protein tyrosine kinase {ECO:0000313|EMBL:CDI96880.1};
GN ORFNames=EmuJ_000060700 {ECO:0000313|EMBL:CDI96880.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDI96880.1};
RN [1] {ECO:0000313|EMBL:CDI96880.1}
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:CDI96880.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN902843; CDI96880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087VXK3; -.
DR STRING; 6211.A0A087VXK3; -.
DR eggNOG; KOG4257; Eukaryota.
DR OMA; RHYLMER; -.
DR GO; GO:0005925; C:focal adhesion; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR049385; FAK1-like_FERM_C.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418:SF367; INACTIVE TYROSINE-PROTEIN KINASE KIN-32; 1.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR Pfam; PF21477; FERM_C_FAK1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF68993; FAT domain of focal adhesion kinase; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:CDI96880.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transferase {ECO:0000313|EMBL:CDI96880.1}.
FT DOMAIN 348..606
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 621..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 798 AA; 90529 MW; 74C87AF27122BD2F CRC64;
MDQSISDIVT VSTLLGYVKI KCSQSTSVDE ITKIAIKKVS ISNNLLMFGL ELRESLSSIG
DRLFLCPYLT WSEIVGLVNE QNILLSIRLF PTNFEDYMRK DRSTLHYLHD QVYSQSCFEI
GCLDIKLSFD CEITEEVLDQ LDKSGGFSTF FPSHVLHRQK AKYLRRDILN YASNLYYYSK
EDCMLEHLNR LLMLTQFDSD SYACYLGAGL GIPIRLLLGP RSQVRVNIKN TDEVRLLCYF
ASIQQIIFSE ISRKEGRRYQ VKLVLSNDPD AEQPIIFTFD SKLTADTVLH TLEGYCKLSP
DMQTNSAAAE HGPLLLNGCP FRPLMDLSAC DQYGKCSQIH QYLLRSHITL ERVLGEGQFG
DVYKGTYRPP EAGFSTILVA VKACKVGLGS EEKQRWLEEA DLHAKLTHPH IIKLYGVCRD
EPVWLVLEFA GEGELRHYLM ERQSRIALST LVTFCHQLSS ALAYLEALKI IHRDVAARNV
LVANDTCVKL ADFGMARQLI QGEDFYVAEQ GGKVPIKWMA PESLKSRIFS SASDVWMFGV
CMWEILSFGL KPFHNTSNAE AVAAIGRGER LARPETCLVS HYRLMLECWM DDPLLRPTFN
TLQPKLRDIL SEAKRLSAEA SNNHVQRKLS SDRNELSKPP IFSEQSATGK PINDAFPTLS
RPATSEADTA VHRAVYCVMQ LILTVAKKPA FSSMKQLLSS VKKIGEQIRT LFVIIQQTVE
EVDDVSLIDS AERQLTDSYH YLVEDVRKLR DLHAKGDVKD ELYRRFLGQA FVVATDTRAL
FQSFQQCRQA HFLLTAHH
//
