GenomeNet

Database: UniProt
Entry: E0VXY7_PEDHC
LinkDB: E0VXY7_PEDHC
Original site: E0VXY7_PEDHC 
ID   E0VXY7_PEDHC            Unreviewed;       751 AA.
AC   E0VXY7;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   Name=8232963 {ECO:0000313|EnsemblMetazoa:PHUM506570-PA};
GN   ORFNames=Phum_PHUM506570 {ECO:0000313|EMBL:EEB18243.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC   Pediculus.
OX   NCBI_TaxID=121224;
RN   [1] {ECO:0000313|EMBL:EEB18243.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18243.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB18243.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18243.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:PHUM506570-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM506570-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) to UniProtKB.
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; AAZO01006161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS235842; EEB18243.1; -; Genomic_DNA.
DR   RefSeq; XP_002430981.1; XM_002430936.1.
DR   AlphaFoldDB; E0VXY7; -.
DR   STRING; 121224.E0VXY7; -.
DR   EnsemblMetazoa; PHUM506570-RA; PHUM506570-PA; PHUM506570.
DR   GeneID; 8232963; -.
DR   KEGG; phu:Phum_PHUM506570; -.
DR   CTD; 8232963; -.
DR   VEuPathDB; VectorBase:PHUM506570; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   HOGENOM; CLU_000288_3_1_1; -.
DR   InParanoid; E0VXY7; -.
DR   OMA; RDPDYQN; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000009046; 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:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.30.505.10; SH2 domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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:SF372; TYROSINE-PROTEIN KINASE SHARK; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 2.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00252; SH2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
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; 2.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
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:UP000009046};
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          9..101
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REPEAT          148..180
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          181..205
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          216..248
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          284..375
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          475..739
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         507
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   751 AA;  85010 MW;  003F0B6FBD83B413 CRC64;
     MSREECISWF HGKLSRDDAE KLIQDLNSEG GFLVRESFAS PGDFVLTLLH NGDIVHYQIL
     RHGEDAFFSI DNEHIFHGLE TLINYHQENE NGLITKLTNF CKKDPPPHDT RCHGKTNLLH
     RATKEGNYTV VSELLKCGYR NTDAKSEDGQ TAAHLASRKG ADDILIKLIE TGANINCRDT
     AGYTPLHYAC QSNHLTTIRL LIQKGEAQVQ SRNANTGWVP LHEAAWRGLS EVIQLLLGLN
     APAHPRTLEG ETPLMLAQRK GFQDCVEILR KYKAPKPVLS KYNWYHGTLD RKEAVELLKE
     YGNKEGSYLV RYSHKNGGVY VLTMIVNDRS FHFQIKNENG YYFIDDGPLL ESLEHVIDYY
     SRMQDGLPTV LQIPVPPKPK PPVPEFPRHG LSATMPLKKK NHQRDVGNSL TVDAESNATT
     MTRRSSTPLI ISTGTGDKST NKKVVTNNCT QVPQVLLKGE EIVSEPPGCI QSCRLKLGNV
     LGEGEYGFVY KGTYQVDDFK TIDVAVKTLH NEHLPVNRCE FIREAKVMTS LNHHCVVKLI
     GLSQGPPLMM VQELVPLGSM LAYLIEFPDR VNPNYELKLW ASQIACGMKY LEEQRFVHRD
     LAARNILLSS RHQAKISDFG LSRVISSDSQ YYKATVGGRW PIKWYAPESF NFGTFSHASD
     VWSFGITLWE MFSFGQQPYG DMKGSEVIKR VEEGERLSKP ENCPEEVYKI MEQCWNFEPT
     MRPTFAQLLN IFSTDPEYIN IRELVIGSDI S
//
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