ID E0VY20_PEDHC Unreviewed; 1368 AA.
AC E0VY20;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=8232996 {ECO:0000313|EnsemblMetazoa:PHUM507390-PA};
GN ORFNames=Phum_PHUM507390 {ECO:0000313|EMBL:EEB18276.1};
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:EEB18276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB18276.1};
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:EEB18276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB18276.1};
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:PHUM507390-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM507390-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; AAZO01006175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235843; EEB18276.1; -; Genomic_DNA.
DR RefSeq; XP_002431014.1; XM_002430969.1.
DR STRING; 121224.E0VY20; -.
DR EnsemblMetazoa; PHUM507390-RA; PHUM507390-PA; PHUM507390.
DR GeneID; 8232996; -.
DR KEGG; phu:Phum_PHUM507390; -.
DR CTD; 8232996; -.
DR VEuPathDB; VectorBase:PHUM507390; -.
DR eggNOG; KOG0612; Eukaryota.
DR HOGENOM; CLU_000288_140_0_1; -.
DR InParanoid; E0VY20; -.
DR OMA; ERDKYNQ; -.
DR OrthoDB; 4221785at2759; -.
DR Proteomes; UP000009046; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR CDD; cd20813; C1_ROCK; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 1.
DR CDD; cd05596; STKc_ROCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.730; Single helix bin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF73; RHO-ASSOCIATED PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF103652; G protein-binding domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01206}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEB18276.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEB18276.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 78..340
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 341..411
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 944..1008
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1116..1322
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1233..1288
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1205..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 427..615
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 695..974
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1016..1096
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1368 AA; 157209 MW; 5C1215502D777C10 CRC64;
MEKIKDDDRK RRLLELEDKI QDPRSAVSID SLLDTVQALI SDCDHPCVKR MKNIEAYTNR
YDKLARDICN LRMKTDDYTL IKVIGRGSFG VVQLVRHNST QKVYAMKLLS KFEMIKRSDS
AFFWEERDIM AHANSEWIVQ LHFAFQDTQY LYMVMDYMPG GDLVNLMSNY DVPEKWAKFY
CAEVVLALDA IHSLGFVHRD VKPDNMLLDK YGHLKLADFG TCMRMGSDGL VRSDTAVGTP
DYISPEVLES QGGEGLYGRE CDWWSVGVVL YEMLVGDTPF YGDSLVETYS KIMDHKNSLS
FPQDIEISKA AKNLIYGFLT DRTQRLGRSG IDEIKAHPFF KNDQWNFDNL RETVPPVVPE
LSGDDDTSNF EDVEKEDAPE ESFPVPKAFA GNHLPFVGFT YSRDYQLLSG KDGYNSIGDT
VDLGLTKLNT SAQKNQLENE LEKEKKKVDE LCFKIQSLTT QLDAMKTRET EITEETSQLE
KSITLIKHNL KEAQRRADNE ADIRRKVEAL LAETKKKLED EQNKRTREMN NNQQTNDKMN
QLEKQVNELQ EKLKAESENA AKQRKLVGEL IVVKATSEQL QSELQGMLTG LQAQRDSLQK
EVATLQSQLS QERSSRTQAS DLTQELEGKL QGLLIDLDLS KEKEEKLSED NRLLVEKVSL
LEKEIAGITL ELKAAHSRYN QEVKAHQETE RSRLLTKEEA NLEAVKALQA KLNEEKSARQ
KADLHSQDKE RQMSMLSVDY RQIQQRLQKL EGEHRQEMEK VKALQANLEQ EQQKKTSLAT
ELGLTQSEVA GLKARETQLT GEISLLRQNK KLVEDELHKV KAQRSVDHLQ MKELQDQFEA
EQHFSTLYKM QAAETKEELE EKQRNVQELE EERGSLTHQL QLALARADSE ALARSVAEET
VAELEKEKTM KELELKDLLV KHRTDQSNKE QTLNVLKDRE SELKKQLDQM SKEREEMTRQ
LRHVQEDMKK RTNQDEEVER LNRVLKQEIV LKQQAVNKLA EIMNRKDMNL RAKPKIKVSS
ADLRRKERDC RKLQQELTQE REKYGQMAAK FQKEIQELQS QVIDESQMKV RLQMEVDSKD
SEIEQLQSRL ALLSSETASL SSGGAENEND DGYAQESRLE GWLSVPNKQN IRRHGWRKQY
VVVSSKKIIF YNSESDKQNT DPVLVLDLSK VFHVRPVTQG DVIRADAKDI PRIFQLLYAG
EGEARKPEEG GVQTLDHSTL RGEDKPGTAI VKGHEFVQIS YHMPTTCEVC PKPLWHMFRP
PPAVECRRCR IKVHKEHLDK KEDAIAPCKL HLDPTSAKDL LLLAHNSDDQ KAWVQRLSRK
IQKCGYKANN CVEGSKISPR ESTRSTMKPY NIQQRSSTLP ANSSANPK
//
