ID A0A132AEK6_SARSC Unreviewed; 1343 AA.
AC A0A132AEK6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=QR98_0079510 {ECO:0000313|EMBL:KPM09416.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM09416.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM09416.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM09416.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM09416.1}.
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DR EMBL; JXLN01013526; KPM09416.1; -; Genomic_DNA.
DR VEuPathDB; VectorBase:SSCA006798; -.
DR OMA; ERDKYNQ; -.
DR OrthoDB; 4221785at2759; -.
DR Proteomes; UP000616769; 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 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; 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; PF08912; Rho_Binding; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 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};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPM09416.1};
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};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
SQ SEQUENCE 1343 AA; 155959 MW; C971E380781F38A0 CRC64;
MAEEKLSKHS TAIIHTDEGV DNQCDDIIDE NRDQRLAKLE ECLLDPKSDL NLDGLLDCVQ
ALVTDFNHSS LRRIKNIDLF LQKYEKYYDL IVNCRMKPDD FDVLKTIGSG AFGEVKLVRQ
KFTKKIYAMK ILSKFEMIKR SDSYFSEEKF IMAHANSEWI VKLHFAFQTT THLFMVMDYM
PGGDLVNLMS KYDIPEKWAK FYCAEVILAL EAIHSMGFVH RDVKPDNMLL DHRGHLKLAD
FGTCMRMDDN GLVHSDTAVG TPDYISPEVL KSQSDRECYG RECDYWSVGV FLYEMLIGDT
PFYAESLVGT YGKIMDHKNH LHFPDDVEIS KEAQNLICAL LTDRQVRLGR KGISEVSVHA
FFQNEQWNFE NIQNCIAPVI PDPSDDDDFN FNANRNDLRK EKEHFPEPRA FAGNHIPFIG
FTYSGDQKLL SRKFHHHSHH HSSNVQSVLI GDDEIDISNK MTLLEKEKLK IVESNEELDH
KFRISMMEIE KHKETIDSLH NEKAYLEKHL NTLRQNLIQV QANLNQERES KQLVDQTLIE
FKKKFETEKK QWIRTQFSLT EKSTKLGKKI NLLTEMLQKE KDNCSRETMK ISELHSTIRN
QEIMIEEFKN KVSMFEKISE CKEKDIAAMR EELNKASISL NNYKNKIKQL ETLRLMLEKE
IFERQQLETI VRAKDQEIDG LRIDRTQLQQ QVESLEKDRS FIEIETNEER ESVNKQYRDD
DLDLIEMKHL VEKLEIADVE NQNSKRQYDE AQKIVKKLNI DLNELKIRFE TEHCFSEIYK
NQLNEISEEL NEKVNEINKL NREKQDTLQE IEHLKNKLKS HINVECTAQE RVSALENEKL
ELEMELSEMK KQISLTKKEY ENIVEALRNH ENELCRNVEM MKKENTELDM KLASISKDID
NLNQLKKETE TLTKQFQQEK LLKEQAVNKL AEIMNRRDMN FNDKKAKSSI VMDLKKKEKE
CRKLQQELNS ERESCNQKIA RAQKEFNEIQ ASLQEETQQK VRLQMELAAK EAELEQLRRK
NLSPSSEENL SSSLLPLTSD SLNSSSQNSV LPVSISNSSA TSIETTEENR LEGWLSIPNK
QNIRRHGWRK QYVVVSSRKI IFYHNELDKA KADPTLILDL SKLFHVRSVS QGDVIRADAK
EIPRIFQLLY AGEGESRKPS DNLYQSESNP TKDPTTIEFK GHEFIPITFH MPTSCELCTK
PMWHMFKPPP ALGCKRCRIK IHREHIEHKG EIVVAPCKVY YSAKELYLLA SSPEQQQKWI
NYLCKKIKQC GYAAINQQRH QSNLSISSNS SGGGGTGGNS SVCSGFVGTG KNPLGRSFAS
SNDLTSAKQF DGYGFKFIIE TKY
//
