ID A0A1I8Q3E9_STOCA Unreviewed; 1376 AA.
AC A0A1I8Q3E9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=106087157 {ECO:0000313|EnsemblMetazoa:SCAU013516-PH};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU013516-PH, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU013516-PH}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU013516-PH};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 RefSeq; XP_013107603.1; XM_013252149.1.
DR EnsemblMetazoa; SCAU013516-RH; SCAU013516-PH; SCAU013516.
DR GeneID; 106087157; -.
DR VEuPathDB; VectorBase:SCAU013516; -.
DR OrthoDB; 4221785at2759; -.
DR Proteomes; UP000095300; 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; 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; 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};
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};
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}.
FT DOMAIN 83..345
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 346..416
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 955..1020
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1116..1323
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1235..1289
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1020..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 445..658
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 706..988
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1376 AA; 159654 MW; 531BD7114A01BF6B CRC64;
MEMNLNDMLP TSDHVLRTHV LEQEMRNPYS ICNVDCLLDT VTALVNDCDH ESLKRLKNIE
QYASKYKPLA QQICQLRMNV EDFDFIKIIG AGAFGEVQLV RHKSSRQVYA MKRLSKFEMM
KRPDSAFFWE ERHIMAHANS EWIVQLHFAF QDTKYLYMVM DYMPGGDIVS LMSMYEIPEK
WAIFYTMEVV LALDTIHRMG FVHRDVKPDN MLLDRQGHLK LADFGTCMRM GANGLVVSSN
AVGTPDYISP EVLQSQGVDN EYGRECDWWS VGIFLYEMLV GDTPFYADSL VGTYGKIMDH
KNSLSFPAEV EISENAKSLI RAFLTDRTQR LGRHGIDEIK EHPFFQNDTW SFDNIRESVP
PVVPELSSDD DTRNFEDIER DETPEEVFPI PKNFDGNHLP FIGFTYTGDY QLLSHNDTVD
AEAKENNINT ANHNHRHRPS NSNEIKRLEA LLERERNHAE TLEKQDKSLR QQLELITRRE
TELQNMASEY EKNLAITQHN YKIALQKFEQ EIELRKKTET LLAETQKNLD NEQKIRTREM
SNNQHHNEKI ITLEKQLKEM EENFKNETEN SQKLKKQAAE WGLAKQELEA KIAQLQVLIA
GLQNQKESLQ QEVAELQAQL AQEKNSRSQL KELHKETENK LQSLANDLER AITREQQAYE
DNRVLSEKIS DLEKAHAGVA FELKAAQGRY QQEVKAHQET EKSRMLSREE ANLQEVKALQ
TKLNEEKSAR IKSDQNSQEK ERQLSMLSVD YRQIQQRLQK LEGECRQEGE KVSALQSQLD
QEYTKKNSLL SDLSLKSSEV AHLKSRESQL QKEVTALREN KRKYEEDMTA LKISLNKEIL
QKKELQDQLD AEQIFSRLYK AQANEHREEI EERCREIQDL KEERVSLKHQ VQVAVARADS
EALARSIAEE TVADLEKEKT IKELELKDFM TKHRNEIAAK EALLSAAKDA ESDYVKKLNQ
KNSEYDELQR QNKNLQDEMN RVKTSKEEDI LKLTEKWKTE ILLKQVAVNK LAEVMNRRDT
DLKQQKGKTR SSAELRKKEK EMRRIQQEMQ QEREKYNQLL LKYQDLNSQV IEDGHIKQKL
QMEIDCKATE IEQLQSKLNE TASLSSADND PEDNQDSVFE GWLSVPNKQN IRRHGWKRQF
VVVSSRKIIF YNSEIDKQNT IDPVLILDLS KVFHVRSVTQ GDVIRADAKE IPRIFQLLYA
GEGEARRPDE QQQLDMSMLR GGAGDERPGS IIHKGHEFVH ITYHMPTACE VCPKPLWHMF
KPPAAYECKR CRNKIHKEHV DNNDPLAPCK LHHDPHSARE MLLLATTPDE QNLWVSRLSK
RIQKCGYKAN SSSNNNSNNS DGSKISPSQS TRSNYKPYAV NVQRSATLPA NSSLKQ
//
