ID A0A182N3Q3_9DIPT Unreviewed; 975 AA.
AC A0A182N3Q3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR002265-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR002265-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR002265-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182N3Q3; -.
DR STRING; 7168.A0A182N3Q3; -.
DR EnsemblMetazoa; ADIR002265-RA; ADIR002265-PA; ADIR002265.
DR VEuPathDB; VectorBase:ADIR002265; -.
DR OrthoDB; 988261at2759; -.
DR Proteomes; UP000075884; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05597; STKc_DMPK_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF66; SERINE_THREONINE-PROTEIN KINASE GENGHIS KHAN; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 135..403
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 404..474
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 492..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 741..775
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 495..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 975 AA; 111744 MW; D5CD0EE661F3376F CRC64;
MASEQKDVLA GLNLSKLSVQ SPAARLKDLE NLILDQVASG GGTNNNYSSN GSNGTTTTNT
GSSPLFSILS GAVAAAGLSA EKFLSVETMV DCLLVLYDEC CNSSLRREKT VSDFIELMKS
VVQSIKQLRL SRDDFEVLKV IGRGAFGEVC VVRMHHTSQI YAMKILNKWE MLKRAETACF
REERDVLVFG DRRWITNLHY AFQDDINLYL IMDYYCGGDL LTLLSKFEDR LPEDMARFYI
AEMVLAIHSI HELKYVHRDI KPDNIVLDAS GHVRLADFGS CLRLGPQGTV QSNVAVGTPD
YISPEILRAM EDGQGKYGPE CDWWSLGVCM YEMLFGETPF YAESLVETYG KIMNHKNSFD
FPNDDDEYGV SDQAKDLIRQ LICAPEYRLG QNGIDDFKAH PWFEGISWDT IRNGQAPYIP
EVSSPTDTSN FDVDDTDIKL SDAVPPTTNP AFSGHHLPFV GFTFTKDSSL SDVGRLSRAI
TTNNNISQPL APLKLEKHGS EEKQRLSPDS TRKLQDEINS LTKRNCELES QIKSFERVGA
LSIGTAASAD SVDGQVDAKL KEHEKMIRLL RQEKEDLQKE QQDSLDRLKQ QDKELKDALE
QRKLAMAEYT EVTDKLSDLR QQKQKLSRQV RDKEEELEVT MQKVDTLRSE LRKTDKQRRE
QDARTQDLIS ELNRERQQRE RSEECYRQLQ MEARSRSSSE LGSSNSLGIS SSDSIRLEID
RLEVEYSEKI NQQQTRYNIE ISALRDQLNE ADNHREMLQR ELQQAREKLD SSRLESLTDS
EETILELRKR HEREKKILLD DNRKLITDLE MISDSNRRLT AERLQMESEY EDLRNRRQAF
SQWERQIAEI IQWVSDEKDA RGYLQALATK MTEELEYLKH TGPLNHNASD NKNWRNRRSQ
KLDKMELLNL QSSLQNEIQA KAVISEELTR TRTDLVAAQK DLRETRQICE TIGGELKRKE
SVIKELQQRL ESNEG
//
