ID A0A182M5Z8_9DIPT Unreviewed; 2289 AA.
AC A0A182M5Z8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA010328-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., 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 culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA010328-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA010328-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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};
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DR EMBL; AXCM01000632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 139723.A0A182M5Z8; -.
DR EnsemblMetazoa; ACUA010328-RA; ACUA010328-PA; ACUA010328.
DR VEuPathDB; VectorBase:ACUA010328; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000075883; Unassembled WGS sequence.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05170; PIKKc_SMG1; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR031559; SMG1.
DR InterPro; IPR039414; SMG1_PIKKc.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF71; SERINE_THREONINE-PROTEIN KINASE SMG1; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF15785; SMG1; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2023..2289
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2289 AA; 258488 MW; D5F5C261EF5F90DD CRC64;
MGGKADTKSS QQCATKRVSR RNKKKPTEQQ RQTKPNAGGT RTSPCEQHDS DQHPMATAGA
PAGGKRYQNA RTQAATQRRD RARKLATEAD RTGATARGSS PHELANIPAD MRISKLLRKL
TSETNVPQFL DLCDRLEVVI LDSSNASYVR KSFDILANTV NTILEGGLCE CHDRVSQLFG
MMLYVLLSNS SDSSALRTWI GRYLTHTKAI RRSALIAIRQ TILLDRTGQK LDAKTISYLL
SALQEILEST DVLEVFVLIT GVMVELADGY PRAFAPHFSD IVDIVVGWQL ENTQSTKVKL
HCARVLLAFQ QYWYEKRDVT FNLLEQFSED IDRLCGDVDY SDQQQRDDTY RLFGSLLTAF
NSVLKCLGNT TTTTNSKMEA FVLQEDELAR FECCSVTIME IVFRLLEAPP TGLVVAAICE
FAMLKLTIDT VPTLATSTEE DFDRLISKLI QYTDTYSDEQ VGALLHLLLR YIDADTAKVQ
QCRVQALLVP LFQEGALYAL RYRQNRTVQR VLLLLCHHIL TLKHVEILQT AYNFILADID
EAMGKLRATG SRTLSKANVL RLQYRIQFSL LLFSPLVMAR NSIFITWTLK DEPVLHVLLD
RLAPTDSRLW NQRIHTHLHY AVLLTAFHHC TANNHFISSS SLLQPARPYG MVDRFRRGSR
AEPSDTDEDE PPESPTADHF GLVLRFLGTI LGQWKGTRAS NRYDSRCTKL LLLLLDWCHG
IVTQTTRYHD VLHDSDEFNR LLVHVGTIAV EEGSESEMIG LRCADCLDAA CQHASLHVSA
YQAIAEACCV HLCSVYGSLR TRYTVLFSKL PLRHSLRQVN EFTGVNRRRW EQIGELKNGL
YQGSGGYGLQ HSATLRMADL RSLFNRISFT RDGSDDYAGG FLHELLTRSF NQPSRYGEMA
LRDLRCLIPW AQWEAAQLCV NHKLRTPFGK PQSTFLRIES IVKQCARILA LKDKFPVRDI
GTSIVNQRHA RILLGFLEAL EKSIYNAAEG TAYALPAPEK PARTFFRVNQ QTCAEWFTRI
RTAVDLVALH CMEPEMVIRY SEAVLRELVA AGKTADPIFE HMLMSLVWAL LRNCESDALY
GVYVWSKRLT GRKYSWIRMA AEEASGHREM AASGFRGILA DPGSVGMDRH IRDFIVDQTI
VSLLFTGDYG QLYEFLLAEE RSGTPRATIP LITVTAAQIS SIIRYEETHD VSVIDISQWE
LVDVGNNIPN DFSCHKMICA VENSLTGIIL QEQIDQRERM IDASTELIQC YLQECLLTRC
REYLFQLTIT NHILYKIAQR IRAPDRSSGS VDSSSAAGLA SLSVEKFYGT FTLMRLLSWS
EFLLADAGYG YEGEQQNIDL RLDMVSIGRK EKNYALSRRV LEKYYHKSNL IGRLEDLGGE
YRQQQQQQRV TLEQVATVLT KYDPAPPEGL WDANLSRAVY EHCKWLYCQP GKRLEAIDFA
ACATAAIDGV WQRQRDEGEK GKQAAQLSER VARFLLTISD WMAGEAGEPL AHELASVTRL
GHLMPSIDVK PIATQHGGIF GPSDRLIGTM LKGAVDRCPP LAKAWFALGS WLYRWGKRIV
EHSAADGSSA RISVDQVTAI LAGPNISLDD CERIVEILND HEPARIVIGV DGDTDDADEL
DLDSSATIGS IGLLDALHRA MPGLQSNVPQ ERLHAIIDIW RSNHRSVYGY YEAAAEAYFR
FLQLSSGRNN AASEGVDSER ARSVTVTLRL LRLIVKHALG LKEVLEEGLA TTPSEPWRVI
TPQLFSRLAH HEPYVRRRVS ELLCRVAKDA PHLIIFPAVV GSVQEEPSQL AVVDVIRDGV
EEISSKINDT NEQVQSSAAS GLGFCFNALL DILSCEIPDT VKQVQTLVHE LRRISLLWEE
LWVVSLQQIY SDYTKRIPTF ESEYRRLYTS GQLTAQRRIL LAEKHRLLLR PLLFVLEQLY
GITSRKAETS HERHFQTRYH RYIRHMLAKL REPADFSRPI EGWNRFRTLY AQLQQRSQKR
FSLFLRLGDV SPNLLRLSNT AIAMPGIDTT LAGSRQPILI RSVDNNIQIL PTKTRPKKLT
FCGNDGRRFG YLSKGLEDLH LDERIMQFLS IANLMMTKSI DCNGNVTHYR AEHYSVIPLG
PRSGLITWVD NTVPIFSLYK KWQQREALQK KETKKGSSAA LRPSELFYGK LTPLLQSHGM
KSSASRREWP LPVLKQVLTE LQQETPRDLL AKELWCHSAT ASSWRLVIRN YSLSLAVMSV
IGYIIGLGDR HLDNVLVKLA TGEIVHIDYN VCFEKGKTLR VPEKVPFRMT PNLEEALGLT
GIEVSGCCF
//
