ID A0A182RD24_ANOFN Unreviewed; 2911 AA.
AC A0A182RD24;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 31.
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 funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN004093-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN004093-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN004093-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 STRING; 62324.A0A182RD24; -.
DR EnsemblMetazoa; AFUN004093-RA; AFUN004093-PA; AFUN004093.
DR VEuPathDB; VectorBase:AFUN004093; -.
DR VEuPathDB; VectorBase:AFUN2_014184; -.
DR OrthoDB; 5478852at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13983; STKc_WNK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR13902:SF12; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 557..818
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1788..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2269..2295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2389..2435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2798..2822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 911..945
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1121..1228
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1452..1486
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2405..2435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2911 AA; 322726 MW; 94172143EAE3AAD5 CRC64;
MGATKRACFG RSNSVQATTP VGNNQETQPN LRVSSGNQQQ FNNHRVRRLR STSQSTSSTS
LNNINNNSSG STAGNTSCIS TGNNTTNCTG SSSSGSSSTN NTTSTNNNIT TYNHNNCSTL
RQQRHHHLHT IRSGTSSTNS TASNTGGLIS RVFEHSSGSG SSNNSLNCTN TTVNTATGTI
SSGGGSTNSP SCSVVTASGG AGTGAGNHFR RVSPGDKKIH SQIKNDDKMD ERRQQQQRTP
VKQHQQTRDT TPTSRKTGNR KDEGGAGAAG GALAISETSP KKHNNTVRCH GMISKVSTVV
TDKEDNEAAE SVVESDITVP VEANERMEMV SSKQEDATTT EDDGGGGTVE EHHPIGSTKM
LPEQEGNEPT TISQEENSTA EAKTTRRSKT TTKDSGIYGE QQLSNHHLDE NGVAEDEKEE
PHENDDKEMD VQIRPTDPEN VHYAEGDSRG SDNAQSRTIL RFVRKSLENT AMSVIYSKNF
IENETIETEY PRNLDDNIEI LSREAENLAL QFKPSEEKLV QYGPIFDLEK FEEQRKQQKK
EDDEDEAIGI SPCGRFLKYD KEVGRGSFKT VYRGLDTQTG VAVAWCELLE KKVNRVERAR
FREEAEMLKK LQHPNIVRFY NYWEAAPTAG NKKKNIVLVT ELMLSGTLKS YLRRFKKINP
KVLKSWCRQI LKGLHFLHSR TPPIIHRDLK CDNIFITGTT GSVKIGDLGL ATLKNRSFAK
SVIGTPEFMA PEMYEEHYDE AVDVYAFGMC MLEMATSEYP YNECNTPAQI YKKVTSGVKP
QSLEKVENPE VREIIERCIH DKKEGRPTCK ELLNCEFFCE DIGIRLEPIS KDLFLTNPEN
VRMEFRLRIM DPKKRVNKHK ENEAIQFDFD IRVDDAEEIA NEMYKSGILM EDDSKTVAKI
LKVQIQTLLK EREERARQQQ VEKDKEALQK QAMFAQQLYQ QQQIQQQLEN DLQVTELQVP
QMTQPVPVQL TQQQLPQASQ GYYQPSSLPS SQAQQLIYQQ QISAPVGNEQ LQQTYQQQSV
GGQFVIGQGI PLQQPMAQVI QQQQQHQQFL NQMVSTQPTQ TNLAATQQPN YIPQQVFVDS
QQQAHIMLQL QQQQGQSQGT NLQYMNQMGA QHQLVQHIFQ LQQQNFAMMQ QQQQQAELQE
QISTLEQQLQ GIIPIHSQPA QNIQQQQQQQ IQQQQQQQIQ QQQQQQQIQQ QQQQQQIQQQ
QQQQQIQQQQ QQQIQQQQQQ QIQQQQQQQI QQQQLKLQQH HQSPQQQPQQ QAQQHVQQQL
QPQHQVQQQS QQQPQQQPHP QLQQMQTQNV YIQQQSQPPA NNLTNNQPQQ IQANPNMYMP
QHLCDTSVQL HQSMPNQIGT SQPPPQPSSS TTILMHHQVV ASQQPPLPQP HFVKQQSPSV
LTQQPSQSQQ TQMTQTNPVQ NALMGQQPSP VSAMVQQTIT QPHSQGTAPQ ELDGSLVVSN
SGPISSNENN LLMQQQLQYQ QQQQQQQQQQ QQQQQQQEQQ QLLQQQNFQQ QTIAQQMVHN
SQDGTLLHQA VASANYNASP INGGQQGTNI MAPTGTTTAG SQSASAGVQD ANVSTATPSI
QAALPKRLTN EMKKRRNHRS TERNPKLHVL GYENNIIECE MENRPKTIKF KFDPSNVNPV
EVAQDLVKQD LLSESQTTIF IEMVRDIQRQ LKENPNQLPI ASQCYRRSME KRDETSTTAA
NFTHIFDPTI IDRQALGTGI SSTTTSSTSS SPLSQQQLIT SLVASQTNDE VASLEKAQSS
DENGTEGTAG PMQDQELNNG ITASSDDNHQ TSVTTVCMIT DESVIDNNSS CDENSRKAST
VSTDYTSHEN TPENTITSGS NLSILQPRLS FGEQDSMVAV ATSGERQLAP SLVPNEGSYA
SEETEPNAMV ANQLEGAQES VASVAGDPAV GAVTSTAISN LQATESSSQN IYQSSLSNVN
NAESSKTNEL MQVGDETVLP ADEGMVESPT NESNKTPMVT PQLKERKLSR FSVTPVILPD
ALVMNEQQTG ILSVVDSPKP ILPNTGTETQ TECAVEMVDP LAEPLVPPQA TDNGPFRSGS
MEYTLQPTSS QLTQTVESVD PNFTNSFNEG FQQQQDMYLQ QQSINLQQQS LAIAQQITTN
FETSAALQQQ QQQLQQQYQL QHQLQNQQFQ QLNLLQQYHQ QQGNNLMLTE ANMTEADQQQ
LQQIQLQHHQ YQSQLQHQQY AYQQQQQQMM PQQQIQQNQQ MRPVEQITLM SAQLSVDQGT
REAMANSNRM PETLEQLKIG LENITHVHVN TNKSSGGSAS LSSQASATAL SAMVSPHPVP
YPSDSGLAQQ SQQPQQVMFY QSHEYGTTDA NGAPLNEMHE GAATGGIVGK AQEYIVEGTS
YAAVVAGEFI SQPAQQQTGS VQDASTVGGL QTDQTQQYVS RRTSAELNNT SIAMVPDSLE
PSGFKESVSI DSSNIDSSSS HNREKPLSNQ GSADRIDSSV TGLQLKLAQL TVGTDASKAV
TIGAPDQQSN LPQQIHSVVT SPSVESSGEM KVLSEPKPLI RKVSRFHVQP VQESLRAVEQ
QSPAVSAQLK PVVTMPDDVQ TNTAFSSPTD EKSCQTFPMQ YQQHQQMQQP TAAVICEVPT
TNDLEAKLNQ VLPKTPNVES AILNAGNTVL QGTIQQATAL PSASTLKTSH TVLSSASVTS
TVQIVQQQHQ QQQLITIQQQ PQTQVQMNAQ AAIPANANNG VQTTLMDSSN YTVVSQQSQH
PQTLAVAPQP QQSQLPPEPN FNNSDIGHNL TAIQTHLCGL QLLPSARQQL QLLLQRQHIE
HEELKLRHFL ELEKFLKQQK EEMKLPSGLA AAAGPHPNQT QPMISTQSSS QSVGSISSTT
APEMMTDVTS PTVAPMNSVG YEMNCQGKPL MTTAASSYNT SCNTDSGAGS ATDTDLELET
YTANASNSID AATMLQQQQF QHQPQNQQFQ Q
//
