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Database: UniProt
Entry: Q16F49_AEDAE
LinkDB: Q16F49_AEDAE
Original site: Q16F49_AEDAE 
ID   Q16F49_AEDAE            Unreviewed;      1088 AA.
AC   Q16F49;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 121.
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=AAEL014900 {ECO:0000313|EMBL:EAT32859.1};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT32859.1, ECO:0000313|Proteomes:UP000682892};
RN   [1] {ECO:0000313|EMBL:EAT32859.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT32859.1};
RA   Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA   Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA   Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA   Rogers Y.-H., Kravitz S., Fraser C.M.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAT32859.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT32859.1};
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
RN   [3] {ECO:0000313|EMBL:EAT32859.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT32859.1};
RG   VectorBase;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CH478512; EAT32859.1; -; Genomic_DNA.
DR   RefSeq; XP_001649972.1; XM_001649922.1.
DR   AlphaFoldDB; Q16F49; -.
DR   STRING; 7159.Q16F49; -.
DR   PaxDb; 7159-AAEL014900-PA; -.
DR   VEuPathDB; VectorBase:AAEL014900; -.
DR   eggNOG; KOG0892; Eukaryota.
DR   HOGENOM; CLU_000178_3_1_1; -.
DR   OMA; RQHFAIN; -.
DR   PhylomeDB; Q16F49; -.
DR   Proteomes; UP000682892; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05171; PIKKc_ATM; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR038980; ATM_plant.
DR   InterPro; IPR003152; FATC_dom.
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; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR044107; PIKKc_ATM.
DR   PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR   PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          26..630
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          734..1045
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          1056..1088
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   1088 AA;  124192 MW;  5E1BEF2050DE9296 CRC64;
     MLTIVECIRM NNQNHSKHTI NLNWLQIAEA SLHCQAYFKA ILYGELWCMT QRDEGVESDV
     ISRNPQLMSI MKTAHLSVGI VDAAKAFLDP IASRSEYYQL ERRFHQSLLY YDVASSSKST
     FERSAYVQTL KASSFYGLAN TVANSESMDF ECAWRLADWN IALDDRANQG KQNVDWQHVF
     EKQHYKALKC LELKDEIATE SAVLEARKAL AEMLKVGSME STQNIYPYLS KLRQLQQIED
     FMNVQFYRVI DGETELLQKW DQQDTLPYSD FSYMEANLTQ RIAILKTARV RAMRKWVPDA
     LNQTLFHLIH EARISGHFDV ATANICAMSQ QTLSETVKAL LMLEDAQLNW ANGDKFLSKR
     LVNEVVAGGK CKDIMVNAAA YRIYGTFLAE THAEDVHNLY KKFFKHSQTL VEEGLRHASQ
     HDKGTAIDYQ RKCLDSDRNF VILHTVAKYA DREFVRLKKH FTSSEFKSKK MNLEHMKAEL
     IMLESEQAKL KESDREKMTN LRRAKISTKQ NATRDEESIN TMMSNMEDYL KLALFYYSAY
     TRKTSIESDL AVFRIVALWL GNHSEKIADT VKESLKVIPT FKFVPVLPQL APRLDNHKEG
     VGRMVWETLE RCAVDHPHHT LPHILAQVHA FADVERKDVP KDDERLLGAQ SLYHKLLKNK
     KISAIVDQTT DMSLALIEMA NKILGTAKGF SDYKMTAKDA LRKCQGLDKV HCPTVELKVQ
     ESGDYNEIIG VHKWDDLIHG VGGINAPKKL VCHCSDGHNR IQLLKGRDDM RQDAVMQQVF
     CILNVLLRND KEAGKQKLAV RTYKVVPLSK QSGILEWCSN TIPIGSWLIP AHSRYRPKDL
     TALDARKAFA ELAKSSLRTK QEKFLKICQQ LSPVFQHFFL ERFLTSGMWF ERRLAYTKSV
     AVSSIIGYIL GIGDRHVQNI LVDEKTAEVI HIDFGIAFEL GKNLPTPETI PFRLTRDIVA
     GMGISGIEGV FKKSCEKTLE ILRNNHAPIM TILEVLLYDP LYTWNVLANK KAARKQISEL
     YGGEGGQDAR SEVVNISAER ALLRVSDKLN GKEDEKFTSV EGQVERLIFT ASSNLNLCQL
     FQGWQPYL
//
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