ID G1QG66_MYOLU Unreviewed; 1083 AA.
AC G1QG66;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000022699.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000022699.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000022699.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AAPE02042922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QG66; -.
DR STRING; 59463.ENSMLUP00000022699; -.
DR Ensembl; ENSMLUT00000029090.1; ENSMLUP00000022699.1; ENSMLUG00000025110.1.
DR eggNOG; KOG0892; Eukaryota.
DR GeneTree; ENSGT00670000098061; -.
DR HOGENOM; CLU_000178_3_0_1; -.
DR InParanoid; G1QG66; -.
DR OMA; AKEECHI; -.
DR TreeFam; TF101182; -.
DR Proteomes; UP000001074; 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-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
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 Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..593
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 713..1026
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1051..1083
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 601..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 123613 MW; E6B82D08621F4896 CRC64;
TNRNLVFEEG SQSTTISSLS EKSKEETGIS LQDLLLEIYR SIGEPDSLYG CGGGKMLQPL
TRLRTYEHEA MWEKALVTYD LETAISSPTR QAGIIQALQN LGLCHILSVY LKGLDDENKE
WCAELQELHY QAAWRNMQWD HCISVNKGIE GPSYHESLYN ALQSLRDKEF STFYESLKYA
RVKEVEELCK GSLESVYSLY PTLSRLQAIG ELESIGELFS RSVVERQPSE VYIKWRKHSQ
LLKDSDFSFQ EPIMALRTVI LELLMEKEME NSQRECFKDI LTKHLVELSI LARTFKNTQL
PERAIFQIKQ YNSTSCGVSG WQLEEAQVFW AKQEQSLALS ILKQMIKKLD ASCSEDDSNQ
KLIYTECLRV CGNWLAETCL ENPAVIMQTY LEKALSQSGT PQGITTCWLR PAPQGIGPKM
AIRHPSGSPG AFGGMSTCQQ EAGLSCSRTS LALLRRQKLF NARYTIKVQR ELELDECALR
ALKEDRKRFL CKAVENYISC LLSGEGHDMW IFRLCSLWLE NSGVSEVSGM MKRYGMKIPS
YKFLPLMYQL AARMGTKMTG GLGFHEILNN LISRISMDHP HHTLFIILAL ANANKDESLT
KSEAARRSRI TKNAPKQNSQ LDEDRTEAAT KIISAIRSRR PQMVRSVETL CDAYIILANF
DATQWKTQRK GIKIPADQPI TKLKDLEDVV VPTMEIKVDP TGEYKNLVTI QSFKAEFRLA
GGVNLPKIID CVGSDGKERR QLVKGRDDLR QDAVMQQVFQ MCNTLLQRNT ETRKRKLTIC
TYKVVPLSQR SGVLEWCTGT VPIGEFLVNN ENGAHKRYRP KDISAYQCQK KMMDAQKKSY
EEKYETFMDI CKNFQPVFRY FCMEKFLDPA VWFEKRLAYT RSVATSSIVG YILGLGDRHV
QNILINEQSA ELVHIDLGVA FEQGKILPTP ETVPFRLTRD IVDGMGITGV EGVFRRCCEK
TMEVMRNSKE TLLTIVEVLL YDPLFDWTMN PLKALYLQQR LEDDTELHPT PNADDRECKR
NLSEIDQSFN KVAERVLMRL QEKLKGVEEG TVLSVDGQVN LLIQQAMDPK NLSRLFPGWK
AWV
//
