ID G0W4S5_NAUDC Unreviewed; 2369 AA.
AC G0W4S5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Serine/threonine-protein kinase MEC1 {ECO:0000256|ARBA:ARBA00021345};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=ATR homolog {ECO:0000256|ARBA:ARBA00033001};
DE AltName: Full=DNA-damage checkpoint kinase MEC1 {ECO:0000256|ARBA:ARBA00030459};
DE AltName: Full=Mitosis entry checkpoint protein 1 {ECO:0000256|ARBA:ARBA00029679};
GN Name=NDAI0A06590 {ECO:0000313|EMBL:CCD22813.1};
GN OrderedLocusNames=NDAI_0A06590 {ECO:0000313|EMBL:CCD22813.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD22813.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD22813.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769}.
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DR EMBL; HE580267; CCD22813.1; -; Genomic_DNA.
DR RefSeq; XP_003668056.1; XM_003668008.1.
DR STRING; 1071378.G0W4S5; -.
DR GeneID; 11494560; -.
DR KEGG; ndi:NDAI_0A06590; -.
DR eggNOG; KOG0890; Eukaryota.
DR HOGENOM; CLU_000178_4_0_1; -.
DR OMA; MVACELN; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000000689; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
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; IPR012993; UME.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF124; SERINE_THREONINE-PROTEIN KINASE MEC1; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1402..1945
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2050..2353
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2337..2369
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2369 AA; 273873 MW; 8477E7501A6EC269 CRC64;
MESHIRYLDE LILAIEGTEF ITKDEYFTYP PNINLNDDTK YIKIIKTLLK NLKESPDTSS
MINDKVFSKS IIVLDILFQK KPYLLVCSDL LDKNLLTIIS LIDEFLIVSN LNYAIRHRQW
FIRKKVGSWC KLTTILFGRQ CKNKISEHFQ ATLASVEREI KGVLMNQCET AIFYSQIARM
WTLLYWLNSP REIFGSCLLF LDSSTGLCKW NFEFQRLIRI IFFVFDSIKI ESQQCLNLQL
DYLSLLVLSL SDKSMMNEKK KLTIISTCEL KYVLSIMHHI LERPRHILPN NASFAKSILR
VYLLCISSDS FDSLLYTFIS NFSIEHWIKH DTLELRKDNA ADLPLSFDIF TNKALLLIYF
DIQRRTASSG ELEYNEKYSI WCSRSSQTTS LIEMATTPFP GNEKQIEKIR ILILESFHKN
KKYSILNSEL NVLSPGMTKR TSNNPRLLFN EISVSIQTCL TTNNTSRLVD NIKILANLTC
FENSNREGLA DWNTCQLCDS VGSCNIFERI DPDRNISAAA SPALTILNKY LLLPEYTNKY
NDSVLASILL CLQRIFMHYQ PPKLDHEELQ LGSSLFRFFT LCFKHPKRYI RLLSSRLLPL
WNLTTLDINR DQQTATLIKF LQANNEENLT EVWVISWTQL TLTTSGEVFD SLLLKLFDIF
SSKKYALFSM MAVQIKIMAF MLHKTPYTLL SPILPILLRQ LGKNLVEKKN TFYRLINLLG
YSAKTILGMF QRYIVPYAIT QYRTDVFSEV AKIMCDCDPT LLLEEKKTLL SKNSRYIFAV
ALVKHGFFSL ETLETLFLNR VPSFDKNYIT AYLPDYKTLA EVVKLYKNSE GSEPEFVENE
KSVLAALRFL LINFTTGKHL LPRYKPNSNS EWSIEQEECF QRNLLQNILG IFQVFSSDIH
DVGGRTTYYE KLRVVNGISF LIKYASKKAI ISALAQISIC LQTGLEICEV RYSALRCWYL
LIENLNDEEL STIIDAFIAY ILQQWSQFDS KTKTIVYEIL DVLVKTKSDL TVVLKPYISV
ALAGSAQVDI LSRDGAFARI IHKIKIISIW FRFFSKNLES NNKYIIHQNL NDLELHLRKQ
NERITNRWMG NTDLSMLLEA LLRTSQKFRT IDDELCKKSA RCIGLIGTFD ITKNKFNERK
SVGDEIFDFN NDVETIKFLI WVINDILVPA FWQSENPSKQ LFVALVLQES LKYCGLSSDS
WDINKRELFP NEWILWNKFN TISKTTLYPL LSSLYLAQSW KEYVPLQYPS FKIEDGYRSW
IKSFTLDLLK TGTDETHPLH VFSSLIREDD GSLSNFLLPY IITVIIVKEE TGSSSSDLMN
NIIMEFKFIF GFSTAGLNHL QLDSLKMCYE SIFKVLEYVR KWITNFRQKY HESNGTSIIR
EEKTLKMLKK VEEFLHSIEP ELLARRSLET NSFERSALFL EQCYRENGKN LGNTELLCNL
QKTYEEIGDV DSIDGILKSF STGNLISKIE ELQYSKSWSM AQDCFSALSG ISDDTAIATR
MVKTLYNHQL YSQVLAKLPA CVNKSYTAAR EMKEWYKMGL SAANVEGNIS LLKEWIHRVE
ILKDVNDPEI NLEYNISKSL NAVASGDLHK TKKYIDQCFA LIGTHLTAAS SGTTLVKKQN
LVMKLHSLYD ILLLSEKDNE YQYHDAISVL DFRMRNIKAA FEPNHYLLSI RKSFGLLHKQ
EYSKKELINT FFEITQLCRM NSRLDIACES LMFCLENGHS QAELEFAEIL WKQGENDRAL
KLVEEIHQRF GRKQDVKKRD RSAVLLKYTE WLDLSNNSAS EQIIKQYKEI FILDPTWDKP
YYSIGQYFAR LLERKIAEGY ITDGQLEYKS VSYFLLAFEK NSIKVRENLP KVITFWLDIA
SDSMKASLQS EKEILQTTTK DICKCIEGAL PQCPTYIWYS VLTQLLSRLL HTHRGSSKLI
MKILLMLTVE YPAHLLWYIS GLLNSSSKPR VIVGQHIIEK YRHHRSQVSA LVDDSSKLTA
ALTKVCLQDV KNISSRSGRS LEKDFNFDVK MVPSNMTVPV RINLEMLSPL SADSMDLYVP
FGEPVTISSF GSSYKVFASL KRPKKLNMIG SNGHIYGIMC KKEDVRQDNQ YMQFATTMDF
LLSKDVESMK RYLGITTYSV LSLREDCGLI EIVPNVITLR SIFVTKYEGM KVKYNLKSLY
ESWQNTSPGQ RIGFYKEQLL KFPPVLYEWF LDTFPDPINW FNARNRYARS YAVMGMVGYI
LGLGDRHCEN ILLDVESGNV LHVDFDCLFE KGKRLPIPEI VPFRLTQNLY DALGITGTDG
TFKKTSEVTL SLMRDNEVAL MNVIETIMYD RNLDDTIQRA LKVIRNKIRG IDPRDELILS
VPGQVDTLIQ ESTTDDNLGK MYIGWLPFW
//
