ID   ATR_CANGA               Reviewed;        2379 AA.
AC   Q6FX42;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Serine/threonine-protein kinase MEC1;
DE            EC=2.7.11.1;
DE   AltName: Full=ATR homolog;
DE   AltName: Full=DNA-damage checkpoint kinase MEC1;
DE   AltName: Full=Mitosis entry checkpoint protein 1;
GN   Name=MEC1; OrderedLocusNames=CAGL0C00473g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC       signaling upon genotoxic stresses such as ionizing radiation (IR),
CC       ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC       a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC       Q. Recruited to DNA lesions in order to initiate the DNA repair by
CC       homologous recombination. Phosphorylates histone H2A to form H2AS128ph
CC       (gamma-H2A) at sites of DNA damage, also involved in the regulation of
CC       DNA damage response mechanism. Required for cell growth and meiotic
CC       recombination (By similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to nuclear
CC       DNA repair foci in response to DNA double strand breaks. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR380949; CAG58106.1; -; Genomic_DNA.
DR   RefSeq; XP_445202.1; XM_445202.1.
DR   AlphaFoldDB; Q6FX42; -.
DR   SMR; Q6FX42; -.
DR   STRING; 5478.XP_445202.1; -.
DR   EnsemblFungi; CAG58106; CAG58106; CAGL0C00473g.
DR   GeneID; 2886754; -.
DR   KEGG; cgr:CAGL0C00473g; -.
DR   CGD; CAL0127418; CAGL0C00473g.
DR   VEuPathDB; FungiDB:CAGL0C00473g; -.
DR   eggNOG; KOG0890; Eukaryota.
DR   HOGENOM; CLU_000178_4_0_1; -.
DR   InParanoid; Q6FX42; -.
DR   OMA; YTVYSQM; -.
DR   Proteomes; UP000002428; Chromosome C.
DR   GO; GO:0070310; C:ATR-ATRIP complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006975; P:DNA damage induced protein phosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:EnsemblFungi.
DR   GO; GO:1901857; P:positive regulation of cellular respiration; IEA:EnsemblFungi.
DR   GO; GO:2000105; P:positive regulation of DNA-templated DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblFungi.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR   Gene3D; 1.10.1070.11; -; 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; IPR014009; PIK_FAT.
DR   InterPro; IPR012993; UME.
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; SSF56112; 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; Chromatin regulator; DNA damage; DNA repair; Kinase; Meiosis;
KW   Nucleotide-binding; Nucleus; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..2379
FT                   /note="Serine/threonine-protein kinase MEC1"
FT                   /id="PRO_0000227710"
FT   DOMAIN          1410..1955
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   DOMAIN          2060..2363
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          2347..2379
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT                   ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          2066..2072
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2232..2240
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2252..2276
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ   SEQUENCE   2379 AA;  275686 MW;  3C0ED0CD6DB7F88E CRC64;
     MESQIRYIDE LIAGFNGSCK IERVNEGNCA AQSSNTEERK LIQAVQALLR ILNDLNHNSA
     DLIFQKCLGG LDRILHHNPY IMALSISSED SGNLMIMDLI DKMLGLTERC SYNIHRMWYI
     RRNIIRWITS STRLFGSDFK RIINLKIKKI LNELETKCKL FLFTHQNVEP QEFISTLTLL
     HTILYWISAD SNKLGDYFYW IQGSSSLNEW DLHFQKYIRI AMYLFTSFQI KIDANSSYFE
     KFNLLQANFI MLVANYQTSR TLSGGFNSIA ISIQHLKFTL EVISEFMRNR SFLSKNETLI
     TKSLLKIYYL SVCKASSNKN DILSIFLDYI PVVECINSKH QFNENYDSEL ERSLLLLYFD
     MKRRYADPDE LQFIDSFDIW SHPDCIDEVS IITQPIKKNS KQIEKLQRSI LKSYTVNIKQ
     IHSFLFKELN SLEPGILDRN GDHYKAVVKE ISISIKRSLK IRDSKKIITW LRVLSRMACI
     EDKLINTKQN ISEFFHTTND FCNYCDSIHD GNFLNNIEPS RPLAQDQSEI FSMINKYFIL
     NPDLKKFSMS IKCGLFIVIE RIFAHFQPTA LMNENNQIAP LFSFIEDSFI DSDRHVRLLI
     CKILPLWNTS NHNNSEDEMS MHLIQFLQKV NSPLLLETVV LSWSKITLTT HGDVFDTLLL
     KLIDLFNSNN FTLHIMMKEQ LIRMSSLLNK TPYQLLSPVL PIILRQLSKN LNEKKLSFQR
     LCDLVGYTGK VILDIFQKYV IPYATVQYKS DVFSEVAKIM CDDDTSMLLQ QKHNLLTKNS
     RQIFAVALVK HGFFSLDTME TLFLNRVPSY DRRYIGAYLP DYKTLAEVTK LYKNNEITDS
     SDIENENMVL CSLRYLITNF ESDKRHGTEY KDINKWSDKK ENQFQNNLQD NILGIFQVFS
     SDMHDVEGKT TYYEKLRVIN GISFLVKHAS NKCIISALAQ LSICLQSGLE IPEVRYLSMR
     CWFLLIQRLN EEELTTVIDA PVAFILRKWP TFNKKLQLKA LEVLTALIRT KNSLLMKMKP
     YISISLLSNE SIPILDIDTN FSRQAARLRN TIDLVPIFVK NLQSNNKFVI EQNLDDIKFH
     LKRRQGELLQ YDKYGNLQLN AVPSLIGALL EVAHKYRTID HEICKKCAKC ISMVGVPDIR
     RIDLRGDRKE KWKVFDFNDY SKTTEFLIWL IDDILVPSFW QSENPNKQLF FALVMQESLK
     YCGLSSQSWD INEPDKFPEQ LELWNKFNSI SKTTLYPLLS SLYLAQSWKE YVPIKYPSLN
     FRDGYKTWIK NFTLDLLKTG TTEDHPLHVF SSLIREDDGS LSSFLLPYIA QDIIIKAQSG
     TEYESLMDNI LIELQSVVTY EIDGLNHLQR DSLKMCYEAV FSILEYCKKW ATMFRQDYNN
     ANGTFLIKED KYLKMLKRID YFINSIPLDL LANKSLETNA FERSALYLEE CYRHSDIHDR
     NLNSTLKSLQ MTYEEIGDID SIDGLLKSFA STSFETKIEE LQYSNKWQMA LECFDILADI
     TKHDSTAQIM TKSMFDHHLY KNVIQTVPKL VPDNIQKLNE SNTNLLIRAL ESSILEGDLK
     SIEKWSSKIE LMTTINDPEL TLQYNLGKAL LSISKGNHIK AGQFLDNCYQ ITGIQYTSTS
     NSTTLLKTQS LLTKLHGLHD LNMLNFSKDD FELQSNMQLL DLRRGKVGPD FDPNYYILSI
     RKTFDKIHKN PITKTDLVDT YFAIAQEARV NSRLDIASKA LIFCLEKGHP YSELEFAEIL
     WKDGENDRAL KLVREINQKN EKSSSVSVRN KAEVLLKYTE WLDISNNSAS EQIITQYKNI
     FALEPEWEQP YYSIGLYFSR LLERRKAEGY VSDGKLEFKS ISYFLLAFEK NTVKVRENLP
     KVITFWLDTA AAVITETSPN RNTILKKVTT DICKQIETAI RNCPTYIWYS VLTQLLSRLL
     HPHLSSAKLI MHILLSLAVE YPSHILWHIS VLCQSNSSKR VKCGQDILEK FRAHSDNQED
     IINSSIYLTS SLTRICLQEV KSSSSRSGRS LVSDFKFDVN IAPTPMTVPV RKNLEMISPL
     SAETMKSYQP FRPTVSIAKF ASSYKIFSSL KKPKKITIIG SDGMLYEIMC KKEDVRQDNQ
     YMQFAATMDF LLSKDLDSSK RDLGITVYSV LSLREDCGLL EIVPDVVTLR SIFTTKYESK
     KIKYSMKALY EKWQGLADEL KPVFFNEQTK KFSPVLHEWF LENFPDPINW YRARNLYSRS
     YAVMAMVGYI LGLGDRHCEN ILLDIKTGKV LHVDFDCLFE KGENLPVPEI VPFRLTQNLQ
     DALGILGTEG TFKKSSEVTL SLMRQNEVAL MNIIETIMYD RNMDHSIQKA LRKLRNKIRG
     IDPRDGLLLS VSGQAETLIQ EATSTENLSK MYIGWLPFW