ID   ATR_CANAL               Reviewed;        2325 AA.
AC   Q59LR2; A0A1D8PNV7; Q59LQ3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 98.
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=CAALFM_C504060CA;
GN   ORFNames=CaO19.1283, CaO19.8870;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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}.
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DR   EMBL; CP017627; AOW29815.1; -; Genomic_DNA.
DR   RefSeq; XP_710664.2; XM_705572.2.
DR   AlphaFoldDB; Q59LR2; -.
DR   SMR; Q59LR2; -.
DR   STRING; 237561.Q59LR2; -.
DR   GeneID; 3647733; -.
DR   KEGG; cal:CAALFM_C504060CA; -.
DR   CGD; CAL0000200852; MEC1.
DR   VEuPathDB; FungiDB:C5_04060C_A; -.
DR   eggNOG; KOG0890; Eukaryota.
DR   HOGENOM; CLU_000178_4_0_1; -.
DR   InParanoid; Q59LR2; -.
DR   OrthoDB; 80538at2759; -.
DR   PRO; PR:Q59LR2; -.
DR   Proteomes; UP000000559; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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   GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
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   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; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 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..2325
FT                   /note="Serine/threonine-protein kinase MEC1"
FT                   /id="PRO_0000227709"
FT   DOMAIN          1363..1886
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   DOMAIN          1993..2309
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          2293..2325
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT                   ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          1999..2005
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2174..2182
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2194..2218
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ   SEQUENCE   2325 AA;  266545 MW;  7F0A008BFE0B9E28 CRC64;
     MTSNQSISTT ELLQFLTDIE TNIDDHETDF RKLLLYLLRF TNEKLIVIAQ EENKTPTELQ
     LLSKLIDTIE LVLSKKTPLL STLLTIEDVN IIHTTGSGSL VYEVPLHEWC ISFALSHIPN
     FVSHTAGLNQ LKRLVFLIVN LVSTQLHSFK VIKSTRIHLL KTLDDNLNFC LQNLLSANTF
     LFKSKLTTAV NLFSIVHDYD ISQKLSLNLN NYQLKFESCS RKIWFILNEI SLVSELDNLN
     LLDCLKSVFI LDQSSALVLN VSVGWNQIGF LLSCIVEYLQ QDFRTLDSNT NNFEFVNLNR
     SISLSLLNVY IVCFDKDLLE NFMSFSNIKG ILSKLIYDDS IPSVIRKTLN IVQYTYQLMS
     NPDGDDIKLY STSVYNDYVW TPFVDSELES LRARLLDLQG NHEDSRKEEL LSFSIDETHK
     LAKSTNSLNY TDEKAWIRTV KKLIGIDKNV LEDETTLYTL VTALSHYPCI LKGDYDYTIN
     ECTKCGFGPL TKNNYSSIDP NRFPLNYSTE ATTLQDIIQQ FLIPKLETQQ DPLLCCNTLL
     LIFNFYASFS PMADMQDHNI LDFLLRLLAT NDNRDVRMLV ARILPLYLIQ SKDDKLLDET
     FKYIFQKVTS IDFSSQHRLH FGESTIRAVV ELATVSTGER LCAIYFKLVD WLGEQNEQHS
     NYVYCGILNL ASAKSLPPHK LLSPYLPSVA EIIIKKPQVF ERIIKVSMVT KNYFLNRTKE
     YTVPRILEYY KDPTLLTQIA NAAGLEVGKL LANCLPRILA TYLTKESVNE RYIMKVLSSV
     CPDYKMIHTE ELFTRIGDIT WYILLEIQMD EFGNIRNLAN ITRALECVCK NVSLRKNGSE
     LTKNNSINDL IEDQVLLLVQ KFSDVTHSSR GAKPYLELKN SFYAIEFLIK GHIDAITSAL
     GQLSTCLQAT LEEPNFHVLS LRCWNELIKK VPPSHLISLI DIIISIILQK FESFGSEAKS
     IAIEILRKIY EEIKDKYNRY SLYFLSLPFL SYMEDYQMVK EFRNMKSPSR AMIFSEFTRR
     LQTSNMYVVK HALFDLSNYF EKYQINCQKD LFKDPGLTPA ITSLVRTILD TAAKFKNKDT
     TVSTACAKAL AIIGALDSNK FQFKTVKSLI IISSDFEDIE ENSTFLVDLI ENHLLKIFWA
     SNDPHKQLFA AYVMQSFLAV MGLDERVLNT KDNRVWNKFT DVAKSTLTPF LKSKYAAPKP
     KLDNLKFPFF KLGMKYETWL VDVTLFLLKR ASIDNGKGNQ KAKTRKLIFQ SYAVLIQREH
     DIPLCEHLLR YVALSHVINE GVPEDLHKEF LHILKMDSKS TSPDRAEQLK LCYQTIFSVL
     DYFNQWVSNM RVVTSNSGSE LTSSDIRHKM DAVAKFSSFP QDLLTTRSAE CDAYERTIMY
     LENCYRDSQS EKSFKLSNLN GAATLQDMYA HIDDYDALNG TLKMFSTNNL NEKLTTFQYS
     DSWSLAHESF EALGSTKNSV SNNTKLLQSL NEHGLYNEVL STLSARTDSN DLKSIPLDWS
     LMGLHAAVYK GDSKQLEKWL QVINSIGKPH DMETMINYEL AKALSFLFQS RIDMFKGSMD
     KLYNIIGCSL VPSVSSNFTR NITLMNQLHA IYDVSLIVLS KDSEDTLDLR IGNVDQDFDT
     QRNILTLHNV ANTVMKNPAM ISKNLLRESS LARKYNRLDI STRSIVQAMS LEDDQANIEF
     AELQWAQGKQ SEAIKCLFDI LKDNKFHDDK SKAKVQLQYA NWLDESNHLS AHQIITEYNK
     AFHLNMVDEK CNFDIGKYYN KLMESSNDES GEYEHLTVRN YIRAVSVGTT YIFEALPKVL
     TIWLDFADKS NKSNAAENRL KQIIDDLYNA IANVPNYSWY TVLTQILSRI VHEHEPSFKV
     LKRIVQNVTL EYPKHCVWYI FSHARSSDKV RKRRVRELLN QVCTQDGNDT LPKSTMAAGN
     LFAKLIKIAE LKIPKTNRKR QMSLLQDFEV DLSEPIDDLV IPIQSNLQIQ IPSHLNSKHK
     GFSRSSSISF DGFDDNVNIF FSLQMPRQLT VRGSDGNAYR LMVKSDDTRK DAKVVEFTTM
     VNRILSTSTE ARKRGLQIAN YSVVPLSDHF GIIEFVMNVQ TMKGVISEQR KRQGIPINER
     KVFMHIDSLQ KAKKKDSKQL DKLVAGFRAI MDRCPPVLHT WFVEQFSDPS AWYMARNAFT
     RSSAVMSMVG YIMGLGDRHC ENILIFKNTG AVLHIDFDCL FEKGTTLPTP EIVPFRLTQN
     MVDAMGITGV DGIYRITCEV TGTLLRENEQ ILMNILETLI YDPLIDWRNH NPREDLSKVR
     KKIRGLINED EGLPMNIHGQ VDVLIQEATS LERLSQMYAG WAAYM