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 27-MAR-2024, entry version 104. 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}. 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; CP017627; AOW29815.1; -; Genomic_DNA. DR RefSeq; XP_710664.2; XM_705572.2. DR AlphaFoldDB; Q59LR2; -. DR SMR; Q59LR2; -. DR STRING; 237561.Q59LR2; -. DR EnsemblFungi; C5_04060C_A-T; C5_04060C_A-T-p1; C5_04060C_A. 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; 8448at2759; -. 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:0051276; P:chromosome organization; IMP:CGD. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central. DR CDD; cd00892; PIKKc_ATR; 1. DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 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 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; SSF48371; ARM repeat; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //