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}.
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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 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
//
