ID   CMR1_CANGA              Reviewed;         534 AA.
AC   Q6FQU2;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=DNA damage-binding protein CMR1 {ECO:0000250|UniProtKB:Q12510};
GN   OrderedLocusNames=CAGL0I03542g;
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: DNA-binding protein that binds to both single- and double-
CC       stranded DNA. Binds preferentially to UV-damaged DNA. May be involved
CC       in DNA-metabolic processes. {ECO:0000250|UniProtKB:Q12510}.
CC   -!- SIMILARITY: Belongs to the WD repeat DDB2/WDR76 family. {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; CR380955; CAG60339.1; -; Genomic_DNA.
DR   RefSeq; XP_447402.1; XM_447402.1.
DR   AlphaFoldDB; Q6FQU2; -.
DR   SMR; Q6FQU2; -.
DR   STRING; 5478.XP_447402.1; -.
DR   EnsemblFungi; CAG60339; CAG60339; CAGL0I03542g.
DR   GeneID; 2889181; -.
DR   KEGG; cgr:CAGL0I03542g; -.
DR   CGD; CAL0132616; CAGL0I03542g.
DR   VEuPathDB; FungiDB:CAGL0I03542g; -.
DR   eggNOG; KOG4328; Eukaryota.
DR   HOGENOM; CLU_017019_1_1_1; -.
DR   InParanoid; Q6FQU2; -.
DR   OMA; TVVRHNC; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR   GO; GO:2000001; P:regulation of DNA damage checkpoint; IEA:EnsemblFungi.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR033052; Cmr1/WDR76.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR14773:SF0; PTHR14773:SF0; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA-binding; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..534
FT                   /note="DNA damage-binding protein CMR1"
FT                   /id="PRO_0000351103"
FT   REPEAT          198..239
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          254..294
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          346..386
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          403..442
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          457..496
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          498..534
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REGION          39..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  60651 MW;  282C04205761DF41 CRC64;
     MVAELTEFQK KRLENIKRNN DLLKKLQLQG TANKIKREAG VDTVSRHEER LKKKKKIVNA
     KKQSEKEASP KTAMPTRRSR RLMGQQVKNE EGIPNVSDTQ LLKMNRNKEL EDLKDIKETA
     VIGDVKLSDL IKTEEGSNED ELLAKFKQFA NKNFSSGDFF DIIKKRQKET ENDSDLTKMQ
     EDFDLHMYDV FQPNEIKITN ERITSMFFHP STDKKLIVGG DTSGTVGLWN VRDEPLAENG
     EDDLVEPDIT KVKFFTKNVG KIECFPTDTS TLLITSYDGS IRTLGLKDLK SADIMTLRNS
     YEEPLGISDC QFSYDNSQVL FLTTLGGEFT QLDLRAKPTE TKFWRLSDKK IGSMAINPQR
     PYEIATGSLD RTLRIWDVRK TVETPEWSQY EDYHSHEIVS TFDSRLSVSA VSYSPTDGTL
     VCNGYDDTIR LFDVNGELPE DLDEKNKTVL KHNCQSGRWT SILKARFKPD QNVFAIANMG
     RAIDIYNSSG QQLAHLTTAT VPAVLGWHPL KNWIAGGNSS GKVFLFTDEL NTSK