ID   CMR1_ASPTN              Reviewed;         530 AA.
AC   Q0CSP9;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=DNA damage-binding protein cmr1 {ECO:0000250|UniProtKB:Q12510};
GN   ORFNames=ATEG_03285;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CH476597; EAU36559.1; -; Genomic_DNA.
DR   RefSeq; XP_001212463.1; XM_001212463.1.
DR   AlphaFoldDB; Q0CSP9; -.
DR   STRING; 341663.Q0CSP9; -.
DR   EnsemblFungi; EAU36559; EAU36559; ATEG_03285.
DR   GeneID; 4317852; -.
DR   VEuPathDB; FungiDB:ATEG_03285; -.
DR   eggNOG; KOG4328; Eukaryota.
DR   HOGENOM; CLU_017019_1_1_1; -.
DR   OMA; TVVRHNC; -.
DR   OrthoDB; 753973at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR14773:SF0; PTHR14773:SF0; 1.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; SSF50978; 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..530
FT                   /note="DNA damage-binding protein cmr1"
FT                   /id="PRO_0000351101"
FT   REPEAT          188..229
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          252..292
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          302..339
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          344..384
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          389..430
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          453..496
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          499..530
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255"
FT   REGION          34..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  58582 MW;  66CB81AE4A4BDEA1 CRC64;
     MGGEELSEFE KQRLANIAER DALLKKLTQD AQSVGLFPPK MPKGASPAGD KAKKKKPAPK
     KVKKEEAAAA APVPRRMSSR LRGIAAESEV AKRKADEHDA ALQEAERAKR MRKSDSFSLS
     EMLVSGQKLS GESLLGVDVV TKGVAMPYQR TFSDEDIKKT TDKDLKALRE EMSGLGLWDA
     WEPNRIKLTP ERIYAMTFHP SESKPLIFAG DKMGHLGVLD ASQTKPVSAA THDEDEEDDD
     DDPDPVLTTL KPHTRTISCM TIHPSKPTHL YTASYDSSIR EMDLEKTTSV ERYAPASTAD
     DVPISGLDMA LDDPHCLYWT TLDGEFGRYD MRTPRQDSAT RWTLSDKKIG GFSLYPTHPH
     YFATASLDRT MRLWDLRKLS HKSPVAVGEH ESRLSVSHAA FNGAGQVATS SYDDSLKIYD
     FGAKGIASWK PGHSLSDAQM KPDVVVRHNC QTGRWVTILR PQWQQNPQSH IQRFCIGNMN
     RFVDIYSGSG DQLAQLGGDG ITAVPAVAVF HRSKNWVAGG TASGKICLWM