CMR1_USTMA
ID CMR1_USTMA Reviewed; 637 AA.
AC Q4PGT8; A0A0D1EDI4;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=DNA damage-binding protein CMR1 {ECO:0000250|UniProtKB:Q12510};
GN ORFNames=UMAG_00675;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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; CM003140; KIS72265.1; -; Genomic_DNA.
DR RefSeq; XP_011386478.1; XM_011388176.1.
DR AlphaFoldDB; Q4PGT8; -.
DR STRING; 5270.UM00675P0; -.
DR EnsemblFungi; KIS72265; KIS72265; UMAG_00675.
DR GeneID; 23561911; -.
DR KEGG; uma:UMAG_00675; -.
DR VEuPathDB; FungiDB:UMAG_00675; -.
DR eggNOG; KOG4328; Eukaryota.
DR HOGENOM; CLU_017019_1_0_1; -.
DR InParanoid; Q4PGT8; -.
DR OMA; TVVRHNC; -.
DR OrthoDB; 753973at2759; -.
DR Proteomes; UP000000561; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
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..637
FT /note="DNA damage-binding protein CMR1"
FT /id="PRO_0000351115"
FT REPEAT 185..226
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 255..295
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 297..321
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 361..401
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 431..470
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 556..598
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 602..637
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 70283 MW; 6C357BCC4B09B8CC CRC64;
MIESNDYEQE RLKNIRENER LMKELGVMGG SSTIGGPSSK RTTPTKPKKQ ATPKKKPDTT
PTRIMPSRSS ARLAGHEADS ETLKRKYEEE AEEARKVAEA AKRARHQPFD LSGMTGGELE
EEAIMALEST LQGLANNTSS AAELVDTKDE NKRRSANKPD PQFSTERREL EDILNKMTLK
SAAKVTPKRI YSMAYHPSTD KDLVFVGDKE GSIGVWDAAP VAFASNRNGV KTADDQDEDA
EERFPEGKAW TLQVHARSPV TCIKFDPVNH NSVLSSSYDS TVRKLDLATA KSEEIWAGEE
DVLLSIFDVL SPSTHPSVYM DTPNPSLDER SMWIADHRGG LLHIDLRERT RRGNNTRRWQ
VCEKKIGAMS VNRLAPHCIA TASLDQHIRL FDVRALASVV KQTADAPYNY KGVDADDLES
AQTKAQFASS KARQACTSVD FSPRGDQLVG VSYDDVVKVW SMEPGSLFSE HGLKNRIATA
KSNKPKGAVK KQVPDSASDT GPGLLSWLSR ATPLGTKKDV AEAIKQEQDA PSPSLSKRPD
DVLANPTRIP HNNQTGKWLT LFRAKWNQNA LLEPHFTIGS MSRRAEVYAA DGTLLRSLWD
ENLVTAVPAV TCMHPVLPAR LVTGNASGRC TFWSPDP
