CMR1_ASPFU
ID CMR1_ASPFU Reviewed; 527 AA.
AC Q4WLU1;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=DNA damage-binding protein cmr1 {ECO:0000250|UniProtKB:Q12510};
GN ORFNames=AFUA_6G12330;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000006; EAL89073.1; -; Genomic_DNA.
DR RefSeq; XP_751111.1; XM_746018.1.
DR AlphaFoldDB; Q4WLU1; -.
DR STRING; 746128.CADAFUBP00007635; -.
DR EnsemblFungi; EAL89073; EAL89073; AFUA_6G12330.
DR GeneID; 3508416; -.
DR KEGG; afm:AFUA_6G12330; -.
DR VEuPathDB; FungiDB:Afu6g12330; -.
DR eggNOG; KOG4328; Eukaryota.
DR HOGENOM; CLU_017019_1_1_1; -.
DR InParanoid; Q4WLU1; -.
DR OMA; TVVRHNC; -.
DR OrthoDB; 753973at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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: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; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
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..527
FT /note="DNA damage-binding protein cmr1"
FT /id="PRO_0000351099"
FT REPEAT 185..226
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 249..289
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 296..336
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 341..381
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 388..427
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 450..493
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 496..527
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 32..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 58445 MW; 13C8B1B6C8B4CE90 CRC64;
MGADNELSEF EKQRLANIAE RDALLKKLSL DAQSSGLFPP KSARSSPGGQ TKPKKKPPPK
KVKKEDEHPV PRRMSSRLRG LAADSEVAKR KADEQYEAAQ QAERAKRVRK SDAFSFSEML
VSGQKLSGDS LIGVDVVTKG VAMPYQRTFG DEDIKKTTDK ELKALREEMS GLRLWEAWEP
NRIKLTPERI YTMTFHPSEA KPLIFAGDKM GNLGVLDASQ EKPTSAVKQE DDEDAEDDDP
DPVLTTLKPH TRTISSLHIH PSKPTHLYSA SYDSSIRELD LEKTTSVEKY APESTSDDIP
ISGIDMAPDD PNTLYWTTLD GAFGRYDTRA SRRSAVATWQ LSEKKIGGFS LFPTHPHFFA
TASLDRTMRL WDIRKLSHDD PVPVGEHVSR LSVSHAAFNS AGQIATSSYD DTLKIYDFGS
KGIAAWEPGY TLSDAEMKPD TIVRHNCQTG RWVTILRPQW QANPQSSIQR FCIGNMNRFV
DVYSSSGDQL AQLGGDGITA VPAVAVFHRS TNWIAGGTAS GKICLWM