ID G2YH49_BOTF4 Unreviewed; 376 AA.
AC G2YH49;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN ORFNames=BofuT4_P023510.1 {ECO:0000313|EMBL:CCD51083.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD51083.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Multiubiquitin chain receptor involved in modulation of
CC proteasomal degradation. Involved in nucleotide excision repair.
CC {ECO:0000256|RuleBase:RU367049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367049}.
CC Cytoplasm {ECO:0000256|RuleBase:RU367049}.
CC -!- SIMILARITY: Belongs to the RAD23 family.
CC {ECO:0000256|RuleBase:RU367049}.
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DR EMBL; FQ790332; CCD51083.1; -; Genomic_DNA.
DR AlphaFoldDB; G2YH49; -.
DR STRING; 999810.G2YH49; -.
DR eggNOG; KOG0011; Eukaryota.
DR HOGENOM; CLU_040364_0_0_1; -.
DR InParanoid; G2YH49; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043130; F:ubiquitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd14281; UBA2_Rad23_like; 1.
DR CDD; cd01805; Ubl_Rad23; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 1.10.10.540; XPC-binding domain; 1.
DR InterPro; IPR004806; Rad23.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015360; XPC-bd.
DR InterPro; IPR036353; XPC-bd_sf.
DR NCBIfam; TIGR00601; rad23; 1.
DR PANTHER; PTHR10621; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR PANTHER; PTHR10621:SF0; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; UBA-like; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF101238; XPC-binding domain; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU367049};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367049};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367049};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367049};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 142..184
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 330..371
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 78..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 39815 MW; 55348A562A064180 CRC64;
MKLTFKDLKQ QKFVLEAEPT ELVSDVKEKI FKEKGWEASQ QKLIYSGKIL QDANTLESYH
IEEKGFIVCM ITKPKAAPAA SSAPKAPSTP APASAATPAP PAAPAHSSST SNTAVPATPS
PAGASIPAPQ ATPSNETTGL AMGAERSAQI AEMESMGFER SQIEAAMRAA FYNSERAIEY
LLNGIPERLL QEQQPTPAAP AAVQASSPPA AGGEDDPVDL FQAAANAGNR GGAARGRPGV
DPLGGAGAGA AAGGLGNLDF LRNNPQFQQL RQVVQQQPQM LEPILQQVGA GNPQLATLIS
QHPEQFLQLL SENADDDAPL PPGAQAIEVT PEERDAIERL CRLGFNREQA IQAYFACDKN
EELAANFLFE QPEDEE
//
