ID G0WDE8_NAUDC Unreviewed; 427 AA.
AC G0WDE8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN Name=NDAI0G00330 {ECO:0000313|EMBL:CCD25809.2};
GN OrderedLocusNames=NDAI_0G00330 {ECO:0000313|EMBL:CCD25809.2};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD25809.2, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD25809.2, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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; HE580273; CCD25809.2; -; Genomic_DNA.
DR RefSeq; XP_003671052.2; XM_003671004.2.
DR AlphaFoldDB; G0WDE8; -.
DR STRING; 1071378.G0WDE8; -.
DR GeneID; 11497205; -.
DR KEGG; ndi:NDAI_0G00330; -.
DR eggNOG; KOG0011; Eukaryota.
DR HOGENOM; CLU_040364_0_0_1; -.
DR OMA; PHMLEPI; -.
DR OrthoDB; 158575at2759; -.
DR Proteomes; UP000000689; Chromosome 7.
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; cd14378; UBA1_Rhp23p_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; 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; 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|RuleBase:RU367049};
KW DNA repair {ECO:0000256|RuleBase:RU367049};
KW Nucleus {ECO:0000256|RuleBase:RU367049};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 2..77
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 168..208
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 384..424
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 117..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 44872 MW; BA1900FDD10D2478 CRC64;
MVNVIFKDFK KEKIPLDLEP SNTILDVKSQ LAQAKACEES QIKIIYSGKV LQDGQTVEEC
QLKEGDQIIF MISKKKSTVT KVTEPPAAAA AQAQAPGANP EITTASNSAT PGLIETAAAS
GTPEGTPQTG NDTTASASAN TATDAGAPAT TTAATELSPS SAGFVTGTQR NETVERIMEM
GYEREEVERA LRAAFNNPDR AVEYLLMGIP ENLQQQHQQQ QQQPTQASPQ NIANEGSATA
TATGDDAHAE EPPAEDDLFA QAAQGSGNAG SAGSAVGGST GEGTPGSIGL TIQDLLSLRQ
AVSGDPESLS SLLENLSTRY PQLREQIMSN PQTFISMLLE AVGDNLQSLE GLGDIGGDLG
EINEGDNDTM GEASAAPPTI QLTPEDEQAI SRLCELGFER SLVIQVYFAC DKNEEIAANM
LFSDYAD
//
