ID G0WFS1_NAUDC Unreviewed; 367 AA.
AC G0WFS1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 13-SEP-2023, entry version 50.
DE RecName: Full=XPA C-terminal domain-containing protein {ECO:0000259|Pfam:PF05181};
GN Name=NDAI0I00630 {ECO:0000313|EMBL:CCD26632.1};
GN OrderedLocusNames=NDAI_0I00630 {ECO:0000313|EMBL:CCD26632.1};
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:CCD26632.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD26632.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPA family. {ECO:0000256|ARBA:ARBA00005548}.
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; HE580275; CCD26632.1; -; Genomic_DNA.
DR RefSeq; XP_003671875.1; XM_003671827.1.
DR AlphaFoldDB; G0WFS1; -.
DR STRING; 1071378.G0WFS1; -.
DR GeneID; 11493486; -.
DR KEGG; ndi:NDAI_0I00630; -.
DR eggNOG; KOG4017; Eukaryota.
DR HOGENOM; CLU_053731_0_1_1; -.
DR OMA; HQWGRSV; -.
DR OrthoDB; 1344100at2759; -.
DR Proteomes; UP000000689; Chromosome 9.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd21077; DBD_Rad14; 1.
DR Gene3D; 3.90.530.10; XPA C-terminal domain; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000465; XPA.
DR InterPro; IPR022656; XPA_C.
DR InterPro; IPR022658; XPA_CS.
DR InterPro; IPR037129; XPA_sf.
DR InterPro; IPR022652; Znf_XPA_CS.
DR NCBIfam; TIGR00598; rad14; 1.
DR PANTHER; PTHR10142; DNA REPAIR PROTEIN COMPLEMENTING XP-A CELLS; 1.
DR PANTHER; PTHR10142:SF0; DNA REPAIR PROTEIN COMPLEMENTING XP-A CELLS; 1.
DR Pfam; PF05181; XPA_C; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR PROSITE; PS00752; XPA_1; 1.
DR PROSITE; PS00753; XPA_2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 219..269
FT /note="XPA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05181"
FT REGION 53..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 42453 MW; 2F5BBF18338241D5 CRC64;
MTPEQKARVE ANRKKALERL KKRGILNKEQ AKTIASRNAQ PVPQPVIQKL ASVSPSTNDL
RDQNRTNING NITNAQPSNS ADSNMTPAAA AAAAVPPKRP LEKIRPSIRM KDYIEYDFST
MQNSNGGYIN PQDRLNRSSE DFDYNDPDFL GSKKQKTLDD WKREQRERKA IYENMPPPEH
ISLAPKCVEC QINIEMDPVL NDVFKLQVCK SCAKEHPEKY SLLTKTECKE DYFLTDPELN
DEELFHRLEK PNPHSGTFAR MQLFVRCEIE AFAFKKWDGE DGLDKEWQRR EEGKSMRREK
KYQQQIKQMR IKTRAQEYTK KLLEKKHGIL HVHEFSEPMN GGKDEDGNDI LRRRCVGCGL
ETEEVSI
//
