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Database: UniProt
Entry: G0VA22_NAUCC
LinkDB: G0VA22_NAUCC
Original site: G0VA22_NAUCC 
ID   G0VA22_NAUCC            Unreviewed;       806 AA.
AC   G0VA22;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   13-SEP-2023, entry version 55.
DE   RecName: Full=XPG N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=NCAS0B06680 {ECO:0000313|EMBL:CCC68752.1};
GN   OrderedLocusNames=NCAS_0B06680 {ECO:0000313|EMBL:CCC68752.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC68752.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC68752.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family.
CC       {ECO:0000256|ARBA:ARBA00024023}.
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DR   EMBL; HE576753; CCC68752.1; -; Genomic_DNA.
DR   RefSeq; XP_003675123.1; XM_003675075.1.
DR   AlphaFoldDB; G0VA22; -.
DR   STRING; 1064592.G0VA22; -.
DR   GeneID; 11524812; -.
DR   KEGG; ncs:NCAS_0B06680; -.
DR   eggNOG; ENOG502QVHA; Eukaryota.
DR   HOGENOM; CLU_378548_0_0_1; -.
DR   InParanoid; G0VA22; -.
DR   OMA; FYQTKVI; -.
DR   OrthoDB; 6876at2759; -.
DR   Proteomes; UP000001640; Chromosome 2.
DR   GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR   GO; GO:0006974; P:DNA damage response; IEA:UniProt.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd09902; H3TH_MKT1; 1.
DR   CDD; cd09858; PIN_MKT1; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   InterPro; IPR022039; MKT1_C.
DR   InterPro; IPR037314; MKT1_H3TH.
DR   InterPro; IPR022040; MKT1_N.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR11081:SF32; POST-TRANSCRIPTIONAL REGULATOR MKT1; 1.
DR   Pfam; PF12246; MKT1_C; 1.
DR   Pfam; PF12247; MKT1_N; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT   DOMAIN          1..103
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          183..252
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          340..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  92100 MW;  14D7487372CA740A CRC64;
     MPIKSLESYL FERGLVGSYP IESLKNATLG IDVNHYVSRL LTSKKEQFLD AIGGFPLSLK
     MYLESDLKIF KEYKITPVFV FNGSLVFNQL ESSGYFTASA AEASSSSNLD ISIPSGSPGT
     QTIKTNRELL LAQRHKGWTQ WSNLMTTSSK TYIDQPIQPQ EPFRYSTSIE YTRYQSNLIN
     YFIDHDITYQ VAPYSSWLQL AYLLEESYID AIYGPTDCLM LKNIDKFILG MEFPNKDFRF
     IEKSRVLKEF RCSQDEFVDI AMAVGNDLQP TTLPPLQIYP GSKVFDFALE MVLNTGTNFY
     AYQLSNPVKE ESAKYVLKYE KGISSLRYMP VLKDSGKVEV YMPNRPSKDK KDIKSKSPDT
     TSSSESVSDS TSSDPQIPND VHDFIAQQLP SEYYFYRSLG LVSGRLFDAI TTGVYPEEPP
     LDGGSSDSYR ELIKLSVDTF KNKEINLLTQ PINRYYQMKP IKQVKWFSPG SSTQLTNRVS
     PSIFEKTNRL VVKTDDVNKV FSIGEFINTL NESTDLSKSF VSEKVIFPNS VPKADKLFAS
     FDLLSTSFLR MLYQLEFFDF DSSKNLLKPT KWGTILLKLN ELEISANYFE SILIFLMFVK
     MNVLSLSEEL KPVVRFALSD STLRSYPQES QYVLLITRIL TLFQVDQKPT NYHGPIDKRT
     LVFREHLDFI KKNMNELYEA TIVSSLTANE FDRLSLDNNE WQKNIVRNAP FKSSSPNTLM
     AMMWEFFLQK YLHNGNVKTD AMAMVATEFG TYKSIPNLEE QFEISHEFLV QVSKVMQELT
     SVGLLKKGDQ NSFEQAVKFS EDAISG
//
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