ID M3JSN0_CANMX Unreviewed; 960 AA.
AC M3JSN0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA repair protein RAD2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=G210_3981 {ECO:0000313|EMBL:EMG45815.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG45815.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG45815.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC {ECO:0000256|ARBA:ARBA00005283}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG45815.1}.
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DR EMBL; AOGT01002318; EMG45815.1; -; Genomic_DNA.
DR AlphaFoldDB; M3JSN0; -.
DR STRING; 1245528.M3JSN0; -.
DR eggNOG; KOG2520; Eukaryota.
DR HOGENOM; CLU_003018_0_0_1; -.
DR OMA; PNSMDFS; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004536; F:DNA nuclease activity; IEA:UniProt.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd09904; H3TH_XPG; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR PRINTS; PR00066; XRODRMPGMNTG.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 708..777
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 320..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 631..698
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 326..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 111791 MW; 33546BD85DD2FC8E CRC64;
MGVHSLWQIV GPSARPVRLE ALSRKKLAID ASIWIYQFLK AVRDQDGNSL PQSHIIGFFR
RICKLLFFGI LPVFVFDGGV PTLKKQTINQ RRERRLKNET STRETAQKLL AIQLQRQAEN
AMNSTRKKKR MINIGDNDDY DDDDDDIVFL EDLPGNKKTN DNSTESNSIR FRKDDEYHLP
TLTEFKVRRG DERIMHDDEL REEYEDFDHV DGININEVDP KSKEFTELPI ATQYMILSHL
RLKSRLRMGY RKEQLEELFP DSMDFSKFQI QQVQRRNFYT QKLMTVTGMD ADSTVSRRIA
GDKDRKYMLI KNDDGWTLSL GEKDGEPVNV TKDNDDDRED ITREVQAYEK QEKEDDSDSD
FEDVPLEDKP ETEEEKNYQK ALIESLYDQY AEKEPPKTTI DSYNEEELKK AVEESKMDYY
KLKEQEDKLE DDGMFDLGSS MLFSSNITAP KPEDKPKVIE SKPVEHKPTT TKNKVTSTEL
GRSFLFNADD HKTGKIELKK NEPVYEPEES EPEEPEIQAS IVEQNEKPTG QQALPEWFQG
EVKSTLNPHN EKFVTYNGLE IQKRKHQEDE DAGLIPWNEA REFLNEEENE EQETEKLEEV
APQEFRIDEK IEDDIEDESD TEQRKAAVID YQFEEEEEQD LMHQLQQEER DHEALKNQIR
TSTNFPISSS IETRITEEQL LREKLQKAKR DSDEVTETMI NDVQELLKRF GIPYITAPME
AEAQCAELFK IGLVDGIVTD DSDCFLFGGD KIYKNMFEQK KYVECYMQDD LSSKMGLTQH
KLIELALLLG SDYTEGIKGV GPVLAMEILA EFGDLNKFKE WFDLHTKTHA DSSNPTTLEK
NLLSKIKKGN FFLPDSFPDN IIEQAYINPE VDSDKTQFKW GVPNLDQIRS FLMYNLSWDQ
SQVDEVMVPL IREMNRRKAE GTQSTIGEFF PQEYIQSRKE LNLGKRMKTA ANKLKKKKKV
//
