ID A0A1E5RLK8_9ASCO Unreviewed; 1049 AA.
AC A0A1E5RLK8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=DNA repair protein RAD2 {ECO:0000313|EMBL:OEJ87782.1};
GN ORFNames=AWRI3578_g2291 {ECO:0000313|EMBL:OEJ87782.1};
OS Hanseniaspora opuntiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=211096 {ECO:0000313|EMBL:OEJ87782.1, ECO:0000313|Proteomes:UP000095605};
RN [1] {ECO:0000313|Proteomes:UP000095605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3578 {ECO:0000313|Proteomes:UP000095605};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
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 -!- 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:OEJ87782.1}.
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DR EMBL; LPNL01000004; OEJ87782.1; -; Genomic_DNA.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000095605; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004536; F:DNA nuclease activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; 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 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 4: Predicted;
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}.
FT DOMAIN 1..110
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 799..868
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 321..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 712..744
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 321..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 120754 MW; 877DCDB349A783E2 CRC64;
MGVHKLWTLL EPSSKPVKLD SLNDQVLAVD ASIWLYQFIT ALKHQKSKNN SGEFSLEENN
VFVNAHLIGF FRRICKLLHY GIKPIFIFDG EVCELKKNTI MERKKRKEGN RESSKDVARR
ILAMQLLKKN MKKKKDTTTE VDESNQNDIN KHMTQRNSEW ELPEQNTIPT EYDDGRLAAI
DEYEKTVNQM EDELQGIDLE SINPASKEFN NLPKSTQYMI LYALRSKSRL RMGYSMEQLK
AMFPDPVEFS KFQIEMVKRR NFFSQKLLDS TGKHGNSMVT TGKVSGTKKM YMLIKTNNGW
AMSLDNNDGS TKETAIDITN DEIEKIKHEQ NNDKKDSDSE DWEDVDLDAG KXXEEVVEDY
SIKALLDATK NRLREKTPKK TEAXDIDEVK FEVPYFNTXN LTXLNDEETN NVSLNKIVQK
XEPEEFEEXE LESEMIKPLK KKQKVMNFNL FDDNKDEKST SFINLVDDHV NVNTPHIIDL
SDDNVDTKAS KDTEKSTGDN KDDSYDNVIL PAGXKELENV LHEKEEAVVX SDKSPSNTTN
LSQKEDVSPI TLNNQSNDLS DVESEKKEAS SSESSVDFIX VESEKEEKQE NLXQSSDDIV
DVENVNEKPQ YDSIDYSAND AADNNQDDNK TVEDSVKSQI KDTHXIDDHH ELKKEKSTGI
FDLEEEDDDQ ELGITKDFVD TKLXKVDDSX DDFLEVADME NNAAEEKKIN QYEFFEDDEE
DLVQQMDKEE EDYRDLVHSK DESQXNQVFV XDGNTAVTEN TPHNDILGYS QLISRYRKLQ
RDAEEVTPQM VEEVQELLQH FGIPYLTAPM EAEAQCAELM RLELVDGIIT DDSDVFLFGG
SKIYRKMFQE KQFVEFYDLE AIYGTLGLSR DFLIDLAFLL GSDYTLGIKG IGPVAAVEIL
ANFGSLEKFK EWYNDGMHNS EKIADEKGFE KALRKKLTSN NIILSEKWPY ADVIKEYKSP
TVDKDETPFK WGKPDLDRLR TLMRNYLSWT DEKTDEVLIP LIKEMNSKSK KTKQRKLTDF
FPVDYSLHSY EXLSSRLKKA VEKLKEMKA
//
