ID A0A1G4J9F1_9SACH Unreviewed; 679 AA.
AC A0A1G4J9F1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=LAMI_0D02388g1_1 {ECO:0000313|EMBL:SCU86507.1};
GN ORFNames=LAMI_0D02388G {ECO:0000313|EMBL:SCU86507.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU86507.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|EMBL:SCU86507.1, ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU86507.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT598463; SCU86507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4J9F1; -.
DR STRING; 1230905.A0A1G4J9F1; -.
DR OrthoDB; 1779469at2759; -.
DR Proteomes; UP000191024; Chromosome d.
DR GO; GO:0004520; F:DNA endonuclease activity; IEA:UniProt.
DR GO; GO:0006281; P:DNA repair; IEA:UniProt.
DR CDD; cd09870; PIN_YEN1; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
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:SF54; FI23547P1; 1.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR Pfam; PF00867; XPG_I; 1.
DR PRINTS; PR00853; XPGRADSUPER.
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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000191024}.
FT DOMAIN 1..111
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 164..242
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 466..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 77948 MW; C2E6ACE174B869C1 CRC64;
MGSPTLWEAL KRNTYHRRIP FKLFVDEFRQ AHRRTPKIAI DAYSWLFECG FIKNLGEGVE
DKYHRTVELA LVSLLSRLKL FISLDITFVL VFDGPRKPSF KNQFKLKKLD AGEQVQDLSA
TDYGVEKDVH DGLHYISTNC YDGATYAYQC FPDQSVNLVR KVLNALNISF VDACGEGEAE
CSRLQKEGLV DFVLANDSDV FVFGATKVLR NFSKFWDDVP ATYRASKSGK DTREYMLTIF
DLDRNSDWNQ ASATLFCVLL GADYNQGVRG LGPKKSTDIA LHKMPCFADE LAEIFKDFRK
NANDRRAQYE AFKTGLFNYC RAESKRLFGR KYFSEETEGF KGWPSDTAVM FYMHPLLNPE
LPLFCFKPGF VNVSGKANMP EVRFRELETI LMEKEYRRIS DLTRWLHEWA HEAFLLKKIL
YEKDNADELT KATKIVEEWM CQLCDKNFSV PCWRIRYNTF LSGVRESANS DSNGLKEPNS
TTHSSPRRRS PTRRQIDKAA YKFMTSIPKN LIDDSHILVE AYQKAKEALT STSPSKRSPR
KRELSQKNNL DDFLKLHTSP RKPAFQEHTQ KEHFAPHEKV FLDAGPSLFV PDEPEPEGND
SSLIILAEHD LDEQPQKETK VADSPKRKLL LSSPATSDND TSPLKKHKQI QGALDFGFTK
RQLFHGLVDL TAEDDESVH
//
