ID A0A2G5VL58_9PELO Unreviewed; 840 AA.
AC A0A2G5VL58;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=XPG-I domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Cnig_chr_I.g2479 {ECO:0000313|EMBL:PIC52326.1};
GN ORFNames=B9Z55_002479 {ECO:0000313|EMBL:PIC52326.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC52326.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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 -!- 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:PIC52326.1}.
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DR EMBL; PDUG01000001; PIC52326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VL58; -.
DR STRING; 1611254.A0A2G5VL58; -.
DR Proteomes; UP000230233; Chromosome i.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd09900; H3TH_XPG-like; 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; 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.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
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:UP000230233}.
FT DOMAIN 1..95
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 480..554
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 370..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..810
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 96692 MW; AAE9F94469D5D98F CRC64;
MGIVGLWKII EPTATEIPLE CLEGKKLAID VSIWIYQAQL AYPSDQPFPH LRLLVNRLSK
LLFYKIRPVF VFDGPQVPVL KRQVLESRRQ KRKNDDDILT NPKKMGKLKE IAAGGLDEDA
LSKAIKEVIS PSKKVVLNDV YKDIPSTSTN LDLPSAHQND QLVYGEIESS GEDSDDSDVI
IETPMKKEEP DQKMFPSRKM EIRNLVEKRE VMRNSRLRPD MIPQDSKSFS NFQMQRLLQR
GRLNAQIEQL AKSNTTSSGA FSSDKINVTG PDGTSHVLKY AHSDEIQEVQ PELKREFDSL
YQPPLEMTLD VFNVEYGGKK LSREVTPDDV REEIVERIEE RLIDKTERGY QSKSGMLEAI
ARKRIRQHYG TETIEDKEEE RRRRREEEQE DELIEVSDDE MDLQKVLFES ASKALDEKMA
SLKKHRPDSD DEEWDPQRND IPSTSSAAQR NLTDDYIHLD YDDDNERTPE LYRDLQEFLT
NAGIPWIEAP GEAEAQCVEL EKLGLVDGVV SDDSDVWAFG VKHVYRHMFA KNRRVQRYGE
QTAANRDNCK LFCLQREDYI SIAILAGGDY CPGLVKVGAI GALELVSEFV EKRNDQSETI
EVIENRILRL LEKAGQLFLS SPDEKRFTSR KAMMLKRHVT EANERELIEN VCSNKDAVHA
YLHPTVDDSS EKLRWRQMNI PLIRQILHQR LQWPDRTQHH EEKNSFNAFE KWNTFLQAGG
RSQMRLDRFF AQKLDSALEL KWSKKVVEAL EKIGKRTKGV SLDEEKLVEQ KEDDEIKVLE
IKKKERKPSE KKKKAAPGRG RGRGRGRGRG GAKISKTTEK KELNLSEDSS SNDSFDDFCK
//
