ID A0A482X0V7_LAOST Unreviewed; 1272 AA.
AC A0A482X0V7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=XPG-I domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LSTR_LSTR001018 {ECO:0000313|EMBL:RZF39497.1};
OS Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Criomorphinae; Laodelphax.
OX NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF39497.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF39497.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF39497.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:RZF39497.1};
RX PubMed=29136191; DOI=.1093/gigascience/gix109;
RA Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL Gigascience 6:1-12(2017).
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:RZF39497.1}.
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DR EMBL; QKKF02019844; RZF39497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482X0V7; -.
DR STRING; 195883.A0A482X0V7; -.
DR InParanoid; A0A482X0V7; -.
DR Proteomes; UP000291343; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; PS00841; XPG_1; 1.
PE 3: Inferred from homology;
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:UP000291343}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 861..930
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 299..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1255
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1272 AA; 142364 MW; 7DD648B4CB0A99A1 CRC64;
MGVHGLWKLL DPVGKPIPVE TLENQVLAVD VSIWLHQLMK GFQDSTGSTV PNAHLVGLFH
RICKLLFFRI KPVFVFDGGV PTLKKKTIAN RNQLKDRAAI ASEKARQQLL KNLLKQRAVG
QVLQDLKAKP GALGSSQRQP DLYELPPIAE EIDNSEDSDD IKECSSSSED DYKKKKKYKD
LHTIDVKSAE FKALPADIRH DILTDLKETR KQNSWGRIHE LPEDMGGFSS YQMNRLLKRR
SVQVSLEEAE KEMGGHTLSL GDIEMLLTEQ GVDTASSVAG RRIASDNVTR YVYANELLKE
GKQPNSKSSG PKSSDVSKKN DEWEDEDEIM IIDDEIICTG AIKVKTEKED ESESLKNPLS
ETMQKIKVEE ESDSSESAIF EDIVKEEMEL RKQFATDDMG ISQEQILLLI KEQKDSSKAK
DLERFSEPST SKEHEDTRFV EMRLNDSDHQ AAESDHDDDT IAKDSQSKNP DYEVVDSDQI
DKSGNNVEKG KFDVSRIQSS DKRDCRMENK EVLQRKDEFS SMTGDWERDS NSGIIKDVAT
PRISLKGSAR DQENVQDVDN SSSVESLLIN KGDLPVVVSE DNKDKSESIE TSQQAKEKSK
FDAESHEITV NSQKKAVDCN SDPHQSNKSN NTKTDDNSLD LITVSTGKKE DDSKVDRDSL
EITVNTQKSA GDEGEDIFAD IFSSDLKESG ENIAKLLEKE GKRDVVEDVE LMSSGTSCSD
DVINEVISGD DTSLDDSEEV DKTNHKNSEE ESRTDDENGK PHSSQYFKSS ESNLKESSEI
SPETAAANRE ENSENVPNNE EGGQTEVDEP KKRILSTKEL RGLQSILEKQ EVELIQVQGR
EERLASTVTE QMRLEAEELL QLFGLPWIKA PMEAEAQCAF LDLVGLTQGT ITDDSDIWLF
GAHRVYKNFF NQKKYVLQFR SDDIKSFFKL SRGDLIELAL LVGSDYTVGI NGIGPVTALE
IISTFRPPNS SGESILNTLQ AFKDWLQHPS NSQTSQLARK LKDVELDEGF PSKDVVDAYL
KPCVDESEEA FSWGSPDVDG LKSYAQRKFG WSPNKVDELL LPVIKSLTQK TSQTRIETFF
NMRPAIPQHN DRVSRRVQRA VERMGGAGEE EEEEALAGGR RRRARHLLAE ESDEGSAARG
RRGRGGGKRG RGGIRDEIRT ATEKDRFRSR QPRSKPKPAP LPLVTVIAGP SSAPADTRQA
TSTEFRHMPK PTAAPPREEL IPQRERDRLE GLKRKIQAIQ VLKSKKKKLK KVSRAPIKRQ
ANLSESSGSS SD
//