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Database: UniProt
Entry: A0A482X0V7_LAOST
LinkDB: A0A482X0V7_LAOST
Original site: A0A482X0V7_LAOST 
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
//
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