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Database: UniProt
Entry: A0A094IKP3_9PEZI
LinkDB: A0A094IKP3_9PEZI
Original site: A0A094IKP3_9PEZI 
ID   A0A094IKP3_9PEZI        Unreviewed;      1194 AA.
AC   A0A094IKP3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=XPG N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=V498_02216 {ECO:0000313|EMBL:KFY97147.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY97147.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY97147.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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   -!- 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:KFY97147.1}.
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DR   EMBL; JPKA01000354; KFY97147.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094IKP3; -.
DR   HOGENOM; CLU_003018_0_0_1; -.
DR   Proteomes; UP000029270; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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.
DR   PROSITE; PS00842; XPG_2; 1.
PE   3: Inferred from homology;
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};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          1..98
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          889..958
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          121..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1174..1194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..740
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..763
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1194
FT                   /evidence="ECO:0000313|EMBL:KFY97147.1"
SQ   SEQUENCE   1194 AA;  134356 MW;  A7B9F69668EC0816 CRC64;
     MGVTQLWSVL HPCARPTKLE ALNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHVVGFFR
     RICKLLYFGI KPVFVFDGGA PALKRQTILG RKRRREGRRD DATRTAGKLL AMQMQRVAED
     AEEKRKREIE VRGRPTEAVE DEELPDDQNL VYVDELGMSN QERQQSRKFV KKDQYHLPDL
     NGDISNMGQP NDPRIMSAEE LEEFARQHNS GENVDLYDFS KIDFDGDFFK CLPPADRYNI
     LNAARLRSRL RMGLSKEQLE EMFPDRMAFS KFQVERVRER NDLTQRLMNL NGMNAEDTMG
     NGRIAGERGR EYMLVKNKGV EGGWALGVVS KDRDRGERNK PIDIDALHER TQVRPNDEEL
     EDDDEFEDVP VEGLNRLPTE QARYQKQMDH IKALQLADDD IVEKEQAPTN SLFVEQDEAG
     DLFEESEHVD EEEELNRAIA MSLEKSFAAE ESEEEADFED VQMPAYEQKS AKDHRPLQKS
     SGNGLIHIVN NRANAAVPKR MATESSDEEE NLQDILAASR KQKGFAGPSA PTPSLRAAEN
     PFGSGPLPFE KLDLKKSIFS GYAKARPNKA KSTEKENEDL AGGFEREDSV EKARPLPPWL
     ASTGDIRADV KEQMAKDQRV NAEDYERRLE EERMYKRDHG VIEIESSDED SDVEIVEAPA
     PKVAVTDGRL SPSNKEKPEQ DSIASISNKP ADLSQQLAEK STPALLEDRA ETNSPSDEEP
     VEWSESDREE PSRKQQQRES SGLPKEPSSS PKNGSQPATA HEKSPSPTFE DVELHEPMAA
     VAPPTLQEQE YIFAAENDDA FNQQPAHTIS DDEFGDFSDP DDEELLAHLA LEAEEHARFA
     SSLNNKAPQF NQEDYERELK QLRNQQKKDR RDADEVSHIM VTECQALLRL FGLPYITAPM
     EAEAQCAELV TLGLVDGIIT DDSDVFLFGG TRVYKNMFNS NKFVECYLAS DLEKELSLPR
     DKLIEFAHLL GSDYTEGLPG IGPVTALEII SEFSSSDGLQ EFKDWWYDVQ HNQRPKEADS
     KSSFRKKFRK SQASKLFLPP AFPSKAVTEA YLHADVDSTP DPFQWGVPDL DNLRSFLMAT
     IGWTPERTDE VLVPVIQDMN RREAEGTQAN ITRYFDGAVG AGARAGGAVG ANKAAGSARM
     KAAVRKLKST TGGGLLNTTF ADEAAEWARK NELSEAAHVA KQQAKKGKPK SKKR
//
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