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
//