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Database: UniProt
Entry: A0A409Y8C0_9AGAR
LinkDB: A0A409Y8C0_9AGAR
Original site: A0A409Y8C0_9AGAR 
ID   A0A409Y8C0_9AGAR        Unreviewed;      1210 AA.
AC   A0A409Y8C0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=XPG-I domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CVT24_009350 {ECO:0000313|EMBL:PPQ99161.1};
OS   Panaeolus cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX   NCBI_TaxID=181874 {ECO:0000313|EMBL:PPQ99161.1, ECO:0000313|Proteomes:UP000284842};
RN   [1] {ECO:0000313|EMBL:PPQ99161.1, ECO:0000313|Proteomes:UP000284842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2629 {ECO:0000313|EMBL:PPQ99161.1,
RC   ECO:0000313|Proteomes:UP000284842};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
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:PPQ99161.1}.
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DR   EMBL; NHTK01001368; PPQ99161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A409Y8C0; -.
DR   STRING; 181874.A0A409Y8C0; -.
DR   InParanoid; A0A409Y8C0; -.
DR   OrthoDB; 5479162at2759; -.
DR   Proteomes; UP000284842; 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; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
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   Reference proteome {ECO:0000313|Proteomes:UP000284842}.
FT   DOMAIN          1..57
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          811..880
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          113..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1064..1210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          770..801
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        122..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1210 AA;  133771 MW;  8B2A5D7F8466409E CRC64;
     MRDKEGRGLV NAHVLGFLRR IAKLLFYGIK PVFVFDGGAP ALKRATLNER KKKKAGAALN
     HAQLAEKILA AKLRREAIQH ASGSKNSGKQ KANDVPLDDS TVYLEDIDHS RSKTPKKAKA
     VHVPSSSEKK KTFHDHDPYN LPDVDLEAAV SQRTQVAATA DPRLATEDEL HAFLASITPE
     DLDITSPEFH TLPTSIQYEI IGDLRLKSRQ TSHARLQKML RSSQTPLDFS KAQIAHLKER
     NQLTQRLLMT TDSIGSAHIA IPVRIASERN REYVLVKNGG MEGGWILGIR DLRGTEEQPI
     VLDHGDGGNQ PIKPNEIVED DSDADMEEVP IADPDLLAYQ REMALDGIAK RSGSNRRTIP
     TSMFLDDTNS NDLSSSGTQG KSQHIQDDDD DDVALAIQQS MEHAKATQLS LEVKSKEVAE
     TGPEETVDDD DDIYVPYSDF TPLGTALSFA NASSRPHSSP SKSFGPGATT TSSSPAAQVP
     TQSTSMFSFK GTGLLGTRNE TNTDNPRSNT QVVDSATHRE QQEMDTLLTQ TNRLFQEHES
     DSSDDMEEVP FPVPASTTFT MTSTVDQKRE AVSIDSDDSN DDMEEVTIES PMHPQQIPVS
     STKSGSEHPS FSNDTQLDLG GTSPSGVTES GMTFADPGLE AIEISVPIIR KSLPALHQHG
     QKGTGVTDDH PQPLPAPAFK NTSISKNLTS GASTDVPSTL QHSESNKGEE SDQDEELIPW
     SRSPSPQRGA QGDQVETADH AAWDAAEEMD LHAEEGEFAM FLSQVKGKTL ESIQQEIDDE
     LQKLNQQRRA AMRDAEDVTQ QMITQIMIML RLFGIPYITA PMEAEAQCAE LVSLGLVDGV
     ITDDSDVFLF GAQRVYKNMF NQSKTVECFL SSDLSRELGL TRDTLIQLAY LLGSDYTEGL
     PGVGPVVAME LLKEFPGRDG LFRFRDWWLA VQSGKDNDHG QSTFRRRFKK RFKDLYLTSD
     WPNTAVRDAY YHPTVDSSEE PFKWGLPDLD GLHQFLHQEL GWQQDKVDEL LLPIIQKMNK
     RREAAAANQQ GVLNEFLDIS GSGTHAPRQR QAYASKRLQQ VISDFRKRQN RGSVSPGSDE
     NMVEEHPDSV PKPATKKRRR KSPTPKSSDS APSKKPKKPR ATKSKKRRVS PDPLDDSSSY
     SDTEDYEANA TRNTQAENPL EADRRVALNL RPRPKPRPTY KGSVHQGGDE EAQPPTMRAS
     SPDVIEQPQL
//
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