ID A0A150VCG9_9PEZI Unreviewed; 1277 AA.
AC A0A150VCG9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYG48232.1};
GN ORFNames=M433DRAFT_61516 {ECO:0000313|EMBL:KYG48232.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48232.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG48232.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG48232.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG48232.1}.
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DR EMBL; JPDO01000053; KYG48232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VCG9; -.
DR STRING; 766039.A0A150VCG9; -.
DR Proteomes; UP000075602; 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; IPR003903; UIM_dom.
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; PS50330; UIM; 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:UP000075602}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 965..1034
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 338..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 921..948
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 596..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..870
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1277 AA; 143901 MW; 58C1BF3C9440B861 CRC64;
MGVTGLWQIV QPCARPIKIE TLNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHIVGFFR
RICKLLFIGI KPVFVFDGGA PALKRQTITA RKRRREGRRE DAARTAGKLL AVQMQRRAEE
EERKRADGPA REMTEVPDDG LVYVEELQMT AQERQQNRKF RKKDAYHLPE LEVSMSEMGG
PNDPRVMSLE ELQAYARQFD TGEDINVYDF SKIDYDSPFF MSLPASDRYN ILNAARLRSR
LRMGHSKEQL DAMFPDRMAF SKFQIDRVKE RNELTTRLMN INDGDTIFTA GLSGPTRVAS
EKAREYVLVK NDGVEGGWAL GVLGGDEGTK QDKAIDVDQP APTVTGDESS EDDDEGFEDV
PIEGLNRLPK RRKLDMDTND SLTKQREALY KSRRLGIQGH AGVPGLGDNP DSLFVADGRT
TFDKEERKNM NKPSERFRED LSDQDDEDLR RAIAMSLNQN FSPTRVDPNE GAQSSLDVDK
DEVRNFLHQQ AADADKPVPP GSARAIASIL NKRANNTTHD SRERASLGTC VPRADESESD
DETVDFQAAL MEVRQKKRKF SPPSPKRTPV RSSPKRGKKE TGFDGPLPFE RLDLGSSLLG
KKKKKNRTEE AEAAGGFEHP ASIEQQKRAE PLPPWFSGNL EDEMEKQRVI EREDRERAKE
FNRRFMFQSK DAPTLKRNPT GEVIDLDDEV VRPDTNTENI VVDLETGDER SLAHAISMDT
QVAMSGVVNS EPVKSADASS AKREARRVMN VPKDAPSVVN EDKAGKIEWG ESENGDSGSA
QTEKIQFPKT RTDDVHPLKR PQQLSHFDFD GGSSLEANMR SSRSVSPEFE NVDIAARLLS
SRPEVPPPEL SDDIEEDEEK EEEEEEEEEG GSVRVRDSGT VQEEYILDDD DDFSDPEEAE
LLNALSLEAE EHARFASTLN NKTKVQNIAD YENELKQLRN QQKKDRRDAD EVTHIMITEC
QELLRLFGLP YVTAPMEAEA QCAELVRLGL VDGIVTDDSD CFLFGGTRIY KNMFNQAKFV
ECYLASDLEK EFDLTRDKLI QIAQLLGSDY TEGLPGVGPV TALEILSEFE NLTEFKEWWN
GVQMNTIPKE VDNDNIFRKK FRRNATKLFL PQTFPDPRVE LAYQNPEVDN DPEAFQWGVP
DLGALRQFLM ATIGWSQDRT DEVLVPVIRD MNRRADEGTQ ANITAFFEGG VGVGAAGVHS
KGEAFAPRKK VDGSKRMGKA LGKMAERAKV KKNSNVVQNE DDQEQRVIVR EVYHAERAGC
ESGTNSLGKV RKRKGKT
//
