ID A0A1B9H0J3_9TREE Unreviewed; 1380 AA.
AC A0A1B9H0J3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=DNA excision repair protein ERCC-5 {ECO:0000313|EMBL:OCF36785.1};
GN ORFNames=I316_01381 {ECO:0000313|EMBL:OCF36785.1};
OS Kwoniella heveanensis BCC8398.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF36785.1, ECO:0000313|Proteomes:UP000092666};
RN [1] {ECO:0000313|EMBL:OCF36785.1, ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|EMBL:OCF36785.1,
RC ECO:0000313|Proteomes:UP000092666};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI669494; OCF36785.1; -; Genomic_DNA.
DR STRING; 1296120.A0A1B9H0J3; -.
DR Proteomes; UP000092666; 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; SM00726; UIM; 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 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:UP000092666}.
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 161..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..820
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 150980 MW; D2561CB83F7E9369 CRC64;
MGVKGLWSLL NPVARPVQIE SMEGKRLAID SSIWLYQFQA TMRDKDGRVL VNAHVLGFLR
RINKLLFHGI KPVFVFDGGA PALKRATIAE RKKKKSGAAA NHAKVAEKLF AAQMRREAVK
AAQAMEEQRA ARNAAASAAQ YPDEAGEQIA EDVIYLEELE NQAGPSRPRP TPIERTSSSS
APIRPSTPVG EVPTDPEKRR KHFKKHDPYR LPEADMPTVS TNEKPDARLA TEEELKQFID
EVGPGDIDVE SAEFRALPTE VQYEIIGDLR SRSRQQSHRR LTDMLRAAPT ALDFSMAQIK
HLSQRNALTQ QLLTVTDMVG KAHLTIPVRI AAERNREYVL VKKGEDEGGG WVLGIREGTK
EKPIAVEDDV KSNNGSESES ESDDSDIQEI ESPRLAPVDP DLRAHRRREM LEAIARRYAP
KRPTKAPLDI AVRPFGASRT ETSKPLFDKA VEEEEDDEIV PTANDEALAL ALQQEELGSD
EEEVDEDLAR ALALSRREIE RRERSVTQEA DWETKSESGE DEDMEEVELV PSGATTPALE
TTPRPVDDSD EDEDLEEVLT DSEPSRQVSE SAIAAVEDPP IVTARQTVAK TKSAGVAPHR
LISPAVIEID GDEEEEDAPL FLETHRNSRV TIPSHDPLPS SKTAPPVPSR QIPVHSQPSS
QTPGSEVFSE FQLIPELQPQ TLESTPKSTP LLSPQPIESS PAKGARLAIP SPTSTPPTEV
PKANLTLPPT SSPARPQPIQ RFPSAIVRPS PLRKVTQPAS SPITIDGEVE EEALLAKSPE
HLETDRVSPA PTPAIFPLPS KPPVPRRMSL PPPSPRQQPP ESSTSPSQTP DEHIPPNPSR
PPLFQSVSTE DDASEDDGDA DDGRSIEWSK SPSPVPRPAL QPTDSSTTIP SEVEDQDGDI
TTGDMAAEED DYARFIAQIK GRDLNEVRTE IDDEIRVLNS ANKVAMRDSD EITQSMVTQI
QTLLRHFGIP YITAPMEAEA QCAKLAELGL VDGIITDDSD VFLFGGTQCF KNIFNDAKYA
ECFLSTDIER ELSLNRDRLI SLAYLLGSDY TIGLPGVGPV VALELLANFP GERGIDNFKE
WWMKVQRGMD TPQESGTKWR ISFKKRYAHT IYLTNDWPNP LVREAYKYPT TDESEEPFHW
GFPKLSALRT FLHEELSWSI TKVDDELTPI VQRIARRGKM GALNKQGILD PFFDTSVVAG
NYAPRRRTTA NVSKRLMAVI KSFREAEATV NGNGNGTGEP PKTEWGEMMA GLDEEDPKGR
GTGKRRNTGS MSVEGDGNGA GVKKRRLSSA SAISRGRKRA GTNASSVSVA ESTGSTESSV
SVSVSAGAGA GANGRGRGRG RGGKARGRGR GRGGTASASR SASARASHSP DIEPIEVLDD
//
