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Database: UniProt
Entry: A0A232LRT4_9EURO
LinkDB: A0A232LRT4_9EURO
Original site: A0A232LRT4_9EURO 
ID   A0A232LRT4_9EURO        Unreviewed;       876 AA.
AC   A0A232LRT4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Rad4 beta-hairpin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Egran_05495 {ECO:0000313|EMBL:OXV06738.1};
OS   Elaphomyces granulatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Elaphomycetaceae; Elaphomyces.
OX   NCBI_TaxID=519963 {ECO:0000313|EMBL:OXV06738.1, ECO:0000313|Proteomes:UP000243515};
RN   [1] {ECO:0000313|EMBL:OXV06738.1, ECO:0000313|Proteomes:UP000243515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSC145934 {ECO:0000313|EMBL:OXV06738.1,
RC   ECO:0000313|Proteomes:UP000243515};
RX   PubMed=25753751; DOI=10.1111/1462-2920.12840;
RA   Quandt C.A., Kohler A., Hesse C.N., Sharpton T.J., Martin F.,
RA   Spatafora J.W.;
RT   "Metagenome sequence of Elaphomyces granulatus from sporocarp tissue
RT   reveals Ascomycota ectomycorrhizal fingerprints of genome expansion and a
RT   Proteobacteria-rich microbiome.";
RL   Environ. Microbiol. 17:2952-2968(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the XPC family. {ECO:0000256|ARBA:ARBA00009525}.
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:OXV06738.1}.
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DR   EMBL; NPHW01005460; OXV06738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A232LRT4; -.
DR   OrthoDB; 181129at2759; -.
DR   Proteomes; UP000243515; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   Gene3D; 2.20.20.110; Rad4, beta-hairpin domain BHD1; 1.
DR   Gene3D; 3.30.70.2460; Rad4, beta-hairpin domain BHD3; 1.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR   InterPro; IPR018327; BHD_2.
DR   InterPro; IPR004583; DNA_repair_Rad4.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR   InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR   InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR   InterPro; IPR042488; Rad4_BHD3_sf.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   PANTHER; PTHR12135:SF0; DNA REPAIR PROTEIN COMPLEMENTING XP-C CELLS; 1.
DR   PANTHER; PTHR12135; DNA REPAIR PROTEIN XP-C / RAD4; 1.
DR   Pfam; PF10403; BHD_1; 1.
DR   Pfam; PF10404; BHD_2; 1.
DR   Pfam; PF10405; BHD_3; 1.
DR   Pfam; PF03835; Rad4; 1.
DR   SMART; SM01030; BHD_1; 1.
DR   SMART; SM01031; BHD_2; 1.
DR   SMART; SM01032; BHD_3; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243515}.
FT   DOMAIN          515..574
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01030"
FT   DOMAIN          576..639
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01031"
FT   DOMAIN          646..720
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01032"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          811..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..842
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..876
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   876 AA;  98472 MW;  EB6A294F0D6890AB CRC64;
     MPPFVSRKRS LSPAPPPPKR AARTPFYQKV IEICDSSDES SLSDLPSSEN EDSESKGIEE
     GEKRNQEEDH DGDGDDSEDA VDWEDAVAAS KPTSHEPPGE DLELTLDKTA VHLSDLLDGR
     KAPSRIEREI RINTHRLHVQ CLLFHNALRN AWINDPEIHT ILLRQLPAGI QKEIQLWRAA
     SALEPLSQSP CKPSHDKKGR RQARSDRTWN DEAYRAEPDQ PDMSHGDPLI SLLRVLAAYW
     KKSFCITAPG LRKRGYCPIS VLEEDTSTFQ RGEHDPVRHG ERIQSKEEFR TLAESRQGSR
     DVGAQLFTAL LRALGIEARL VASLQPLGFG WANAEVYQTS PVIESSPVEN SDDEIGGSLT
     KDENASYDHD LPFPIYWVEA ASPVTHRIIP VDPLVLSNSV ATTPDQVAAF EPRGSRAAKA
     KQVIAYVVAY SADGTAKDVT TRYLRRRTWP GKTKGSRLPV EKITVSQSRA TTRYIEYDWF
     RVTMRGYTRQ IDRRTKVDEI ENAQDLVPNQ PERKTATGEA DTLQNLRAST EFVLERFLRR
     EEAIRPGAQH VRTFISGRGN KTREEKVFRR ADIVKCLSAE SWHKEGRQVR AGQVPLKRVP
     IRVVTLLRKR AVDELERQTG AKPLQGLYAR HQTEVIIPPP IENGVIPKNE YGNIDCFVPS
     MVPHGAVHLP WGGTARVCKK LGIDYAEAVT GFEFGSKMAV PVIEGVVIAE ENGDLVRDAW
     RVDQEARHQR QRLQQEKRIL QTWRKFLMGL RITERVRAEY GEDGDVETMN PFAIRPSVRA
     EPTATVDHGG GFLLPGDDDD NATLVVERPG TAAEIGESRA RGQEQQRNNY SVRHREEVES
     TSGNAPERIG HFLSNENDDS SNDDDGEDDY EEVEDD
//
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