ID A0A0C9WW61_9AGAR Unreviewed; 1038 AA.
AC A0A0C9WW61;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Rad4-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=K443DRAFT_10332 {ECO:0000313|EMBL:KIJ96835.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIJ96835.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIJ96835.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIJ96835.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPC family. {ECO:0000256|ARBA:ARBA00009525}.
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DR EMBL; KN838709; KIJ96835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9WW61; -.
DR STRING; 1095629.A0A0C9WW61; -.
DR HOGENOM; CLU_003639_2_0_1; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000054477; 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:UP000054477}.
FT DOMAIN 477..531
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 533..611
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 618..692
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 115807 MW; 47810A9BC9BB1081 CRC64;
MSEQDSFADA DSDDEFDWEE VEMPVHQPQE HQDFEITLQT RPKPDAVKNK GTSHAERLIR
IDCHKIHTVA LLTNARIRNK WINDPLLHAR IMSLTPLHLQ NAFATIHKSR IPDQNQRGRT
FEAALRNLVE WWSTSFFAVE QGGHIRSRTF EEIQKQLEIR GLHVKDENDP DATINYESLQ
DIVGDDGEEI RSPKSLMKHA LMRSGSRDTS AQLFTALCRG MGIPARLVVS LQSVPWQAGV
GKSKPTYQRK SQGKGKDKTG EGDFDEEMED DAASTSGIDI KGKGKAKEFT GTGQRLDGAP
VIEKSEKAKG KEKARPVINL RKTKSKGQVL GSASSSRLPS PDPTTSPPIF WTEVFSRPDA
RWLPVDPIRG ITNRRKVFDP SPAAQATSDP TKKVKTKQEN RMVYVMAFEE DGYARDVTRR
YAREYGSKVA KVQGGSASGG GGKARHAWWS RVVDIVKRPY RLHRDDLEDE ELEAAQMMEG
MPSTISGFKD HLLYVLTRHL KHNETIHPPP PGTPELGKFR GEPVYPRSSI VTLKTAELWM
RSEGRMVKEG VQALKFVKVR AGTLNKMREL EVLKDGLREA GGEERQNDHG TGGEVMQGLY
ARFQTEPYVP DPIVDGKIPK NNFGNIDLYV PSMLPKGGVH VPFKGVAKIA RKLGFDFAEA
VTGFEFKKRR AFPIIEGVVI ASENEAALLE AYWEAERAAE EKARIKREER VLKQWTRLVQ
GLRIRQRLQE QYAPKLQETQ ASTSANTQQR ADASSAAPDG DDDLQVGEEA ASTSTHAHGG
GFLVGADDVV QAFHLPKYTH VRLPSTPPPP GAVGGNDRKD LELLEAESTP DYMTYDLEMM
DVDESDLLET PNDGGMQEEE SRIPKTMQEL AEDAARKLQA IIRDQDAETV NQTRRKNLDG
GDGEYRPSPP PPPPASKKVV KITMPAGKAS STAVVTRNGG ATSNVKPKPK PKTKTRSTRA
LARKRARTRE DSDPDDSDAV EEEEKEKPIK RSRLPATSNS IPAPTRTLRP RALKTRAQIE
EERENEEAYR RAVDGYDL
//
