ID A0A0C9ZF96_9AGAM Unreviewed; 953 AA.
AC A0A0C9ZF96;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Rad4-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PISMIDRAFT_98382 {ECO:0000313|EMBL:KIK24599.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK24599.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK24599.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK24599.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., 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:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
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; KN833715; KIK24599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9ZF96; -.
DR STRING; 765257.A0A0C9ZF96; -.
DR HOGENOM; CLU_003639_2_0_1; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000054018; 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; 3.30.60.290; Rad4, beta-hairpin domain BHD2; 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:UP000054018}.
FT DOMAIN 458..508
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 510..581
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 588..662
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 107129 MW; EAC437A970EC1925 CRC64;
MVDDIDEPEF SASEGSDEEF EWEEVHVPEE LPADSKLELE LSAPSRSIEI TLHAQPKKDD
SKKKVAAALH AQRVLRTTCH KIHTVCLLAN ARVRNRWIND ELLHARLLSL TPMNLQNAFA
MIHKSHVPDH NKRGRLFEAT VTRLVEWWAD TFFIVVPTGH IRNRTFEEVQ QEIETGSSAS
RSFDDDTDGT ERVRSVNSLM KHALIHRGSR DTSAQLFTAL CRALDIPARL VVSLQSVPWR
SSVGKHARPS SKGKALMSRE DEVDGSQDVE HSDMDEESAS ESLQQGKKRL RSVKGKEREH
PVIKLRKSKS KPTTRRGTPT LVGKSKPSDP RLTPPVFWTE VFSRADSRWL PVDPIRGIVN
KRHVFDPSGY QPEESKLSRI EDNRMLYVVA LEEDGFGRDV TARYARDYTA KVVKAQGIGS
GPPGGRKEWW ARVVQAITRP YRLNRDDLED DELHIHQLTE GMPTTLAGFK DHPLYVLARH
LKRDQVIDPP TELGKFRGEP VYPRSSVISL KTAENWMRQG RIVRPGCQPM KMVKQRAVTI
SRQREMELAV ERAKSEGHSA ADGEAMQGLY AFSQTELYKP DPIKDGVIPK NEFGNIDLYV
PSMLPGGATH IPFKGVAKIA KKLGFDYAEA VIGFEFKKRR AYPVLEGIVV AAENESAIIE
AYLEAEQDAE ERARAKRFDQ VCKRWIRLIQ GLRIRDRLQK QYGSNQVGDG PKEETRQEHW
QDAEIPESIE HDHEPGGFLT TADDVVQPFH LPSNIHQVPL STGPERSDVP AARGGVPDRR
TPVDSETPPL SPRWEAPSGT EGMDIVPDND TMRPTAYTGM VPKTMRELAE LHNNDQEESS
DAVFQSQVSS LVNAKSSGKQ SGRQLPVSGS EAPTPIASAK RTRSSRKRTR ARSQSDSGDE
ASIVLRKHAR RPDPATGDPV PTRVLRPRVP KSAAKVQEEY KMEKAHRRAV KDQ
//
