ID A0A167MSB8_CALVF Unreviewed; 954 AA.
AC A0A167MSB8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Rad4-domain-containing protein {ECO:0000313|EMBL:KZO97015.1};
GN ORFNames=CALVIDRAFT_536481 {ECO:0000313|EMBL:KZO97015.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO97015.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO97015.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO97015.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV417281; KZO97015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167MSB8; -.
DR STRING; 1330018.A0A167MSB8; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000076738; 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:UP000076738}.
FT DOMAIN 489..539
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 541..603
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 610..684
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 954 AA; 106975 MW; 5F54F902C940138D CRC64;
MPPKRSKRLQ PIVTGQAASS SSAALTRHQR SQTGMDGLDS AVVKSSTGAP ASSQDVQEGS
EDETEWEEVD VEAGLAPLQT PIEVEIAGPS RPIEVTINRQ KRSEEEVRKR AAANAERLYR
LEAHKLHTLA LLANARIRNR WLNDPLLQAR LLSLTPLHLQ TAFIAITKRN QPDVIRRGRM
FETAIVRLTA WWNSMFEVED DKGIRSRTWH EVQSTNSELI SDRKGKGREA PLLHDDDPIR
STKSLMKHAL MMKGSRDISA QLFTALVRAL GVPARLVTSL QSVPWQSMKK YASNSSSKAS
QRAGVAGNYS GSDGIRSPAS PAQLGEWSVN GLASESDAAS SVAKKNGGAR RSLVMRQKSW
APSDSRSVTP EPAGLSDLPV FWTEVFSRPD QRWLPVDPVR DLVNAKRKFE PQSVDRRNRM
VYVIAFEEDG HARDVTARYT RQFGARVMKS RPPSRPGSDW WDDAMKPLTR PYRFHRDDVE
DAEFQANQSA EGMPNSVAAF KNHPLYALER HLRREETIHP RTQVGTFRGE AVFHRKFVLA
LKTAENWMRQ GRKVKEGEHP LKSVKQRAVT LEKRRAQEMA QMDGEEVTQG LYARWQTEVF
RPDPVVDGRV PKNAFGNIDL YVPSMLPYGG VHLPYKGIAR VAKGLGFDYA EAVVGFEFRK
RRAVPILEGI VVAVEHEETL LEAYWETAHI AEEQERSKVR DRALKRWIRL IQGLRIRQRL
QTQYSTDRTN AAPGSGVTDN DDDDRREAGG FLTSVADVIQ PYHLPKAVSY VRSAPPAPMN
DLQDNSDHWQ RDNSYLADSI ALSPTPHSDN LSLNDGKALQ QSPISRRTPH LKTVAQLAAE
EMHPPLGFMD LQKQEDSPDS RPLEKALQKA DRNEATAAPE RAGKRRRSAV GPTSPSETST
AKRSRRQPAQ KNNVPSPSTR ALRPRKQKAA DIIRAEKELE EAIRRAAEES EGEV
//
