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Database: UniProt
Entry: A0A4U0TJQ4_9PEZI
LinkDB: A0A4U0TJQ4_9PEZI
Original site: A0A4U0TJQ4_9PEZI 
ID   A0A4U0TJQ4_9PEZI        Unreviewed;      1202 AA.
AC   A0A4U0TJQ4;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Rad4-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B0A50_08440 {ECO:0000313|EMBL:TKA22060.1};
OS   Salinomyces thailandica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Salinomyces.
OX   NCBI_TaxID=706561 {ECO:0000313|EMBL:TKA22060.1, ECO:0000313|Proteomes:UP000308549};
RN   [1] {ECO:0000313|EMBL:TKA22060.1, ECO:0000313|Proteomes:UP000308549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 6315 {ECO:0000313|EMBL:TKA22060.1,
RC   ECO:0000313|Proteomes:UP000308549};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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}.
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:TKA22060.1}.
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DR   EMBL; NAJL01000086; TKA22060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U0TJQ4; -.
DR   Proteomes; UP000308549; 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:UP000308549}.
FT   DOMAIN          644..701
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01030"
FT   DOMAIN          703..766
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01031"
FT   DOMAIN          773..847
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01032"
FT   REGION          1..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          905..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..83
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..119
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..921
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..975
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1009
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1025
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1097
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1127..1151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1168..1185
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1202 AA;  133758 MW;  2E88DC6F386B9883 CRC64;
     MPPFISRKRQ RSPSPAATPP SGKVKAAPKA VPTQKRNKTS VFEAVDAPAD RKRDAVANRK
     LLDELNDNND DDDESLSEAD SDEFEDVPAP KRRKTLPQAE PDGEGEEEDD DDEEMDWEDA
     ITQTAPSSTA KPEPEIGDIS FTVKEDGSYT APDAGVSVPG LGKKGPSKRE KQVRTQTHCL
     HVQTLLWHNT VRNSWVNDRE AQKTLVEGLP EGVKREVTRW REAMGTLSKE ELEAKKKAAA
     ARQKGRKGKK GKKGGGRDWN FDAEHLEQGV PNLSAGDPLL RLLKVLAAYW RKRFAITAPG
     LRKQGYMTIR RLGEEIKDWD KNKGDAQEHS ERIEDIAGFR RLAKKCEGSR DVGAQLFCGL
     LRGLGLDTRM VANLQPAGLG WSKAEEANAK KPKKDRKDEK DEQESQKQEQ KVKTEVNGSG
     KKFRQELKPE KPSRKSNRGN KAEPISLDDD SDSPLSSAPS DAEAEMIEID DDDDESVVDV
     TPAIPKRKPN KNYDRDLAFP NYWVEVCSPA SHKYIPVDPI VLSTIASNDE LLQTFEPRGK
     KAEVGKQVMA YTIAFSSDGT AKDVTVRYLK KHQLPGKTKG TRMAVEKVPI YNRKGKVRRY
     EEYDWFRTVM SLYDRPENKR TAADELEETT DLKPQKPAKE DGKEVEKESL QWYKQSADFV
     LEQHLRREEA IKPGAKAVKT FTQGKGDKVK DHPVFKRSDV LACKTVESWH KEGRALKAGE
     HPMKLVPMRA VTLIRKREME DAQRETGEKL KQGLYSVGQT DWIIPPPIED GVIPKNAYGN
     MDVYVPTMVP EGAKHLPLKG SAKLCRKLGI DYAEACTGFE FGKQRAVPVL TGVVVAEEHV
     EMVRDAWRVE QAEVKRKEDV KRTAAALSSW RKMLLGLRVL ERMHTEYAGS AGKEEEYNPF
     LARAKREERE DGGERAVDVG AEGDEFGGGG FFPEGYDEEE VPQQTGRRKA AEDDNTGEDG
     GFLVEEDHDN EVEAGGFLVE EMPQDAARAS KGYAPTTPVS LQSMHNAADN ANGEEVEDVK
     TEDTAAEEQL VSTALALHPR KRPTRAPRKQ PTKATAKPAA RPQARSEKTD VEDSSLSELE
     EASEQDKEDD STEGPSDPDD TDTATPPPTT KSKATRKPAS PKVQVTPRGK PTASTTRATR
     SAGTRNGNAK TAVRSKYFVA SDSEDEAESK KGEEEEKEEE EEESEAEVVK PRRTTRRTSA
     RV
//
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