ID E5AEW1_LEPMJ Unreviewed; 1014 AA.
AC E5AEW1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DNA repair protein Rad4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LEMA_P005370.1 {ECO:0000313|EMBL:CBY01750.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBY01750.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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; FP929139; CBY01750.1; -; Genomic_DNA.
DR RefSeq; XP_003845229.1; XM_003845181.1.
DR AlphaFoldDB; E5AEW1; -.
DR STRING; 985895.E5AEW1; -.
DR EnsemblFungi; CBY01750; CBY01750; LEMA_P005370.1.
DR GeneID; 13290846; -.
DR eggNOG; KOG2179; Eukaryota.
DR HOGENOM; CLU_003639_1_0_1; -.
DR InParanoid; E5AEW1; -.
DR OMA; KPSKFEP; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000002668; Genome.
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:SF3; DNA REPAIR PROTEIN RAD4; 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:UP000002668}.
FT DOMAIN 528..586
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 588..650
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 657..731
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1014
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 112269 MW; 1B99E333F2552B0B CRC64;
MARPRGKLHR ATEPVTPRRS ARKTRSSQQD EAIPDIFQDM LHEAHVAEAD EDDRPRKKRR
TALSRKSQSP VAKAGPVQTP IRDPVPPSPS RPVITAATPS QSRTAAEPIA ESEGPTNVRM
RQTIEDSDES DEDSDMEWEN ALEDVDDSDD AGEGKEAASK IGDINIAIGG KKAADTTVQR
KVRRRAITSV DKKRRLDIHK MHIMCLLYHV HRRNTWCNDR RVQSTLRKIV SPSILADLVP
NPDLTQYSAS RRFVDGMNEL KLLWTKRFKI TARGMYKPRW ADAEADVRPF SDFDELDDPM
DKDDFRIAAF TLRGSQDVGT QLFCALLRGI GIEVRLVCSL QPLPFASAAE RTTPQKASPK
NTITIDPYNK PSQTTPTRPK GKKLSRMERV MGERHAVLHS TGVAPKKQKA FHAPYPVYWV
EAFNHAHQKW VPIDTHSTFT VNAPEKLEPP LAYTQNSLSY AIAFDEDHTA KDVTRRYAKA
YSAKTRKFRV ESTPGGEKWW KRVMKFFERS TILDRDQIED ALLARKVAAE GIPKNVQDFK
GHPVYVLERH LKHNEVIYPL EPVGKVNCGT SMNPKMEPIY RRSNVHVVRS ADKWYRMGRD
VKGGEQPLKH AKPKKNRRVS LGPDADVDEE VDEAGAGLYA EFQTELYIPP PVVKGRVPRN
AYGNLDLYVP SMCPAGGTHI RHKLASKAAR ILGIDSADAV TGFSFKGRHG TAIIQGVVVA
TEYADAVTAV IEGMEYAVEE AEAAAKRAES LRLWRRFFLG LRIAQRVNDI VIDGERGPRL
DVQDEIAKED RKLAAQDMAG GFFPDEGDAG GIEGEGYEPP TRNYEGGGGF MHDDANEGGG
FVPNQGPDDV AGGGFVPETL EQRTAPGMSR EFSFESAILD SQALRPRRRS SFGKSYSSDE
DGEGGGFLPG DYVLDDDDLA DHPGCTDQTD GAVDDDGGFV PKDLSDKDVD QVDGQDEAPP
SPQPAVKEDD VKPEDGAITS KSPTPTSSAS ETGSLPLEDP EDEDADPDWL VDAT
//
