ID A0A395N5E5_9HYPO Unreviewed; 1040 AA.
AC A0A395N5E5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Xeroderma pigmentosum group c-complementing protein {ECO:0000313|EMBL:RFN54869.1};
GN ORFNames=FIE12Z_836 {ECO:0000313|EMBL:RFN54869.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN54869.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN54869.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN54869.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFN54869.1}.
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DR EMBL; PXXK01000014; RFN54869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395N5E5; -.
DR STRING; 2594813.A0A395N5E5; -.
DR Proteomes; UP000265631; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000265631}.
FT DOMAIN 589..648
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 650..713
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 720..794
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 782..816
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1040
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 117523 MW; D95BADE30A73628D CRC64;
MPPLVPRKRL RESPPPGQGR ASKAAKDKSD ASRRKATLYD DLDASATPNS NSILHGFDND
DDDGSSLTSL SDDEFEDVVP PKKPEGAEDD SGDDDDIEFE DVEAPVAALP DAPVTSGDLE
LTLTRDTRIS LTNTSDRKGP TKREKKVRHA SHCVHVMLLL WHNATRNSWL CDPEVQATMI
SHIPPRLWDE VDRWRWNSGL EKRPIPKKST KENAKVKGKG KKVPDRRARD WGAEAERLEE
GAVDMSHGDP LFRLMKTLAA WWKQRFRITA PGLRKWGYMS LERLDRLTKA QKAEPHDPEQ
FGEKIEGLEG LRHCARNCDG SRDVGAQLFT ALLRGLGLEA RMVANLPCLG FGWTKLEEAE
PEKTDSTQTK STPDKQTKLA TKKESNKKAT QNKKPARKAR AKPEVVSDSD GLELEYKDSD
DESVEMEITP RKTSTKKHDA DMDFPHYWTE VLSPVTNKFL PVDAIVKNVV GTNRDLIESL
EPRGAKADKA RQIMAYIIGY SQDGTAKDVT VRYLKRNTFP GRTKGVRMTP VKVPVYNRHG
KIKRYDQFDW FKTAISGYRR GSKKYPITEI DEAEEATDLK PAKPEKKEVK EGQETLQYYK
QSKEFVLERH LKREEALKPD AKPAKVFKNK VKGGKVEEED VFLRSDVLNV KSAETWHKQG
RAPKAGEQPL KRVPYRAATL NRRREIMEAE AATGEKVLQG LYSWEQTDWI IPPPIKDGVI
PKNDYGNIDL FAEHMCPEGA VHVPFRGAMR VCKKLQIDYA EAVVDFEFGH RMAVPVIQGV
VIAEENHDMV MVELEKDEAE RARKEDEKRR KKALAQWRRF LMGMRIAERI RQEYGEITDD
ISVFGHARDS ALSKKPAPVE DEDMAGGFLP DGYEEEEEEK EAPAHHTSSF FPAIDEDDDG
DDGLVMEHDG ADQQRAMIPM EVDEEEAPSK PDAEAGLDPE PQPKLESEMD ETPERGAIPE
DEEPKPEPET HSEAESEPPR TSARSRKRAP AKQIKKEKQP PVRATRRSTR SGRNIVSYDE
DVGGNDEEIG DSYAESEDDE
//
