RAD5_GIBZE
ID RAD5_GIBZE Reviewed; 1154 AA.
AC Q4IJ84; A0A098D800; A0A0E0RUZ9; V6R2R3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=DNA repair protein RAD5;
DE EC=3.6.4.-;
GN Name=RAD5; ORFNames=FGRRES_02724, FGSG_02724;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
CC -!- FUNCTION: Probable helicase, member of the UBC2/RAD6 epistasis group.
CC Functions with DNA repair protein RAD18 in error-free postreplication
CC DNA repair. Involved in the maintenance of wild-type rates of
CC instability of simple repetitive sequences such as poly(GT) repeats.
CC Seems to be involved in maintaining a balance which acts in favor of
CC error-prone non-homologous joining during DNA double-strand breaks
CC repairs (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; DS231663; ESU08197.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF75074.1; -; Genomic_DNA.
DR RefSeq; XP_011318682.1; XM_011320380.1.
DR AlphaFoldDB; Q4IJ84; -.
DR SMR; Q4IJ84; -.
DR STRING; 5518.FGSG_02724P0; -.
DR EnsemblFungi; ESU08197; ESU08197; FGSG_02724.
DR GeneID; 23550087; -.
DR KEGG; fgr:FGSG_02724; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G06539; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; Q4IJ84; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..1154
FT /note="DNA repair protein RAD5"
FT /id="PRO_0000056124"
FT DOMAIN 506..716
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 988..1144
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 900..945
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 667..670
FT /note="DEAH box"
FT COMPBIAS 13..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 519..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1154 AA; 129896 MW; ADF01FEFAE5823B1 CRC64;
MEQPLGDMSP WHPDNHMDPE PPTKRRRFLA DPDEASSDPV AHDSSPLPPS KRFFENEDET
VPKTERLETI DEKPNNASPK SSSTELPTSQ QEPSPSFDQE TFETFIGDKV SEDVLSAIRS
NCGNNIERAV NMYFDGTYKK FMKKSTRPAP PRPAASSSRT PNVSGERTIP IQTSKRMPNE
RYIGAFGVEG WATRSGTNLL KHGDIVKIER QKRAPPPTKS KGKAGPVTPS RGFGAPRRQD
VVVRFTTQSG TEVGRLAREA ANWVSALIDE KICRFEGTVV YAPERLRTND TIFLQLRCSL
LNSAFFSRPF QLADDRSAAF FNQNETNDEK TLRMRQVALV KLFQEINLHP TLTNSATKDG
RKGLLQAAEQ DEEKQKEVKK SDGNGTNNTK EANSSQSSDT EDGEELEQDQ LDALYKKAQS
FDFNTPEAEP ADTFAMTLRK YQKQALHWMM AKEKDEKSHR EPLMHPLWEQ YEWPLKDVDE
NDLPQIEGQS KFYVNPYSGD LSLDFPVQEQ HCLGGILADE MGLGKTIQML SLVHTHRSEV
ALEARQSVVA RSNVNQLTRL GKNSESILDA PCTTLVVAPM SLLSQWQSEA EKASKDGTMK
TELYYGNEKS SNLQALCCAS NAANAPDLVI TSYGVVLSEF SSLAARNGDK SFHNGLFSLR
FFRIIIDEAH HIKNRSSKTS KACYEISATH RWALTGTPIV NKLEDLFSLV RFLGVEPWNN
FSFWRTFITV PFESGDFMRA LDVVQTVLEP LVLRRTKDMK TPDGEPLVLL PPKQIEIVNV
ELSETERDVY NYIFNKAKRT FSQNVEAGTV MKAFTTIFAQ ILRLRQSCCH PILVRNRDIV
ADEVEAGAAA DAAAGLADDM DLESLITSFT AVTDKASKES NQTFGAHALE QIRDEAENEC
PLCFEEPMND QTVTGCWHSA CKKCLLDYIK HQTDKAEVPR CFSCREPINK RDLFEVVRHD
DDSDMMSKKP RISLQRVGVN ASSAKVVALM SELRALRREH PKMKSVVFSQ FTSFLSLIEP
ALTRANIKFL RLDGSMAQKA RAAVLNEFTE KKGFTILLLS LRAGGVGLNL TSAGRVFMMD
PWWSFAVEAQ AIDRVHRMGQ EAEVQVKRFV VKESVEERML KVQERKKFIA TSLGMMNDEE
KKLQRIEDIK ELLS
