ID   RAD5_USTMA              Reviewed;        1387 AA.
AC   Q4PGG5; A0A0D1EB15;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=DNA repair protein RAD5;
DE            EC=3.6.4.-;
GN   Name=RAD5; ORFNames=UMAG_00798;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003140; KIS72396.1; -; Genomic_DNA.
DR   RefSeq; XP_011386570.1; XM_011388268.1.
DR   AlphaFoldDB; Q4PGG5; -.
DR   SMR; Q4PGG5; -.
DR   STRING; 5270.UM00798P0; -.
DR   PRIDE; Q4PGG5; -.
DR   EnsemblFungi; KIS72396; KIS72396; UMAG_00798.
DR   GeneID; 23562003; -.
DR   KEGG; uma:UMAG_00798; -.
DR   VEuPathDB; FungiDB:UMAG_00798; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; Q4PGG5; -.
DR   OMA; WSNFSFW; -.
DR   OrthoDB; 132523at2759; -.
DR   Proteomes; UP000000561; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
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; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 2.
DR   Gene3D; 3.40.50.300; -; 2.
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; 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   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00910; HIRAN; 1.
DR   SMART; SM00184; RING; 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..1387
FT                   /note="DNA repair protein RAD5"
FT                   /id="PRO_0000056128"
FT   DOMAIN          645..880
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1213..1379
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         1108..1154
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           831..834
FT                   /note="DEAH box"
FT   COMPBIAS        151..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         658..665
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1387 AA;  152271 MW;  B0DB7AFE8DF34146 CRC64;
     MTTQSSAGPQ SQPSRDFFAS SPSATPGSPS KQASQASKQP DALVTPSSVT ANTSVCADNL
     LDHHQHEPQH DAASVVIGIE GSINDSAAIH RRRQQPRRAA VQNAKPLFLA EDEDDAINWP
     VADQEEGDDF FSTQLADQKV KRPARATVNS DEKDFQPSTL SSLSSPPSET VYKRSPPSDD
     VQASNGPAKR PKKSWSTPAS VATTKSAPRH CSPTPDPRLR HDAFDRRYIG TFVLSAWSLS
     KGSSYVKPGD AVRIFRPRKK HATAEPKIAS KLTNGGMQKA KQTTLNFRGA SAGPTNFFTS
     KQKSKEKEHF IVRFSNMRGF EVGRLPLEVA IWMSKLIDAG IAEFEGVVVD CPPSLTVGCD
     IILQVKAYIK FDAFFSTLLG SREFDDQNEA LRPETAESDL EKTLRERKIS LLRMFRVCDL
     KPRLSNAILK SHKASDDFSS EAMLDQYGGD IQGAVKHAGS DLAISTENGT QLPHAGEDAS
     STAIDLDVEG DTDAVAHLEI ADQLQSAKRQ TDGDADTEEN DGTELNLNQL DQVYRKAQAN
     DAHLPEVEPP ESFVLTLRPY QKQALGWMKN MEMAPGQSSS SQEQSVTQQG NGDTGERNVS
     LHPLWEEYEF PLDYDNPQAN ERLILSATRL FYFNPYTGDL SLDFQRASKG SRGGILADEM
     GLGKTIMVAS LLHANRTSDP GEESEGEINA VDAAEGDVST KRKGSAKQTS LASAFAASTS
     SVDQRKALLK ASVSKGKASL VVAPMSLIGQ WRDELIRASA PGSLTPVLYY ADTKGDLLAQ
     LESGKVDVVI TSYGTLVTEY RRFLDGGGAS NRHLSVSAPL YCIDWLRVIL DEAHNIKNRS
     TMNARACCDL VSRRRWALTG TPIINRLTDL FSLLKFLRVE PWGDFSFFNS FVCKPFQAKS
     TKALDVVQVI LESVLLRREK KMKDKDGKPI VELPPKTIVV KELEFSELER RIYDNVYRRA
     YLQFASLKAN GTVTRNLSVI FSVLMRLRQA VCHPSLVLKA GSKVQSGGIR KDHVDRNGEV
     GVGEGDHVEV DADAVEFGLD SDHVGGNGTP STQDLRELVA QFQLDEAGEA GDDSTESYTK
     ATVERLIGEM HGDQATVPPV VSDGENECPI CLEESQISPC YLPRCMHSAC KACLVDYLGQ
     CKQKGDQGAC PTCRKGPVQE TDLIEAIRTR PATRAASGGA SPTDRPGKAC TLTSVPSVIY
     VRNNLRTSTK LSALISHLNT LRATEAAFKG VIFSQFTSFL DLIEPVLTRY RFHFLRLDGS
     TPQKVRDKLV LEFQSPSPTN HVVLFLISLK AGGVGLNLTA ANKIWLLDFW WNSSIENQAI
     DRIHRFGQTS PVSVFRYIIK DSIEDRILLI QKRKDMLIKH ALNTDNHPHG TKPNSEMLAN
     LDLLFGE