ID   RAD5_CANGA              Reviewed;        1151 AA.
AC   Q6FY76;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=DNA repair protein RAD5;
DE            EC=3.6.4.-;
GN   Name=RAD5; OrderedLocusNames=CAGL0A03432g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380947; CAG57810.1; -; Genomic_DNA.
DR   RefSeq; XP_444917.1; XM_444917.1.
DR   AlphaFoldDB; Q6FY76; -.
DR   SMR; Q6FY76; -.
DR   STRING; 5478.XP_444917.1; -.
DR   EnsemblFungi; CAG57810; CAG57810; CAGL0A03432g.
DR   GeneID; 2886385; -.
DR   KEGG; cgr:CAGL0A03432g; -.
DR   CGD; CAL0126887; CAGL0A03432g.
DR   VEuPathDB; FungiDB:CAGL0A03432g; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; Q6FY76; -.
DR   OMA; WSNFSFW; -.
DR   Proteomes; UP000002428; Chromosome A.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
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:0000400; F:four-way junction DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0000403; F:Y-form DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR   GO; GO:0042275; P:error-free postreplication DNA repair; IEA:EnsemblFungi.
DR   GO; GO:0070987; P:error-free translesion synthesis; IEA:EnsemblFungi.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
DR   GO; GO:0010994; P:free ubiquitin chain polymerization; IEA:EnsemblFungi.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:EnsemblFungi.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF13639; zf-RING_2; 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; PS00518; ZF_RING_1; 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..1151
FT                   /note="DNA repair protein RAD5"
FT                   /id="PRO_0000056120"
FT   DOMAIN          500..711
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          979..1146
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         897..944
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          35..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           662..665
FT                   /note="DEGH box"
FT   BINDING         513..520
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1151 AA;  132346 MW;  66FAC065F9ED046C CRC64;
     MDQNANQKKR FFKDELESSI ETTLTDKSSF LFEPQVDAIQ EENANDPEEQ IAQGTQESPF
     IEQLRAVLPT IRLEVALALE EKYRDIDDGL DLAISEYFDQ YQTGNDDAPP SSLELQHSQE
     VLTVPDNEEK DTDLQLVSVK RKREDDFMQS SQSKKPQRAN SSWKKFVGSL QVTVMVTRPT
     MRPVPYGTPL IFKRSNNNVP LKKIYEQLNK KKTGLAAFVK IYSANDEREI GRVPEDIARI
     VFPLLHRNEV HFKLTMIYPG DKRLSIGDNI IIQMDSFLTS TLFNRKENPT FSTQNGNGRE
     RFGAIVETEQ ELEERNIRMG LIMLFDKIKL RPVKDEAKFL EKLKQDGDDN EIVDLEDDES
     FGNFLSQEPL NDELPTQHQE DTMNINQLTS FYKATQSSKQ LNSLIPTTPP PELVKVELRK
     YQKQGLTWML RREGISIGHD NEDKSEDDTT LLNPLWRQFQ WPRNMSWHNQ STGSENDNSN
     PKLIFFYGNL HTGEFSLERP TMNSFKNGGI LSDEMGLGKT ISALSLVLMR PKDEHTTSQS
     LFHQESSNLS SDDVIEIKEP ERSYAYKTTL IIVPMSLLTQ WRDEFDKVNN NAGLTCELYY
     GGNVSSLKSL LIKRKNPPTV VLTTYGIVQN EWTKLSKDGT NIRSLGRTSG IFSIEFFRII
     LDEGHTIRNK STITSKAVLE LSSKYRWILT GTPIINRLDD LYSLVKFLKL EPWSQIGYWK
     QFITNPFEER NFKQAFDVVN AIMEPVLLRR TKQMKDTDGN PLVQLPPKEI VIEKLQLSKK
     QKLIYEEFLQ RAEKTFRSGL QSGDLLKKYS TILVHILRLR QVCCDSNLIG TLDENDEDLS
     SGNNKLITES VDVKTLIPDT EEEEDEVPPF ENDELDKLIE SVEAKFIDSN QLIPVECSIC
     TAEPIESSSA VVTECEHVFC KECLEEYGNF QKEKSLQQKC PNCRRDINLN RCLAFEKGSD
     GILKLIHFDR KERPAKLNAL IRHLQQLQDS SAGEQVVVFS QFSSYLDILE SQLNEVYSSN
     KLKVYKFDGR LSLKERTAVL EDFKVKDYAV QKVLLLSLKA GGVGLNLTCA SYAFMMDPWW
     SPSMEDQAID RIHRIGQTNS VKVIRFVIDG SIEEKMLRIQ DRKRTLGEAM DTDEDERRKR
     RIEEIQMLFE S