ID   RAD5_CANAL              Reviewed;        1084 AA.
AC   Q5ACX1; A0A1D8PG21;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=DNA repair protein RAD5;
DE            EC=3.6.4.-;
GN   Name=RAD5; OrderedLocusNames=CAALFM_C200350WA;
GN   ORFNames=CaO19.2097, CaO19.9644;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP017624; AOW27089.1; -; Genomic_DNA.
DR   RefSeq; XP_719543.2; XM_714450.2.
DR   BioGRID; 1221851; 1.
DR   STRING; 237561.Q5ACX1; -.
DR   PRIDE; Q5ACX1; -.
DR   GeneID; 3638827; -.
DR   KEGG; cal:CAALFM_C200350WA; -.
DR   CGD; CAL0000193075; orf19.9644.
DR   VEuPathDB; FungiDB:C2_00350W_A; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; Q5ACX1; -.
DR   OrthoDB; 132523at2759; -.
DR   PRO; PR:Q5ACX1; -.
DR   Proteomes; UP000000559; Chromosome 2.
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; -; 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..1084
FT                   /note="DNA repair protein RAD5"
FT                   /id="PRO_0000056119"
FT   DOMAIN          450..643
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          913..1071
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         816..863
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          11..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           594..597
FT                   /note="DEGH box"
FT   COMPBIAS        35..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         463..470
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1084 AA;  125021 MW;  E8B89C9ECF45B415 CRC64;
     MKVIKKRFFK PKEETLPSDE VPDPQSSAEP LHSLFVPDES EEEETTTSPK TNFEKDIIAI
     VGDISPIIMK YLYAKYSQKR NGAKFAVTEL LTNPPDVEKL QQDSIASQSA KRPHTIVSYQ
     EPPNKKVNIN PDSASSNNEP LMWQRLIGSL NIQAMATXPD HETVEIPGKX KLKRITTKNS
     TMANSAIVRV YHNEREIGRI PEDWTRILSP LFDLNIAVFE ASVLEETKSR LSTGDSFVIE
     IEVYLTNSSF AKNLDATENP IDLKKSNFDY SKESESEAAL RLRQFAISNL FDRLAIKPLK
     VNDDTEDEED ISSQEINSGD VEHPVPEINL DQMKEFYQSN NQLKILEGLP ETTTPPKENF
     ALDLRSYQKH GLSWMLAREK ELDVLEMLSN EDKLSSQSRK ELENLGTMNP LWRKYKWPYA
     TEATQDPTQN QTEKYFYANM YNGELSLEKP VIKSSLRGGI LADEMGLGKT IATLALVNSV
     PYDNFPEPKS DRPYASQTTL IVVPMSLLFQ WKSEFEKCNN NSRHVCRLHY GEDQETNLAW
     SLCNPDNSKI PIVMITTYGT VLNEFTRLSK RRNSKGELPK VGLYSVKFFR IILDEGHNIR
     NRNTKTAKSV YELQSSRKWI LTGTPIVNRL DDLYSLTKFL ELDPWNNFSY WKTFVTLPFE
     QKKISQTLDV VKSILEPIFL RRTKSQKKNG KPLVELPAKE VVIEQIKFND DEEKLYQWFK
     DRAYASFAEG IKSGQLLRRY TQILTHILRL RQVCCHVDLI GGAHEMDDEI IEAEQDEDMR
     KFLTSIKENQ IRFANDTDVK EKMYNLYGKI KEENECSICT QVPIPYSEMV VTPCAHTFCL
     SCILEHLDFQ KELKKEKLCP NCRSPISKYQ LFRIRNQPTK GNEIRFHIQK DAPDYSFQLY
     LYDPNRSSSK IQALVRHLKA LHSQSPNSKV IVFSQFSSYL DIIQSELKLA SEEFIVFKFD
     GRLNMNDRTK LLESFNQPLE DGKVAILLLS LKAGGVGLNL TTASRAYMMD PWWSPSIEDQ
     AIDRIHRIGQ NETVKVVRFI MENSIETKML KIQERKKQIG EAVAAEEEER RKRRIEEIQI
     LFEE