ID   RAD5_CRYNB              Reviewed;        1198 AA.
AC   P0CQ67; Q560G8; Q5KPG8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=DNA repair protein RAD5;
DE            EC=3.6.4.-;
GN   Name=RAD5; OrderedLocusNames=CNBA2720;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000001; EAL23625.1; -; Genomic_DNA.
DR   RefSeq; XP_778272.1; XM_773179.1.
DR   AlphaFoldDB; P0CQ67; -.
DR   SMR; P0CQ67; -.
DR   EnsemblFungi; EAL23625; EAL23625; CNBA2720.
DR   GeneID; 4933526; -.
DR   KEGG; cnb:CNBA2720; -.
DR   VEuPathDB; FungiDB:CNBA2720; -.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   Proteomes; UP000001435; 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; Zinc; Zinc-finger.
FT   CHAIN           1..1198
FT                   /note="DNA repair protein RAD5"
FT                   /id="PRO_0000410244"
FT   DOMAIN          509..737
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1021..1180
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         920..964
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           688..691
FT                   /note="DEAH box"
FT   COMPBIAS        37..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         522..529
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1198 AA;  134427 MW;  C0EC5CF3E8A3BDAA CRC64;
     MSAEASPETG RFRTKSSPEL FFPATDSEGE EQNDVPLTIV HPTQSTSSKF SINIASSSRP
     QHGITTGDFE TTSQTSAHDD VDDDFSIVGH NPASSHPQGT IVAPRRKRSL QQAHSHHSSS
     SSSPVPSAPV IRADFRKGFL GEFVCEGWSL SKGRGYCSPG TKIVIERPKS KSTDVGAPKP
     GRKDSGPVRL VNGKVVGGVK SKQMTLGSMM AKKVEPAKKV KATTDQIIRF RNERGFEIGR
     LSIHEAGFLT HLLDTGVIQL SGNVIDCPQN LTTGCTILLN IKVYLARKAF ENFGKHKREE
     HFSFWKDQRE TAMEEAMRLR KDSLRSLFER IGVKPIQSSA LSKVTPIQGV LNRQKGPDLE
     GSRLRSSPST STAEEKGKGR AAMRAVDDDE EDSGDEAEKL DEKQMNEIDS IYRKAQQGDT
     RLDEMDPPST FLYTLRPYQK QALTWMNARE KGDSSVRNES LHPLWEEYLF KKDQLPGEPI
     EISDDDEQPD STRKFYWNPY SGELSLKFPT SQNLSRGGIL ADAMGMGKTC MMASLIHTNR
     EEKPAGNLES QTRDGVEGEI DEEPASKRIK FKQVTLSNQW RAVPTAPKVE SFPRATLVVC
     PVSLAAQWHD ELRKMSQQGS INSYVWYGGD RVDIEALLAG DGKERVDVIV TSYGTLTSEY
     QKWLRTKDRP NYEGGSLYDH EFLRIVLDEA HNIRNRLAMV SKACYELKGQ RRWALTGTPI
     VNRLEDLYSL LHFLRITPWG NYSFFRSFVT VPFLNQDHKA LNVVQYILES CLLRREKTMR
     DKDGRLIVDL PPKTVEIKVL QFSRAERQIY KFLEERAKKR FIELDADGRA MSNYTSILAM
     LMKLRQCVDH PLLVLGKSGE DGELGEKILE SGAGNGEGNL RDMIAMYAGG IRAETPDDVD
     KAYAAKVLKE LGEQEDTPIC ELCSNEMFDE VLLPCYHRSC QDCIVEWIGT CEDQNKIASC
     PSCGKGPIKL ADLRSVQRRH KRVNPITDAY PGGRDPNSKS SNDTTVTLGK VDLVTSTKLR
     ALLRQLEEIR QEDPKAKALV FSQFTSFLDL IEATLTKQGI RWLRFDGTMS QAQRANTIEE
     FGRKTNEPLI LLISLKAGGV GLNLTMANYV FLMDTWWNEA IEQQAIDRVH RLGQNKPVYV
     TRYIIKGTVE KRIMKIQRSK TALVNASLSN GAKTKETTLA DIKKIFGMDE EDSEGEVY