ID   RAD5_CRYNJ              Reviewed;        1198 AA.
AC   P0CQ66; Q560G8; Q5KPG8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=DNA repair protein RAD5;
DE            EC=3.6.4.-;
GN   Name=RAD5; OrderedLocusNames=CNA02850;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
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; AE017341; AAW40874.1; -; Genomic_DNA.
DR   RefSeq; XP_566693.1; XM_566693.1.
DR   AlphaFoldDB; P0CQ66; -.
DR   SMR; P0CQ66; -.
DR   STRING; 5207.AAW40874; -.
DR   PaxDb; P0CQ66; -.
DR   EnsemblFungi; AAW40874; AAW40874; CNA02850.
DR   GeneID; 3253723; -.
DR   KEGG; cne:CNA02850; -.
DR   VEuPathDB; FungiDB:CNA02850; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; P0CQ66; -.
DR   OMA; WSNFSFW; -.
DR   OrthoDB; 132523at2759; -.
DR   Proteomes; UP000002149; 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; -; 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..1198
FT                   /note="DNA repair protein RAD5"
FT                   /id="PRO_0000056121"
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..401
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   MOTIF           688..691
FT                   /note="DEAH box"
FT   COMPBIAS        37..81
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;  134261 MW;  51B6B2350A89E127 CRC64;
     MSAEASPETG RFRTKSSPEL FFPATDSEGE EQNDVPLTIV HPTQSTSSKF SINIASSSRP
     QHGITTGDFE ATSQTSAHDN VDDDFSIVGH NPASSHPQGT IVAPRRKRSL QQAHSHHSSS
     SSSPVPSAPV IRADFRKGFL GEFVCEGWSL SKGRGYCSPG TKIVIERPKS KSTDVGAPKP
     GRKDSGPVRL VNGKVVGGVK SKQMTLGSMM AKKVEPAKKV KATTDQIIRF RNERGFEIGR
     LSIHEAGFLA HLLDTGVIQL SGNVIDCPQN LTTGCTILLN IKVYLARKAF ENFGKHKREE
     HFSFWKDQRE TAMEEAMRLR KDSLRSLFER IGVKPIQSSA LSKVTPIQGV LNRQKGPDLE
     GSRLRSSPST STAEEKGKGR AAMPAVDDDG 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 FIDLDADGRA MSNYTSILAM
     LMKLRQCVDH PLLVLGKSGE DGELGEKILE SGAGNGEGNL RDMIAMYAGG IRAETPEDVD
     KAYAAKVLKE LGEQEDTPIC ELCSNEMFDE VLLPCYHRSC QDCIVEWIGT CEDQNKIASC
     PSCGKGPIKL ADLRSVQRRH KRVNPITDAY PGGRDPNLKS SNDTTVTLGK VDLVTSTKLR
     ALLRQLEEIR QEDPKAKALV FSQFTSFLDL IEATLTKQGI RWLRFDGTMS QAQRANTIEE
     FGRKTNEPLI LLISLKAGGV GLNLTMANYV FLMDTWWNEA IEQQAIDRVH RLGQNKPVYV
     TRYIIKGTVE KRIMKIQRSK TALVNASLSN GAKTKETTLA DIKKIFGMDE EDSEGEVY