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 27-MAR-2024, entry version 57.
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}.
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; AAEY01000001; EAL23625.1; -; Genomic_DNA.
DR RefSeq; XP_778272.1; XM_773179.1.
DR AlphaFoldDB; P0CQ67; -.
DR SMR; P0CQ67; -.
DR GeneID; 4933526; -.
DR KEGG; cnb:CNBA2720; -.
DR VEuPathDB; FungiDB:CNBA2720; -.
DR HOGENOM; CLU_000315_2_5_1; -.
DR OrthoDB; 200191at2759; -.
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 CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR049730; SNF2/RAD54-like_C.
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 PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
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
//
