ID   RAD5_NEUCR              Reviewed;        1228 AA.
AC   Q7S1P9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 3.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=DNA repair protein rad5;
DE            EC=3.6.4.-;
DE   AltName: Full=Mutagen-sensitive protein 41;
GN   Name=mus-41; Synonyms=rad5; ORFNames=NCU09516;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Probable helicase, member of the UBC2/RAD6 epistasis group.
CC       Functions with DNA repair protein uvs-2/rad18 in error-free
CC       postreplication DNA repair. Involved in the maintenance of wild-type
CC       rates of instability of simple repetitive sequences such as poly(GT)
CC       repeats. Seems to be involved in maintaining a balance which acts in
CC       favor of error-prone non-homologous joining during DNA double-strand
CC       breaks 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; CM002238; EAA29275.2; -; Genomic_DNA.
DR   RefSeq; XP_958511.2; XM_953418.2.
DR   AlphaFoldDB; Q7S1P9; -.
DR   SMR; Q7S1P9; -.
DR   STRING; 5141.EFNCRP00000009196; -.
DR   EnsemblFungi; EAA29275; EAA29275; NCU09516.
DR   GeneID; 3874658; -.
DR   KEGG; ncr:NCU09516; -.
DR   VEuPathDB; FungiDB:NCU09516; -.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; Q7S1P9; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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..1228
FT                   /note="DNA repair protein rad5"
FT                   /id="PRO_0000056126"
FT   DOMAIN          574..784
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1060..1216
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         967..1012
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           735..738
FT                   /note="DEAH box"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..86
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         587..594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1228 AA;  137947 MW;  855962EB4C184E98 CRC64;
     MDRHDTMDFT NEPLSKKRRF LGDQGDSDHV AGGPSSSPQF SAPPSSPPRK KLLQDPNSEV
     QPRVSKDADH NDDDDDDDDD DDEERPRFFT DDGTLTPHAT KICAPWLNDM PKPDPRKGYL
     LKDVDTPIAT PRDVAPPVVE SPQLAFDKDT FEAFVGEKVA SDILHVISKN CGNNIERAVN
     MYLDGTWKKL HRAPPVRVNS HSPLVVGGQS PKKSSTSQAR SRSHAQAQPQ PQSNTPTKVL
     PSMPDARYVG AFGVEGWATR SGTGLLRHGD SVKIERQKIQ PPTVARKGQT KPGTPQSIPR
     VSAAAAKRVD VIVRFNDASG RELGRLAKDT ANWVSTLIDQ NICRFEGICV YAPERLRTNE
     TVFLQLKCYM LRSAFLGRTL QLADNRAAGF HEKDETTEEK DLRLRQVALV RLFQEINIVP
     SRGNAAAAKD ARKDLLEAAD SAEKKAMDKA KAGDHNTNGL ASPPEEAEEG QELEQDQLDA
     LYKKAQSFDF STPEAEPANT FAMTLRPYQK QSLYWMLAKE KNQRTEDRET SMHPLWEEYV
     WPTKDHDDKD LPVVPDQPCF YVNPYSGDLS LDFPKQEQHC LGGILADEMG LGKTIQMLSL
     IHSHRSEVAI KAREAGPTSV NNLPRLPTVS GQKTTIDAPC TTLVVAPMSL LAQWQSEAEN
     ASKEGTFKTM MYYGAEKNVD LVTMCCEANA ANAPDVIITS YGVVLSEFTQ LATKNGDRLS
     SRGLFSLNFF RVILDEAHNI KNRQAKTSRA CYEIAAEHRW VLTGTPIVNR LEDLFSLVRF
     LRVEPWNNFS FWRTFITVPF ESKNFVRALD VVQTVLEPLV MRRTKDMKTP DGQFLVPLPP
     KHIEIVDIEL SEPERAVYDY VFNRAKRTLF DNMQAGTVMK AFTSIFAQIL RLRQSCCHPV
     LVRNQEILAD EEEANMAADV AAGLADDMDL QTLIERFTAT TDDASKTNNN FGAHVLRQIR
     DEAVNECPIC AEEPMIDQAV TGCWHSACKK CLLDYIKHQT DRNEVPRCFQ CREHINIRDI
     FEVIRHDDDL ETSSTPGASP EPRISLQRVG ANDSSAKIVA LISHLRTLRQ EHPKMKSLVI
     SQFTSFLSLI SSALTRHKIS FLRLDGSMSQ KARAAVLTEF QSTNKFCVLL LSLKAGGVGL
     NLTSAKRVYM MDPWWSFAVE AQAIDRVHRM GQEDEVRVYR FIVKQSVEMR MLRVQERKKF
     IATSLGMMSD EEKKMQRIED IKELLSSD