ID   RAD5_ASPFU              Reviewed;        1245 AA.
AC   Q4WVM1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=DNA repair protein rad5;
DE            EC=3.6.4.-;
GN   Name=rad5; ORFNames=AFUA_5G12600;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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   -!- SEQUENCE CAUTION:
CC       Sequence=EAL91355.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000003; EAL91355.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_753393.1; XM_748300.1.
DR   AlphaFoldDB; Q4WVM1; -.
DR   SMR; Q4WVM1; -.
DR   STRING; 746128.CADAFUBP00005889; -.
DR   GeneID; 3511286; -.
DR   KEGG; afm:AFUA_5G12600; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; Q4WVM1; -.
DR   OrthoDB; 132523at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
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; -; 2.
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   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 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..1245
FT                   /note="DNA repair protein rad5"
FT                   /id="PRO_0000056118"
FT   DOMAIN          551..753
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1047..1227
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         941..986
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          999..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1110..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           704..707
FT                   /note="DEAH box"
FT   COMPBIAS        7..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1022
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1110..1125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         564..571
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1245 AA;  139336 MW;  A537FE6D3929860D CRC64;
     MVFGDLNERP LKKRRFFVDE EDTHPPSSEA APVTTNLDTS TISSAGPEGS DVRQQQLNGA
     VPFPNVKESS RESPGLGPED KQDNLLKEDE ENNGTVDYEI LNHSPSIHAQ QDQRVDQGLT
     NGFGGQPSGE RTVSETQAFQ SSGGFDTSTF ASIIGEHLSP ESLEKIRKAS GDDLERAVNI
     YFDGSWKSSN NSLSQPLVAP HQQTLSNPCT PVNESISQTV NTKISKKPNQ APSSRCLSQS
     SRYIGAFGVG AWATRSGVGL LKHGEHVNVE RARSQPVSKR GRGGKLITNQ KGDVLTRFTN
     KSGQEIGRLP RETAEWVSTL IDQKICRFEG ICVFAPDRVR VNDTIYLQLW CYLRKEAFLP
     RNLWNMGDDN RSTAFFEEQE SAEEKQLRLR QVALVKLFDE IGLQPTTVND MTKKHKKEGL
     LRAAEIAEQY DKTKREGKSN ESSEDEESPE LEEDQLDTLY KKAQSFDFNM PEAQPPPSFV
     LNLRKYQRQA LHWMLAKEKD KKSGRELSMH PLWEEYTWPT KDVDDKDLPA VEGQAHFYVN
     PYSGELSLDF PAQEQHCLGG ILADEMGLGK TIEMLSLIHS HRNVSPSRQG PSSSTELVRM
     PSSSSAILPA PNTTLVVAPT SLLSQWESEA MKASEQGTMK VLMYYGVDKS TNLQELCSAG
     NPAAPNIIIT SYGVVLSESR QLAMFNSNTQ GGLFSVDFFR VILDEAHVIK NRRSKTARAC
     YELRATHRWV LTGTPIVNRL EDLFSLVRFL QVEPWNNFSF WKTFITVPFE SKDYVRALNV
     VQTVLEPLVL RRTKTMKTPE GEPLVPLPRR TIDIVEVELS EQEREIYDYI FTRAKRTFND
     NIEAGTLLKS FSTIFAQILR LRQTCCHPIL TRNKTIVADE EDAAATADAA NELKDDMDLQ
     ELIDRFSASM ENADTAEAQD PSAKFTTHAL RQIQTESSGE CPICSEEPMI DPAVTACWHS
     ACKKCLEDYI RHQTDKGVPP RCFSCRAPVT SRDIFQVIRH QSPSSTPTET DLYSSTPASS
     PHPAPRISLR RIHPLSPSAH TSAKIHALIN HLNRVPANTK SVVFSQFTSF LDLIGAQLTK
     AGISYVRLDG TMPQKARAEV LAEFNRTETF HQEEIDEDEG PDTPRVRISS KNSRSSPKSP
     AVLLISLRAG GVGLNLTAAS NVFMMDPWWS FAIEAQAIDR VHRMGQLRDV SVTRFIVKDS
     IEGRMLRVQE RKMNIAGSLG LRVGGDGSED EKRKERIEEL KLLFE