ID   RAD5_EMENI              Reviewed;        1202 AA.
AC   Q5BHD6; C8VRD8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=DNA repair protein rad5;
DE            EC=3.6.4.-;
GN   Name=rad5; ORFNames=AN0044;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000002; EAA65363.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF90313.1; -; Genomic_DNA.
DR   RefSeq; XP_657648.1; XM_652556.1.
DR   AlphaFoldDB; Q5BHD6; -.
DR   SMR; Q5BHD6; -.
DR   STRING; 162425.CADANIAP00002711; -.
DR   PRIDE; Q5BHD6; -.
DR   EnsemblFungi; CBF90313; CBF90313; ANIA_00044.
DR   EnsemblFungi; EAA65363; EAA65363; AN0044.2.
DR   GeneID; 2875817; -.
DR   KEGG; ani:AN0044.2; -.
DR   VEuPathDB; FungiDB:AN0044; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; Q5BHD6; -.
DR   OMA; WSNFSFW; -.
DR   OrthoDB; 132523at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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   SMART; SM00184; RING; 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..1202
FT                   /note="DNA repair protein rad5"
FT                   /id="PRO_0000056123"
FT   DOMAIN          504..703
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1003..1198
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         892..937
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1071..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           654..657
FT                   /note="DEAH box"
FT   COMPBIAS        33..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..973
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         517..524
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1202 AA;  133801 MW;  79D76032AA0B4F65 CRC64;
     MNFDASNDRP LKKRRFFVDD PLDTAVTPAE KSPALDASSS ASTHTDPNYS ANGSPAQIQT
     QQEYNFSNGG HATQPATAAG TRTHQAQSPA HDTLSDFDTE AFVSIVGEQV SPETLSQIRK
     LSDGSLEKAI NVYFDGSWKN AGSPGSSQTT LLSCERNASR PSPLHTSREQ GTGPAENGAD
     SVTEPISRSK LQPARRYLGA FGVEAWATRS GIGLIKHGDT VNIERARSQP LSTRGRTGKL
     RVNQKGDVLT RFTNTAGQEI GRLPRETAEW VSTLLDQKIC EFRGVCVFAP DRLRVNDTIY
     LQLRCFMRIE AFQPKELPQK QDDNRATTIF EQEESAEEKQ LRLRQVALVQ LFDEIGLKST
     TQDDEIKKQR KEGLLRAAEM ADQEAKKLAK SGNTDSGDEE PAELEQDQLD ALYKKAQSFD
     FSMPEAQPPS SFAMDLRKYQ KQALYWMLSK EKDKKSGREV SIHPLWEEYD WPLKDVDDKD
     LPIIEGINHF YVNPYSGELS LDFPAQEQHC LGGILADEMG LGKTIEMLSL VHSHRNLPPT
     QSLGNLTRLP VSGVVPAPYT TLVVAPMSLL AQWEGEALKA SRNGSMKVLM YYGNEKNVNL
     REMCSAGNAA APNMILTSYG VVMSEHRTHQ ALAPGTSWTP GNLFSVDFFR VILDEAHIIK
     NRRSKTARAC YDLKATHRWV LTGTPIVNRL EDLFSLVRFL RVEPWNNFSF WKTFITAPFE
     SKEVVRAISV VQTVLEPLVL RRTKSMKTPE GEPLVPLPKR TIRIEKVELI EQEREIYNHI
     YTRAKQTFNS NVAAGTLLKS YSTIFAQLLR LRQTCCHPIL TRNKAIVADE EDAAAAADQD
     SDLKDDMDLQ ELINRFTATT SDAESSNEPP DPSMKFTAHA LRQIQTESAG ECPICSEEPM
     IDPAVTACWH SACKGCLKDY IQHQRDKGVQ PRCFSCRADL NPQDIFEVVR YQSPNTTPTE
     QTPSSIGGDN VYSSSQPPPP PRISLRRINP LSPSAHTSAK IHALLAHLVR VPAGTKSVVF
     SQFTSFLDLI GPQLTKAGIS FVRLDGTMAQ KARAEVLAQF TKFETFTQEE LDQAESTSAP
     SGLTPTPKTP KQSSSPSSPT VLLISLKAGG VGLNLTAASN VFMMDPWWSF AIEAQAIDRV
     HRMGQLRDVN VVRFIVKDSI EERMLRVQER KMGIAGSLGL MGEGNEEERR KERIEELRLL
     FE