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Database: UniProt
Entry: G3XMF3_ASPNA
LinkDB: G3XMF3_ASPNA
Original site: G3XMF3_ASPNA 
ID   G3XMF3_ASPNA            Unreviewed;      1116 AA.
AC   G3XMF3;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=DNA repair protein rad5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPNIDRAFT_212656 {ECO:0000313|EMBL:EHA28266.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA28266.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA28266.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHA28266.1}.
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DR   EMBL; ACJE01000001; EHA28266.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XMF3; -.
DR   STRING; 380704.G3XMF3; -.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 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   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00910; HIRAN; 1.
DR   SMART; SM00184; RING; 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 {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          452..650
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          838..883
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          942..1098
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          330..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1116 AA;  125477 MW;  CB6B93719CFB7410 CRC64;
     MDDSTRVEDH AVPHVEQEIV QAEHHNADSR TEGALLQVDY DGFDITTFTS IIGENLSADS
     IQRIRSAAGD DLERAVNIYF DGSWKKSPTP RAQNQTTLTA RQRPLPTQPH KIATPLSAAC
     KPHTQTLPPD KVTSRPATQP PLRYIGAFGV GAWATRSGAG FLRHGDLVNI ERTRSQPLSK
     RNRAGKLVSN QKSDVLTRFT TKSGQEIGRL PRETAEWVST LLDQRVCTFE GVCVYVPDRV
     RVNDTIYLQL RCYLRIEAFQ PRIFSQSMDD NRSVAIFEEK ESADEKALRL RQVALVKLFD
     EIHLQPTSVN DMTRNHKKEG LLRAAEMAEQ HERVKKENQT NDDSSEEDSP ELEEDQLDTL
     YKKAQSFDFS MPEAEPASSF TLHLRKYQRQ ALYWMLAKEK DNKSARETSL HPLWEEYSWP
     SRDVDDKELP VVAGIDHFYV NPYSGELSLD FPVQEQHCLG GILADEMGLG KTIEMLSLVH
     SHRIMPQKPT DLVRLPQSAS GVVPAPYTTL VIAPTSLLSQ WESEALKASQ PGTMNVLMYY
     GADKNINLKN LCASGNAAAP NLIITSYGVV LSEYRQHMSA LLSSMSSGGL FSVDFFRVIV
     DEAHVIKNRL SKTAKACYEL KATHRWVLTG TPIVNRLEDL FSLVRFLKVE PWNNFSFWKT
     FITVPFESKD YVRALNVVQS VLEPLVLRRT KTMKTPEGEP LVPLPRRTIT IEEVELPDQE
     REIYDLIFTR AKQTFNHNVE AGTLLKSYST IFAQILRLRQ TCCHPILTRN KAIVADEEDA
     AAAADAANDL KDDMDLQDLI DRFKASTEAA ESNEPQDPSA KFTAHALKQI QNEASGECPI
     CSEEPMIDPA VTACWHSACK KCLEDYIRHQ TDKGMDPRCF SCRAPTTSRD IFEVVRHESP
     NTTPEDDIYS STPTPSQAPP RISLRRIHPL SPSAHTSAKV HALLAHLARV PANTKSVVFS
     QFTSFLDLIS PQLTRAGIHH VRLDGTMPHK ARAETLAQFN RHRHSTAPPP PTVLLISLRA
     GGVGLNLTAA SNVFMMDPWW SFAIEAQAID RVHRMGQTRD VQVTRFVVKD SIEGRMLRVQ
     ERKMNIAGSL GLRVGGDGSE DDKKKERIEE LRLLFE
//
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