ID G7XP69_ASPKW Unreviewed; 1214 AA.
AC G7XP69;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=DNA repair protein rad5 {ECO:0000313|EMBL:GAA88820.1};
GN ORFNames=AKAW_06934 {ECO:0000313|EMBL:GAA88820.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA88820.1};
RN [1] {ECO:0000313|EMBL:GAA88820.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA88820.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; DF126464; GAA88820.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XP69; -.
DR STRING; 1033177.G7XP69; -.
DR VEuPathDB; FungiDB:AKAW_06934; -.
DR eggNOG; KOG1001; Eukaryota.
DR InParanoid; G7XP69; -.
DR Proteomes; UP000006812; 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; 2.
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 522..720
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 908..953
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1012..1196
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1214 AA; 136163 MW; 428C6FC9446BD848 CRC64;
MNIHHDDDDD RPLKKRRFFA DDEDLLTPQP STDSVTASLH TPASSSLTDQ GAQLQPTRSE
NGPEIIDVPW PGSSSRVEGH TVPQVEQEAV QGEHNAIPRR TEDASPRVDY DGFDVLTFTS
IIGERLSADS IQNIRKAAGD DLERAVNIYF DGSWKKSPAP RAQNQTTLTA RQRPLSAQSH
RTSTPLSASS HPRTQTPTPD KATTRPAAQP PLRYIGAFGV GAWATRSGSG FLRHGDLVNI
ERTRSQPLSK RNRAGKLVSN LKSDFLTRFT TKSGQEIGRL PREIAEWVST LLDQRVCTFE
GVCVYVPDRV RVNDTIYLQL RCYLRIEAFQ PRIFSQSMDD NRSVAYFEEK ESADEKALRL
RQVALVKLFD EIHLQPTSTN DMTRNHKKEG LLRAAEMAEQ HERVKKENQA NDDSSEEDSP
ELEEDQLDTL YKKAQSFDFS MPEAEPASSF TMHLRKYQRQ ALYWMLAKEK DNKSARETSL
HPLWEEYSWP SRDVDDKELP AVDGIDHFYV NPYSGELSLD FPVQEQHCLG GILADEMGLG
KTIEMLSLVH SHRITPQKPS NLVRLPQSAS GAVPAPYTTL VIAPTSLLSQ WESEALKASQ
PGTMNVLMYY GADTKINLRD LCASGNAAAP NLIITSYGVV LSEYRQYMSA LLSSMSSGGL
FSVDFFRVIV DEAHVIKNRL SKTAKACYEL KATHRWVLTG TPIVNRLEDL FSLVRFLKVE
PWNNFSFWKT FITVPFESKD YVRALNVVQT VLEPLVLRRT KTMKTPEGEP LVPLPRRTIT
IEEVELPDQE RQIYDLIYTR AKQTFNHNVE AGTLLKSYST IFAQILRLRQ TCCHPILTRN
KAIVADEEDA AAAADATNDL KDDMDLQELI DRFKASTEAA ESNEPQDSSA KFTTHALKQI
QNDASGECPI CSEEPMIDPA VTACWHSACK KCLENYIRHQ TDKGMDPRCF SCRAPTTSRD
IFEVVRHETP NATPEDDIYS STPIPSQAPP RITLRRIHPL SPSAHTSAKV HALLAHLTRV
PANTKSVVFS QFTSFLDLIS PQLTRAGIHH VRLDGTMPHK ARAETLAQFN RAETFADQTD
IDNDVEANDS AQLPLSKSKH GHSTGPAPPT VLLISLRAGG VGLNLTAASN VFMMDPWWSF
AIEAQAIDRV HRMGQTRDVQ VTRFVVKDSI EGRMLRVQER KMNIAGSLGL RVGGDGSEDD
KKKERIEELR LLFE
//
