RAD5_ASHGO
ID RAD5_ASHGO Reviewed; 1085 AA.
AC Q753V5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DNA repair protein RAD5;
DE EC=3.6.4.-;
GN Name=RAD5; OrderedLocusNames=AFR220W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 72.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53591.2; -; Genomic_DNA.
DR RefSeq; NP_985767.2; NM_211121.2.
DR AlphaFoldDB; Q753V5; -.
DR SMR; Q753V5; -.
DR STRING; 33169.AAS53591; -.
DR EnsemblFungi; AAS53591; AAS53591; AGOS_AFR220W.
DR GeneID; 4622029; -.
DR KEGG; ago:AGOS_AFR220W; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; Q753V5; -.
DR OMA; WSNFSFW; -.
DR Proteomes; UP000000591; Chromosome VI.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13639; zf-RING_2; 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; PS00518; ZF_RING_1; 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..1085
FT /note="DNA repair protein RAD5"
FT /id="PRO_0000056117"
FT DOMAIN 447..652
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 914..1072
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 832..880
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 92..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 603..606
FT /note="DEGH box"
FT COMPBIAS 103..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 460..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1085 AA; 123255 MW; DD76632734F2A889 CRC64;
MQRTGDGERP RFFQQDLDVI PDDKGSDLFI QTAEGPDGHV DDEVIEDKTR FITNLKEVLG
ALPDDILEGY WNSYGASKDG LSKAIQQHFE GKETKGCSDA HDDLNTETQN SQNTIVNGHV
SNQIKRASEG GLPILKRKKQ LCCWRRFLGS TQVNAMATRP TAQPLKYGSE LLIRRTSGQP
NNSGLRSRKK PGFSQYVRFC DATSSRELGR LPEDISEILH TLLQTPGVEF KATMIFCNSK
RLSVGDLFVV RLDCFVTSLL FDPALPGKAE DEQFQQRNRA LMLLFKNLNM TPLAEGADLV
PEKPEFYDLE EDESITDATV NSPTASDDYM DLNQLRNFYR STQESASIFK LRETTPPVDK
FQLELRRYQK QGLTWMLLRE REHAILEPGS QDALADGPMD PMWRMFKWPR DTSWDVSRGT
TYVSLEADIP DKFYANLHTG EFSLVKPISK SILKGGILAD EMGLGKTISI LALITMVPSD
TKHLLTTAQE KPPVGHLSLE LGISTVKPYT ASTTLIVVPM SLLPQWRNEF VRVNDGNGLY
CEVYYAGNVS NLRTLLVKQK SPPSVVLTTY GVVQTEWSKL QQFDYEASNE GLFSVEFFRI
ILDEGHNIRN RTTKTSKAVM ALTSRRKWVL TGTPIMNRLD DLFSLIKFMN FEPWCKIDYW
RQFVSDPFEK KDYSSALEVI QAVMGPILLR RTKNMKDEDG NPLVQLPPKE VVIEMIRFSD
TEAGLYKYFL SKAEHSVKES LARGDLLKKY STILLHILRL RQVCCHFKLL GSQDENDEDL
KNMKLINDIP DISTLLGEDS QSPGSSSEGM PDFIEDFKTK YPNSDALKDL ECSICTCEAI
SPLTSVVFTR CGHPFCESCL LEYIQFQNKK GSETICPNCR AAVESRYLLK LEDINGKLEP
VPYSNTKKSS KIVALIRHLK HLQDTSANEQ VVVFSQFSSY LDILENELRQ SFASDICEIY
KFDGRLDLKE RSNVLAKFTE KSLVKMKVLL LSLKAGGVGL NLTCASHAFI MDPWWSPGME
DQAMDRIHRI GQSNTVKIYR FIVENSIEEK MLRIQEKKRS LGEFVDADEE ERRRSRIEEI
KMLFA
