RAD5_DEBHA
ID RAD5_DEBHA Reviewed; 1190 AA.
AC Q6BIP2; B5RV54;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA repair protein RAD5;
DE EC=3.6.4.-;
GN Name=RAD5; OrderedLocusNames=DEHA2G08800g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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=CAR65933.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR382139; CAR65933.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002770598.1; XM_002770552.1.
DR AlphaFoldDB; Q6BIP2; -.
DR SMR; Q6BIP2; -.
DR STRING; 4959.XP_002770598.1; -.
DR EnsemblFungi; CAR65933; CAR65933; DEHA2G08800g.
DR GeneID; 8999151; -.
DR KEGG; dha:DEHA2G08800g; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; Q6BIP2; -.
DR OrthoDB; 132523at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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 InterPro; IPR017907; Znf_RING_CS.
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; 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..1190
FT /note="DNA repair protein RAD5"
FT /id="PRO_0000056122"
FT DOMAIN 531..727
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1017..1181
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 916..963
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 678..681
FT /note="DEGH box"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 544..551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1190 AA; 138356 MW; 853B83DB16453FFC CRC64;
MTMEKKRYFS VMSEDRSPNL VTAEQNEELK NSSVSKDSQE DSLFVVDDSD IEEQTESNIL
ENTNPVPHVH RLEYEEFESQ IKSVVGTISS HAMNHLFKKY HDKQNYLKLA VQEYLQGIDE
NDTDIRIVGN SPDGNNSPNV HRKRIYEQEQ DDLMSRLQRE CQRSQDEEKK KSWNRFIGSL
NVQAWATRPT TKPLKYLEKL ELRRLMPKKL NVGKPTKEKT KFGDSSIIRI YTIPKYTEES
GREIGRIPED ITRILVPLID LDISSFYTTV MIDTEKRLST GDSFYIQIDC YLSQNAFSGK
ELERSMSQSD QDLNALKRQK KMDTRTRFDF STETNTEAIL RLRQYSLSRF FQRLNIKPIP
QKSDHADDIN EASETPIIID SENEDDHIVK EDHEQQNLDQ LKQIMQANQQ SELLDSLPET
TKPPIFNFKL DLRKYQKHGL SWMLTREREI AVLETLSKND DDDNDNDILT TQDKANIQER
NDAFMNPLWD IFEWPKDTSM HKSESSPTED RMDDNYFYAN MYNGELSLTK PVIRSMVKGG
ILADEMGLGK TISTLALINS VPIDVMFEEN KELEDKTIYA SKTTLIIVPM SLLSQWQKEF
DKANNNSNHK CFIYYGDSAT TDLSPVLCNK KKDIPIVMIT TYGTVLNEFT RISNRRDAKG
FLPKIGLFSV KFFRIVLDEG HNIRNRTAKT SKAIYEILSN RKWVLTGTPV INRLDDLYSL
VKFLELEPWS NFSYWKTFVT LPFEQRKISQ TLDVVKSILE PIFIRRTKNM KQSNGKPLVE
LPPKEVVIEE VKFNEVEEKL YNWFKARASQ SFKDGIKSGD LFKKYSQILT HILRLRQVCC
HVDLVGSANE MEQELVDPNT DLSEANGESD SISMVNNVLD SYHADNNHDE KFKNNTEVRS
VMFPLYEKID LKESECSICT QSPIPLGEMA LTPCGHAYCL NCVLEHFDFQ EKNSQKPLCP
NCREPISKYK IFKLRHRDTS VKEIRFHTKQ EMEDPSQNFK FQLYLYDPTK TSSKIQCLIN
HLKILKEQSP NEQVVVFSQF SSYLDIIENE LKIQISNDFV VYKFDGRLNM NERQKILENF
SSQKHENKVM ILLLSLKAGG VGLNLTTASR AFMMDPWWSP SVEDQAIDRL HRIGQNSNVK
VTRFIMADSI ETKMLKIQER KKQIGEAVGA EEDERRKRRI EEMQILFEDD
