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Database: UniProt
Entry: Q6BIP2
LinkDB: Q6BIP2
Original site: Q6BIP2 
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   13-NOV-2019, entry version 98.
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 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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
CC       group. Functions with DNA repair protein RAD18 in error-free
CC       postreplication DNA repair. Involved in the maintenance of wild-
CC       type rates of instability of simple repetitive sequences such as
CC       poly(GT) repeats. Seems to be involved in maintaining a balance
CC       which acts in favor of error-prone non-homologous joining during
CC       DNA double-strand breaks repairs (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAR65933.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CR382139; CAR65933.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002770598.1; XM_002770552.1.
DR   STRING; 4959.XP_002770598.1; -.
DR   PRIDE; Q6BIP2; -.
DR   EnsemblFungi; CAR65933; CAR65933; DEHA2G08800g.
DR   GeneID; 8999151; -.
DR   KEGG; dha:DEHA2G08800g; -.
DR   HOGENOM; HOG000040492; -.
DR   InParanoid; Q6BIP2; -.
DR   KO; K15505; -.
DR   OrthoDB; 132523at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000400; F:four-way junction DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0000403; F:Y-form DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR   GO; GO:0042275; P:error-free postreplication DNA repair; IEA:EnsemblFungi.
DR   GO; GO:0070987; P:error-free translesion synthesis; IEA:EnsemblFungi.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
DR   GO; GO:0010994; P:free ubiquitin chain polymerization; IEA:EnsemblFungi.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:EnsemblFungi.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 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_N; 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; Complete proteome; Cytoplasm; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN         1   1190       DNA repair protein RAD5.
FT                                /FTId=PRO_0000056122.
FT   DOMAIN      531    727       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1017   1181       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     544    551       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   ZN_FING     916    963       RING-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00175}.
FT   MOTIF       678    681       DEGH box.
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
//
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