(data stored in ACNUC13479 zone)

SWISSPROT: CHR8_ARATH

ID   CHR8_ARATH              Reviewed;        1187 AA.
AC   Q9ZV43;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   07-JUN-2017, entry version 114.
DE   RecName: Full=Protein CHROMATIN REMODELING 8 {ECO:0000303|PubMed:16547115};
DE            Short=AtCHR8;
DE            Short=AtCSB {ECO:0000303|PubMed:15645454};
DE            EC=3.6.4.-;
GN   Name=CHR8 {ECO:0000303|PubMed:16547115};
GN   Synonyms=CSB {ECO:0000303|PubMed:15645454}, ERCC6, RAD26,
GN   RAD54 {ECO:0000303|PubMed:15748650};
GN   OrderedLocusNames=At2g18760 {ECO:0000312|Araport:AT2G18760};
GN   ORFNames=MSF3.14 {ECO:0000312|EMBL:AAD08945.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   REVIEW.
RX   PubMed=15645454; DOI=10.1002/em.20094;
RA   Kunz B.A., Anderson H.J., Osmond M.J., Vonarx E.J.;
RT   "Components of nucleotide excision repair and DNA damage tolerance in
RT   Arabidopsis thaliana.";
RL   Environ. Mol. Mutagen. 45:115-127(2005).
RN   [4]
RP   INDUCTION BY BLEOMYCIN.
RC   STRAIN=cv. Columbia;
RX   PubMed=15748650; DOI=10.1016/j.mrfmmm.2004.09.016;
RA   Molinier J., Oakeley E.J., Niederhauser O., Kovalchuk I., Hohn B.;
RT   "Dynamic response of plant genome to ultraviolet radiation and other
RT   genotoxic stresses.";
RL   Mutat. Res. 571:235-247(2005).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16547115; DOI=10.1534/genetics.105.051664;
RA   Shaked H., Avivi-Ragolsky N., Levy A.A.;
RT   "Involvement of the Arabidopsis SWI2/SNF2 chromatin remodeling gene
RT   family in DNA damage response and recombination.";
RL   Genetics 173:985-994(2006).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
CC   -!- FUNCTION: Essential factor involved in transcription-coupled
CC       nucleotide excision repair (TCR) which allows RNA polymerase II-
CC       blocking lesions to be rapidly removed from the transcribed strand
CC       of active genes. Upon DNA-binding, it locally modifies DNA
CC       conformation by wrapping the DNA around itself, thereby modifying
CC       the interface between stalled RNA polymerase II and DNA. It is
CC       required for transcription-coupled repair complex formation.
CC       {ECO:0000250|UniProtKB:Q03468}.
CC   -!- SUBUNIT: Homodimer. Binds DNA. {ECO:0000250|UniProtKB:Q03468}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03468,
CC       ECO:0000255|PROSITE-ProRule:PRU00768}.
CC   -!- INDUCTION: Accumulates after genotoxic agents treatment such as
CC       bleomycin (BLM), a small peptide that create DNA double strand
CC       breaks (DSBs). {ECO:0000269|PubMed:15748650}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; AC005724; AAD08945.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06805.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61954.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61955.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61956.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61957.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61958.1; -; Genomic_DNA.
DR   PIR; C84568; C84568.
DR   RefSeq; NP_001318246.1; NM_001335605.1.
DR   RefSeq; NP_001324143.1; NM_001335606.1.
DR   RefSeq; NP_001324144.1; NM_001335610.1.
DR   RefSeq; NP_001324145.1; NM_001335609.1.
DR   RefSeq; NP_001324146.1; NM_001335608.1.
DR   RefSeq; NP_179466.1; NM_127432.2.
DR   UniGene; At.39947; -.
DR   ProteinModelPortal; Q9ZV43; -.
DR   BioGrid; 1748; 1.
DR   STRING; 3702.AT2G18760.1; -.
DR   iPTMnet; Q9ZV43; -.
DR   PaxDb; Q9ZV43; -.
DR   PRIDE; Q9ZV43; -.
DR   EnsemblPlants; AT2G18760.1; AT2G18760.1; AT2G18760.
DR   EnsemblPlants; AT2G18760.2; AT2G18760.2; AT2G18760.
DR   EnsemblPlants; AT2G18760.4; AT2G18760.4; AT2G18760.
DR   EnsemblPlants; AT2G18760.5; AT2G18760.5; AT2G18760.
DR   EnsemblPlants; AT2G18760.6; AT2G18760.6; AT2G18760.
DR   EnsemblPlants; AT2G18760.7; AT2G18760.7; AT2G18760.
DR   GeneID; 816391; -.
DR   Gramene; AT2G18760.1; AT2G18760.1; AT2G18760.
DR   Gramene; AT2G18760.2; AT2G18760.2; AT2G18760.
DR   Gramene; AT2G18760.4; AT2G18760.4; AT2G18760.
DR   Gramene; AT2G18760.5; AT2G18760.5; AT2G18760.
DR   Gramene; AT2G18760.6; AT2G18760.6; AT2G18760.
DR   Gramene; AT2G18760.7; AT2G18760.7; AT2G18760.
DR   KEGG; ath:AT2G18760; -.
DR   Araport; AT2G18760; -.
DR   TAIR; locus:2054011; AT2G18760.
DR   eggNOG; KOG0387; Eukaryota.
DR   eggNOG; ENOG410XP4Z; LUCA.
DR   HOGENOM; HOG000170952; -.
DR   InParanoid; Q9ZV43; -.
DR   KO; K10841; -.
DR   OMA; RQGGYAN; -.
DR   OrthoDB; EOG093600SY; -.
DR   PhylomeDB; Q9ZV43; -.
DR   Reactome; R-ATH-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-ATH-6782135; Dual incision in TC-NER.
DR   Reactome; R-ATH-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   PRO; PR:Q9ZV43; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZV43; baseline and differential.
DR   Genevisible; Q9ZV43; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0010332; P:response to gamma radiation; IMP:TAIR.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q9ZV43.
DR   SWISS-2DPAGE; Q9ZV43.
KW   ATP-binding; Coiled coil; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN         1   1187       Protein CHROMATIN REMODELING 8.
FT                                /FTId=PRO_0000430854.
FT   DOMAIN      397    594       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      730    890       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     410    417       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED      110    170       {ECO:0000255}.
FT   COILED      987   1016       {ECO:0000255}.
FT   MOTIF       162    169       Nuclear localization signal 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00768}.
FT   MOTIF       290    297       Nuclear localization signal 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00768}.
FT   MOTIF       310    317       Nuclear localization signal 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00768}.
FT   MOTIF       545    548       DEGH box. {ECO:0000250|UniProtKB:Q03468,
FT                                ECO:0000255|PROSITE-ProRule:PRU00541}.
SQ   SEQUENCE   1187 AA;  133593 MW;  EAF19FDB2BA63333 CRC64;
     MEEDEDQFLL SSLGVTSANP EDLEQKILDE ATKKPDNDEG GSVEEKSTQL EGTNLLSSSQ
     NELLNKLRAV KFEIDAVAST VENVDEIAAE KGLKKDDESD LQGLHSGSAL QHALATDRLR
     SLKKRKIQLE KELTGLHGQS ASSSADHGNL LRDLVKEKPS LKRKLKEIRK PSRRDGKKVK
     VVSFREDTDF DAVFDGASAG FVETERDELV RKGILTPFHK LDGFERRLQQ PGPSNSRNLP
     EGDDENEDSS IIDRAVQSMS LAAKARPTTK LLDAEDLPKL EPPTAPFRRL RKLYKTPNSP
     DNEAKKRKAG KKSKKTRPLP EKKWRKRISR EDSSLQGSGD GRRILTTSSC EEEELDDFDD
     ADDNERSSVQ LEGGLNIPEC IFRKLFDYQR VGVQWLWELH CQRAGGIIGD EMGLGKTIQV
     LSFLGSLHFS KMYKPSIIIC PVTLLRQWRR EAQKWYPDFH VEILHDSAQD SGHGKGQGKA
     SESDYDSESS VDSDHEPKSK NTKKWDSLLN RVLNSESGLL ITTYEQLRLQ GEKLLNIEWG
     YAVLDEGHRI RNPNSDITLV CKQLQTVHRI IMTGAPIQNK LTELWSLFDF VFPGKLGVLP
     VFEAEFSVPI TVGGYANASP LQVSTAYRCA VVLRDLIMPY LLRRMKADVN AHLTKKTEHV
     LFCSLTVEQR STYRAFLASS EVEQIFDGNR NSLYGIDVMR KICNHPDLLE REHSHQNPDY
     GNPERSGKMK VVAEVLKVWK QQGHRVLLFS QTQQMLDILE SFLVANEYSY RRMDGLTPVK
     QRMALIDEFN NSEDMFVFVL TTKVGGLGTN LTGANRVIIF DPDWNPSNDM QARERAWRIG
     QKKDVTVYRL ITRGTIEEKV YHRQIYKHFL TNKILKNPQQ RRFFKARDMK DLFILKDDGD
     SNASTETSNI FSQLAEEINI VGVQSDKKPE SDTQLALHKT AEGSSEQTDV EMTDKTGEAM
     DEETNILKSL FDAHGIHSAV NHDAIMNAND EEEKMRLEHQ ASQVAQRAAE ALRQSRMLRS
     RESISVPTWT GRSGCAGAPS SVRRRFGSTV NSRLTQTGDK PSAIKNGISA GLSSGKAPSS
     AELLNRIRGS REQAIGVGLE QPQSSFPSSS GSSSRVGSLQ PEVLIRKICS FVQQKGGSAD
     TTSIVNHFRD IVSFNDKQLF KNLLKEIATL EKDQNRSFWV LKSEYKD
//

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