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 03-AUG-2022, entry version 135.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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 family
RT 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 family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
CC -!- FUNCTION: Essential factor involved in transcription-coupled nucleotide
CC excision repair (TCR) which allows RNA polymerase II-blocking lesions
CC to be rapidly removed from the transcribed strand of active genes. Upon
CC DNA-binding, it locally modifies DNA conformation by wrapping the DNA
CC around itself, thereby modifying the interface between stalled RNA
CC polymerase II and DNA. It is required for transcription-coupled repair
CC complex formation. {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 breaks
CC (DSBs). {ECO:0000269|PubMed:15748650}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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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 AlphaFoldDB; Q9ZV43; -.
DR SMR; Q9ZV43; -.
DR BioGRID; 1748; 1.
DR STRING; 3702.AT2G18760.1; -.
DR iPTMnet; Q9ZV43; -.
DR PaxDb; Q9ZV43; -.
DR PRIDE; Q9ZV43; -.
DR ProteomicsDB; 246990; -.
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 HOGENOM; CLU_000315_7_0_1; -.
DR InParanoid; Q9ZV43; -.
DR OMA; DFVFPMR; -.
DR PhylomeDB; Q9ZV43; -.
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; 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:0016787; F:hydrolase 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:0010332; P:response to gamma radiation; IMP:TAIR.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IBA:GO_Central.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1187
FT /note="Protein CHROMATIN REMODELING 8"
FT /id="PRO_0000430854"
FT DOMAIN 397..594
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 730..890
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 110..170
FT /evidence="ECO:0000255"
FT COILED 987..1016
FT /evidence="ECO:0000255"
FT MOTIF 162..169
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 290..297
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 310..317
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 545..548
FT /note="DEGH box"
FT /evidence="ECO:0000250|UniProtKB:Q03468,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 23..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..323
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410..417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="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
