CHR5_ARATH
ID CHR5_ARATH Reviewed; 1724 AA.
AC F4IV99; Q9SI41;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Protein CHROMATIN REMODELING 5 {ECO:0000303|PubMed:16547115};
DE Short=AtCHR5;
DE EC=3.6.4.-;
GN Name=CHR5 {ECO:0000303|PubMed:16547115};
GN OrderedLocusNames=At2g13370 {ECO:0000312|Araport:AT2G13370};
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 {ECO:0000312|Proteomes:UP000006548};
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 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 [4]
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: DNA-binding helicase that specifically binds to the promoter
CC of target genes, leading to chromatin remodeling, possibly by promoting
CC deposition of histone H3.3 (By similarity). Probable chromatin
CC remodeling factor. {ECO:0000250|UniProtKB:E9PZM4,
CC ECO:0000303|PubMed:16547115}.
CC -!- INTERACTION:
CC F4IV99; Q9LJG8: ASIL2; NbExp=4; IntAct=EBI-15203078, EBI-4427947;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD28668.1; Type=Erroneous gene model prediction;
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DR EMBL; AC007209; AAD28668.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06230.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62965.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62966.1; -; Genomic_DNA.
DR PIR; C84507; C84507.
DR RefSeq; NP_001325086.1; NM_001335390.1.
DR RefSeq; NP_001325087.1; NM_001335389.1.
DR RefSeq; NP_178970.3; NM_126926.5.
DR AlphaFoldDB; F4IV99; -.
DR SMR; F4IV99; -.
DR BioGRID; 1184; 5.
DR IntAct; F4IV99; 3.
DR STRING; 3702.AT2G13370.1; -.
DR iPTMnet; F4IV99; -.
DR PaxDb; F4IV99; -.
DR PRIDE; F4IV99; -.
DR ProteomicsDB; 246964; -.
DR EnsemblPlants; AT2G13370.1; AT2G13370.1; AT2G13370.
DR EnsemblPlants; AT2G13370.2; AT2G13370.2; AT2G13370.
DR EnsemblPlants; AT2G13370.3; AT2G13370.3; AT2G13370.
DR GeneID; 815823; -.
DR Gramene; AT2G13370.1; AT2G13370.1; AT2G13370.
DR Gramene; AT2G13370.2; AT2G13370.2; AT2G13370.
DR Gramene; AT2G13370.3; AT2G13370.3; AT2G13370.
DR KEGG; ath:AT2G13370; -.
DR Araport; AT2G13370; -.
DR TAIR; locus:2041644; AT2G13370.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_28_0_1; -.
DR InParanoid; F4IV99; -.
DR OMA; CSWGARE; -.
DR OrthoDB; 57339at2759; -.
DR PRO; PR:F4IV99; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IV99; baseline and differential.
DR Genevisible; F4IV99; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR025260; DUF4208.
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; PF00385; Chromo; 1.
DR Pfam; PF13907; DUF4208; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Coiled coil; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1724
FT /note="Protein CHROMATIN REMODELING 5"
FT /id="PRO_0000430853"
FT DOMAIN 420..499
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 533..597
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 637..809
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 943..1094
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 24..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 138..164
FT /evidence="ECO:0000255"
FT COILED 505..525
FT /evidence="ECO:0000255"
FT COILED 1126..1163
FT /evidence="ECO:0000255"
FT MOTIF 320..327
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 760..763
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 1224..1231
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 1348..1355
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 650..657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1724 AA; 197270 MW; EABFB4A4DFB91476 CRC64;
MAFFRNYSND TVSHNVLDEN EERQNAATFQ SSPLNEDVDG TYSERGFDMN MDVQYQSDPE
PGCSIRQPNE TAVDNVADPV DSHYQSSTKR LGVTGRWGST FWKDCQPMGQ REGSDPAKDS
QSGYKEAYHS EDNHSNDRSE KLDSENENDN ENEEEDNEMN KHQSGQADVP ADEMLSDEYY
EQDEDNQSDH VHYKGYSNPT NSRSLPKAGS AVHSNSRTSR AIHKNIHYSD SNHDHNGDAD
MDYEEEEDED DPEDADFEPY DAADDGGASK KHGQGWDVSD EDPESDEEID LSDYEDDYGT
KKPKVRQQSK GFRKSSAGLE RKSFHVSSRQ KRKTSYQDDD SEEDSENDND EGFRSLARRG
TTLRQNNGRS TNTIGQSSEV RSSTRSVRKV SYVESEDSED IDDGKNRKNQ KDDIEEEDAD
VIEKVLWHQL KGMGEDVQTN NKSTVPVLVS QLFDTEPDWN EMEFLIKWKG QSHLHCQWKT
LSDLQNLSGF KKVLNYTKKV TEEIRYRTAL SREEIEVNDV SKEMDLDIIK QNSQVERIIA
DRISKDGLGD VVPEYLVKWQ GLSYAEATWE KDVDIAFAQV AIDEYKAREV SIAVQGKMVE
QQRTKGKASL RKLDEQPEWL IGGTLRDYQL EGLNFLVNSW LNDTNVILAD EMGLGKTVQS
VSMLGFLQNT QQIPGPFLVV VPLSTLANWA KEFRKWLPGM NIIVYVGTRA SREVCQQYEF
YNEKKVGRPI KFNALLTTYE VVLKDKAVLS KIKWIYLMVD EAHRLKNSEA QLYTALLEFS
TKNKLLITGT PLQNSVEELW ALLHFLDPGK FKNKDEFVEN YKNLSSFNES ELANLHLELR
PHILRRVIKD VEKSLPPKIE RILRVEMSPL QKQYYKWILE RNFHDLNKGV RGNQVSLLNI
VVELKKCCNH PFLFESADHG YGGDINDNSK LDKIILSSGK LVILDKLLVR LRETKHRVLI
FSQMVRMLDI LAEYLSLRGF QFQRLDGSTK AELRQQAMDH FNAPASDDFC FLLSTRAGGL
GINLATADTV VIFDSDWNPQ NDLQAMSRAH RIGQQEVVNI YRFVTSKSVE EEILERAKRK
MVLDHLVIQK LNAEGRLEKR ETKKGSNFDK NELSAILRFG AEELFKEDKN DEESKKRLLS
MDIDEILERA EQVEEKHTDE TEHELLGAFK VANFCNAEDD GSFWSRWIKP DSVVTAEEAL
APRAARNTKS YVDPSHPDRT SKRKKKGSEP PEHTERSQKR RKTEYFVPST PLLEGTSAQV
RGWSYGNLPK RDAQRFYRTV MKFGNHNQMA CIAEEVGGVV EAAPEEAQVE LFDALIDGCK
ESVETGNFEP KGPVLDFFGV PVKANELLKR VQGLQLLSKR ISRYNDPISQ FRVLSYLKPS
NWSKGCGWNQ IDDARLLLGI LYHGFGNWEK IRLDESLGLT KKIAPVELQH HETFLPRAPN
LKERATALLE MELAAAGGKN TNAKASRKNS KKVKDNLINQ FKAPARDRRG KSGPANVSLL
STKDGPRKTQ KAEPLVKEEG EMSDDGEVYE QFKEQKWMEW CEDVLADEIK TLGRLQRLQT
TSADLPKEKV LFKIRRYLEI LGRRIDAIVL EHEEDLYKQD RMTMRLWNYV STFSNLSGDR
LNQIYSKLKQ EKEEEEGVGP SHLNGSRNFQ RQQKFKTAGN SQGSQQVHKG IDTAKFEAWK
RRRRTENDVQ TERPTITNSN SLGILGPGPL DRSHRARQTG FPPR
