CHR27_ARATH
ID CHR27_ARATH Reviewed; 1047 AA.
AC Q9LHE4; A0A1I9LTB0;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Helicase-like transcription factor CHR27 {ECO:0000305};
DE EC=3.6.4.- {ECO:0000305};
DE AltName: Full=Protein CHROMATIN REMODELING 27 {ECO:0000305};
DE AltName: Full=Protein SNF2-RING-HELICASE-LIKE 1 {ECO:0000303|PubMed:25425661};
GN Name=CHR27 {ECO:0000303|PubMed:25420628};
GN Synonyms=FRG1 {ECO:0000303|PubMed:25425661};
GN OrderedLocusNames=At3g20010 {ECO:0000312|Araport:AT3G20010};
GN ORFNames=MZE19.6 {ECO:0000312|EMBL:BAB03166.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, AND INTERACTION
RP WITH SUVR2.
RX PubMed=25420628; DOI=10.1038/cr.2014.156;
RA Han Y.F., Dou K., Ma Z.Y., Zhang S.W., Huang H.W., Li L., Cai T., Chen S.,
RA Zhu J.K., He X.J.;
RT "SUVR2 is involved in transcriptional gene silencing by associating with
RT SNF2-related chromatin-remodeling proteins in Arabidopsis.";
RL Cell Res. 24:1445-1465(2014).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH SUVR2.
RX PubMed=25425661; DOI=10.1073/pnas.1420515111;
RA Groth M., Stroud H., Feng S., Greenberg M.V., Vashisht A.A.,
RA Wohlschlegel J.A., Jacobsen S.E., Ausin I.;
RT "SNF2 chromatin remodeler-family proteins FRG1 and -2 are required for RNA-
RT directed DNA methylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:17666-17671(2014).
CC -!- FUNCTION: Probable helicase-like transcription factor involved in
CC transcriptional gene silencing. Associates with SUVR2 and contributes
CC to transcriptional gene silencing at RNA-directed DNA methylation
CC (RdDM) target loci but also at RdDM-independent target loci. May be
CC involved in nucleosome positioning to form ordered nucleosome arrays on
CC chromatin (PubMed:25420628). Associates with SUVR2 and functions
CC redundantly with FRG2. Required for the efficient methylation of a
CC broad range of RdDM target loci (PubMed:25425661).
CC {ECO:0000269|PubMed:25420628, ECO:0000269|PubMed:25425661}.
CC -!- SUBUNIT: Interacts with SUVR2 (PubMed:25420628, PubMed:25425661).
CC Interacts with itself (PubMed:25420628). {ECO:0000269|PubMed:25420628,
CC ECO:0000269|PubMed:25425661}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ZUL5}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000305}.
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DR EMBL; AP002050; BAB03166.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76318.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65816.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65818.1; -; Genomic_DNA.
DR RefSeq; NP_001319598.1; NM_001338440.1.
DR RefSeq; NP_001327760.1; NM_001338444.1.
DR RefSeq; NP_188635.1; NM_112891.3.
DR AlphaFoldDB; Q9LHE4; -.
DR SMR; Q9LHE4; -.
DR STRING; 3702.AT3G20010.1; -.
DR iPTMnet; Q9LHE4; -.
DR PaxDb; Q9LHE4; -.
DR PRIDE; Q9LHE4; -.
DR ProteomicsDB; 246962; -.
DR EnsemblPlants; AT3G20010.1; AT3G20010.1; AT3G20010.
DR EnsemblPlants; AT3G20010.5; AT3G20010.5; AT3G20010.
DR EnsemblPlants; AT3G20010.7; AT3G20010.7; AT3G20010.
DR GeneID; 821539; -.
DR Gramene; AT3G20010.1; AT3G20010.1; AT3G20010.
DR Gramene; AT3G20010.5; AT3G20010.5; AT3G20010.
DR Gramene; AT3G20010.7; AT3G20010.7; AT3G20010.
DR KEGG; ath:AT3G20010; -.
DR Araport; AT3G20010; -.
DR TAIR; locus:2095360; AT3G20010.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_3_1; -.
DR InParanoid; Q9LHE4; -.
DR OrthoDB; 132523at2759; -.
DR PhylomeDB; Q9LHE4; -.
DR PRO; PR:Q9LHE4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHE4; baseline and differential.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IGI:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 3.
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 InterPro; IPR018957; Znf_C3HC4_RING-type.
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; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 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.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-mediated gene silencing; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1047
FT /note="Helicase-like transcription factor CHR27"
FT /id="PRO_0000435117"
FT DOMAIN 296..597
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 887..1042
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 751..790
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1047 AA; 115475 MW; B943AF8CAC11E619 CRC64;
MDSAIEISSG SDSDDEVPPQ PVWPQTRTRM DPTWLSRRPL PTVDSHARAE HTNQAPPNGA
SSDTSRPGVS KPFTGNGNTV NSRISSGSGA DYVRLSSEQA LKRTLPPSFN SPPLPARSGT
NNISNASGSR VGVDYERPLS QQALKRTLPP SFNPPPLPSR SGTNNIRNAG GSRFGADYSH
PAVSAVGNKS TFGDHYSGAH AEIGIQRGVN GVRILPPSLT HGTSASVLHH AGSSDPMHRF
GGGEDRNPDN DERLVYQAAL QVLNQPMTES DLPPGTLSVP LMRHQKIALA WMFQKETSSF
NCPGGILADD QGLGKTVSTI ALILKQKIVS QLKSESSCKQ ETEALVLDAD DESDNAKHES
GSHVKPELKV SSNSETSVLS ACGNDENDSS DMEKAEDEEA NSSTRAFQWK RPAAGTLIVC
PASVVRQWAR ELDEKVSEES KLSVLVYHGS NRTKDPNELA EYDVVVTTYA IVTNEAPNKF
LVDEDENDEK NTDRYGLASG FSNNKKRKVV VGASKKSKRR GRKSTNDTSS EPDCGPLGKV
GWFRIVLDEA QTIKNYRTQM ARSCCTLRAK RRWCLSGTPI QNTIDDLYSY FRFLRYDPYA
VYKSFYSTIK VPISRNSCQG YKKLQAVLRA IMLRRTKGTL LDGKPIINLP PKVVNLSQVD
FSVAERSFYK KLEADSRSQF KAYADAGTLS QNYANILLLL LRLRQACDHP QLVKRYNSDP
VGKVSEAAVR RLPREARSRL INRLESSSAI CYECNEPPEK PVVTLCGHIF CYECVLEYIT
GDENTCPVPR CKQQLARDVV FSESSLRNCT SDDSGCSSSH DNGLDRSVFQ KRDFCSSKIK
AVLDILQSLS QPDSPNSAQH GQMPSSSRPY DDDDVTIVEP MRLHSSSPSQ GAVKTIIFSQ
WTGMLDLVEL RILESGIEFR RLDGTMSLAA RDRAVKEFSK KPDVKVMLMS LKAGNLGLNM
VAACHVILLD LWWNPTTEDQ AIDRAHRIGQ TRPVTVTRIT IKDTVEDRIL KLQEEKRTMV
ASAFGEEHGG SSATRLTVDD LKYLFMV
