CHR7_ARATH
ID CHR7_ARATH Reviewed; 1202 AA.
AC F4JTF6; Q9SZ57;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=CHD3-type chromatin-remodeling factor CHR7 {ECO:0000305};
DE EC=3.6.4.- {ECO:0000305};
DE AltName: Full=Protein CHROMATIN REMODELING 7 {ECO:0000305};
DE AltName: Full=Protein PICKLE RELATED 2 {ECO:0000305};
GN Name=CHR7 {ECO:0000305}; Synonyms=PKR2 {ECO:0000312|EMBL:AEE85976.1};
GN OrderedLocusNames=At4g31900 {ECO:0000312|Araport:AT4G31900};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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).
CC -!- FUNCTION: Chromatin remodeling factor that represses the expression of
CC embryonic trait genes upon and after seed germination and thus enables
CC the developmental switch to post-germinative growth.
CC {ECO:0000250|UniProtKB:Q9S775}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9S775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=F4JTF6-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40760.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79908.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049607; CAB40760.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161580; CAB79908.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85976.1; -; Genomic_DNA.
DR PIR; T06312; T06312.
DR RefSeq; NP_194918.2; NM_119341.2. [F4JTF6-1]
DR AlphaFoldDB; F4JTF6; -.
DR SMR; F4JTF6; -.
DR STRING; 3702.AT4G31900.1; -.
DR PaxDb; F4JTF6; -.
DR PRIDE; F4JTF6; -.
DR EnsemblPlants; AT4G31900.1; AT4G31900.1; AT4G31900. [F4JTF6-1]
DR GeneID; 829320; -.
DR Gramene; AT4G31900.1; AT4G31900.1; AT4G31900. [F4JTF6-1]
DR KEGG; ath:AT4G31900; -.
DR Araport; AT4G31900; -.
DR TAIR; locus:2116747; AT4G31900.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_000315_31_1_1; -.
DR InParanoid; F4JTF6; -.
DR OrthoDB; 54215at2759; -.
DR PRO; PR:F4JTF6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JTF6; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR009463; DUF1087.
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; 2.
DR Pfam; PF06461; DUF1086; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 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 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Chromatin regulator; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..1202
FT /note="CHD3-type chromatin-remodeling factor CHR7"
FT /id="PRO_0000435120"
FT DOMAIN 45..109
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 142..201
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 237..405
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 528..679
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 838..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 356..359
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1202 AA; 139417 MW; 3B2830053C35AD2A CRC64;
MANLLQRLRR RTGPKPDYIE DKLDEYIREE QVEETGGSNQ DCPLGEIEKI LDREWRPTAS
NNPNSSDNGT PTLVVVKQYL VKWKGLSYLH CSWVPEQEFE KAYKSHPHLK LKLRVTRFNA
AMDVFIAENG AHEFIAIRPE WKTVDRIIAC REGDDGEEYL VKYKELSYRN SYWESESDIS
DFQNEIQRFK DINSSSRRDK YVENERNREE FKQFDLTPEF LTGTLHTYQL EGLNFLRYSW
SKKTNVILAD EMGLGKTIQS IAFLASLFEE NLSPHLVVAP LSTIRNWERE FATWAPHMNV
VMYTGDSEAR DVIWEHEFYF SEGRKSKFDV LLTTYEMVHP GISVLSPIKW TCMIIDEGHR
LKNQKSKLYS SLSQFTSKHI VLLTGTPLQN NLNELFALMH FLDADKFGSL EKFQDINKEE
QISRLHQMLA PHLLRRLKKD VLKDKVPPKK ELILRVDMSS QQKEVYKAVI TNNYQVLTKK
RDAKISNVLM KLRQVCSHPY LLPDFEPRFE DANEAFTKLL EASGKLQLLD KMMVKLKEQG
HRVLIYTQFQ HTLYLLEDYF TFKNWNYERI DGKISGPERQ VRIDRFNAEN SNRFCFLLST
RAGGIGINLA TADTVIIYDS DWNPHADLQA MARVHRLGQT NKVMIYRLIH KGTVEERMME
ITKNKMLLEH LVVGKQHLCQ DELDDIIKYG SKELFSEEND EAGRSGKIHY DDAAIEQLLD
RNHVDAVEVS LDDEEETDFL KNFKVASFEY VDDENEAAAL EEAQAIENNS SVRNADRTSH
WKDLLKDKYE VQQAEELSAL GKRKRNGKQV MYAEDDLDGL EEISDEEDEY CLDDLKVTSD
EEEEADEPEA ARQRKPRTVT RPYRKRARDN SEEIPLMEGE GRYLMVLGFN ETERDIFLRT
FKRYGAGNFD WKEFVNPLYM KTYDEINKYG ILFLKHIAEN PTDNSTNFKV ITAMVYADGV
PKEGISSDEL LVSMTFMMLV KEKCQFLDNH PTAPVFSNYV ISKYNLRNGA FSKEEHDRIL
IPAVSKHGYG RWVAIVEDEE IGFQEVACKD LNIPFPPDTK SARKRICDHV GKRVKKMEDA
IKYEYAEKIL AEQAKAETKG TSFVDAEKEM LKNDPITSKK NSATAVDNKQ GRVEMAQSYD
QSVNEKSGES FQTYLDIQPL NRMPRESFKP LEPINEEIST RLSVGTDHDV EMDAADNIIV
LD
