CHR24_ARATH
ID CHR24_ARATH Reviewed; 1090 AA.
AC Q8W103; Q9LVN8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein CHROMATIN REMODELING 24 {ECO:0000303|PubMed:16547115};
DE Short=AtCHR24;
DE EC=3.6.4.-;
DE AltName: Full=DNA excision repair protein CHR24 {ECO:0000250|UniProtKB:Q2NKX8};
GN Name=CHR24 {ECO:0000303|PubMed:16547115};
GN OrderedLocusNames=At5g63950 {ECO:0000312|Araport:AT5G63950};
GN ORFNames=MBM17.5 {ECO:0000312|EMBL:BAA96898.1};
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 {ECO:0000312|EMBL:AAL58917.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=21968679; DOI=10.4238/vol10-3gmr1347;
RA Johnson R.A., Hellens R.P., Love D.R.;
RT "A transient assay for recombination demonstrates that Arabidopsis SNM1 and
RT XRCC3 enhance non-homologous recombination.";
RL Genet. Mol. Res. 10:2104-2132(2011).
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: DNA helicase that acts as an essential component of the
CC spindle assembly checkpoint (By similarity). Probable chromatin
CC remodeling factor that regulate homologous recombination (HR) and non-
CC homologous recombination (NHR). {ECO:0000250|UniProtKB:Q2NKX8,
CC ECO:0000269|PubMed:21968679, ECO:0000303|PubMed:16547115}.
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=BAA96898.1; Type=Erroneous gene model prediction;
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DR EMBL; AB019227; BAA96898.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97819.1; -; Genomic_DNA.
DR EMBL; AF462829; AAL58917.1; -; mRNA.
DR EMBL; AY142010; AAM98274.1; -; mRNA.
DR RefSeq; NP_201200.2; NM_125791.3.
DR AlphaFoldDB; Q8W103; -.
DR SMR; Q8W103; -.
DR STRING; 3702.AT5G63950.1; -.
DR iPTMnet; Q8W103; -.
DR PaxDb; Q8W103; -.
DR PRIDE; Q8W103; -.
DR ProteomicsDB; 246961; -.
DR EnsemblPlants; AT5G63950.1; AT5G63950.1; AT5G63950.
DR GeneID; 836516; -.
DR Gramene; AT5G63950.1; AT5G63950.1; AT5G63950.
DR KEGG; ath:AT5G63950; -.
DR Araport; AT5G63950; -.
DR TAIR; locus:2160811; AT5G63950.
DR eggNOG; KOG0387; Eukaryota.
DR HOGENOM; CLU_000315_17_0_1; -.
DR InParanoid; Q8W103; -.
DR OMA; NDKHASD; -.
DR OrthoDB; 372069at2759; -.
DR PhylomeDB; Q8W103; -.
DR PRO; PR:Q8W103; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W103; baseline and differential.
DR Genevisible; Q8W103; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0015616; F:DNA translocase activity; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0045951; P:positive regulation of mitotic recombination; IDA:UniProtKB.
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 recombination; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1090
FT /note="Protein CHROMATIN REMODELING 24"
FT /id="PRO_0000430858"
FT DOMAIN 389..564
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 736..895
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1043..1069
FT /evidence="ECO:0000255"
FT MOTIF 44..51
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 515..518
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 402..409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1090 AA; 122803 MW; 6E3CA54E6B1DCAE2 CRC64;
MAENTASHRR KPRSLNDRHY SILQDLSAPP RQPPSSSHGE DEETKKSMIK LAGRRRLCKA
LPKEDEADGY DDPDLVDFYS PVKGETSLDS AGIGNKFTSW DESKEANTEL AGEPNFSIIT
DFCSPSPQLK QKEEMQGDGG RNEIMGILDD LTSKLGTMSI QKKKDSQSND FDACGVKSQV
DKFDFEDAKS SFSLLSDLSK SSPDVVTTYN AGVNSIKDKQ GKSGFAIREE QTSKEFSREW
EERISNVGKQ NSYSGRHFDD NSEDNRQGYN LDRGKSQCKE VDQSMKTTRH IEVSEKIRTV
GRSNAAKLRD LDEDDDDDDC LILSGKKAAE MKINKPARSY NAKRHGYDER SLEDEGSITL
TGLNLSYTLP GKIATMLYPH QREGLNWLWS LHTQGKGGIL GDDMGLGKTM QICSFLAGLF
HSKLIKRALV VAPKTLLPHW MKELATVGLS QMTREYYGTS TKAREYDLHH ILQGKGILLT
TYDIVRNNTK ALQGDDHYTD EDDEDGNKWD YMILDEGHLI KNPNTQRAKS LLEIPSSHRI
IISGTPIQNN LKELWALFNF SCPGLLGDKN WFKQNYEHYI LRGTDKNATD REQRIGSTVA
KNLREHIQPF FLRRLKSEVF GDDGATSKLS KKDEIVVWLR LTACQRQLYE AFLNSEIVLS
AFDGSPLAAL TILKKICDHP LLLTKRAAED VLEGMDSTLT QEEAGVAERL AMHIADNVDT
DDFQTKNDSI SCKLSFIMSL LENLIPEGHR VLIFSQTRKM LNLIQDSLTS NGYSFLRIDG
TTKAPDRLKT VEEFQEGHVA PIFLLTSQVG GLGLTLTKAD RVIVVDPAWN PSTDNQSVDR
AYRIGQTKDV IVYRLMTSAT VEEKIYRKQV YKGGLFKTAT EHKEQIRYFS QQDLRELFSL
PKGGFDVSPT QQQLYEEHYN QIKLDEKLES HVKFLETLGI AGVSHHSLLF SKTAPIQAIQ
KDEEEQIRRE TALLLGRASA SISQDTVING ADYAFKPKDV NLDKRINISP VDDKELSESV
IKARLNRLTM LLQNKGTVSR LPDGGAKIQK QIAELTRELK DMKAAERINM PQVIDLEEDI
SRKMQKGLNL
