SM3L3_ARATH
ID SM3L3_ARATH Reviewed; 1277 AA.
AC Q9FIY7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=DNA repair protein RAD5B {ECO:0000305};
DE EC=3.6.4.- {ECO:0000305};
DE AltName: Full=Putative SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3-like 3 {ECO:0000305};
DE Short=SMARCA3-like protein 3 {ECO:0000305};
DE AltName: Full=RAD5 homolog B {ECO:0000303|PubMed:18310306};
DE Short=AtRAD5B {ECO:0000303|PubMed:18310306};
GN Name=RAD5B {ECO:0000303|PubMed:18310306}; OrderedLocusNames=At5g43530;
GN ORFNames=K9D7.2;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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.
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).
RN [4]
RP FUNCTION.
RX PubMed=18310306; DOI=10.1104/pp.108.116806;
RA Chen I.P., Mannuss A., Orel N., Heitzeberg F., Puchta H.;
RT "A homolog of ScRAD5 is involved in DNA repair and homologous recombination
RT in Arabidopsis.";
RL Plant Physiol. 146:1786-1796(2008).
CC -!- FUNCTION: Possesses intrinsic ATP-dependent nucleosome-remodeling
CC activity. This activity may be required for DNA repair. Does not seem
CC to be required for DNA repair and regulation of homologous
CC recombination (HR) (PubMed:18310306). {ECO:0000250,
CC ECO:0000269|PubMed:18310306}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB016875; BAB11616.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94978.1; -; Genomic_DNA.
DR RefSeq; NP_199166.1; NM_123719.2.
DR AlphaFoldDB; Q9FIY7; -.
DR SMR; Q9FIY7; -.
DR STRING; 3702.AT5G43530.1; -.
DR PaxDb; Q9FIY7; -.
DR PRIDE; Q9FIY7; -.
DR ProteomicsDB; 228442; -.
DR EnsemblPlants; AT5G43530.1; AT5G43530.1; AT5G43530.
DR GeneID; 834373; -.
DR Gramene; AT5G43530.1; AT5G43530.1; AT5G43530.
DR KEGG; ath:AT5G43530; -.
DR Araport; AT5G43530; -.
DR TAIR; locus:2158357; AT5G43530.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; Q9FIY7; -.
DR OMA; QCRFQVD; -.
DR OrthoDB; 132523at2759; -.
DR PhylomeDB; Q9FIY7; -.
DR PRO; PR:Q9FIY7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIY7; baseline and differential.
DR Genevisible; Q9FIY7; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
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; IPR014905; HIRAN.
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; PF08797; HIRAN; 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 SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 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 3: Inferred from homology;
KW ATP-binding; Chromatin regulator; DNA damage; DNA repair; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..1277
FT /note="DNA repair protein RAD5B"
FT /id="PRO_0000056189"
FT DOMAIN 674..871
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1113..1277
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 1040..1080
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 271..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 822..825
FT /note="DEAH box"
FT BINDING 687..694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1277 AA; 144333 MW; DA69FDE966145339 CRC64;
MAIVDDAEMR LTESEAVSSS DDRKIVADTP DFIDESSLVI RTTTGVRISA LPAEQSLVDS
DGSNSEVTLP AKDEVISDGF TCVNKEIVES DSFREQNLEI GEPDLDVENR KEAMIIDSIE
NSVVEIVSSA SGDDCNVKVE VVEPELLVEN LVVAKEEEEM IVDSIEDSVV EIVSTASGCD
CNVKVEVVDP ELCVDNLVVV KEEEMIADSI AESVVETVSR GLDYECVDVK VKEEPDLGTK
LEEDSVFPNV LEKKDEVIKV LEDQPSEINK KLEQENDDLF SSGDSDGTSA KRRKMEMESY
APVGVESCIL APTPLRVVKP EKLDTPEVID LESEKSYTHV KMEPVEEIKV EAVKMSSQVE
DVKFSREQKS VYVKKEPVGA RKVKVEDGDF PVEKDWYLVG RSLVTATSTS KGRKLEDNEI
VNFTFSSVAK WKVPNIVRFS TKRCGEIGRL PMEWSNWAVS LLRSGKVKML GRCVAAPPFL
TMMQEIMLYV SFYIHSSIFT DVSKSTWRIG SSPNLESTLH PLLQLFKHLT IKPYQKAEFT
PEELNSRKRS LNLEDDYDER AALLAIAKRR KGCQQSLEQN KDEEEAPESY MNRVVGAADS
YNLEEMEAPS TLTCNLRPYQ KQALYWMSES EKGIDVEKAA ETLHPCWEAY RICDERAPSI
YLNIFSGEAT IQFPTATQMA RGGILADAMG LGKTVMTIAL ILARPGRGNP ENEDVLVADV
NADKRNRKEI HMALTTVKAK GGTLIICPMA LLSQWKDELE THSKPDTVSV LVYYGGDRTH
DAKAIASHDV VLTTYGVLTS AYKQDMANSI FHRIDWYRIV LDEAHTIKSW KTQAAKATFE
LSSHCRWCLT GTPLQNKLED LYSLLCFLHV EPWCNWAWWS KLIQKPYENG DPRGLKLIKA
ILRPLMLRRT KETRDKEGSL ILELPPTDVQ VIECEQSEAE RDFYTALFKR SKVQFDQFVA
QGKVLHNYAN ILELLLRLRQ CCNHPFLVMS RADSQQYADL DSLARRFLDN NPDSVSQNAP
SRAYIEEVIQ DLRDGNSKEC PICLESADDP VLTPCAHRMC RECLLTSWRS PSCGLCPICR
TILKRTELIS CPTDSIFRVD VVKNWKESSK VSELLKCLEK IKKSGSGEKS IVFSQWTSFL
DLLEIPLRRR GFEFLRFDGK LAQKGREKVL KEFNETKQKT ILLMSLKAGG VGLNLTAASS
VFLMDPWWNP AVEEQAIMRI HRIGQKRTVF VRRFIVKDTV EERMQQVQAR KQRMIAGALT
DEEVRSARLE ELKMLFR
