SM3L2_ARATH
ID SM3L2_ARATH Reviewed; 1029 AA.
AC Q9FNI6; Q0WQK0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=DNA repair protein RAD5A {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 2 {ECO:0000305};
DE Short=SMARCA3-like protein 2 {ECO:0000305};
DE AltName: Full=RAD5 homolog A {ECO:0000303|PubMed:18310306};
DE Short=AtRAD5a {ECO:0000303|PubMed:18310306};
GN Name=RAD5A {ECO:0000303|PubMed:18310306}; Synonyms=RAD5 {ECO:0000305};
GN OrderedLocusNames=At5g22750; ORFNames=MDJ22.17;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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).
RN [5]
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).
RN [6]
RP FUNCTION.
RX PubMed=20971895; DOI=10.1105/tpc.110.078568;
RA Mannuss A., Dukowic-Schulze S., Suer S., Hartung F., Pacher M., Puchta H.;
RT "RAD5A, RECQ4A, and MUS81 have specific functions in homologous
RT recombination and define different pathways of DNA repair in Arabidopsis
RT thaliana.";
RL Plant Cell 22:3318-3330(2010).
RN [7]
RP FUNCTION.
RX PubMed=21549648; DOI=10.1016/j.dnarep.2011.04.009;
RA Wang S., Wen R., Shi X., Lambrecht A., Wang H., Xiao W.;
RT "RAD5a and REV3 function in two alternative pathways of DNA-damage
RT tolerance in Arabidopsis.";
RL DNA Repair 10:620-628(2011).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF 425-LYS-THR-426.
RX PubMed=27458713; DOI=10.1111/tpj.13283;
RA Kobbe D., Kahles A., Walter M., Klemm T., Mannuss A., Knoll A., Focke M.,
RA Puchta H.;
RT "AtRAD5A is a DNA translocase harboring a HIRAN domain which confers
RT binding to branched DNA structures and is required for DNA repair in
RT vivo.";
RL Plant J. 88:521-530(2016).
CC -!- FUNCTION: Functions in error-free postreplication DNA repair or DNA-
CC damage tolerance (DTT) pathway (PubMed:18310306, PubMed:21549648).
CC Required for homologous recombination (HR) induced by DNA double-strand
CC break (DSB) in somatic cells (PubMed:18310306). Required for damage-
CC induced DNA repair, independently of MUS81 and RECQL4A. Plays a role in
CC synthesis-dependent strand annealing (SDSA) but not in single-strand
CC annealing (SSA) (PubMed:20971895). Possesses double-stranded DNA-
CC dependent ATPase activity. Is able to regress replication forks with
CC preference for forks with a leading strand gap. Is able to catalyze
CC branch migration of Holliday junctions and is unaffected by protein
CC blockades (PubMed:27458713). {ECO:0000269|PubMed:18310306,
CC ECO:0000269|PubMed:20971895, ECO:0000269|PubMed:21549648,
CC ECO:0000269|PubMed:27458713}.
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; AB006699; BAB11681.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93070.1; -; Genomic_DNA.
DR EMBL; AK228695; BAF00599.1; -; mRNA.
DR RefSeq; NP_197667.1; NM_122181.3.
DR AlphaFoldDB; Q9FNI6; -.
DR SMR; Q9FNI6; -.
DR BioGRID; 17613; 5.
DR STRING; 3702.AT5G22750.1; -.
DR PaxDb; Q9FNI6; -.
DR PRIDE; Q9FNI6; -.
DR ProteomicsDB; 232563; -.
DR EnsemblPlants; AT5G22750.1; AT5G22750.1; AT5G22750.
DR GeneID; 832338; -.
DR Gramene; AT5G22750.1; AT5G22750.1; AT5G22750.
DR KEGG; ath:AT5G22750; -.
DR Araport; AT5G22750; -.
DR TAIR; locus:2162504; AT5G22750.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; Q9FNI6; -.
DR OMA; WSNFSFW; -.
DR OrthoDB; 132523at2759; -.
DR PhylomeDB; Q9FNI6; -.
DR PRO; PR:Q9FNI6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNI6; baseline and differential.
DR Genevisible; Q9FNI6; AT.
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 GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:TAIR.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IDA:TAIR.
DR GO; GO:0036297; P:interstrand cross-link repair; IGI:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 2.
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; 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 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 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; DNA damage; DNA recombination;
KW DNA repair; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1029
FT /note="DNA repair protein RAD5A"
FT /id="PRO_0000056188"
FT DOMAIN 406..622
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 864..1029
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 794..834
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 83..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 573..576
FT /note="DEAH box"
FT BINDING 419..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 425..426
FT /note="KT->AA: Abolishes double-stranded DNA-dependent
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:27458713"
SQ SEQUENCE 1029 AA; 114287 MW; 39E72DCB3B713C22 CRC64;
MGTKVSDDLV STVRSVVGSD YSDMDIIRAL HMANHDPTAA INIIFDTPSF AKPDVATPTP
SGSNGGKRVD SGLKGCTFGD SGSVGANHRV EEENESVNGG GEESVSGNEW WFVGCSELAG
LSTCKGRKLK SGDELVFTFP HSKGLKPETT PGKRGFGRGR PALRGASDIV RFSTKDSGEI
GRIPNEWARC LLPLVRDKKI RIEGSCKSAP EALSIMDTIL LSVSVYINSS MFQKHSATSF
KTASNTAEES MFHPLPNLFR LLGLIPFKKA EFTPEDFYSK KRPLSSKDGS AIPTSLLQLN
KVKNMNQDAN GDENEQCISD GDLDNIVGVG DSSGLKEMET PHTLLCELRP YQKQALHWMT
QLEKGNCTDE AATMLHPCWE AYCLADKREL VVYLNSFTGD ATIHFPSTLQ MARGGILADA
MGLGKTVMTI SLLLAHSWKA ASTGFLCPNY EGDKVISSSV DDLTSPPVKA TKFLGFDKRL
LEQKSVLQNG GNLIVCPMTL LGQWKTEIEM HAKPGSLSVY VHYGQSRPKD AKLLSQSDVV
ITTYGVLTSE FSQENSADHE GIYAVRWFRI VLDEAHTIKN SKSQISLAAA ALVADRRWCL
TGTPIQNNLE DLYSLLRFLR IEPWGTWAWW NKLVQKPFEE GDERGLKLVQ SILKPIMLRR
TKSSTDREGR PILVLPPADA RVIYCELSES ERDFYDALFK RSKVKFDQFV EQGKVLHNYA
SILELLLRLR QCCDHPFLVM SRGDTAEYSD LNKLSKRFLS GKSSGLEREG KDVPSEAFVQ
EVVEELRKGE QGECPICLEA LEDAVLTPCA HRLCRECLLA SWRNSTSGLC PVCRNTVSKQ
ELITAPTESR FQVDVEKNWV ESSKITALLE ELEGLRSSGS KSILFSQWTA FLDLLQIPLS
RNNFSFVRLD GTLSQQQREK VLKEFSEDGS ILVLLMSLKA GGVGINLTAA SNAFVMDPWW
NPAVEEQAVM RIHRIGQTKE VKIRRFIVKG TVEERMEAVQ ARKQRMISGA LTDQEVRSAR
IEELKMLFT
