SUV3M_ARATH
ID SUV3M_ARATH Reviewed; 571 AA.
AC Q9SMX1; O23335; Q0WMU8;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=DExH-box ATP-dependent RNA helicase DExH16, mitochondrial {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:10570936};
DE AltName: Full=ATP-dependent RNA helicase SUV3 {ECO:0000303|PubMed:10570936};
DE Short=AtSUV3 {ECO:0000303|PubMed:10570936};
DE AltName: Full=Protein EMBRYO SAC DEVELOPMENT ARREST 15 {ECO:0000303|PubMed:15634699};
DE AltName: Full=Protein POLLEN DEVELOPMENT DEFECTIVE 17 {ECO:0000303|PubMed:19237690};
DE AltName: Full=Protein POLLEN DEVELOPMENT DEFECTIVE 26 {ECO:0000303|PubMed:19237690};
DE AltName: Full=Protein SUPPRESSOR OF VAR 3 {ECO:0000303|PubMed:10570936};
DE Flags: Precursor;
GN Name=SUV3 {ECO:0000303|PubMed:10570936};
GN Synonyms=EDA15 {ECO:0000303|PubMed:15634699},
GN PDD17 {ECO:0000303|PubMed:19237690}, PDD26 {ECO:0000303|PubMed:19237690};
GN OrderedLocusNames=At4g14790 {ECO:0000312|Araport:AT4G14790};
GN ORFNames=dl3435c {ECO:0000312|EMBL:CAB10258.1},
GN FCAALL.309 {ECO:0000312|EMBL:CAB78521.1};
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:CAB53782.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10570936; DOI=10.1016/s0014-5793(99)01168-0;
RA Gagliardi D., Kuhn J., Spadinger U., Brennicke A., Leaver C.J., Binder S.;
RT "An RNA helicase (AtSUV3) is present in Arabidopsis thaliana
RT mitochondria.";
RL FEBS Lett. 458:337-342(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19237690; DOI=10.1534/genetics.108.090852;
RA Boavida L.C., Shuai B., Yu H.J., Pagnussat G.C., Sundaresan V.,
RA McCormick S.;
RT "A collection of Ds insertional mutants associated with defects in male
RT gametophyte development and function in Arabidopsis thaliana.";
RL Genetics 181:1369-1385(2009).
RN [9]
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: Major helicase player in mitochondrial RNA metabolism.
CC Component of the mitochondrial degradosome (mtEXO) complex, that
CC degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality
CC in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate
CC helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA
CC heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA
CC surveillance system in mitochondria; regulates the stability of mature
CC mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation
CC of non coding processing intermediates (By similarity). Required during
CC pollen development (PubMed:19237690). {ECO:0000250|UniProtKB:Q8IYB8,
CC ECO:0000269|PubMed:19237690}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:10570936};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IYB8};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8IYB8};
CC -!- ACTIVITY REGULATION: Activated by the presence of mitochondrial RNA.
CC {ECO:0000269|PubMed:10570936}.
CC -!- SUBUNIT: Homodimer; in free form. Component of the mitochondrial
CC degradosome (mtEXO) complex which is a heteropentamer containing 2
CC copies of SUPV3L1 and 3 copies of PNPT1.
CC {ECO:0000250|UniProtKB:Q8IYB8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IYB8}.
CC Mitochondrion matrix {ECO:0000269|PubMed:10570936}. Mitochondrion
CC matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q8IYB8}.
CC -!- TISSUE SPECIFICITY: Weakly expressed. {ECO:0000269|PubMed:10570936}.
CC -!- DISRUPTION PHENOTYPE: Variant nuclear number and positions
CC (PubMed:15634699). Pollen development defective (PubMed:19237690).
CC {ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:19237690}.
CC -!- SIMILARITY: Belongs to the DExH box helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10258.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78521.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ132843; CAB53782.1; -; mRNA.
DR EMBL; Z97337; CAB10258.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78521.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83499.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66324.1; -; Genomic_DNA.
DR EMBL; AY139995; AAM98137.1; -; mRNA.
DR EMBL; BT008910; AAP68349.1; -; mRNA.
DR EMBL; AK229714; BAF01552.1; -; mRNA.
DR PIR; H71410; H71410.
DR PIR; T52576; T52576.
DR RefSeq; NP_001328228.1; NM_001340972.1.
DR RefSeq; NP_193215.2; NM_117564.4.
DR AlphaFoldDB; Q9SMX1; -.
DR SMR; Q9SMX1; -.
DR STRING; 3702.AT4G14790.1; -.
DR PaxDb; Q9SMX1; -.
DR PRIDE; Q9SMX1; -.
DR ProteomicsDB; 226794; -.
DR EnsemblPlants; AT4G14790.1; AT4G14790.1; AT4G14790.
DR EnsemblPlants; AT4G14790.2; AT4G14790.2; AT4G14790.
DR GeneID; 827134; -.
DR Gramene; AT4G14790.1; AT4G14790.1; AT4G14790.
DR Gramene; AT4G14790.2; AT4G14790.2; AT4G14790.
DR KEGG; ath:AT4G14790; -.
DR Araport; AT4G14790; -.
DR TAIR; locus:2130235; AT4G14790.
DR eggNOG; KOG0953; Eukaryota.
DR HOGENOM; CLU_010647_2_0_1; -.
DR InParanoid; Q9SMX1; -.
DR OMA; AKTVFPH; -.
DR OrthoDB; 1106167at2759; -.
DR PhylomeDB; Q9SMX1; -.
DR PRO; PR:Q9SMX1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SMX1; baseline and differential.
DR Genevisible; Q9SMX1; AT.
DR GO; GO:0045025; C:mitochondrial degradosome; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblPlants.
DR GO; GO:0003678; F:DNA helicase activity; IEA:EnsemblPlants.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IDA:TAIR.
DR GO; GO:0009561; P:megagametogenesis; IMP:TAIR.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0010929; P:positive regulation of auxin mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0080038; P:positive regulation of cytokinin-activated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IEA:EnsemblPlants.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0016070; P:RNA metabolic process; IDA:TAIR.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022192; SUV3_C.
DR InterPro; IPR041082; Suv3_C_1.
DR InterPro; IPR044774; Suv3_DEXQc.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 1.
DR Pfam; PF18147; Suv3_C_1; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Mitochondrion nucleoid;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 57..571
FT /note="DExH-box ATP-dependent RNA helicase DExH16,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431533"
FT DOMAIN 83..212
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q80YD1"
FT DOMAIN 213..399
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 176..179
FT /note="DEIH box; degenerate"
FT /evidence="ECO:0000305"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 449
FT /note="L -> W (in Ref. 6; BAF01552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 63642 MW; 8A9B52CD180C5851 CRC64;
MAYSVVRLRK VSALGISRVL QADKGSLWRF HFEPEFGDLL RLGVLTRNYR KNSGSPKFDF
TGTGTTSKFD FTDLTCPHTW YPIARKKKRK VILHVGPTNS GKTYSALKHL EQSSSGVYCG
PLRLLAWEVA KRLNKANVPC DLITGQEKDL VEGATHKAVT VEMADVTSVY DCAIIDEIQM
VGCKQRGFAF TRALLGIAAD ELHLCGDPAV VPLVEDILKV TGDDVEVHTY ERLSPLVPLK
VPVSSVSSIK TGDCLVTFSR KDIYAYKKTI ERAGKHLCSV VYGSLPPETR TAQATRFNDE
TNDFDVLVAS DAIGMGLNLN ISRIIFSTLQ KYDGSETRDL TVSEIKQIAG RAGRFQSKFP
IGEVTCLHKE DLPLLHSSLK SPSPILERAG LFPTFDLLSG YSQAHPTHGL YQILEHFVEN
AKLSSNYFIS NVEDMMKVAA IVDELPLGLQ EKYLFVVSPV DVNDEISGQG LAQFAQNFSK
AGIVRLREIL APDRVKVPKT PTELKELESI HKVLDLYVWL SLRLEDSFPD REVAASQKSI
CNLLIEQFLE GNRLNSPARF SRYLRRQKLS E
