SUV3M_ORYSJ
ID SUV3M_ORYSJ Reviewed; 579 AA.
AC Q10D00; A0A0P0W2Y0; B9FBT0; Q94GP3;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=ATP-dependent RNA helicase SUV3, mitochondrial {ECO:0000303|PubMed:23808500};
DE Short=OsSUV3 {ECO:0000303|PubMed:23808500};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9SMX1};
DE AltName: Full=Protein SUPPRESSOR OF VAR 3 {ECO:0000303|PubMed:23808500};
DE Flags: Precursor;
GN Name=SUV3 {ECO:0000303|PubMed:23808500};
GN OrderedLocusNames=LOC_Os03g53500 {ECO:0000305}, Os03g0746500 {ECO:0000305};
GN ORFNames=OJ1124_H03.19 {ECO:0000312|EMBL:AAK71567.1},
GN OsJ_12550 {ECO:0000312|EMBL:EEE59922.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947 {ECO:0000312|Proteomes:UP000059680};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY
RP SALT.
RC STRAIN=cv. Nipponbare;
RX PubMed=23808500; DOI=10.1111/tpj.12277;
RA Tuteja N., Sahoo R.K., Garg B., Tuteja R.;
RT "OsSUV3 dual helicase functions in salinity stress tolerance by maintaining
RT photosynthesis and antioxidant machinery in rice (Oryza sativa L. cv.
RT IR64).";
RL Plant J. 76:115-127(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP FUNCTION.
RX PubMed=25184028; DOI=10.1186/s12284-014-0017-2;
RA Sahoo R.K., Ansari M.W., Tuteja R., Tuteja N.;
RT "OsSUV3 transgenic rice maintains higher endogenous levels of plant
RT hormones that mitigates adverse effects of salinity and sustains crop
RT productivity.";
RL Rice 7:17-19(2014).
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 (By similarity). ATPase and ATP-dependent
CC multisubstrate helicase, able to unwind double-stranded (ds) DNA and
CC RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction
CC (PubMed:23808500). Plays a role in the RNA surveillance system in
CC mitochondria; regulates the stability of mature mRNAs, the removal of
CC aberrantly formed mRNAs and the rapid degradation of non coding
CC processing intermediates (By similarity). Confers salinity and drought
CC stress tolerances by maintaining both photosynthesis and antioxidant
CC machinery, probably via an increase in plant hormones levels such as
CC gibberellic acid (GA(3)), the cytokinin zeatin (Z) and indole-3-acetic
CC acid (IAA) (PubMed:23808500, PubMed:25184028).
CC {ECO:0000250|UniProtKB:Q8IYB8, ECO:0000269|PubMed:23808500,
CC ECO:0000269|PubMed:25184028}.
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:23808500};
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 -!- 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:0000250|UniProtKB:Q9SMX1}. Mitochondrion
CC matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q8IYB8}.
CC -!- INDUCTION: Induced in seedlings in response to high levels of salt.
CC {ECO:0000269|PubMed:23808500}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK71567.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EEE59922.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GQ982584; ACX50964.1; -; mRNA.
DR EMBL; AC087852; AAK71567.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF98846.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13164.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86357.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE59922.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015628092.1; XM_015772606.1.
DR AlphaFoldDB; Q10D00; -.
DR SMR; Q10D00; -.
DR STRING; 4530.OS03T0746500-01; -.
DR PaxDb; Q10D00; -.
DR PRIDE; Q10D00; -.
DR EnsemblPlants; Os03t0746500-01; Os03t0746500-01; Os03g0746500.
DR GeneID; 4334089; -.
DR Gramene; Os03t0746500-01; Os03t0746500-01; Os03g0746500.
DR KEGG; osa:4334089; -.
DR eggNOG; KOG0953; Eukaryota.
DR HOGENOM; CLU_010647_2_0_1; -.
DR InParanoid; Q10D00; -.
DR OMA; AKTVFPH; -.
DR OrthoDB; 1106167at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q10D00; baseline and differential.
DR Genevisible; Q10D00; OS.
DR GO; GO:0045025; C:mitochondrial degradosome; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009561; P:megagametogenesis; IEA:EnsemblPlants.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IEA:EnsemblPlants.
DR GO; GO:0010929; P:positive regulation of auxin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0080038; P:positive regulation of cytokinin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
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; Auxin signaling pathway; Cytokinin signaling pathway;
KW Gibberellin signaling pathway; Glycoprotein; Helicase; Hydrolase;
KW Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding; Nucleus;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 60..579
FT /note="ATP-dependent RNA helicase SUV3, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431534"
FT DOMAIN 72..213
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q80YD1"
FT DOMAIN 214..388
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 5
FT /note="A -> S (in Ref. 6; EEE59922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 65183 MW; 979420494E9599FA CRC64;
MAVAAALLRR RALYSALASP SWLHDTSSCY ICSISGTHSL VNHPNLRLQR GYHNSGKFDL
TDLTHPHIWY PNAREKKRNV FLHVGPTNSG KTHNALKRLE ASSSGVYCGP LRLLAREVAQ
RLNKANVPCN LITGQEREEI EGAKHSSVTV EMADMTTEYQ CAVIDEIQMV GCRSRGFSFT
RALLGLCSDE LHVCGDPAVV PLIQRILEPT GDVVTVQYYE RLSPLVPLKT TLGSFSNIKA
GDCVVTFSRR SIYMLKRRIE MGGKHLCSVV YGSLPPETRT KQATMFNDQD SNLNVLVASD
AIGMGLNLNI SRIIFSTLEK FDGICNRELT VAEIKQIAGR AGRYGSKFPV GEVTCLNSDH
LPLLHSALKS PSPIIERAGL FPTFDVLSLY SRLHGTDFFQ PILERFLDKA KLSPDYFIAD
CEDMLKVAAI VDELPLGLYD KYLFCLSPVD IRDDISTKGL IQFAENYAKK GIVRLKEIFT
PGTLQVPKSH NQLKELESIH KVLELYVWLS FRLEDSYPDR ELAASQKSIC SMLIEEYLER
SGWQQNGRKD FLQKPKRLHQ EYDASQLRKY FQEIDVRSK