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Database: UniProt
Entry: Q10D00
LinkDB: Q10D00
Original site: Q10D00 
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   16-OCT-2019, entry version 97.
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},
GN   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
RP   INDUCTION BY 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
RT   maintaining photosynthesis and antioxidant machinery in rice (Oryza
RT   sativa L. cv. 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.,
RA   Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L.,
RA   Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S.,
RA   Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S.,
RA   Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J.,
RA   de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H.,
RA   Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F.,
RA   Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A.,
RA   Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J.,
RA   Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L.,
RA   Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A.,
RA   Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W.,
RA   Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome
RT   3 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.,
RA   McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
RA   Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
RA   Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
RA   Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using
RT   next 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.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   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'
CC       directionality in an ATP-dependent manner (By similarity). ATPase
CC       and ATP-dependent multisubstrate helicase, able to unwind double-
CC       stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-
CC       to-3' direction (PubMed:23808500). Plays a role in the RNA
CC       surveillance system in mitochondria; regulates the stability of
CC       mature mRNAs, the removal of aberrantly formed mRNAs and the rapid
CC       degradation of non coding processing intermediates (By
CC       similarity). Confers salinity and drought stress tolerances by
CC       maintaining both photosynthesis and antioxidant machinery,
CC       probably via an increase in plant hormones levels such as
CC       gibberellic acid (GA(3)), the cytokinin zeatin (Z) and indole-3-
CC       acetic 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
CC       salt. {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};
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   SMR; Q10D00; -.
DR   STRING; 4530.OS03T0746500-01; -.
DR   PaxDb; 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   eggNOG; ENOG410XSEY; LUCA.
DR   HOGENOM; HOG000175283; -.
DR   InParanoid; Q10D00; -.
DR   KO; K17675; -.
DR   OMA; AKTVFPH; -.
DR   OrthoDB; 1106167at2759; -.
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:ATPase 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:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
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   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022192; SUV3_C.
DR   InterPro; IPR041082; Suv3_C_1.
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; Complete proteome;
KW   Cytokinin signaling pathway; Gibberellin signaling pathway;
KW   Glycoprotein; Helicase; Hydrolase; Mitochondrion;
KW   Mitochondrion nucleoid; Nucleotide-binding; Nucleus;
KW   Reference proteome; Stress response; Transit peptide.
FT   TRANSIT       1     59       Mitochondrion. {ECO:0000255}.
FT   CHAIN        60    579       ATP-dependent RNA helicase SUV3,
FT                                mitochondrial. {ECO:0000255}.
FT                                /FTId=PRO_0000431534.
FT   DOMAIN       72    213       Helicase ATP-binding.
FT                                {ECO:0000250|UniProtKB:Q80YD1}.
FT   DOMAIN      214    388       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      85     92       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   CARBOHYD    309    309       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CONFLICT      5      5       A -> S (in Ref. 6; EEE59922).
FT                                {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
//
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