SUV3L_ORYSJ
ID SUV3L_ORYSJ Reviewed; 734 AA.
AC Q7X745; A0A0P0WAY9; B9FFJ0; Q0JCN6; Q7FAT2;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ATP-dependent RNA helicase SUV3L, mitochondrial {ECO:0000305};
DE Short=OsSUV3L {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9SMX1};
DE AltName: Full=Protein SUPPRESSOR OF VAR 3-like {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=LOC_Os04g38630 {ECO:0000305}, Os04g0459800 {ECO:0000305};
GN ORFNames=OsJ_15051 {ECO:0000312|EMBL:EEE61124.1},
GN OSJNBa0036B21.27 {ECO:0000312|EMBL:CAE03376.1},
GN OSJNBa0072F16.4 {ECO:0000312|EMBL:CAD40979.2};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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). Confers
CC salinity and drought stress tolerances by maintaining both
CC photosynthesis and antioxidant machinery, probably via an increase in
CC plant hormones levels such as gibberellic acid (GA(3)), the cytokinin
CC zeatin (Z) and indole-3-acetic acid (IAA) (By similarity).
CC {ECO:0000250|UniProtKB:Q10D00, ECO:0000250|UniProtKB:Q8IYB8}.
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:0000250|UniProtKB:Q9SMX1};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7X745-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7X745-2; Sequence=VSP_057327;
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE03376.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EEE61124.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL606460; CAD40979.2; -; Genomic_DNA.
DR EMBL; AL606636; CAE03376.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF14901.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS89537.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS89538.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE61124.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK073573; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK105401; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015633519.1; XM_015778033.1. [Q7X745-1]
DR AlphaFoldDB; Q7X745; -.
DR SMR; Q7X745; -.
DR STRING; 4530.OS04T0459800-01; -.
DR PaxDb; Q7X745; -.
DR PRIDE; Q7X745; -.
DR EnsemblPlants; Os04t0459800-01; Os04t0459800-01; Os04g0459800. [Q7X745-1]
DR EnsemblPlants; Os04t0459800-02; Os04t0459800-02; Os04g0459800. [Q7X745-2]
DR GeneID; 4336047; -.
DR Gramene; Os04t0459800-01; Os04t0459800-01; Os04g0459800. [Q7X745-1]
DR Gramene; Os04t0459800-02; Os04t0459800-02; Os04g0459800. [Q7X745-2]
DR KEGG; osa:4336047; -.
DR eggNOG; KOG0953; Eukaryota.
DR InParanoid; Q7X745; -.
DR OMA; KEETFPY; -.
DR OrthoDB; 1106167at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7X745; 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; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0080038; P:positive regulation of cytokinin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; ISS:UniProtKB.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; ISS:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; ISS: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; 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 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Glycoprotein; Helicase; Hydrolase;
KW Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding; Nucleus;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..60
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 61..734
FT /note="ATP-dependent RNA helicase SUV3L, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431535"
FT DOMAIN 198..356
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q80YD1"
FT DOMAIN 357..525
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 58..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 211..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 29..153
FT /note="Missing (in isoform 2)"
FT /id="VSP_057327"
FT CONFLICT 15
FT /note="S -> Y (in Ref. 6; AK073573)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="Y -> L (in Ref. 6; AK073573)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="R -> W (in Ref. 6; AK105401)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="D -> G (in Ref. 6; AK073573)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="Y -> C (in Ref. 6; AK073573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 734 AA; 82856 MW; 3C584233C592C0C3 CRC64;
MAAAAAIAAA LLRRSTSSQH HRRILLLPLL SHLQRAAPRS PSPWDPPPHH RFFFSSDVTA
EGDSKPRPPL DGKQLWREVS TSEPATGASR LPKATWDAVV ALLRRFGKDP AMSDQALALY
IPASAFPTYA RRFRHFLPAR LSLESAEHLL SLPADDAHAL LLPAFAEFCV THLADELRKH
ESVMAAADLT APHAWYPFAR AMRRRVVYHC GPTNSGKTHN ALTRFAAAKS GVYCSPLRLL
AMEVFDKVNA LGVYCSLRTG QEIKEVPFSN HVACTIEMLS TEEPYEVAVV DEIQMMADPV
RGYAWTRAVL GLKADEIHLC GDPSVLKIVR KICADTGDDL EVHQYERFKP LVVEAKTLLG
DLKNVRSGDC IVAFSRREIF EVKLAIEKFT KHKCCVIYGA LPPETRRQQA KLFNEQDNEY
DVLVASDAVG MGLNLNIRRV VFYSLAKYNG DRMVPVAASQ VKQIAGRAGR RGSIYPDGLT
TTFLLDDLDY LIQCLQQPFE EAKKVGLFPC FEQVESFAIQ FPDLTFNELL DKFRENCRVD
STYFMCHQES IKKVANMLER IQGLSLKDRY NFCFAPVNIR DPKAMYHLLR FATNYSQSRR
VSIAMGMPKG SAKNDTELLD LETKHQVLSM YLWLSHHFEE DHFPHVQKAE EMSINIADLL
AKSLAKASWK PTSRQQAKPR RENEEDNDVE QASDDNAKND SEDGYERSIS RIKPFMRKRL
DRPSQDPSSL NFVA
