SUV3L_ORYSI
ID SUV3L_ORYSI Reviewed; 734 AA.
AC Q01IJ3;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
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 ORFNames=H0219H12.4 {ECO:0000312|EMBL:CAH67447.1},
GN OSIGBa0097P08.9 {ECO:0000312|EMBL:CAH67079.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
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).
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).
CC {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 -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; CR855169; CAH67079.1; -; Genomic_DNA.
DR EMBL; CR855203; CAH67447.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01IJ3; -.
DR SMR; Q01IJ3; -.
DR iPTMnet; Q01IJ3; -.
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; IEA:RHEA.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Helicase; Hydrolase; Mitochondrion;
KW Mitochondrion nucleoid; Nucleotide-binding; Nucleus; 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_0000431536"
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"
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
