SUV3L_ARATH
ID SUV3L_ARATH Reviewed; 776 AA.
AC F4KFV7; Q9FLF1;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=DExH-box ATP-dependent RNA helicase DExH18, mitochondrial {ECO:0000305};
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase SUV3L {ECO:0000305};
DE Short=AtSUV3L;
DE AltName: Full=Protein SUPPRESSOR OF VAR 3-like {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At5g39840 {ECO:0000312|Araport:AT5G39840};
GN ORFNames=K13H13.20 {ECO:0000312|EMBL:BAB10208.1};
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|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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. {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 DExH box helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10208.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010077; BAB10208.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB024023; BAB10208.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED94482.1; -; Genomic_DNA.
DR RefSeq; NP_198800.1; NM_123347.2.
DR AlphaFoldDB; F4KFV7; -.
DR SMR; F4KFV7; -.
DR STRING; 3702.AT5G39840.1; -.
DR PaxDb; F4KFV7; -.
DR PRIDE; F4KFV7; -.
DR ProteomicsDB; 226793; -.
DR EnsemblPlants; AT5G39840.1; AT5G39840.1; AT5G39840.
DR GeneID; 833980; -.
DR Gramene; AT5G39840.1; AT5G39840.1; AT5G39840.
DR KEGG; ath:AT5G39840; -.
DR Araport; AT5G39840; -.
DR TAIR; locus:2151911; AT5G39840.
DR eggNOG; KOG0953; Eukaryota.
DR HOGENOM; CLU_010647_3_1_1; -.
DR InParanoid; F4KFV7; -.
DR OMA; AKNGLYC; -.
DR OrthoDB; 1106167at2759; -.
DR PRO; PR:F4KFV7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KFV7; baseline and differential.
DR Genevisible; F4KFV7; AT.
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; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
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; SM00487; DEXDc; 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; Helicase; Hydrolase; Mitochondrion; Mitochondrion nucleoid;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..84
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 85..776
FT /note="DExH-box ATP-dependent RNA helicase DExH18,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431537"
FT DOMAIN 268..426
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q80YD1"
FT DOMAIN 427..595
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 80..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 361..364
FT /note="DEIH box; degenerate"
FT /evidence="ECO:0000305"
FT COMPBIAS 85..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 281..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 776 AA; 88194 MW; F66E617ACD0611C6 CRC64;
MARGVAGVLR RAYSSRVTVL FSTRNLHSFR ESESRSLCNS DFDVPTNRFC SGNRVRIQFP
WNDYRFGCFE IGKVRSFSST VDNNGENDDI EESVGSESDD YDEEGLINEL SDVDEGLLND
SVVAETDEIG SEAARALNDR YHDPVELYRE LRGSEVRSKL QHSEWDSLHE IFGFFAQSGW
AANQALAIYI GKSFFPTAVS KFRDFFIEKC GIEVVQDLVR VGPTDVAVKF LFPVFVEFCI
EEFPDEIKRF KSIVDTADLT KPATWFPFAR AMKRKIVYHC GPTNSGKTYN ALQRFMEAKN
GLYCSPLRLL AMEVFDKVNA LGIYCSLLTG QEKKYVPFAN HVSCTVEMVS TDELYEVAVL
DEIQMMADPS RGHAWTKALL GLKADEIHLC GDPSVLDIVR KMCADTGDEL VEEHYERFKP
LVVEAKTLLG ELKNVKSGDC VVAFSRREIF EVKMAIEKHT NHRCCVIYGA LPPETRRQQA
KLFNDQENEY DVLVASDAVG MGLNLNIRRV VFYSLNKYNG DKIVPVAASQ VKQIAGRAGR
RGSRYPDGLT TTLHLEDLNY LIECLQQPFD EVTKVGLFPF FEQIELFAAQ VPDMAFSNLL
EHFGKHCRLD GSYFLCRHDH VKKVANMLEK VEGLSLEDRF NFCFAPVNIR NPRAMHNLYR
FASSYSQNMP VNVAMGIPKS SAKSDAQLLD LESRHQILSM YLWLSNQFEE NFPFVEKVEA
MATNIAELLG ESLSKASWKM ESKEEKVKGQ MKEDRGYERP ASLIKLVKKR KDEKLV
