SUV3_DROME
ID SUV3_DROME Reviewed; 763 AA.
AC Q9VN03; H1UUI2; Q95TU1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP-dependent RNA helicase SUV3 homolog, mitochondrial {ECO:0000303|PubMed:26152302};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q8IYB8};
DE Flags: Precursor;
GN Name=Suv3 {ECO:0000312|FlyBase:FBgn0037232};
GN ORFNames=CG9791 {ECO:0000312|FlyBase:FBgn0037232};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:AEX93152.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26152302; DOI=10.1093/nar/gkv692;
RA Clemente P., Pajak A., Laine I., Wibom R., Wedell A., Freyer C.,
RA Wredenberg A.;
RT "SUV3 helicase is required for correct processing of mitochondrial
RT transcripts.";
RL Nucleic Acids Res. 43:7398-7413(2015).
CC -!- FUNCTION: Major helicase player in mitochondrial RNA metabolism and
CC maintenance (PubMed:26152302). Likely component of the mitochondrial
CC degradosome (mtEXO) complex, that degrades 3' overhang double-stranded
CC RNA with a 3'-to-5' directionality in an ATP-dependent manner (By
CC similarity). ATPase and ATP-dependent multisubstrate helicase, able to
CC unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in
CC the 5'-to-3' direction (By similarity). Regulates mRNA stability and is
CC required for the correct processing and maturation of mitochondrial
CC transcripts (PubMed:26152302). {ECO:0000250|UniProtKB:Q8IYB8,
CC ECO:0000269|PubMed:26152302}.
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:Q8IYB8};
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:26152302}.
CC Note=Unlike in mammals, does not localize to the nucleus.
CC {ECO:0000269|PubMed:26152302}.
CC -!- DISRUPTION PHENOTYPE: Lethal due to mitochondrial dysfunction. 3 days
CC after egg laying (ael) larvae display a severe decrease in size and a
CC significant increase in mitochondrial mRNA steady-state levels which
CC results in larval lethality by 4 days ael. RNAi-mediated knockdown is
CC pupal lethal. Larvae display significant increases in mitochondrial
CC mRNA and anti-sense RNA steady-state levels but rRNA (12S and 16S)
CC steady-state levels and de novo transcription are not affected. Larvae
CC also display severe decreases in mitochondrial tRNA steady state levels
CC and accumulation of unprocessed precursor transcripts. These defects
CC result in a general decrease in mitochondrial translation and severe
CC decreases in the activity of respiratory chain complexes I, I+III,
CC II+III and IV, whereas the nuclear encoded complex II displays a
CC relatively small decrease. Also displays a small decrease in the
CC peptide steady-state levels of the mitochondrial encoded subunit cox3
CC and the nuclear encoded subunit ND-30. {ECO:0000269|PubMed:26152302}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13756.1; Type=Frameshift; 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; AE014297; AAF52149.3; -; Genomic_DNA.
DR EMBL; AE014297; ALI30527.1; -; Genomic_DNA.
DR EMBL; AY058527; AAL13756.1; ALT_FRAME; mRNA.
DR EMBL; BT133067; AEX93152.1; -; mRNA.
DR RefSeq; NP_001303458.1; NM_001316529.1.
DR RefSeq; NP_649452.3; NM_141195.4.
DR AlphaFoldDB; Q9VN03; -.
DR SMR; Q9VN03; -.
DR BioGRID; 65764; 1.
DR IntAct; Q9VN03; 2.
DR STRING; 7227.FBpp0271517; -.
DR PaxDb; Q9VN03; -.
DR PRIDE; Q9VN03; -.
DR EnsemblMetazoa; FBtr0273009; FBpp0271517; FBgn0037232.
DR EnsemblMetazoa; FBtr0347365; FBpp0312545; FBgn0037232.
DR GeneID; 40543; -.
DR KEGG; dme:Dmel_CG9791; -.
DR UCSC; CG9791-RC; d. melanogaster.
DR CTD; 40543; -.
DR FlyBase; FBgn0037232; Suv3.
DR VEuPathDB; VectorBase:FBgn0037232; -.
DR eggNOG; KOG0953; Eukaryota.
DR GeneTree; ENSGT00390000003100; -.
DR HOGENOM; CLU_010647_3_2_1; -.
DR InParanoid; Q9VN03; -.
DR OMA; AKTVFPH; -.
DR OrthoDB; 1106167at2759; -.
DR PhylomeDB; Q9VN03; -.
DR BioGRID-ORCS; 40543; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 40543; -.
DR PRO; PR:Q9VN03; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037232; Expressed in thoracico-abdominal ganglion (Drosophila) and 26 other tissues.
DR Genevisible; Q9VN03; DM.
DR GO; GO:0045025; C:mitochondrial degradosome; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IMP:FlyBase.
DR GO; GO:0097222; P:mitochondrial mRNA polyadenylation; IMP:FlyBase.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0000963; P:mitochondrial RNA processing; IMP:FlyBase.
DR GO; GO:0090646; P:mitochondrial tRNA processing; IMP:FlyBase.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:FlyBase.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IMP:FlyBase.
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 InterPro; IPR041453; Suv3_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 1.
DR Pfam; PF18147; Suv3_C_1; 1.
DR Pfam; PF18114; Suv3_N; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..763
FT /note="ATP-dependent RNA helicase SUV3 homolog,
FT mitochondrial"
FT /id="PRO_0000310552"
FT DOMAIN 181..321
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 330..508
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 724..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 763 AA; 86625 MW; DA7236B10764ADCC CRC64;
MQNCRRCISL TGLLRMTLYL RPSFSIDLSL RRLHRAAFLF SRKKPETNLS TLFKPVQVHA
YVDSEDVGSE LSGKLEKAEL LKILNKFTQR REIKSLCNEN GLDDYLQQQA FGSFRRFCIE
AENLPVDLHI TFSDITQGAG HIDDIFPYFL RHAKTVFPHL DCMDDLKKIS DLRQPANWYS
NARAITRKIV FHAGPTNSGK TYHAMERYLS AKTGVYCGPL KLLATEVYNK ANERGTPCDL
VTGEERKFGI SESLPANHVA CTVEMTSVNT PYEVAVIDEI QQIRDPQRGW AWTRAFLGLI
ADEVHVCGEP GALDLLQKIC ETTGETVEVR LYDRLTELTV ENTALGSLDN IVPGDCIVCF
SKHDIYTVSR EIEARGKEVA VIYGGLPPGT KLAQAAKFND PANSCKVMVA TDAIGMGLNL
SIRRIIFYSL IKPSMNERGE REIDTISVSS ALQIAGRAGR FRTQWEHGYV TAFKSEDLQT
LQRILARTPE PIKQAGLHPT ADQIELYAYH LPSSSLSNLM DIFVNLCTVD DSLYFMCNIE
DFKFLAEMIQ HVALPLRARY VFCCAPINRK MPFVCSMFLK VARQYSRNEP ITFDFIKKNC
GWPFKLPKTI LDLVHLEAVF DVMDLYLWLS YRFMDLFPEA AYVRDAQKEL DEIIQQGVFQ
ITRLLKNTEA SQDGETSNYA IRRITHVKEP RLPSLSRGRL TERLLAQGLL TPGMLSELRK
EWDAQQLGKS NSQSNENSEP VVNSDDEDNY SGIGRKTRKK RRK
