SUV3_DROPS
ID SUV3_DROPS Reviewed; 762 AA.
AC Q295E6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ATP-dependent RNA helicase SUV3 homolog, mitochondrial {ECO:0000250|UniProtKB:Q9VN03};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q8IYB8};
DE Flags: Precursor;
GN ORFNames=GA22038;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Major helicase player in mitochondrial RNA metabolism and
CC maintenance. Likely component of the mitochondrial degradosome (mtEXO)
CC complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5'
CC directionality in an ATP-dependent manner. ATPase and ATP-dependent
CC multisubstrate helicase, able to unwind double-stranded (ds) DNA and
CC RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Regulates
CC mRNA stability and is required for the correct processing and
CC maturation of mitochondrial transcripts. {ECO:0000250|UniProtKB:Q8IYB8,
CC ECO:0000250|UniProtKB:Q9VN03}.
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:0000250|UniProtKB:Q9VN03}.
CC Note=Unlike in mammals, does not localize to the nucleus.
CC {ECO:0000250|UniProtKB:Q9VN03}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; CM000070; EAL28766.1; -; Genomic_DNA.
DR AlphaFoldDB; Q295E6; -.
DR SMR; Q295E6; -.
DR STRING; 7237.FBpp0281337; -.
DR eggNOG; KOG0953; Eukaryota.
DR HOGENOM; CLU_010647_3_2_1; -.
DR InParanoid; Q295E6; -.
DR OMA; AKTVFPH; -.
DR PhylomeDB; Q295E6; -.
DR Proteomes; UP000001819; Genome assembly.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
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; IEA:UniProtKB-EC.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
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; IPR041082; Suv3_C_1.
DR InterPro; IPR044774; Suv3_DEXQc.
DR InterPro; IPR041453; Suv3_N.
DR Pfam; PF00271; Helicase_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 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..762
FT /note="ATP-dependent RNA helicase SUV3 homolog,
FT mitochondrial"
FT /id="PRO_0000310553"
FT DOMAIN 181..321
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 331..508
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 716..762
FT /note="Disordered"
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 762 AA; 85932 MW; 834C75D387F41148 CRC64;
MQNTRRCISL ICVTRQPPSL RATYGAVAAA RCLHRAPPQS SRKKHETNVS TLFKPVQVQA
NVDCEDVGSE LVGKLEKSEL LKILNKFTQR RETKSLCSEN GLDSYLQQQA FGSFRRYCIE
AENLPVDLHI IFSDIMQGAG HIDDIFPYFL RHAKTVFPHL DCMDDLKKIS DLRQPANWYT
NARALTRKIV FHSGPTNSGK TYHAMERYLS AKTGVYCGPL KLLATEVYNK ANERGTPCDL
VTGEERKFGI SDNSPANHVA CTVEMTSVNT PYEVAVIDEI QQIRDPQRGW AWTRAFLGLI
ADEVHVCGEA GALELLQKIC ETTGETVEVR RYDRLTELTV EDSALGSLDN VMPGDCIVCF
SKHDIYTVSR EIEARGKEVA VIYGGLPPGT KLAQAAKFND PANSCKVMVA TDAIGMGLNL
SIRRIIFYSL VKPTMNERGE REIDTISVSS ALQIAGRAGR FRTQWEHGYV TAFKSEDLQT
LQRILAQTPE PLKQAGLHPT ADQIELYAYH LPNSSLSNLM DIFVNLCTVD DSLYFMCNIE
DFKFLAEMIQ HVPLPLRARY VFCCAPINRK MPFVCSMFLK IARQYSRNEP ITFEFIKSNC
GWPFKLPKTI LDLVHLESVF DVMDLYRFMD LFPEAGNVRE AQKELDEIIQ QGVFQITRLL
KNTEASQEGE TPNYSMRRVT HVKEPRLPSA SRGRLTDRLL AQGLLTPGML SELRKEWDAQ
QVGQAAAAST SSKESQESPP DDSDDEDSYP GSYKKTRRKR RK
