SUV3_SACPA
ID SUV3_SACPA Reviewed; 737 AA.
AC O74727;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=ATP-dependent RNA helicase SUV3, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=SUV3;
OS Saccharomyces paradoxus (Yeast) (Saccharomyces douglasii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=27291;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=CX1;
RX PubMed=14734028; DOI=10.1016/s1567-1356(03)00160-0;
RA Golik P., Zwolinska U., Stepien P.P., Lazowska J.;
RT "The SUV3 gene from Saccharomyces douglasii is a functional equivalent of
RT its Saccharomyces cerevisiae orthologue and is essential for respiratory
RT growth.";
RL FEMS Yeast Res. 4:477-485(2004).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase involved in a variety of
CC mitochondrial post-transcriptional processes and in translation. It is
CC a key control element in nuclear-mitochondrial interactions.
CC {ECO:0000269|PubMed:14734028}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; AJ011586; CAA09716.1; -; Genomic_DNA.
DR AlphaFoldDB; O74727; -.
DR SMR; O74727; -.
DR GO; GO:0005739; C:mitochondrion; 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; 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; IPR044774; Suv3_DEXQc.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 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; Nucleotide-binding;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..737
FT /note="ATP-dependent RNA helicase SUV3, mitochondrial"
FT /id="PRO_0000013305"
FT DOMAIN 226..365
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 390..546
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 737 AA; 84283 MW; E24DD4C2097CA961 CRC64;
MTLVKYSTIA FPLRSFRLFI FVKKALYHNE PHSIDPFHDK NWIVKRPKFL NLPKNEHSKL
DVFQFNFNKS KSNNVYLRDP LFRDNLDKAM QIIYNEKLSS LDAKQVPIKN LAWLKLRDSI
YQQLEDPKQQ TKNYVPSISE IIYPSSPGNL ISLLINCNKI GNSVWKSILK NGQSNNISTL
DKFIHVLQQT FDHMYEQEIL PMMTNTDDTD GAHNVDITNP AEWFSEARKI RRHIIMHIGP
TNSGKTYRAL QKLKSVDRGY YAGPLRLLAR EVYDRFQSEK VRCNLLTGEE VIRDLDDKGN
PAGLTSGTVE MVPINQKFDV VVLDEIQMMS DADRGWAWTN ALLGVVSKEV HLVGEKSVLP
LVKSIVKMTG DKLTINEYER LGKLSVEDKP VKDGIKGLRK GDCVVAFSKK KVLDLKLKIE
KDTNLKVAVI YGSLPPETRV QQAALFNNGE YDIMVASDAI GMGLNLSIDR VVFTTNMKYN
GEELMEMTSS QIKQIGGRAG RFKSKSTSGG VPQGFITSFE SKVLKSVRKA IESPIEYLKT
AVTWPTDEIC AQLMTQFPPG TPTSDLLQTI SDELERSSDN LFTLSDLKSK LKVIGLFEHM
EDIPFFDKLK LSNAPVKDMP MVTKAFTKFC ETIAKRHTRG LLSYRLPFNL LDYNCIPNES
YSLEVYESLY NIITLYFWLS NRYPNYFIDM ESAKDLKYFC EMIIFEKLDR LKKNPYAHKP
FGSTRGQFPS SRGRLRT