SUV3_YEAST
ID SUV3_YEAST Reviewed; 737 AA.
AC P32580; D6W3Y4; Q02649;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=ATP-dependent RNA helicase SUV3, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=SUV3; OrderedLocusNames=YPL029W; ORFNames=LPB2W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF VAL-272.
RX PubMed=1379722; DOI=10.1073/pnas.89.15.6813;
RA Stepien P.P., Margossian S.P., Landsman D., Butow R.A.;
RT "The yeast nuclear gene suv3 affecting mitochondrial post-transcriptional
RT processes encodes a putative ATP-dependent RNA helicase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6813-6817(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12426313; DOI=10.1074/jbc.m208287200;
RA Dziembowski A., Piwowarski J., Hoser R., Minczuk M., Dmochowska A.,
RA Siep M., van der Spek H., Grivell L.A., Stepien P.P.;
RT "The yeast mitochondrial degradosome. Its composition, interplay between
RT RNA helicase and RNase activities and the role in mitochondrial RNA
RT metabolism.";
RL J. Biol. Chem. 278:1603-1611(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Required for intron-independent turnover and processing of
CC mitochondrial RNA. It is a key control element in nuclear-mitochondrial
CC interactions. {ECO:0000269|PubMed:12426313}.
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 -!- SUBUNIT: MSU1 and SUV3 are the two components of the mitochondrial
CC degradosome (mtEXO). {ECO:0000269|PubMed:12426313}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14576278}.
CC -!- MISCELLANEOUS: Present with 1440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; M91167; AAA35135.1; -; Genomic_DNA.
DR EMBL; U36624; AAB68158.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11400.1; -; Genomic_DNA.
DR PIR; S63453; S63453.
DR RefSeq; NP_015296.1; NM_001183843.1.
DR AlphaFoldDB; P32580; -.
DR SMR; P32580; -.
DR BioGRID; 36149; 230.
DR ComplexPortal; CPX-3180; Mitochondrial degradosome complex.
DR DIP; DIP-6302N; -.
DR IntAct; P32580; 3.
DR STRING; 4932.YPL029W; -.
DR MaxQB; P32580; -.
DR PaxDb; P32580; -.
DR PRIDE; P32580; -.
DR EnsemblFungi; YPL029W_mRNA; YPL029W; YPL029W.
DR GeneID; 856078; -.
DR KEGG; sce:YPL029W; -.
DR SGD; S000005950; SUV3.
DR VEuPathDB; FungiDB:YPL029W; -.
DR eggNOG; KOG0953; Eukaryota.
DR GeneTree; ENSGT00390000003100; -.
DR HOGENOM; CLU_010647_2_2_1; -.
DR InParanoid; P32580; -.
DR OMA; ISNPAEW; -.
DR BioCyc; YEAST:G3O-33944-MON; -.
DR PRO; PR:P32580; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32580; protein.
DR GO; GO:0045025; C:mitochondrial degradosome; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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; IDA:SGD.
DR GO; GO:0000372; P:Group I intron splicing; IGI:SGD.
DR GO; GO:0006264; P:mitochondrial DNA replication; IMP:SGD.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0000957; P:mitochondrial RNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IEA:GOC.
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 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; 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_0000013306"
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"
FT MUTAGEN 272
FT /note="V->L: In suv3-1; probably excised introns are less
FT efficiently released."
FT /evidence="ECO:0000269|PubMed:1379722"
FT CONFLICT 165
FT /note="W -> R (in Ref. 1; AAA35135)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="E -> D (in Ref. 1; AAA35135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 84324 MW; 17D18200E5D18099 CRC64;
MALVKYSTVF FPLRSLRLFV SIKKAYYHSE PHSIDLFHDK DWIVKRPKFL NLPKNEHSKL
DIFQFNFNKS ESNNVYLQDS SFKDNLDKAM QFIYNDKLSS LDAKQVPIKN LAWLKLRDYI
YQQLKDPKLQ AKTYVPSVSE IIHPSSPGNL ISLLINCNKI SNLVWKSVLK YSLSNNITTL
DKFIHVLQQT FDHVYEQEIL PMMTNTDDTD GAHNVDITNP AEWFPEARKI RRHIIMHIGP
TNSGKTYRAL QKLKSVDRGY YAGPLRLLAR EVYDRFHAEK IRCNLLTGEE VIRDLDDRGN
SAGLTSGTVE MVPINQKFDV VVLDEIQMMS DGDRGWAWTN ALLGVVSKEV HLCGEKSVLP
LVKSIVKMTG DKLTINEYER LGKLSVEEKP IKDGIKGLRK GDCVVAFSKK KILDLKLKIE
KDTNLKVAVI YGSLPPETRV QQAALFNNGE YDIMVASDAI GMGLNLSIDR VVFTTNMKYN
GEELMEMTSS QIKQIGGRAG RFKSRSASGG VPQGFITSFE SKVLKSVRKA IEAPVEYLKT
AVTWPTDEIC AQLMTQFPPG TPTSVLLQTI SDELEKSSDN LFTLSDLKSK LKVIGLFEHM
EDIPFFDKLK LSNAPVKDMP MVTKAFTKFC ETIAKRHTRG LLSYRLPFNL LDYNCIPNES
YSLEVYESLY NIITLYFWLS NRYPNYFIDM ESAKDLKYFC EMIIFEKLDR LKKNPYAHKP
FGSTRGHLSS SRRRLRT
