SUV3_SCHPO
ID SUV3_SCHPO Reviewed; 647 AA.
AC O94445;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ATP-dependent RNA helicase suv3, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=suv3; ORFNames=SPAC637.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Required for intron-independent turnover and processing of
CC mitochondrial RNA. It is a key control element in nuclear-mitochondrial
CC interactions (By similarity). {ECO:0000250}.
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 matrix
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the helicase family. {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; CU329670; CAA22590.1; -; Genomic_DNA.
DR PIR; T39003; T39003.
DR RefSeq; NP_594629.1; NM_001020057.2.
DR AlphaFoldDB; O94445; -.
DR SMR; O94445; -.
DR BioGRID; 280092; 5.
DR STRING; 4896.SPAC637.11.1; -.
DR MaxQB; O94445; -.
DR PaxDb; O94445; -.
DR PRIDE; O94445; -.
DR EnsemblFungi; SPAC637.11.1; SPAC637.11.1:pep; SPAC637.11.
DR GeneID; 2543678; -.
DR KEGG; spo:SPAC637.11; -.
DR PomBase; SPAC637.11; -.
DR VEuPathDB; FungiDB:SPAC637.11; -.
DR eggNOG; KOG0953; Eukaryota.
DR HOGENOM; CLU_010647_2_3_1; -.
DR InParanoid; O94445; -.
DR PhylomeDB; O94445; -.
DR PRO; PR:O94445; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0045025; C:mitochondrial degradosome; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
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; ISS:PomBase.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IMP:PomBase.
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 Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..647
FT /note="ATP-dependent RNA helicase suv3, mitochondrial"
FT /id="PRO_0000310786"
FT DOMAIN 166..303
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 326..486
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 647 AA; 73120 MW; C82F2770A7D869F1 CRC64;
MFLETLIHGV TFCVPFFSKS ARIHTLSKDV FQQRKFPGNT LWAAALNRFT AYLFASKELS
SKQAYLAQDF VNVCKDASVF QNVYYYELKK NILTDLGFSD LKNSDKSLAL SKSSSTFDLQ
KIKKIHDCLL SEYRKYVRYQ ERIEETRPDL QKQLTDLKNP IEWYPGARKL RRHIIMHVGP
TNSGKTHRAL ERLKTCKKGI FAGPLRLLAH EIYNRLQANG IACNLYTGEE IRNDYPFPQV
VSCTVEMCNL STTFDVAVID EIQMMADPSR GYAWTQCLLG LQAKEIHLCG EESVVKLVRS
IAKMTQDDFT VYRYERLNPL HVAEKSLNGK LSELKDGDCV VAFSRKNIFT LKSKIDQALG
KKSAVIYGSL PPEVRNQQAS LFNSKSSDEN ILLASDAIGM GLNLGVKRIV FSDLKKFSGV
STIDIPVPQI KQIAGRAGRH NPNGSKQSAG IVTTLYQKDF AKLNRAMNLP TKNLFNACIG
AKDDLFFRYL SLFSDDIPQK LIFDRYFKLA KTTTPFVVSE GALSTFIIEY LDHIKGLTIK
DKIKLLGCPV LKHSKYAPLF IREIGCVIAQ GKRLQIYDLK SVPLEILERG IPTTETELQQ
LEQLHKLIVA YMWASIRYPA ILQNGAAEKT KAIAEAFLIK GISKLQK
