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ATP-dependent RNA helicase SUPV3L1, mitochondrial (EC 3.6.4.13) (Suppressor of var1 3-like protein 1) (SUV3-like protein 1)

 SUV3_HUMAN              Reviewed;         786 AA.
Q8IYB8; A8K301; O43630;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
20-JUN-2018, entry version 146.
RecName: Full=ATP-dependent RNA helicase SUPV3L1, mitochondrial;
EC=3.6.4.13 {ECO:0000269|PubMed:12466530};
AltName: Full=Suppressor of var1 3-like protein 1;
Short=SUV3-like protein 1;
Flags: Precursor;
Name=SUPV3L1; Synonyms=SUV3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=10453991;
Dmochowska A., Kalita K., Krawczyk M., Golik P., Mroczek K.,
Lazowska J., Stepien P.P., Bartnik E.;
"A human putative Suv3-like RNA helicase is conserved between
Rhodobacter and all eukaryotes.";
Acta Biochim. Pol. 46:155-162(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-207.
PubMed=12466530; DOI=10.1093/nar/gkf647;
Minczuk M., Piwowarski J., Papworth M.A., Awiszus K., Schalinski S.,
Dziembowski A., Dmochowska A., Bartnik E., Tokatlidis K.,
Stepien P.P., Borowski P.;
"Localisation of the human hSuv3p helicase in the mitochondrial matrix
and its preferential unwinding of dsDNA.";
Nucleic Acids Res. 30:5074-5086(2002).
[7]
ENZYME REGULATION.
PubMed=12694177; DOI=10.1046/j.1432-1033.2003.03540.x;
Borowski P., Deinert J., Schalinski S., Bretner M., Ginalski K.,
Kulikowski T., Shugar D.;
"Halogenated benzimidazoles and benzotriazoles as inhibitors of the
NTPase/helicase activities of hepatitis C and related viruses.";
Eur. J. Biochem. 270:1645-1653(2003).
[8]
ENZYME REGULATION.
PubMed=14561097; DOI=10.1021/jm030277k;
Zhang N., Chen H.-M., Koch V., Schmitz H., Minczuk M., Stepien P.,
Fattom A.I., Naso R.B., Kalicharran K., Borowski P., Hosmane R.S.;
"Potent inhibition of NTPase/helicase of the West Nile Virus by ring-
expanded ('fat') nucleoside analogues.";
J. Med. Chem. 46:4776-4789(2003).
[9]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MUTAGENESIS OF
LYS-213.
PubMed=15096047; DOI=10.1021/bi0356449;
Shu Z., Vijayakumar S., Chen C.-F., Chen P.-L., Lee W.-H.;
"Purified human SUV3p exhibits multiple-substrate unwinding activity
upon conformational change.";
Biochemistry 43:4781-4790(2004).
[10]
INTERACTION WITH LAMTOR5/HBXIP.
PubMed=16176273; DOI=10.1111/j.1742-4658.2005.04910.x;
Minczuk M., Mroczek S., Pawlak S.D., Stepien P.P.;
"Human ATP-dependent RNA/DNA helicase hSuv3p interacts with the
cofactor of survivin HBXIP.";
FEBS J. 272:5008-5019(2005).
[11]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=17352692; DOI=10.1042/BC20060108;
Szczesny R.J., Obriot H., Paczkowska A., Jedrzejczak R.,
Dmochowska A., Bartnik E., Formstecher P., Polakowska R.,
Stepien P.P.;
"Down-regulation of human RNA/DNA helicase SUV3 induces apoptosis by a
caspase- and AIF-dependent pathway.";
Biol. Cell 99:323-332(2007).
[12]
FUNCTION, AND INTERACTION WITH WRN AND BLM.
PubMed=17961633; DOI=10.1016/j.mad.2007.09.001;
Pereira M., Mason P., Szczesny R.J., Maddukuri L., Dziwura S.,
Jedrzejczak R., Paul E., Wojcik A., Dybczynska L., Tudek B.,
Bartnik E., Klysik J., Bohr V.A., Stepien P.P.;
"Interaction of human SUV3 RNA/DNA helicase with BLM helicase; loss of
the SUV3 gene results in mouse embryonic lethality.";
Mech. Ageing Dev. 128:609-617(2007).
[13]
SUBCELLULAR LOCATION, ASSOCIATION WITH MITOCHONDRIAL DNA, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18063578; DOI=10.1074/jbc.M708444200;
Bogenhagen D.F., Rousseau D., Burke S.;
"The layered structure of human mitochondrial DNA nucleoids.";
J. Biol. Chem. 283:3665-3675(2008).
[14]
FUNCTION.
PubMed=18678873; DOI=10.1074/jbc.M802991200;
Khidr L., Wu G., Davila A., Procaccio V., Wallace D., Lee W.H.;
"Role of SUV3 helicase in maintaining mitochondrial homeostasis in
human cells.";
J. Biol. Chem. 283:27064-27073(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-725, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL DEGRADOSOME COMPLEX,
RNA-BINDING, HOMODIMERIZATION, AND MUTAGENESIS OF LYS-213 AND
576-THR--LYS-581.
PubMed=19509288; DOI=10.1074/jbc.M109.009605;
Wang D.D., Shu Z., Lieser S.A., Chen P.L., Lee W.H.;
"Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-
kDa heteropentamer to cooperatively degrade double-stranded RNA with a
3'-to-5' directionality.";
J. Biol. Chem. 284:20812-20821(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-99 AND LYS-220, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19864255; DOI=10.1093/nar/gkp903;
Szczesny R.J., Borowski L.S., Brzezniak L.K., Dmochowska A.,
Gewartowski K., Bartnik E., Stepien P.P.;
"Human mitochondrial RNA turnover caught in flagranti: involvement of
hSuv3p helicase in RNA surveillance.";
Nucleic Acids Res. 38:279-298(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-725, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Major helicase player in mitochondrial RNA metabolism.
Component of the mitochondrial degradosome (mtEXO) complex, that
degrades 3' overhang double-stranded RNA with a 3'-to-5'
directionality in an ATP-dependent manner. ATPase and ATP-
dependent multisubstrate helicase, able to unwind double-stranded
(ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3'
direction. Plays a role in the RNA surveillance system in
mitochondria; regulates the stability of mature mRNAs, the removal
of aberrantly formed mRNAs and the rapid degradation of non coding
processing intermediates. Also implicated in recombination and
chromatin maintenance pathways. May protect cells from apoptosis.
Associates with mitochondrial DNA. {ECO:0000269|PubMed:12466530,
ECO:0000269|PubMed:15096047, ECO:0000269|PubMed:17352692,
ECO:0000269|PubMed:17961633, ECO:0000269|PubMed:18678873,
ECO:0000269|PubMed:19509288, ECO:0000269|PubMed:19864255}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:12466530}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15096047};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15096047};
-!- ENZYME REGULATION: Helicase activity toward DNA substrate is
inhibited by micromolar concentrations of 5,6-dichloro-1-(beta-D-
ribofuranosyl)benzotriazole (DRBT) and 4,5,6,7-
tetrabromobenzotriazole (TBBT). Helicase activity toward RNA
substrate is inhibited by elevated concentrations of TBBT.
Inhibited by some ring-expanded nucleoside analogs.
{ECO:0000269|PubMed:12694177, ECO:0000269|PubMed:14561097}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=41.9 uM for ATP {ECO:0000269|PubMed:12466530,
ECO:0000269|PubMed:15096047};
pH dependence:
Optimum pH is 5.0. {ECO:0000269|PubMed:12466530,
ECO:0000269|PubMed:15096047};
Temperature dependence:
Optimum temperature is 30 degrees Celsius.
{ECO:0000269|PubMed:12466530, ECO:0000269|PubMed:15096047};
-!- SUBUNIT: Homodimer; in free form. Component of the mitochondrial
degradosome (mtEXO) complex which is a heteropentamer containing 2
copies of SUPV3L1 and 3 copies of PNPT1. Interacts with
LAMTOR5/HBXIP, WRN and BLM. {ECO:0000269|PubMed:16176273,
ECO:0000269|PubMed:17961633, ECO:0000269|PubMed:19509288}.
-!- INTERACTION:
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-2876787, EBI-741037;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17352692}.
Mitochondrion matrix {ECO:0000269|PubMed:12466530,
ECO:0000269|PubMed:17352692, ECO:0000269|PubMed:19864255}.
Mitochondrion matrix, mitochondrion nucleoid
{ECO:0000269|PubMed:18063578}.
-!- TISSUE SPECIFICITY: Broadly expressed.
{ECO:0000269|PubMed:10453991}.
-!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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EMBL; AF042169; AAB97370.1; -; mRNA.
EMBL; AK290416; BAF83105.1; -; mRNA.
EMBL; AL596223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54314.1; -; Genomic_DNA.
EMBL; BC036112; AAH36112.1; -; mRNA.
CCDS; CCDS7287.1; -.
RefSeq; NP_001288612.1; NM_001301683.1.
RefSeq; NP_003162.2; NM_003171.4.
UniGene; Hs.106469; -.
PDB; 3RC3; X-ray; 2.08 A; A=47-722.
PDB; 3RC8; X-ray; 2.90 A; A=47-722.
PDBsum; 3RC3; -.
PDBsum; 3RC8; -.
ProteinModelPortal; Q8IYB8; -.
SMR; Q8IYB8; -.
BioGrid; 112699; 27.
IntAct; Q8IYB8; 9.
MINT; Q8IYB8; -.
STRING; 9606.ENSP00000352678; -.
ChEMBL; CHEMBL3642; -.
iPTMnet; Q8IYB8; -.
PhosphoSitePlus; Q8IYB8; -.
BioMuta; SUPV3L1; -.
DMDM; 74759699; -.
EPD; Q8IYB8; -.
MaxQB; Q8IYB8; -.
PaxDb; Q8IYB8; -.
PeptideAtlas; Q8IYB8; -.
PRIDE; Q8IYB8; -.
ProteomicsDB; 71153; -.
DNASU; 6832; -.
Ensembl; ENST00000359655; ENSP00000352678; ENSG00000156502.
GeneID; 6832; -.
KEGG; hsa:6832; -.
UCSC; uc001jpe.2; human.
CTD; 6832; -.
DisGeNET; 6832; -.
EuPathDB; HostDB:ENSG00000156502.13; -.
GeneCards; SUPV3L1; -.
HGNC; HGNC:11471; SUPV3L1.
HPA; HPA038380; -.
HPA; HPA038405; -.
MIM; 605122; gene.
neXtProt; NX_Q8IYB8; -.
OpenTargets; ENSG00000156502; -.
PharmGKB; PA36257; -.
eggNOG; KOG0953; Eukaryota.
eggNOG; ENOG410XSEY; LUCA.
GeneTree; ENSGT00390000003100; -.
HOGENOM; HOG000175283; -.
HOVERGEN; HBG108522; -.
InParanoid; Q8IYB8; -.
KO; K17675; -.
OMA; ADMIQHI; -.
OrthoDB; EOG091G02NO; -.
PhylomeDB; Q8IYB8; -.
TreeFam; TF106432; -.
ChiTaRS; SUPV3L1; human.
GeneWiki; SUPV3L1; -.
GenomeRNAi; 6832; -.
PRO; PR:Q8IYB8; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000156502; -.
CleanEx; HS_SUPV3L1; -.
ExpressionAtlas; Q8IYB8; baseline and differential.
Genevisible; Q8IYB8; HS.
GO; GO:0045025; C:mitochondrial degradosome; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0034458; F:3'-5' RNA helicase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
GO; GO:0003678; F:DNA helicase activity; IMP:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; TAS:ProtInc.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0070827; P:chromatin maintenance; IMP:UniProtKB.
GO; GO:0032508; P:DNA duplex unwinding; IMP:UniProtKB.
GO; GO:0006310; P:DNA recombination; IMP:UniProtKB.
GO; GO:0000958; P:mitochondrial mRNA catabolic process; IMP:UniProtKB.
GO; GO:0035946; P:mitochondrial mRNA surveillance; IMP:UniProtKB.
GO; GO:0035945; P:mitochondrial ncRNA surveillance; IMP:UniProtKB.
GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IMP:UniProtKB.
GO; GO:2000827; P:mitochondrial RNA surveillance; IMP:UniProtKB.
GO; GO:0070584; P:mitochondrion morphogenesis; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; IDA:UniProtKB.
GO; GO:0006401; P:RNA catabolic process; IMP:UniProtKB.
CDD; cd00079; HELICc; 1.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR022192; SUV3_C.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF12513; SUV3_C; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51194; HELICASE_CTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Helicase;
Hydrolase; Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transit peptide.
TRANSIT 1 22 Mitochondrion. {ECO:0000255}.
CHAIN 23 786 ATP-dependent RNA helicase SUPV3L1,
mitochondrial.
/FTId=PRO_0000310545.
DOMAIN 194 334 Helicase ATP-binding.
DOMAIN 353 518 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 207 214 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00499}.
REGION 650 786 Interaction with LAMTOR5, important for
protein stability.
{ECO:0000269|PubMed:16176273}.
MOD_RES 99 99 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 220 220 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 725 725 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VARIANT 2 2 S -> F (in dbSNP:rs33998366).
/FTId=VAR_061214.
VARIANT 30 30 P -> T (in dbSNP:rs34596380).
/FTId=VAR_037076.
MUTAGEN 207 207 G->V: Abolishes ATPase and dsDNA and
dsRNA helicase activities.
{ECO:0000269|PubMed:12466530}.
MUTAGEN 213 213 K->A,R: Abolishes ATPase activity.
Abolishes helicase activity and reduces
double-stranded RNA degradation. Does not
abolish formation of the mitochondrial
RNA-degrading complex.
{ECO:0000269|PubMed:15096047,
ECO:0000269|PubMed:19509288}.
MUTAGEN 576 581 Missing: Does not abolish ATPase
activity. Shows a loss of double-stranded
RNA-binding, helicase and degrading
activities.
{ECO:0000269|PubMed:19509288}.
CONFLICT 234 235 KL -> TS (in Ref. 1; AAB97370).
{ECO:0000305}.
CONFLICT 254 254 V -> E (in Ref. 1; AAB97370).
{ECO:0000305}.
HELIX 61 63 {ECO:0000244|PDB:3RC3}.
HELIX 90 102 {ECO:0000244|PDB:3RC3}.
HELIX 104 112 {ECO:0000244|PDB:3RC3}.
HELIX 117 133 {ECO:0000244|PDB:3RC3}.
HELIX 139 149 {ECO:0000244|PDB:3RC3}.
HELIX 155 158 {ECO:0000244|PDB:3RC3}.
HELIX 159 169 {ECO:0000244|PDB:3RC3}.
HELIX 171 174 {ECO:0000244|PDB:3RC3}.
HELIX 176 182 {ECO:0000244|PDB:3RC3}.
HELIX 188 191 {ECO:0000244|PDB:3RC3}.
HELIX 193 196 {ECO:0000244|PDB:3RC3}.
STRAND 201 206 {ECO:0000244|PDB:3RC3}.
STRAND 208 212 {ECO:0000244|PDB:3RC8}.
HELIX 213 223 {ECO:0000244|PDB:3RC3}.
STRAND 224 233 {ECO:0000244|PDB:3RC3}.
HELIX 234 246 {ECO:0000244|PDB:3RC3}.
STRAND 251 254 {ECO:0000244|PDB:3RC3}.
STRAND 263 266 {ECO:0000244|PDB:3RC8}.
STRAND 270 275 {ECO:0000244|PDB:3RC3}.
HELIX 276 278 {ECO:0000244|PDB:3RC3}.
STRAND 281 283 {ECO:0000244|PDB:3RC3}.
STRAND 285 290 {ECO:0000244|PDB:3RC3}.
HELIX 293 297 {ECO:0000244|PDB:3RC3}.
TURN 299 301 {ECO:0000244|PDB:3RC3}.
HELIX 302 311 {ECO:0000244|PDB:3RC3}.
STRAND 314 321 {ECO:0000244|PDB:3RC3}.
HELIX 323 325 {ECO:0000244|PDB:3RC3}.
HELIX 326 336 {ECO:0000244|PDB:3RC3}.
STRAND 340 344 {ECO:0000244|PDB:3RC3}.
STRAND 351 353 {ECO:0000244|PDB:3RC3}.
HELIX 361 363 {ECO:0000244|PDB:3RC3}.
STRAND 368 371 {ECO:0000244|PDB:3RC3}.
HELIX 375 387 {ECO:0000244|PDB:3RC3}.
STRAND 393 395 {ECO:0000244|PDB:3RC3}.
HELIX 401 412 {ECO:0000244|PDB:3RC3}.
STRAND 420 423 {ECO:0000244|PDB:3RC3}.
HELIX 425 428 {ECO:0000244|PDB:3RC3}.
STRAND 435 441 {ECO:0000244|PDB:3RC3}.
HELIX 461 468 {ECO:0000244|PDB:3RC3}.
TURN 475 477 {ECO:0000244|PDB:3RC8}.
STRAND 479 487 {ECO:0000244|PDB:3RC3}.
HELIX 490 499 {ECO:0000244|PDB:3RC3}.
STRAND 508 510 {ECO:0000244|PDB:3RC3}.
HELIX 514 523 {ECO:0000244|PDB:3RC3}.
HELIX 529 539 {ECO:0000244|PDB:3RC3}.
STRAND 546 548 {ECO:0000244|PDB:3RC3}.
HELIX 552 560 {ECO:0000244|PDB:3RC3}.
TURN 561 563 {ECO:0000244|PDB:3RC3}.
HELIX 568 576 {ECO:0000244|PDB:3RC3}.
HELIX 584 598 {ECO:0000244|PDB:3RC3}.
HELIX 605 611 {ECO:0000244|PDB:3RC3}.
HELIX 622 642 {ECO:0000244|PDB:3RC3}.
TURN 646 648 {ECO:0000244|PDB:3RC3}.
HELIX 652 671 {ECO:0000244|PDB:3RC3}.
HELIX 673 682 {ECO:0000244|PDB:3RC3}.
SEQUENCE 786 AA; 87991 MW; FD3BC8EC64C23E42 CRC64;
MSFSRALLWA RLPAGRQAGH RAAICSALRP HFGPFPGVLG QVSVLATASS SASGGSKIPN
TSLFVPLTVK PQGPSADGDV GAELTRPLDK NEVKKVLDKF YKRKEIQKLG ADYGLDARLF
HQAFISFRNY IMQSHSLDVD IHIVLNDICF GAAHADDLFP FFLRHAKQIF PVLDCKDDLR
KISDLRIPPN WYPDARAMQR KIIFHSGPTN SGKTYHAIQK YFSAKSGVYC GPLKLLAHEI
FEKSNAAGVP CDLVTGEERV TVQPNGKQAS HVSCTVEMCS VTTPYEVAVI DEIQMIRDPA
RGWAWTRALL GLCAEEVHLC GEPAAIDLVM ELMYTTGEEV EVRDYKRLTP ISVLDHALES
LDNLRPGDCI VCFSKNDIYS VSRQIEIRGL ESAVIYGSLP PGTKLAQAKK FNDPNDPCKI
LVATDAIGMG LNLSIRRIIF YSLIKPSINE KGERELEPIT TSQALQIAGR AGRFSSRFKE
GEVTTMNHED LSLLKEILKR PVDPIRAAGL HPTAEQIEMF AYHLPDATLS NLIDIFVDFS
QVDGQYFVCN MDDFKFSAEL IQHIPLSLRV RYVFCTAPIN KKQPFVCSSL LQFARQYSRN
EPLTFAWLRR YIKWPLLPPK NIKDLMDLEA VHDVLDLYLW LSYRFMDMFP DASLIRDLQK
ELDGIIQDGV HNITKLIKMS ETHKLLNLEG FPSGSQSRLS GTLKSQARRT RGTKALGSKA
TEPPSPDAGE LSLASRLVQQ GLLTPDMLKQ LEKEWMTQQT EHNKEKTESG THPKGTRRKK
KEPDSD


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