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Protein

ATP-dependent RNA helicase MSS116, mitochondrial

Gene

MSS116

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Specifically involved in the ATP-dependent splicing of the bl1 intron of COB. Also required for efficient mitochondrial translation.4 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi152 – 1598ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: SGD
  • RNA binding Source: SGD
  • RNA strand annealing activity Source: SGD

GO - Biological processi

  • Group II intron splicing Source: SGD
  • Group I intron splicing Source: SGD
  • mRNA processing Source: UniProtKB-KW
  • regulation of translation Source: UniProtKB-KW
  • RNA folding Source: SGD
  • RNA secondary structure unwinding Source: GO_Central
  • transcription elongation from mitochondrial promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29781-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase MSS116, mitochondrial (EC:3.6.4.13)
Gene namesi
Name:MSS116
Ordered Locus Names:YDR194C
ORF Names:YD9346.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR194C.
SGDiS000002602. MSS116.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionSequence analysisAdd
BLAST
Chaini27 – 664638ATP-dependent RNA helicase MSS116, mitochondrialPRO_0000030812Add
BLAST

Proteomic databases

MaxQBiP15424.

Interactioni

Protein-protein interaction databases

BioGridi32246. 50 interactions.
DIPiDIP-5368N.
IntActiP15424. 29 interactions.
MINTiMINT-525340.

Structurei

Secondary structure

1
664
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi89 – 935Combined sources
Helixi104 – 1096Combined sources
Helixi115 – 1228Combined sources
Turni123 – 1253Combined sources
Helixi131 – 14111Combined sources
Beta strandi142 – 15110Combined sources
Helixi158 – 17215Combined sources
Turni173 – 1753Combined sources
Beta strandi183 – 1864Combined sources
Helixi190 – 20617Combined sources
Helixi208 – 2103Combined sources
Beta strandi215 – 2184Combined sources
Helixi224 – 23411Combined sources
Beta strandi237 – 2415Combined sources
Helixi243 – 25715Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi263 – 2675Combined sources
Helixi269 – 2724Combined sources
Turni275 – 2773Combined sources
Helixi278 – 29114Combined sources
Beta strandi300 – 3078Combined sources
Helixi311 – 3155Combined sources
Turni316 – 3194Combined sources
Beta strandi322 – 33110Combined sources
Beta strandi333 – 3353Combined sources
Beta strandi342 – 35110Combined sources
Helixi354 – 36916Combined sources
Turni370 – 3723Combined sources
Beta strandi375 – 3795Combined sources
Helixi383 – 39715Combined sources
Turni398 – 4003Combined sources
Beta strandi403 – 4075Combined sources
Helixi412 – 42413Combined sources
Beta strandi426 – 4327Combined sources
Helixi434 – 4363Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi447 – 4526Combined sources
Beta strandi455 – 4573Combined sources
Helixi459 – 4646Combined sources
Helixi469 – 4713Combined sources
Beta strandi474 – 4818Combined sources
Helixi482 – 4843Combined sources
Helixi485 – 49511Combined sources
Beta strandi501 – 5055Combined sources
Helixi509 – 51810Combined sources
Helixi523 – 53917Combined sources
Helixi541 – 5444Combined sources
Helixi548 – 5569Combined sources
Helixi558 – 5625Combined sources
Beta strandi570 – 5723Combined sources
Helixi574 – 5807Combined sources
Beta strandi583 – 5853Combined sources
Helixi586 – 5916Combined sources
Beta strandi592 – 5943Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3I5XX-ray1.90A37-597[»]
3I5YX-ray2.49A37-597[»]
3I61X-ray2.10A37-597[»]
3I62X-ray1.95A37-597[»]
3SQWX-ray1.91A88-664[»]
3SQXX-ray2.11A88-597[»]
4DB2X-ray3.16A/B/C/D342-596[»]
4DB4X-ray3.60A/B342-596[»]
4TYNX-ray2.96A88-596[»]
4TYWX-ray2.20A88-595[»]
4TYYX-ray2.74A88-596[»]
4TZ0X-ray2.35A88-596[»]
4TZ6X-ray3.21A88-596[»]
ProteinModelPortaliP15424.
SMRiP15424. Positions 88-596.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15424.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini139 – 326188Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini355 – 512158Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi106 – 13429Q motifAdd
BLAST
Motifi267 – 2704DEAD box

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00830000128925.
HOGENOMiHOG000113654.
InParanoidiP15424.
KOiK17679.
OMAiPEAHENI.
OrthoDBiEOG7TBC9R.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTSILIKGR TPVLASRNLL AALSNCNHIT WAVSRRLYND GNRDQRNFGR
60 70 80 90 100
NQRNNNSNRY RNSRFNSRPR TRSREDDDEV HFDKTTFSKL IHVPKEDNSK
110 120 130 140 150
EVTLDSLLEE GVLDKEIHKA ITRMEFPGLT PVQQKTIKPI LSSEDHDVIA
160 170 180 190 200
RAKTGTGKTF AFLIPIFQHL INTKFDSQYM VKAVIVAPTR DLALQIEAEV
210 220 230 240 250
KKIHDMNYGL KKYACVSLVG GTDFRAAMNK MNKLRPNIVI ATPGRLIDVL
260 270 280 290 300
EKYSNKFFRF VDYKVLDEAD RLLEIGFRDD LETISGILNE KNSKSADNIK
310 320 330 340 350
TLLFSATLDD KVQKLANNIM NKKECLFLDT VDKNEPEAHE RIDQSVVISE
360 370 380 390 400
KFANSIFAAV EHIKKQIKER DSNYKAIIFA PTVKFTSFLC SILKNEFKKD
410 420 430 440 450
LPILEFHGKI TQNKRTSLVK RFKKDESGIL VCTDVGARGM DFPNVHEVLQ
460 470 480 490 500
IGVPSELANY IHRIGRTARS GKEGSSVLFI CKDELPFVRE LEDAKNIVIA
510 520 530 540 550
KQEKYEPSEE IKSEVLEAVT EEPEDISDIV ISLISSYRSC IKEYRFSERR
560 570 580 590 600
ILPEIASTYG VLLNDPQLKI PVSRRFLDKL GLSRSPIGKA MFEIRDYSSR
610 620 630 640 650
DGNNKSYDYD DDSEISFRGN KNYNNRSQNR DYDDEPFRRS NNNRRSFSRS
660
NDKNNYSSRN SNIY
Length:664
Mass (Da):76,269
Last modified:April 1, 1990 - v1
Checksum:iDAEECCA4ED0CB2BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48784 Genomic DNA. Translation: CAA88707.1.
BK006938 Genomic DNA. Translation: DAA12036.1.
PIRiS02116.
RefSeqiNP_010480.1. NM_001180502.1.

Genome annotation databases

EnsemblFungiiYDR194C; YDR194C; YDR194C.
GeneIDi851775.
KEGGisce:YDR194C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48784 Genomic DNA. Translation: CAA88707.1.
BK006938 Genomic DNA. Translation: DAA12036.1.
PIRiS02116.
RefSeqiNP_010480.1. NM_001180502.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3I5XX-ray1.90A37-597[»]
3I5YX-ray2.49A37-597[»]
3I61X-ray2.10A37-597[»]
3I62X-ray1.95A37-597[»]
3SQWX-ray1.91A88-664[»]
3SQXX-ray2.11A88-597[»]
4DB2X-ray3.16A/B/C/D342-596[»]
4DB4X-ray3.60A/B342-596[»]
4TYNX-ray2.96A88-596[»]
4TYWX-ray2.20A88-595[»]
4TYYX-ray2.74A88-596[»]
4TZ0X-ray2.35A88-596[»]
4TZ6X-ray3.21A88-596[»]
ProteinModelPortaliP15424.
SMRiP15424. Positions 88-596.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32246. 50 interactions.
DIPiDIP-5368N.
IntActiP15424. 29 interactions.
MINTiMINT-525340.

Proteomic databases

MaxQBiP15424.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR194C; YDR194C; YDR194C.
GeneIDi851775.
KEGGisce:YDR194C.

Organism-specific databases

EuPathDBiFungiDB:YDR194C.
SGDiS000002602. MSS116.

Phylogenomic databases

GeneTreeiENSGT00830000128925.
HOGENOMiHOG000113654.
InParanoidiP15424.
KOiK17679.
OMAiPEAHENI.
OrthoDBiEOG7TBC9R.

Enzyme and pathway databases

BioCyciYEAST:G3O-29781-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP15424.
PROiP15424.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mitochondrial splicing requires a protein from a novel helicase family."
    Seraphin B., Simon M., Boulet A., Faye G.
    Nature 337:84-87(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Overexpression of DEAD box protein pMSS116 promotes ATP-dependent splicing of a yeast group II intron in vitro."
    Niemer I., Schmelzer C., Boerner G.V.
    Nucleic Acids Res. 23:2966-2972(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Overexpressed yeast mitochondrial putative RNA helicase Mss116 partially restores proper mtRNA metabolism in strains lacking the Suv3 mtRNA helicase."
    Minczuk M., Dmochowska A., Palczewska M., Stepien P.P.
    Yeast 19:1285-1293(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  9. "The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function."
    Huang H.-R., Rowe C.E., Mohr S., Jiang Y., Lambowitz A.M., Perlman P.S.
    Proc. Natl. Acad. Sci. U.S.A. 102:163-168(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMS116_YEAST
AccessioniPrimary (citable) accession number: P15424
Secondary accession number(s): D6VSH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 6, 2016
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 10300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.