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Protein

Mitochondrial metalloendopeptidase OMA1

Gene

OMA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Protease that is part of the quality control system in the inner membrane of mitochondria. Cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Can cleave the misfolded multi-pass membrane protein OXA1.1 Publication

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi203 – 2031Zinc; catalyticPROSITE-ProRule annotation
Active sitei204 – 2041PROSITE-ProRule annotation
Metal bindingi207 – 2071Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi257 – 2571Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: SGD

GO - Biological processi

  • misfolded or incompletely synthesized protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32050-MONOMER.

Protein family/group databases

MEROPSiM48.018.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial metalloendopeptidase OMA1 (EC:3.4.24.-)
Gene namesi
Name:OMA1
Ordered Locus Names:YKR087C
ORF Names:YKR407
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKR087C.
SGDiS000001795. OMA1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6767Mitochondrial intermembraneSequence analysisAdd
BLAST
Transmembranei68 – 8821HelicalSequence analysisAdd
BLAST
Topological domaini89 – 223135Mitochondrial matrixSequence analysisAdd
BLAST
Transmembranei224 – 24421HelicalSequence analysisAdd
BLAST
Topological domaini245 – 345101Mitochondrial intermembraneSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi204 – 2041E → Q: Loss of protease activity. 1 Publication
Mutagenesisi207 – 2071H → Y: Loss of protease activity. 1 Publication
Mutagenesisi212 – 2121H → Y: Loss of protease activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Mitochondrial metalloendopeptidase OMA1PRO_0000203225Add
BLAST

Proteomic databases

MaxQBiP36163.

Interactioni

Protein-protein interaction databases

BioGridi34218. 17 interactions.
DIPiDIP-5087N.
MINTiMINT-544282.

Structurei

3D structure databases

ProteinModelPortaliP36163.
SMRiP36163. Positions 170-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M48 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000007027.
HOGENOMiHOG000266075.
InParanoidiP36163.
OMAiICANDDG.
OrthoDBiEOG7R573W.

Family and domain databases

InterProiIPR001915. Peptidase_M48.
[Graphical view]
PfamiPF01435. Peptidase_M48. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36163-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRNIIRFKG FGKGTSGGFL KPVSFRVQLT RCYRYDNGPS YRRFNNGEYS
60 70 80 90 100
QKSSFKSILL DKSSRKYLAL LFGGCSLFYY THLDKAPVSD RSRFIWVSRP
110 120 130 140 150
LELTIGNYTY KSIWRQTQQE ILPPQHPLSI KIENIFMKIV EAAYKDPSVD
160 170 180 190 200
NSLLDGIKWE IHVVNDPTAS PNAFVLPGGK VFIFSSILPI CANDDGIATV
210 220 230 240 250
LAHEFAHQLA RHTAENLSKA PIYSLLGLVL YTVTGAHAIN NILLDGFLRM
260 270 280 290 300
PASRQMETEA DYIGLMIMSR ACFQPQESIK VWERMANFEK QMNRGGVVNM
310 320 330 340
EFLSTHPAST RRIENMSKWL PKANEIYEQS DCSSMGNYYK SFFSM
Length:345
Mass (Da):39,328
Last modified:May 16, 2006 - v2
Checksum:i95B0EBCD25F435CF
GO

Sequence cautioni

The sequence CAA81638.1 differs from that shown. Reason: Frameshift at position 33. Curated
The sequence CAA82166.1 differs from that shown. Reason: Frameshift at position 33. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z27116 Genomic DNA. Translation: CAA81638.1. Frameshift.
Z28312 Genomic DNA. Translation: CAA82166.1. Frameshift.
BK006944 Genomic DNA. Translation: DAA09237.1.
PIRiS38165.
RefSeqiNP_013013.2. NM_001179877.1.

Genome annotation databases

EnsemblFungiiYKR087C; YKR087C; YKR087C.
GeneIDi853962.
KEGGisce:YKR087C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z27116 Genomic DNA. Translation: CAA81638.1. Frameshift.
Z28312 Genomic DNA. Translation: CAA82166.1. Frameshift.
BK006944 Genomic DNA. Translation: DAA09237.1.
PIRiS38165.
RefSeqiNP_013013.2. NM_001179877.1.

3D structure databases

ProteinModelPortaliP36163.
SMRiP36163. Positions 170-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34218. 17 interactions.
DIPiDIP-5087N.
MINTiMINT-544282.

Protein family/group databases

MEROPSiM48.018.

Proteomic databases

MaxQBiP36163.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR087C; YKR087C; YKR087C.
GeneIDi853962.
KEGGisce:YKR087C.

Organism-specific databases

EuPathDBiFungiDB:YKR087C.
SGDiS000001795. OMA1.

Phylogenomic databases

GeneTreeiENSGT00390000007027.
HOGENOMiHOG000266075.
InParanoidiP36163.
OMAiICANDDG.
OrthoDBiEOG7R573W.

Enzyme and pathway databases

BioCyciYEAST:G3O-32050-MONOMER.

Miscellaneous databases

NextBioi975389.
PROiP36163.

Family and domain databases

InterProiIPR001915. Peptidase_M48.
[Graphical view]
PfamiPF01435. Peptidase_M48. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open reading frames."
    Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G., Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.
    Yeast 10:231-245(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [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. "Oma1, a novel membrane-bound metallopeptidase in mitochondria with activities overlapping with the m-AAA protease."
    Kaeser M., Kambacheld M., Kisters-Woike B., Langer T.
    J. Biol. Chem. 278:46414-46423(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-204; HIS-207 AND HIS-212.
  5. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF FRAMESHIFT.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiOMA1_YEAST
AccessioniPrimary (citable) accession number: P36163
Secondary accession number(s): D6VXE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 16, 2006
Last modified: May 11, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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.