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Protein

Mitochondrial-processing peptidase subunit beta

Gene

MAS1

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

Cleaves presequences (transit peptides) from mitochondrial protein precursors.

Catalytic activityi

Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi70ZincPROSITE-ProRule annotation1 Publication1
Active sitei73Proton acceptor1
Metal bindingi74ZincPROSITE-ProRule annotation1 Publication1
Metal bindingi150ZincPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32293-MONOMER.
YEAST:G3O-32293-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.
SABIO-RKP10507.

Protein family/group databases

MEROPSiM16.980.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial-processing peptidase subunit beta (EC:3.4.24.64)
Alternative name(s):
Beta-MPP
PEP
Gene namesi
Name:MAS1
Synonyms:MIF1
Ordered Locus Names:YLR163C
ORF Names:L9632.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR163C.
SGDiS000004153. MAS1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi73E → Q: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 20Mitochondrion1 PublicationAdd BLAST20
ChainiPRO_000002678421 – 462Mitochondrial-processing peptidase subunit betaAdd BLAST442

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei243PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10507.
PRIDEiP10507.

PTM databases

iPTMnetiP10507.

Interactioni

Subunit structurei

Heterodimer of alpha and beta subunits.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAS2P119145EBI-11212,EBI-11205

Protein-protein interaction databases

BioGridi31436. 22 interactors.
DIPiDIP-2402N.
IntActiP10507. 14 interactors.
MINTiMINT-614379.

Structurei

Secondary structure

1462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 30Combined sources4
Beta strandi36 – 41Combined sources6
Beta strandi46 – 55Combined sources10
Helixi58 – 60Combined sources3
Turni63 – 67Combined sources5
Helixi68 – 75Combined sources8
Beta strandi78 – 82Combined sources5
Helixi85 – 94Combined sources10
Beta strandi98 – 103Combined sources6
Beta strandi105 – 115Combined sources11
Helixi116 – 118Combined sources3
Helixi119 – 131Combined sources13
Helixi137 – 154Combined sources18
Helixi158 – 170Combined sources13
Turni171 – 173Combined sources3
Helixi175 – 177Combined sources3
Helixi184 – 189Combined sources6
Helixi192 – 202Combined sources11
Helixi205 – 207Combined sources3
Beta strandi208 – 215Combined sources8
Helixi218 – 229Combined sources12
Beta strandi254 – 259Combined sources6
Beta strandi264 – 273Combined sources10
Helixi282 – 292Combined sources11
Beta strandi294 – 296Combined sources3
Turni297 – 299Combined sources3
Beta strandi302 – 305Combined sources4
Helixi308 – 314Combined sources7
Beta strandi321 – 329Combined sources9
Beta strandi334 – 343Combined sources10
Turni344 – 346Combined sources3
Helixi349 – 364Combined sources16
Helixi370 – 385Combined sources16
Helixi391 – 405Combined sources15
Helixi411 – 419Combined sources9
Helixi423 – 433Combined sources11
Beta strandi434 – 436Combined sources3
Beta strandi439 – 445Combined sources7
Helixi447 – 449Combined sources3
Helixi453 – 461Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HR6X-ray2.50B/D/F/H21-462[»]
1HR7X-ray2.55B/D/F/H21-462[»]
1HR8X-ray2.70B/D/F/H21-462[»]
1HR9X-ray3.01B/D/F/H21-462[»]
ProteinModelPortaliP10507.
SMRiP10507.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10507.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00550000074701.
HOGENOMiHOG000242450.
InParanoidiP10507.
KOiK17732.
OMAiLWGIYLT.
OrthoDBiEOG092C25X9.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10507-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSRTASKFR NTRRLLSTIS SQIPGTRTSK LPNGLTIATE YIPNTSSATV
60 70 80 90 100
GIFVDAGSRA ENVKNNGTAH FLEHLAFKGT QNRSQQGIEL EIENIGSHLN
110 120 130 140 150
AYTSRENTVY YAKSLQEDIP KAVDILSDIL TKSVLDNSAI ERERDVIIRE
160 170 180 190 200
SEEVDKMYDE VVFDHLHEIT YKDQPLGRTI LGPIKNIKSI TRTDLKDYIT
210 220 230 240 250
KNYKGDRMVL AGAGAVDHEK LVQYAQKYFG HVPKSESPVP LGSPRGPLPV
260 270 280 290 300
FCRGERFIKE NTLPTTHIAI ALEGVSWSAP DYFVALATQA IVGNWDRAIG
310 320 330 340 350
TGTNSPSPLA VAASQNGSLA NSYMSFSTSY ADSGLWGMYI VTDSNEHNVQ
360 370 380 390 400
LIVNEILKEW KRIKSGKISD AEVNRAKAQL KAALLLSLDG STAIVEDIGR
410 420 430 440 450
QVVTTGKRLS PEEVFEQVDK ITKDDIIMWA NYRLQNKPVS MVALGNTSTV
460
PNVSYIEEKL NQ
Length:462
Mass (Da):51,084
Last modified:July 1, 1989 - v1
Checksum:i084CE63C495EDFC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07649 Genomic DNA. Translation: CAA30489.1.
U51921 Genomic DNA. Translation: AAB67487.1.
AY693198 Genomic DNA. Translation: AAT93217.1.
BK006945 Genomic DNA. Translation: DAA09485.1.
PIRiS00552.
RefSeqiNP_013264.1. NM_001182050.1.

Genome annotation databases

EnsemblFungiiYLR163C; YLR163C; YLR163C.
GeneIDi850860.
KEGGisce:YLR163C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07649 Genomic DNA. Translation: CAA30489.1.
U51921 Genomic DNA. Translation: AAB67487.1.
AY693198 Genomic DNA. Translation: AAT93217.1.
BK006945 Genomic DNA. Translation: DAA09485.1.
PIRiS00552.
RefSeqiNP_013264.1. NM_001182050.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HR6X-ray2.50B/D/F/H21-462[»]
1HR7X-ray2.55B/D/F/H21-462[»]
1HR8X-ray2.70B/D/F/H21-462[»]
1HR9X-ray3.01B/D/F/H21-462[»]
ProteinModelPortaliP10507.
SMRiP10507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31436. 22 interactors.
DIPiDIP-2402N.
IntActiP10507. 14 interactors.
MINTiMINT-614379.

Protein family/group databases

MEROPSiM16.980.

PTM databases

iPTMnetiP10507.

Proteomic databases

MaxQBiP10507.
PRIDEiP10507.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR163C; YLR163C; YLR163C.
GeneIDi850860.
KEGGisce:YLR163C.

Organism-specific databases

EuPathDBiFungiDB:YLR163C.
SGDiS000004153. MAS1.

Phylogenomic databases

GeneTreeiENSGT00550000074701.
HOGENOMiHOG000242450.
InParanoidiP10507.
KOiK17732.
OMAiLWGIYLT.
OrthoDBiEOG092C25X9.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32293-MONOMER.
YEAST:G3O-32293-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.
SABIO-RKP10507.

Miscellaneous databases

EvolutionaryTraceiP10507.
PROiP10507.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMPPB_YEAST
AccessioniPrimary (citable) accession number: P10507
Secondary accession number(s): D6VYG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 172 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 1360 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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