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Reviewed, UniProtKB/Swiss-Prot Q9Y8B5 (MPPB_LENED)

Last modified June 16, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mitochondrial-processing peptidase subunit beta
    EC=3.4.24.64
Alternative name(s):
    Beta-MPP
Gene names
Name: mppB
OrganismLentinula edodes (Shiitake mushroom) (Lentinus edodes)
Taxonomic identifier5353 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaHomobasidiomycetesAgaricomycetidaeAgaricalesTricholomataceaeLentinula

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Cleaves presequences (transit peptides) from mitochondrial protein precursors.

Catalytic activity

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

Cofactor

Divalent cations By similarity.

Subunit structure

Heterodimer of alpha and beta subunits By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the peptidase M16 family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 466Mitochondrial-processing peptidase subunit betaPRO_0000026781

Sites

Active site761Proton acceptor By similarity
Metal binding731Zinc By similarity
Metal binding771Zinc By similarity
Metal binding1531Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Y8B5-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: CE3E6E797A1C29D6

FASTA46651,163
        10         20         30         40         50         60 
MLGRVLKSAA RSQRGLRSFA TTTNLGPFTE ISTLSNGLTV ATESQPHAQT ATVGVWIDAG 

        70         80         90        100        110        120 
SRAETDKTNG TAHFLEHMAF KGTGRRSQHA LELEVENIGA HLNAYTSREQ TVYYAKSFSK 

       130        140        150        160        170        180 
DVPVAVDIIS DILQNSKLES GAIERERDVI LREQQEVDKQ LEEVVFDHLH AVAFQGQPLG 

       190        200        210        220        230        240 
RTILGPKNNI LSIQRDDLAS YIQTNYTADR MVLVGTGGVD HQSLVKLAEK HFSSLPVSAN 

       250        260        270        280        290        300 
PLALGRLSSE RKPTFVGSEA RIRDDELPTA HVAIAVEGVG WSSPDYFPMM VMQSIFGNWD 

       310        320        330        340        350        360 
RSLGASSLLS SRLSHIISSN SLANSFMSFS TSYSDTGLWG IYLVSENLMN LDDTLHFTLK 

       370        380        390        400        410        420 
EWTRMSIAPT EGEVERAKSQ LKAGLLLSLD GTTAVAEDIG RQIVTSGKRM TPAQIENAVD 

       430        440        450        460 
AVSVDDIKRV AQKYLWDKDF ALAAFGNIDG LKDYGRIRND MSSMLY 

« Hide

References

[1]"Cloning and characterization of the gene encoding beta subunit of mitochondrial processing peptidase from the basidiomycete Lentinula edodes."
Zhang M., Xie W., Leung G.S., Deane E.E., Kwan H.S.
Gene 206:23-27(1998) [PubMed: 9461410] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

AF146393 Genomic DNA. Translation: AAD37722.1.
PIRJC6525.

3D structure databases

HSSPHSSP built from PDB template 1HR6 based on UniProtKB P10507.
ModBaseSearch...

Protein family/group databases

MEROPSM16.003.
M16.980.

Enzyme and pathway databases

BRENDA3.4.24.64. 260981.

Family and domain databases

InterProIPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
Gene3DG3DSA:3.30.830.10. Pept_M16_core. 2 hits.
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMPPB_LENED
AccessionPrimary (citable) accession number: Q9Y8B5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: November 1, 1999
Last modified: June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents