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Reviewed, UniProtKB/Swiss-Prot O94745 (MPPA_SCHPO)

Last modified June 16, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Probable mitochondrial-processing peptidase subunit alpha
    EC=3.4.24.64
Alternative name(s):
    Alpha-MPP
Gene names
Name: mas2
ORF Names: SPBC18E5.12c, SPBC23G7.02c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Cleaves presequences (transit peptides) from mitochondrial protein precursors By similarity.

Catalytic activity

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

Subunit structure

Heterodimer of alpha and beta subunits By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the peptidase M16 family.

Caution

Does not seem to have a protease activity as it lack the zinc-binding site.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete proteome
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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 494Probable mitochondrial-processing peptidase subunit alphaPRO_0000026772

Sequences

Sequence LengthMass (Da)Tools
O94745-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 714F2F4DBF03A276

FASTA49454,672
        10         20         30         40         50         60 
MLSEYQCLKN IGFSHKTVLK RRLFRKECTP ALKSFYSTQD PALNEVRTEK LKNGVTYVCD 

        70         80         90        100        110        120 
PRPGHFSGLG VYVKAGSRYE TKKFSGVSHF MDRLAFQATE RTPVGEMKAK LENLGGNYMC 

       130        140        150        160        170        180 
STSRESMIYQ AAVFNDDVKS MSKLLAETVL APKIQEDDLV HYRDSIIYEN SELWTKPDAL 

       190        200        210        220        230        240 
LGEFAHVTAF QNNTLGNCLL CTPDKVNGIT ATSIREYLKY FYRPEHLTLA YAGIPQEIAK 

       250        260        270        280        290        300 
EITKELYGHL PSSSLPPLEA IPSHYTGGFM GIKKSEAPPV PYQQEFTHVV IAMEGLPVTD 

       310        320        330        340        350        360 
PDIYALACLQ FLLGGGGSFS AGGPGKGMYS RLYLNVLNQY PWVETCMAFN HSYTDSGLFG 

       370        380        390        400        410        420 
MFVTILDDAA HLAAPLIIRE LCNTVLSVTS EETERAKNQL KSSLLMNLES RMISLEDLGR 

       430        440        450        460        470        480 
QIQTQNGLYI TPKEMIEKID ALTPSDLSRV ARRVLTGNVS NPGNGTGKPT VLIHGNVDEV 

       490 
GDVFALCKKA GIGH 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

Cross-references

Sequence databases

CU329671 Genomic DNA. Translation: CAA22672.1.
PIRT39763.
RefSeqNP_595859.1.

3D structure databases

HSSPHSSP built from PDB template 1HR6 based on UniProtKB P11914.
ModBaseSearch...

Protein family/group databases

MEROPSM16.971.

Genome annotation databases

GeneID2540713.
KEGGspo:SPBC18E5.12c.
NMPDRfig|4896.1.peg.1725.

Organism-specific databases

GeneDB_SpombeSPBC18E5.12c.

Phylogenomic databases

OMAO94745. YRGNTVG.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-003745-MON.
BRENDA3.4.24.64. 653.

Gene expression databases

ArrayExpressO94745.

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 nameMPPA_SCHPO
AccessionPrimary (citable) accession number: O94745
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 50 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

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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