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Reviewed, UniProtKB/Swiss-Prot P23955 (MPPA_NEUCR)

Last modified January 20, 2009. Version 81. 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 alpha
    EC=3.4.24.64
Alternative name(s):
    Alpha-MPP
Gene names
Name: mpp
ORF Names: NCU06270
OrganismNeurospora crassa [Complete proteome]
Taxonomic identifier5141 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Subcellular location

Mitochondrion matrix.

Domain

Appears to contain two domains of approximately equal size which are separated by a loop-like sequence.

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
Direct protein sequencing
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 – 3535Mitochondrion
Chain36 – 577542Mitochondrial-processing peptidase subunit alpha
PRO_0000026771

Regions

Compositional bias259 – 30749Ser-rich

Experimental info

Sequence conflict1071T → S AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23955-1 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 029491B2FBA01ADB

FASTA57763,041
        10         20         30         40         50         60 
MLNRFRPARL VAQSSRCLPL TRARAGPLPV NNARTLATRA AAVNTKEPTE RDNITTLSNG 

        70         80         90        100        110        120 
VRVASEDLPD AFSGVGVYID AGSRYENDYV RGASHIMDRL AFKSTSTRTA DEMLETVEKL 

       130        140        150        160        170        180 
GGNIQCASSR ESMMYQAATF NKAIPTAVEL MAETIRDPKL TDEELEGQIM TAQYEVNEIW 

       190        200        210        220        230        240 
SKAELILPEL VHMAAFKDNT LGNPLLCPKE RLDYINRDVI QTYRDAFYRP ERLVVAFAGV 

       250        260        270        280        290        300 
PHERAVKLAE KYFGDMKASD APGLSRTGSE TSVDSLVSES SEASSESSSS SSDSSESSGG 

       310        320        330        340        350        360 
LLSKLFSPKA KKATPNPFLT RVPISTEDLT RPAHYTGGFL TLPSQPPPLN PNLPTFTHIQ 

       370        380        390        400        410        420 
LAFEGLAISD DDIYALATLQ TLLGGGGSFS AGGPGKGMYS RLYTNVLNQH GWVESCVAFN 

       430        440        450        460        470        480 
HSYTDSGLFG IAASCYPGRT LPMLQVMCRE LHALTTDHGY SALGELEVSR AKNQLRSSLL 

       490        500        510        520        530        540 
MNLESRMVEL EDLGRQVQVH GRKIPVREMT RRINELTVKD LRRVAKRVVG GMANNAGQGS 

       550        560        570 
GAPTVVLQEA TVQGLKTTEL GWDQIQDTIA QWKLGRR 

« Hide

References

« Hide 'large scale' references
[1]"Matrix processing peptidase of mitochondria. Structure-function relationships."
Schneider H., Arretz M., Wachter E., Neupert W.
J. Biol. Chem. 265:9881-9887(1990) [PubMed: 2141023] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE OF N-TERMINUS.
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed: 12712197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases

J05484 mRNA. Translation: AAA33597.1. Sequence problems.
AABX02000025 Genomic DNA. Translation: EAA33638.1.
PIRA36442.
RefSeqXP_962874.1.

3D structure databases

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

Protein family/group databases

MEROPSM16.971.

Genome annotation databases

GeneID3879027.
KEGGncr:NCU06270.
NMPDRfig|5141.1.peg.4058.

Enzyme and pathway databases

BioCycNCRA-XX3-01:NCRA-XX3-01-010018-MON.
BRENDA3.4.24.64. 266.

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_NEUCR
AccessionPrimary (citable) accession number: P23955
Secondary accession number(s): Q7RVH4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 2004
Last modified: January 20, 2009
This is version 81 of the entry and version 2 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