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B0Y7Q2 (PMIP_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial intermediate peptidase

Short name=MIP
EC=3.4.24.59
Alternative name(s):
Octapeptidyl aminopeptidase
Gene names
Name:oct1
ORF Names:AFUB_074600
OrganismNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]
Taxonomic identifier451804 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length801 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane By similarity.

Catalytic activity

Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

Cofactor

Binds 1 zinc ion By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the peptidase M3 family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Mitochondrion Potential
Chain42 – 801760Mitochondrial intermediate peptidase
PRO_0000338570

Sites

Active site5651 By similarity
Metal binding5641Zinc; catalytic By similarity
Metal binding5681Zinc; catalytic By similarity
Metal binding5711Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
B0Y7Q2 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 4EAE66D5ECCD8269

FASTA80189,667
        10         20         30         40         50         60 
MKDQLLVPLR RRPWTCQKCL QRLQLPRHQT RRSFETAASP FPRPLDSLPA DYARTKTVDD 

        70         80         90        100        110        120 
DTLRRVFDSQ QFWREFSQQR AAQPKPTGLV QNQYLTSPDG FRTFANVSLQ KCQAIVSKVL 

       130        140        150        160        170        180 
AASTLEEYRT MARDLDRLSD LLCRVIDLSD FIRVIHPDPQ VQEAATQAYA LMFEYMNVLN 

       190        200        210        220        230        240 
TTTGLNDQLK KAAANPEVTS QWSDEEKIVA QILIKDFSNS AIHMPPHERQ RFVNLSNDIS 

       250        260        270        280        290        300 
QLGSSFVNGA EPAKSHVSVA TNNLRGLDPI LVQQIKRWNR TAAVPTTGMI PRLALRSVHD 

       310        320        330        340        350        360 
ENVRREVYLA SRTSSKRQLH RLEELLLKRA ELAKLSGYES FAHMTLSDKM AKSPEAVSNF 

       370        380        390        400        410        420 
LTALVESNRK LVREELSQLQ VMKGAPLQPW DHAYYVHQRV LQYSQARRSR ELSAVPEFFS 

       430        440        450        460        470        480 
LGTVMQGLSR LFDRLYGVRL VPQEPAPGET WNPDVRRLDV VDEAGRHIAV IYCDLFSRPN 

       490        500        510        520        530        540 
KHPNPAHFTL RCSREISAEE VAECASLDQS SHPNDGMATA VDPVTQTLRQ LPTIALVCDF 

       550        560        570        580        590        600 
PEPGTNGGGR PSLLSEHSVR TLFHEMGHAV HSILGQTRLQ SISGTRCATD FAELPSVLME 

       610        620        630        640        650        660 
HFATAPSVLA LYARHWRTDE PLSEGMIRSM ERDRTAHGSI YGAVENEAQI LMALVDQAYH 

       670        680        690        700        710        720 
SRPADGGRID STALYQQVSQ QHSSLPEPAD ATTPPTSWQG FFGHLYGYGA TYYSYIFDRA 

       730        740        750        760        770        780 
IANKLWVDVF GAGRHAVDRA AGERYKNEVL RWGGGRSGWE CVAGALGSAN ESNADGRLVE 

       790        800 
GGDQAMREVG RWGLGRDGVS G 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS499599 Genomic DNA. Translation: EDP49433.1.

3D structure databases

ProteinModelPortalB0Y7Q2.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUBT00007400; CADAFUBP00007267; CADAFUBG00007400.

Phylogenomic databases

HOGENOMHOG000076521.
OrthoDBEOG71GB4R.
PhylomeDBB0Y7Q2.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMIP_ASPFC
AccessionPrimary (citable) accession number: B0Y7Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: April 8, 2008
Last modified: April 16, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries