Reviewed,
UniProtKB/Swiss-Prot Q0CI79 (PMIP_ASPTN)
Last modified
June 16, 2009.
Version 19.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Mitochondrial intermediate peptidase Short name=MIP EC=3.4.24.59 Alternative name(s): Octapeptidyl aminopeptidase | ||||
| Gene names |
| ||||
| Organism | Aspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome] | ||||
| Taxonomic identifier | 341663 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 802 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred 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. |
| Sequence caution | The sequence EAU33149.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAU33149.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 24 | 24 | Mitochondrion Potential | ||||||
| Chain | 25 – 802 | 778 | Mitochondrial intermediate peptidase | PRO_0000338574 | |||||
Sites | |||||||||
| Active site | 566 | 1 | By similarity | ||||||
| Metal binding | 565 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 569 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 572 | 1 | Zinc; catalytic By similarity | ||||||
Sequences
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References
| [1] | "Annotation of the Aspergillus terreus NIH2624 genome." Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K. Madden K.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CH476602 Genomic DNA. Translation: EAU33149.1. Sequence problems. | |
| RefSeq | XP_001215783.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M03.006. |
Genome annotation databases | |
| GeneID | 4322361. |
Family and domain databases | |
| InterPro | IPR001567. Pept_M3A_M3B. IPR006025. Pept_M_Zn_BS. [Graphical view] |
| Pfam | PF01432. Peptidase_M3. 1 hit. [Graphical view] |
| PROSITE | PS00142. ZINC_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PMIP_ASPTN | ||||||||
| Accession | Primary (citable) accession number: Q0CI79 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


