Reviewed,
UniProtKB/Swiss-Prot Q5KKA9 (PMIP1_CRYNE)
Last modified
November 3, 2009.
Version 33.
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 1 Short name=MIP 1 EC=3.4.24.59 Alternative name(s): Octapeptidyl aminopeptidase 1 | ||||
| Gene names |
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| Organism | Cryptococcus neoformans (Filobasidiella neoformans) [Complete proteome] | ||||
| Taxonomic identifier | 5207 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex |
Protein attributes
| Sequence length | 761 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. |
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 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 761 | Mitochondrial intermediate peptidase 1 | PRO_0000338581 | ||||||
Regions | |||||||||
| Compositional bias | 24 – 35 | 12 | Poly-Pro | ||||||
Sites | |||||||||
| Active site | 531 | 1 | By similarity | ||||||
| Metal binding | 530 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 534 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 537 | 1 | Zinc; catalytic By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 110 | 1 | R → H in strain: B-3501A. | ||||||
Sequences
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References
| [1] | "The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans." Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S. Hyman R.W.Science 307:1321-1324(2005) [PubMed: 15653466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B-3501A and JEC21. |
Cross-references
Sequence databases | |
|---|---|
| AE017343 Genomic DNA. Translation: AAW42284.1. AAEY01000013 Genomic DNA. Translation: EAL22217.1. | |
| RefSeq | XP_569591.1. XP_776864.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M03.006. |
Genome annotation databases | |
| GeneID | 3256482. 4935020. |
| GenomeReviews | Gene locus CNC03660 in contig AE017343_GR. Gene locus CNBC3550 in contig CM000042_GR. |
| KEGG | cnb:CNBC3550. cne:CNC03660. |
Phylogenomic databases | |
| HOGENOM | Q5KKA9. |
| OMA | AMGERYR. |
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 | PMIP1_CRYNE | ||||||||
| Accession | Primary (citable) accession number: Q5KKA9 Secondary accession number(s): Q55VY2 | ||||||||
| 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


