Q7SDD5 (PMIP_NEUCR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 61.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Mitochondrial intermediate peptidase Short name=MIP EC=3.4.24.59 Alternative name(s): Octapeptidyl aminopeptidase | ||||
| Gene names |
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| Organism | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome] | ||||
| Taxonomic identifier | 367110 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora ›  |
Protein attributes
| Sequence length | 805 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 25 | 25 | Mitochondrion Potential | ||||||
| Chain | 26 – 805 | 780 | Mitochondrial intermediate peptidase | PRO_0000338590 | |||||
Sites | |||||||||
| Active site | 579 | 1 | By similarity | ||||||
| Metal binding | 578 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 582 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 585 | 1 | Zinc; catalytic By similarity | ||||||
Sequences
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References
| [1] | "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.  Birren B.W.Nature 422:859-868(2003) [PubMed] [Europe PMC] [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 | |
|---|---|
| EMBL GenBank DDBJ | AABX02000003 Genomic DNA. Translation: EAA34783.1. |
| RefSeq | XP_964019.1. XM_958926.1. |
3D structure databases | |
| ProteinModelPortal | Q7SDD5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 5141.NCU02063.1. |
Protein family/group databases | |
| MEROPS | M03.006. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | EFNCRT00000001042; EFNCRP00000001042; EFNCRG00000001041. |
| GeneID | 3880168. |
| KEGG | ncr:NCU02063. |
Phylogenomic databases | |
| eggNOG | COG0339. |
| HOGENOM | HOG000076521. |
| KO | K01410. |
| OrthoDB | EOG4GJ2XS. |
Family and domain databases | |
| Gene3D | 1.10.1370.10. 2 hits. 1.20.1050.40. 1 hit. 3.40.390.10. 2 hits. |
| InterPro | IPR024079. MetalloPept_cat_dom. IPR024077. Neurolysin/TOP_dom2. IPR024080. Neurolysin/TOP_N. IPR001567. Pept_M3A_M3B. [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_NEUCR | ||||||||
| Accession | Primary (citable) accession number: Q7SDD5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |