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A5DI46 (PMIP_PICGU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 39. 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:PGUG_02947
OrganismMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) [Complete proteome]
Taxonomic identifier294746 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeMeyerozyma

Protein attributes

Sequence length786 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 – 2929Mitochondrion Potential
Chain30 – 786757Mitochondrial intermediate peptidase
PRO_0000338592

Sites

Active site5681 By similarity
Metal binding5671Zinc; catalytic By similarity
Metal binding5711Zinc; catalytic By similarity
Metal binding5741Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A5DI46 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: 784FAB0D1430E2E3

FASTA78690,517
        10         20         30         40         50         60 
MSSILLRSYR HHAKVWTRPS SKSSFIRSLA SRSNPTSSFE HVRRVFDDDK YYQDFNNGTL 

        70         80         90        100        110        120 
SRKIFSGPRT GLFKNEKLTT PQGLIDFSGQ CLTEAQTLVD TMIREAETSD QGKIHYIRRL 

       130        140        150        160        170        180 
DQLSDILCRV IDVAEFIRVA HPNSKWTHAA QQTHELMFEY MNQLNTNVQL HTILGNILAD 

       190        200        210        220        230        240 
KSITSKLSSE EIMVGEYLKQ DFERSGIYME PHTRENFVAL TQEISVLGSH FNNGIHELKD 

       250        260        270        280        290        300 
YWCEISQQEY EAIDNADLKR EIRRFQQKSP RSSRNSVYIP LAGSLPYSIL QRCSMESVRR 

       310        320        330        340        350        360 
KVWIALHNAS EEQISTLNLF LKYRATLSKM LGYESFAHYQ LEHKMAKNPE NVLTFLENLQ 

       370        380        390        400        410        420 
RKMVDGENSG LISELESLYA MSNHWKPGAS KSDIIHAIQP WDRDYLLHKL QEEKKETQLD 

       430        440        450        460        470        480 
DNISEYLSVG TIMSGLSQLF HSIYSIELLP EPSASGETWA SQVRKIKVFD NETQSTLGFL 

       490        500        510        520        530        540 
YLDFWSPNVL PSHFTIVCSR QLNKDLGEKV EVMKPLVQLD ETESHQLPVI SLVCNFHQGN 

       550        560        570        580        590        600 
SFIGRFAGLE TSKPTLLTLD QVDTIFHEMG HAMHSMIGRT KLQNLSGTRC STDFVELPSV 

       610        620        630        640        650        660 
LMESFSKDPR VLGRIARHYS TNELLPHDIL AKHQHYRNVL ENSETYMQSK MAMLDQVLHG 

       670        680        690        700        710        720 
KSIVKQLEMA RDDIDSTTMY HSLEKELKVF SDQWSTWHGK FPHLFSYGAV YFSYLFDRAI 

       730        740        750        760        770        780 
AEKIWKSLFQ NDPWSREAGT TYKEAILKWG GTRDPWHCLA DALSNQELSK GDEKAMRIIG 


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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH408157 Genomic DNA. Translation: EDK38849.2.
RefSeqXP_001485218.1. XM_001485168.1.

3D structure databases

ProteinModelPortalA5DI46.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4929.A5DI46.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5127052.
KEGGpgu:PGUG_02947.

Phylogenomic databases

eggNOGCOG0339.
KOK01410.
OrthoDBEOG71GB4R.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
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_PICGU
AccessionPrimary (citable) accession number: A5DI46
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 10, 2009
Last modified: November 13, 2013
This is version 39 of the entry and version 2 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