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Q6BJ61 (PMIP_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 63. 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
Ordered Locus Names:DEHA2G04928g
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces

Protein attributes

Sequence length794 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 – 3939Mitochondrion Potential
Chain40 – 794755Mitochondrial intermediate peptidase
PRO_0000338583

Sites

Active site5821 By similarity
Metal binding5811Zinc; catalytic By similarity
Metal binding5851Zinc; catalytic By similarity
Metal binding5881Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6BJ61 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: C4E8BCE83A403C84

FASTA79490,794
        10         20         30         40         50         60 
MRVTSSRLLQ GGSLVSRVLK RRLNNASRTK KGWFSTRTLA DSNEHLRRVF DDQAYFDNFT 

        70         80         90        100        110        120 
KSGAPEGAMN SLFGGNGVGL FRNRALISPQ GLVDFSEESL ERAKMLVSNM MAEVKTSEQG 

       130        140        150        160        170        180 
RLEYIKKLDQ LSDVLCRVID VAEFIRVSHP SQKWVDAAQR THEIMFEYMN QLNTNVELYE 

       190        200        210        220        230        240 
SLRDLLIDPA ITTKLSKEEI EVGEYLRQDF ERSGIHMDPN TRNNFVAITQ EISLLGSHFN 

       250        260        270        280        290        300 
NDIHSLESYW CNISRSEFDK ISDTVVKSEI YGYQSSSPAS QNKDSGNIYI PLAGHIPYTI 

       310        320        330        340        350        360 
LSKCEVESVR RKVWISLHNS PKEQIDTLNA FVKYRALLAK MLGYKSFAHY QLEHKMAKNP 

       370        380        390        400        410        420 
ENVLTLLRNL QQGLISKEYG VCEEVKKLHS FKNGDDAVMT DEEILEDVKP WDREYLLAQL 

       430        440        450        460        470        480 
QSQTLKDEEP LEDISEYFSV GTIVSGLSKL FYSIYNVNLI PEATLKGETW DSNQVRKLNV 

       490        500        510        520        530        540 
FDVTSNKKLG YLYLDFWSPK VLPSHFTIVC SRKLNTDIGS ESRDEMREMV QLDENEQHQL 

       550        560        570        580        590        600 
PVISLVCNLS KPQGTGVGRF TGMDSRKPTL LSLDQVDTIF HEMGHAMHSM IGKTDLHNLS 

       610        620        630        640        650        660 
GTRCVTDFVE LPSVLMESFS KDPRVLCKIA KHYRTKEPLS KETLAKHQSH RVLLEESETF 

       670        680        690        700        710        720 
MQSKMAMLDQ VLHNEDIINC GIKDFDSTAV YHHLESQLKV FADKWSTWHG KFPHLFSYGA 

       730        740        750        760        770        780 
VYYSYLLDRA IAEKIWHGLF KDDPWSREAG QKYKDSILKW GGTRDPWVCL ADALGDERLG 

       790 
KGDSKAMEII GQKV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382139 Genomic DNA. Translation: CAG90217.2.
RefSeqXP_461760.2. XM_461760.1.

3D structure databases

ProteinModelPortalQ6BJ61.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4959.Q6BJ61.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2904636.
KEGGdha:DEHA2G04928g.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
KOK01410.
OMAVTEMNIE.
OrthoDBEOG71GB4R.

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_DEBHA
AccessionPrimary (citable) accession number: Q6BJ61
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: December 16, 2008
Last modified: November 13, 2013
This is version 63 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