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A6SHZ5 (PMIP_BOTFB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 36. 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:BC1G_12067
OrganismBotryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Taxonomic identifier332648 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotryotinia

Protein attributes

Sequence length762 AA.
Sequence statusFragment.
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.

Sequence caution

The sequence EDN33764.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMitochondrion
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
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

Chain‹1 – 762›762Mitochondrial intermediate peptidase
PRO_0000338575

Regions

Compositional bias260 – 2645Poly-Ala

Sites

Active site5441 By similarity
Metal binding5431Zinc; catalytic By similarity
Metal binding5471Zinc; catalytic By similarity
Metal binding5501Zinc; catalytic By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
A6SHZ5 [UniParc].

Last modified June 10, 2008. Version 2.
Checksum: 383090D54BF577B9

FASTA76285,181
        10         20         30         40         50         60 
RRLATASTQY RESRPVPVDN SAPGAKRDDR TLRQIFDSPN FWAEFSQSSK QSYNRPAVGL 

        70         80         90        100        110        120 
FQNRYLVNPQ GFEVFANTSL RKAQRIVDKV LSASTVEEYR HVARELDRLS DLLCRVIDLS 

       130        140        150        160        170        180 
DFVRATHPNA AIQAAASRAY AKMFEYMNIL NTTTGLDKQL EIAMATPEIV AGWTEEEVVV 

       190        200        210        220        230        240 
ADILRKDFAK SAIDLPRAQR ERFVALSQEI SEIGPEFVDY MTPAKPYLTF ESSKLKGMDP 

       250        260        270        280        290        300 
VLVRQYTTWG QTKIPTIGGA AAAAIRSVQN EDVRKEIFMA TRTASRNTVY KLEELMRKRA 

       310        320        330        340        350        360 
ELAKLSRYES YSHLALGDKM AKSPASVSQF LEALSKDNNQ IVEGEVSELL KFKMSNSHGS 

       370        380        390        400        410        420 
SPGLQPWDKD YYMSQILASV RSHSRNSDFL SAYFSLGTVM QGLSRLFTRL YGVRLAPHET 

       430        440        450        460        470        480 
MPGETWNSDV RRLDVISETD GHVAVLYCDL FSRPGKSPNP AHFTLRCSRE ITTPELEEAS 

       490        500        510        520        530        540 
SLSQNGLFKT NEEAANDGMA TSRASGVLKQ LPTIALICDF VTMSGKSSRP ALLSFNEVQT 

       550        560        570        580        590        600 
LFHEMGHAIH SILGRTSLQN VSGTRCATDF AELPSVLMEH FAADPSVLSL FARHYETDQP 

       610        620        630        640        650        660 
LPYEMVAEKL ALDKRFEGSD TENQIILSML DLAYHSDLPL SPSFSSTQIY HSLQQKHGAL 

       670        680        690        700        710        720 
PVDPPGTCWQ GFFGHLFGYG STYYSYLFDR VLARRIWQVV FKDGEAGGSI QRDNGEKMKE 

       730        740        750        760 
EVLKWGGGRD PWKCLAGVLD DGRVENGDEK AMAIVGSWGV KE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476940 Genomic DNA. Translation: EDN33764.1. Different initiation.
RefSeqXP_001549090.1. XM_001549040.1.

3D structure databases

ProteinModelPortalA6SHZ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING332648.A6SHZ5.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5429605.
KEGGbfu:BC1G_12067.

Phylogenomic databases

eggNOGCOG0339.
KOK01410.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
3.40.390.10. 2 hits.
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_BOTFB
AccessionPrimary (citable) accession number: A6SHZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: November 13, 2013
This is version 36 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