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A4RF25 (PMIP_MAGO7) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 49. 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:MGG_00487
OrganismMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) [Complete proteome]
Taxonomic identifier242507 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe

Protein attributes

Sequence length812 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 – 3535Mitochondrion Potential
Chain36 – 812777Mitochondrial intermediate peptidase
PRO_0000338587

Regions

Compositional bias296 – 2994Poly-Ala

Sites

Active site5881 By similarity
Metal binding5871Zinc; catalytic By similarity
Metal binding5911Zinc; catalytic By similarity
Metal binding5941Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A4RF25 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: ADBC3C60189F33E9

FASTA81290,362
        10         20         30         40         50         60 
MLKLLRPRPW VCNSCLNRVA FPKPYPVGSR STRWLSTAQS AAPAVSIPPV NPVPADHTTS 

        70         80         90        100        110        120 
GTHDDALLGK IFDCSSAWRD FSARSAKFPT ENAGLFRNAY LTSPDGFLTF AQSSLSKASA 

       130        140        150        160        170        180 
IVNRVLGAST IEEYKTIVRD LDRLSDLLCR VIDLSDFVRV THPDVRIQRA ASEAWYMVYQ 

       190        200        210        220        230        240 
YMNQLNTMTG LNDQLGKAME NSDVTKTWSE EEMAVAQLLK LDFMKSAVNL PQAARDRFVD 

       250        260        270        280        290        300 
LSQRISEIGS DFVNEMAPEQ RRVVLPSSKF QGMDPQIARR FTKHGYMQLP TMSGEAAAAL 

       310        320        330        340        350        360 
RTVHDEETRK AVYLAIRTAS SRSVGLLEAL LKHRAELADL AGFESYGHMT LRDRMMAKTP 

       370        380        390        400        410        420 
ESINKFLVEL SKNNAPRVLQ EVDSLLQEKK TLLASPSATL NPWDREYYIQ RIRNAQGKNV 

       430        440        450        460        470        480 
KHDNFFASYF SVGRVMQGLS RLFTRLYGIR FVPRETLPGE KWHPDVRRLD VVSDTDGHVA 

       490        500        510        520        530        540 
VLYCDLFYRE DKSPNPAHFT IRCSRAISED EISEAAVSTS EGGPAFGSPE SAANDGMAAS 

       550        560        570        580        590        600 
RGASGGPLKQ LPTIALVCDF PQRDNPLSGS KSKPASLTFA SLETLFHEMG HAIHSVLART 

       610        620        630        640        650        660 
SFQNVAGTRC ATDLAELPST LMEYFASDPS VLSLFARHAE TDEPLDYDLL AERVRSRGRF 

       670        680        690        700        710        720 
EGCDTDYQII LAMLDQAYHS PLASSESFDT TRAYHDLQRE HSPLGPDPSS TRWQGFFGHL 

       730        740        750        760        770        780 
FGYGSTYYSY LFDQVLAERA WKKVFSSGQD GAALSREAGE HLKESLLKWG GSREPWRCVS 

       790        800        810 
DVLRDERIAG GGEEAMALVG SWGTSNKSTM KH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM001235 Genomic DNA. Translation: EHA48991.1.
RefSeqXP_003718575.1. XM_003718527.1.

3D structure databases

ProteinModelPortalA4RF25.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING148305.A4RF25.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiMGG_00487T0; MGG_00487T0; MGG_00487.
GeneID2674708.
KEGGmgr:MGG_00487.

Phylogenomic databases

eggNOGCOG0339.
KOK01410.
OrthoDBEOG71GB4R.

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_MAGO7
AccessionPrimary (citable) accession number: A4RF25
Secondary accession number(s): G4NBT3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: May 15, 2007
Last modified: November 13, 2013
This is version 49 of the entry and version 1 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