Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A1DMR2 (PMIP_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 40. 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:NFIA_054290
OrganismNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]
Taxonomic identifier331117 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya

Protein attributes

Sequence length801 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 – 4242Mitochondrion Potential
Chain43 – 801759Mitochondrial intermediate peptidase
PRO_0000338589

Sites

Active site5661 By similarity
Metal binding5651Zinc; catalytic By similarity
Metal binding5691Zinc; catalytic By similarity
Metal binding5721Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A1DMR2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 906514456D11365F

FASTA80189,774
        10         20         30         40         50         60 
MKDQLLVPLR RRPWTCRKCL QRLQLLPQHQ TRRSFETAAS PFPRQLDSLP ADYSRTKTVD 

        70         80         90        100        110        120 
DDTLRRVFDS QQFWREFSQQ RSAQPKPTGL VQNQYLTSPD GFRTFANVSL QKCQAIVSKV 

       130        140        150        160        170        180 
LAASTLEEYR TMARDLDRLS DLLCRVIDLS DFIRVIHPDP QVQEAATQAY ALMFEYMNVL 

       190        200        210        220        230        240 
NTTTGLNDQL KKAAANPEVT SQWSDEEKIV AQILIKDFSN SAIHMPPHER QRFVNLSNDI 

       250        260        270        280        290        300 
SQLGSSFVNG AEPAKSHVSV ATNNLRGLDP ILVQQIKRWN RTAAVPTTGM IPRLALRSVH 

       310        320        330        340        350        360 
DENVRREVYL ASRTSSKRQL HRLEELLLKR AELAKLSGYE SFAHMTLSDK MAKSPEAVSN 

       370        380        390        400        410        420 
FLTALVDSNR KLVREELSQL QAMKGAPLQP WDHAYYVHQR VMQYSQARRS RELSAVPEFF 

       430        440        450        460        470        480 
SLGTVMQGLS RLFDRLYGVR LVPQEPAPGE TWNPDVRRLD VVDESGRHIA VIYCDLFSRP 

       490        500        510        520        530        540 
NKHPNPAHFT LRCSREISTE EVAECASLDQ SSHPNDGMAT AVDPVTKTLR QLPTIALVCD 

       550        560        570        580        590        600 
FSEPGTNGGG RPSLLSEHSV RTLFHEMGHA VHSILGQTRL QSISGTRCAT DFAELPSVLM 

       610        620        630        640        650        660 
EHFATAPSVL ALYARHWRTD EPLSEGMIRS MERDRTAHGS IYGAVENEAQ ILMALVDQAY 

       670        680        690        700        710        720 
HSRPADGGRI DSTALYQQVS QQHSSLPEPA DVTPPTSWQG FFGHLYGYGA TYYSYIFDRA 

       730        740        750        760        770        780 
IANKLWVDVF GAGRQAVDRA AGERYKNEVL RWGGGRSGWE CVAGALGSAN ESNADGRLVE 

       790        800 
GGDEAMREVG RWGLGRDGVS G 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027698 Genomic DNA. Translation: EAW16083.1.
RefSeqXP_001257980.1. XM_001257979.1.

3D structure databases

ProteinModelPortalA1DMR2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36630.CADNFIAP00004862.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00004990; CADNFIAP00004862; CADNFIAG00004990.
GeneID4584495.
KEGGnfi:NFIA_054290.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
KOK01410.
OMAPQVFAHY.
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_NEOFI
AccessionPrimary (citable) accession number: A1DMR2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 40 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