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A2QWM4

- PMIP_ASPNC

UniProt

A2QWM4 - PMIP_ASPNC

Protein

Mitochondrial intermediate peptidase

Gene

oct1

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

    Cofactori

    Binds 1 zinc ion.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi562 – 5621Zinc; catalyticPROSITE-ProRule annotation
    Active sitei563 – 5631PROSITE-ProRule annotation
    Metal bindingi566 – 5661Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi569 – 5691Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM03.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial intermediate peptidase (EC:3.4.24.59)
    Short name:
    MIP
    Alternative name(s):
    Octapeptidyl aminopeptidase
    Gene namesi
    Name:oct1
    ORF Names:An11g05710
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 7R

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 799Mitochondrial intermediate peptidasePRO_0000338572
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00008739.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QWM4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M3 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0339.
    HOGENOMiHOG000076521.
    KOiK01410.
    OrthoDBiEOG71GB4R.

    Family and domain databases

    Gene3Di1.10.1370.10. 2 hits.
    3.40.390.10. 1 hit.
    InterProiIPR024079. MetalloPept_cat_dom.
    IPR024077. Neurolysin/TOP_dom2.
    IPR001567. Pept_M3A_M3B.
    [Graphical view]
    PfamiPF01432. Peptidase_M3. 1 hit.
    [Graphical view]
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A2QWM4-1 [UniParc]FASTAAdd to Basket

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    MGASLLLPLR RRPWTCRTCL LQARRSLETA ASPATHRAAF DYLPSKNDAQ    50
    KKSDDDTLRR VFDSQPFWRE FSQRSAAHLK PTGLVQNQYL TSPDGFRVFA 100
    TTTLQKCQAI VAKVLAGTTL EDYQSMARDL DRLSDLLCRV IDLSDFIRVI 150
    HPDPRVQEAA TQAYALMFEY MNVLNTTTGL NDQLKKAAAN PEVTARWSDE 200
    EKIVAQILIK DFSNSAIHMP PHARQRFVNL SNDISQLGNT FVNAAEPAKS 250
    HVTVSANSLR GLDPILVQQI KRWNRTASVP SMGLIPRLAL RSVHDEGVRR 300
    EVYLATRTSS ARQIQRLEQL LAKRAELAQL SGYDSFAHMT LSDKMAKSPE 350
    AVSNFLTSLV GSNRPYVQEE LAQLQSMKGS AGRLQPWDHA YYVHQRVLQY 400
    SQSRRSRELS AVPEFFSLGT VMQGLSRLFD RLYGVRLVPQ ETAAGETWNS 450
    DVRRLDVVDE ADRHIAVIYC DLFSRPNKHP NPAHYTLRCA REISAEEVAE 500
    CATTMDASAH PNDGMATAVD RDAKTLRQLP TIALVCDFPE PPATGTGRPS 550
    LLSEHSVRTL FHEMGHALHS ILGQTRLQSI SGTRCATDFA ELPSVLMERF 600
    ATAPEVLALY ARHWETDAPL SESMMQHMEK DRTAHGSIYG AMENESQILM 650
    ALVDQAYHSL PAGQATSIDS TAVFHQVSAE HCTLPDPTDT KPPTSWQGFF 700
    GHLHGYGATY YSYIFDRAIA NKLWEDVFQQ GKAAVDRQAG ERYKNEVLRW 750
    GGGRNGWNCV AGVLGSAHPA NADGRLVEGG DEAMREVGRW GLGRDGVSE 799
    Length:799
    Mass (Da):88,989
    Last modified:March 6, 2007 - v1
    Checksum:iBE7D0384194750AD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270239 Genomic DNA. Translation: CAK40728.1.
    RefSeqiXP_001394557.1. XM_001394520.2.

    Genome annotation databases

    EnsemblFungiiCADANGAT00008906; CADANGAP00008739; CADANGAG00008906.
    GeneIDi4984800.
    KEGGiang:ANI_1_762094.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270239 Genomic DNA. Translation: CAK40728.1 .
    RefSeqi XP_001394557.1. XM_001394520.2.

    3D structure databases

    ProteinModelPortali A2QWM4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00008739.

    Protein family/group databases

    MEROPSi M03.006.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00008906 ; CADANGAP00008739 ; CADANGAG00008906 .
    GeneIDi 4984800.
    KEGGi ang:ANI_1_762094.

    Phylogenomic databases

    eggNOGi COG0339.
    HOGENOMi HOG000076521.
    KOi K01410.
    OrthoDBi EOG71GB4R.

    Family and domain databases

    Gene3Di 1.10.1370.10. 2 hits.
    3.40.390.10. 1 hit.
    InterProi IPR024079. MetalloPept_cat_dom.
    IPR024077. Neurolysin/TOP_dom2.
    IPR001567. Pept_M3A_M3B.
    [Graphical view ]
    Pfami PF01432. Peptidase_M3. 1 hit.
    [Graphical view ]
    PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry nameiPMIP_ASPNC
    AccessioniPrimary (citable) accession number: A2QWM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 49 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3