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A6SHZ5

- PMIP_BOTFB

UniProt

A6SHZ5 - PMIP_BOTFB

Protein

Mitochondrial intermediate peptidase

Gene

oct1

Organism
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 2 (10 Jun 2008)
      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 bindingi543 – 5431Zinc; catalyticPROSITE-ProRule annotation
    Active sitei544 – 5441PROSITE-ProRule annotation
    Metal bindingi547 – 5471Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi550 – 5501Zinc; 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:BC1G_12067
    OrganismiBotryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
    Taxonomic identifieri332648 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotrytis

    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‹1 – 762›762Mitochondrial intermediate peptidasePRO_0000338575Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi332648.A6SHZ5.

    Structurei

    3D structure databases

    ProteinModelPortaliA6SHZ5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi260 – 2645Poly-Ala

    Sequence similaritiesi

    Belongs to the peptidase M3 family.Curated

    Phylogenomic databases

    eggNOGiCOG0339.
    KOiK01410.

    Family and domain databases

    Gene3Di1.10.1370.10. 2 hits.
    3.40.390.10. 2 hits.
    InterProiIPR024079. MetalloPept_cat_dom.
    IPR024077. Neurolysin/TOP_dom2.
    IPR001567. Pept_M3A_M3B.
    [Graphical view]
    PfamiPF01432. Peptidase_M3. 1 hit.
    [Graphical view]
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    A6SHZ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    RRLATASTQY RESRPVPVDN SAPGAKRDDR TLRQIFDSPN FWAEFSQSSK    50
    QSYNRPAVGL FQNRYLVNPQ GFEVFANTSL RKAQRIVDKV LSASTVEEYR 100
    HVARELDRLS DLLCRVIDLS DFVRATHPNA AIQAAASRAY AKMFEYMNIL 150
    NTTTGLDKQL EIAMATPEIV AGWTEEEVVV ADILRKDFAK SAIDLPRAQR 200
    ERFVALSQEI SEIGPEFVDY MTPAKPYLTF ESSKLKGMDP VLVRQYTTWG 250
    QTKIPTIGGA AAAAIRSVQN EDVRKEIFMA TRTASRNTVY KLEELMRKRA 300
    ELAKLSRYES YSHLALGDKM AKSPASVSQF LEALSKDNNQ IVEGEVSELL 350
    KFKMSNSHGS SPGLQPWDKD YYMSQILASV RSHSRNSDFL SAYFSLGTVM 400
    QGLSRLFTRL YGVRLAPHET MPGETWNSDV RRLDVISETD GHVAVLYCDL 450
    FSRPGKSPNP AHFTLRCSRE ITTPELEEAS SLSQNGLFKT NEEAANDGMA 500
    TSRASGVLKQ LPTIALICDF VTMSGKSSRP ALLSFNEVQT LFHEMGHAIH 550
    SILGRTSLQN VSGTRCATDF AELPSVLMEH FAADPSVLSL FARHYETDQP 600
    LPYEMVAEKL ALDKRFEGSD TENQIILSML DLAYHSDLPL SPSFSSTQIY 650
    HSLQQKHGAL PVDPPGTCWQ GFFGHLFGYG STYYSYLFDR VLARRIWQVV 700
    FKDGEAGGSI QRDNGEKMKE EVLKWGGGRD PWKCLAGVLD DGRVENGDEK 750
    AMAIVGSWGV KE 762
    Length:762
    Mass (Da):85,181
    Last modified:June 10, 2008 - v2
    Checksum:i383090D54BF577B9
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476940 Genomic DNA. Translation: EDN33764.1. Different initiation.
    RefSeqiXP_001549090.1. XM_001549040.1.

    Genome annotation databases

    GeneIDi5429605.
    KEGGibfu:BC1G_12067.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476940 Genomic DNA. Translation: EDN33764.1 . Different initiation.
    RefSeqi XP_001549090.1. XM_001549040.1.

    3D structure databases

    ProteinModelPortali A6SHZ5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 332648.A6SHZ5.

    Protein family/group databases

    MEROPSi M03.006.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5429605.
    KEGGi bfu:BC1G_12067.

    Phylogenomic databases

    eggNOGi COG0339.
    KOi K01410.

    Family and domain databases

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

    Publicationsi

    1. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
      Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
      , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
      PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: B05.10.

    Entry informationi

    Entry nameiPMIP_BOTFB
    AccessioniPrimary (citable) accession number: A6SHZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 39 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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