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Protein

Mitochondrial intermediate peptidase

Gene

oct1

Organism
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Zn2+By similarityNote: 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

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
Complete GO annotation...

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

        10         20         30         40         50
RRLATASTQY RESRPVPVDN SAPGAKRDDR TLRQIFDSPN FWAEFSQSSK
60 70 80 90 100
QSYNRPAVGL FQNRYLVNPQ GFEVFANTSL RKAQRIVDKV LSASTVEEYR
110 120 130 140 150
HVARELDRLS DLLCRVIDLS DFVRATHPNA AIQAAASRAY AKMFEYMNIL
160 170 180 190 200
NTTTGLDKQL EIAMATPEIV AGWTEEEVVV ADILRKDFAK SAIDLPRAQR
210 220 230 240 250
ERFVALSQEI SEIGPEFVDY MTPAKPYLTF ESSKLKGMDP VLVRQYTTWG
260 270 280 290 300
QTKIPTIGGA AAAAIRSVQN EDVRKEIFMA TRTASRNTVY KLEELMRKRA
310 320 330 340 350
ELAKLSRYES YSHLALGDKM AKSPASVSQF LEALSKDNNQ IVEGEVSELL
360 370 380 390 400
KFKMSNSHGS SPGLQPWDKD YYMSQILASV RSHSRNSDFL SAYFSLGTVM
410 420 430 440 450
QGLSRLFTRL YGVRLAPHET MPGETWNSDV RRLDVISETD GHVAVLYCDL
460 470 480 490 500
FSRPGKSPNP AHFTLRCSRE ITTPELEEAS SLSQNGLFKT NEEAANDGMA
510 520 530 540 550
TSRASGVLKQ LPTIALICDF VTMSGKSSRP ALLSFNEVQT LFHEMGHAIH
560 570 580 590 600
SILGRTSLQN VSGTRCATDF AELPSVLMEH FAADPSVLSL FARHYETDQP
610 620 630 640 650
LPYEMVAEKL ALDKRFEGSD TENQIILSML DLAYHSDLPL SPSFSSTQIY
660 670 680 690 700
HSLQQKHGAL PVDPPGTCWQ GFFGHLFGYG STYYSYLFDR VLARRIWQVV
710 720 730 740 750
FKDGEAGGSI QRDNGEKMKE EVLKWGGGRD PWKCLAGVLD DGRVENGDEK
760
AMAIVGSWGV KE
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. Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CH476940 Genomic DNA. Translation: EDN33764.1. Different initiation.
RefSeqiXP_001549090.1. XM_001549040.1.

3D structure databases

ProteinModelPortaliA6SHZ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi332648.A6SHZ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5429605.
KEGGibfu:BC1G_12067.

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]
ProtoNetiSearch...

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(2010) [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: January 7, 2015
This is version 42 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.