SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A6SHZ5

- PMIP_BOTFB

UniProt

A6SHZ5 - PMIP_BOTFB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Mitochondrial intermediate peptidase

Gene
oct1, BC1G_12067
Organism
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Status
Reviewed - 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.

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; catalytic By similarity
Active sitei544 – 5441 By similarity
Metal bindingi547 – 5471Zinc; catalytic By similarity
Metal bindingi550 – 5501Zinc; catalytic By similarity

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

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
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.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the peptidase M3 family.

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.

Non-terminal residue

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: July 9, 2014
This is version 38 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