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Protein

Mitochondrial intermediate peptidase

Gene

oct1

Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
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 bindingi566 – 5661Zinc; catalyticPROSITE-ProRule annotation
Active sitei567 – 5671PROSITE-ProRule annotation
Metal bindingi570 – 5701Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi573 – 5731Zinc; 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:SS1G_01296
OrganismiSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Taxonomic identifieri665079 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia
ProteomesiUP000001312: Unassembled WGS sequence

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
Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
BLAST
Chaini28 – 785758Mitochondrial intermediate peptidasePRO_0000338594Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi665079.A7E7L8.

Structurei

3D structure databases

ProteinModelPortaliA7E7L8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi283 – 2875Poly-Ala

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
InParanoidiA7E7L8.
KOiK01410.
OrthoDBiEOG71GB4R.

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: Complete.

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

A7E7L8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKAVMPRPW VCSRCVKRQI QSSRGLATAS TQYREPRPVP TDHSAPGAKH
60 70 80 90 100
DDRTLRQIFD SPDFWADFSQ SSKQSYYRPG VGLFQNRYLV NPQGFEVFAN
110 120 130 140 150
TSLRKAQRIV DKVLKASTVE EYRHVARDLD RLSDLLCRVI DLSDFVRATH
160 170 180 190 200
PNAAIQAAAS RAYAKMFEYM NILNTTTGLD KQLEVAMGTP EIVAGWTEEE
210 220 230 240 250
VVVADILKKD FAKSAIDLPR AQREKFVALS QEISEIGPDF VDYMTPAKSY
260 270 280 290 300
LTFESSKLKG MDPVLVREHT TWGQTKIPTI GGAAAAAIRT VQNEEVRREI
310 320 330 340 350
FMATRTASRN TVHKLEELMR KRAELAKLSR YESYSQLALG DKMAKSPASV
360 370 380 390 400
TQFLEALAKD NNKIVQGEVS ELLKFKFSNP NASSPGLQPW DKDYYMSRIL
410 420 430 440 450
ASVRSHSRNS DFLSAYFSLG TVMQGLSRLF TRLYGVRLAP HETMPGETWN
460 470 480 490 500
SDVRRLDVIS ETDGHVAVLY CDLFSRPGKS PNPAHFTLRC SREITTAELE
510 520 530 540 550
EASMLSQNGL FKTDEEAAND GMATSKSSGV LKQLPTIALI CDFVTMSGKS
560 570 580 590 600
SRPALLSFNE VQTLFHEMGH AIHSILGRTS LQNVSGTRCA TDFAELPSVL
610 620 630 640 650
MEHFAADPSV LSLFARHYET DQQLPYEMVA EKLALDKRFE GSDTENQIIL
660 670 680 690 700
SMLDLAYHSD LPLSPTFNST EIYHSLQQKH GALPVDPPGT CWQGFFGHLF
710 720 730 740 750
GYGSTYYSYL FDRVLARRIW QVVFQGGEAG GSVHRGNGEK MKEEVLKWGG
760 770 780
GRDPWKCLAG VLDDGRVENG DEKAMAIVGS WGVKE
Length:785
Mass (Da):87,723
Last modified:June 10, 2008 - v2
Checksum:i22354DF6D7047D4F
GO

Sequence cautioni

The sequence EDN96370.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476622 Genomic DNA. Translation: EDN96370.1. Different initiation.
RefSeqiXP_001597102.1. XM_001597052.1.

Genome annotation databases

EnsemblFungiiEDN96370; EDN96370; SS1G_01296.
GeneIDi5493674.
KEGGissl:SS1G_01296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476622 Genomic DNA. Translation: EDN96370.1. Different initiation.
RefSeqiXP_001597102.1. XM_001597052.1.

3D structure databases

ProteinModelPortaliA7E7L8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi665079.A7E7L8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDN96370; EDN96370; SS1G_01296.
GeneIDi5493674.
KEGGissl:SS1G_01296.

Phylogenomic databases

eggNOGiCOG0339.
InParanoidiA7E7L8.
KOiK01410.
OrthoDBiEOG71GB4R.

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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 18683 / 1980 / Ss-1.

Entry informationi

Entry nameiPMIP_SCLS1
AccessioniPrimary (citable) accession number: A7E7L8
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

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

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.