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A2QWM4

- PMIP_ASPNC

UniProt

A2QWM4 - PMIP_ASPNC

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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

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
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: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. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MGASLLLPLR RRPWTCRTCL LQARRSLETA ASPATHRAAF DYLPSKNDAQ
60 70 80 90 100
KKSDDDTLRR VFDSQPFWRE FSQRSAAHLK PTGLVQNQYL TSPDGFRVFA
110 120 130 140 150
TTTLQKCQAI VAKVLAGTTL EDYQSMARDL DRLSDLLCRV IDLSDFIRVI
160 170 180 190 200
HPDPRVQEAA TQAYALMFEY MNVLNTTTGL NDQLKKAAAN PEVTARWSDE
210 220 230 240 250
EKIVAQILIK DFSNSAIHMP PHARQRFVNL SNDISQLGNT FVNAAEPAKS
260 270 280 290 300
HVTVSANSLR GLDPILVQQI KRWNRTASVP SMGLIPRLAL RSVHDEGVRR
310 320 330 340 350
EVYLATRTSS ARQIQRLEQL LAKRAELAQL SGYDSFAHMT LSDKMAKSPE
360 370 380 390 400
AVSNFLTSLV GSNRPYVQEE LAQLQSMKGS AGRLQPWDHA YYVHQRVLQY
410 420 430 440 450
SQSRRSRELS AVPEFFSLGT VMQGLSRLFD RLYGVRLVPQ ETAAGETWNS
460 470 480 490 500
DVRRLDVVDE ADRHIAVIYC DLFSRPNKHP NPAHYTLRCA REISAEEVAE
510 520 530 540 550
CATTMDASAH PNDGMATAVD RDAKTLRQLP TIALVCDFPE PPATGTGRPS
560 570 580 590 600
LLSEHSVRTL FHEMGHALHS ILGQTRLQSI SGTRCATDFA ELPSVLMERF
610 620 630 640 650
ATAPEVLALY ARHWETDAPL SESMMQHMEK DRTAHGSIYG AMENESQILM
660 670 680 690 700
ALVDQAYHSL PAGQATSIDS TAVFHQVSAE HCTLPDPTDT KPPTSWQGFF
710 720 730 740 750
GHLHGYGATY YSYIFDRAIA NKLWEDVFQQ GKAAVDRQAG ERYKNEVLRW
760 770 780 790
GGGRNGWNCV AGVLGSAHPA NADGRLVEGG DEAMREVGRW GLGRDGVSE
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.

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 29, 2014
This is version 50 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