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Protein

Mitochondrial intermediate peptidase

Gene

oct1

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
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 bindingi565 – 5651Zinc; catalyticPROSITE-ProRule annotation
Active sitei566 – 5661PROSITE-ProRule annotation
Metal bindingi569 – 5691Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi572 – 5721Zinc; 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:NFIA_054290
OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Taxonomic identifieri331117 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya
ProteomesiUP000006702: 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 – 4242MitochondrionSequence AnalysisAdd
BLAST
Chaini43 – 801759Mitochondrial intermediate peptidasePRO_0000338589Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi36630.CADNFIAP00004862.

Structurei

3D structure databases

ProteinModelPortaliA1DMR2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000076521.
KOiK01410.
OMAiPQVFAHY.
OrthoDBiEOG71GB4R.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
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.

A1DMR2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKDQLLVPLR RRPWTCRKCL QRLQLLPQHQ TRRSFETAAS PFPRQLDSLP
60 70 80 90 100
ADYSRTKTVD DDTLRRVFDS QQFWREFSQQ RSAQPKPTGL VQNQYLTSPD
110 120 130 140 150
GFRTFANVSL QKCQAIVSKV LAASTLEEYR TMARDLDRLS DLLCRVIDLS
160 170 180 190 200
DFIRVIHPDP QVQEAATQAY ALMFEYMNVL NTTTGLNDQL KKAAANPEVT
210 220 230 240 250
SQWSDEEKIV AQILIKDFSN SAIHMPPHER QRFVNLSNDI SQLGSSFVNG
260 270 280 290 300
AEPAKSHVSV ATNNLRGLDP ILVQQIKRWN RTAAVPTTGM IPRLALRSVH
310 320 330 340 350
DENVRREVYL ASRTSSKRQL HRLEELLLKR AELAKLSGYE SFAHMTLSDK
360 370 380 390 400
MAKSPEAVSN FLTALVDSNR KLVREELSQL QAMKGAPLQP WDHAYYVHQR
410 420 430 440 450
VMQYSQARRS RELSAVPEFF SLGTVMQGLS RLFDRLYGVR LVPQEPAPGE
460 470 480 490 500
TWNPDVRRLD VVDESGRHIA VIYCDLFSRP NKHPNPAHFT LRCSREISTE
510 520 530 540 550
EVAECASLDQ SSHPNDGMAT AVDPVTKTLR QLPTIALVCD FSEPGTNGGG
560 570 580 590 600
RPSLLSEHSV RTLFHEMGHA VHSILGQTRL QSISGTRCAT DFAELPSVLM
610 620 630 640 650
EHFATAPSVL ALYARHWRTD EPLSEGMIRS MERDRTAHGS IYGAVENEAQ
660 670 680 690 700
ILMALVDQAY HSRPADGGRI DSTALYQQVS QQHSSLPEPA DVTPPTSWQG
710 720 730 740 750
FFGHLYGYGA TYYSYIFDRA IANKLWVDVF GAGRQAVDRA AGERYKNEVL
760 770 780 790 800
RWGGGRSGWE CVAGALGSAN ESNADGRLVE GGDEAMREVG RWGLGRDGVS

G
Length:801
Mass (Da):89,774
Last modified:January 23, 2007 - v1
Checksum:i906514456D11365F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027698 Genomic DNA. Translation: EAW16083.1.
RefSeqiXP_001257980.1. XM_001257979.1.

Genome annotation databases

EnsemblFungiiCADNFIAT00004990; CADNFIAP00004862; CADNFIAG00004990.
GeneIDi4584495.
KEGGinfi:NFIA_054290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027698 Genomic DNA. Translation: EAW16083.1.
RefSeqiXP_001257980.1. XM_001257979.1.

3D structure databases

ProteinModelPortaliA1DMR2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi36630.CADNFIAP00004862.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADNFIAT00004990; CADNFIAP00004862; CADNFIAG00004990.
GeneIDi4584495.
KEGGinfi:NFIA_054290.

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000076521.
KOiK01410.
OMAiPQVFAHY.
OrthoDBiEOG71GB4R.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

Entry informationi

Entry nameiPMIP_NEOFI
AccessioniPrimary (citable) accession number: A1DMR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 45 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

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.