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A1DMR2

- PMIP_NEOFI

UniProt

A1DMR2 - PMIP_NEOFI

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Protein
Mitochondrial intermediate peptidase
Gene
oct1, NFIA_054290
Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
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 bindingi565 – 5651Zinc; catalytic By similarity
Active sitei566 – 5661 By similarity
Metal bindingi569 – 5691Zinc; catalytic By similarity
Metal bindingi572 – 5721Zinc; 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: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 – 4242Mitochondrion Reviewed prediction
Add
BLAST
Chaini43 – 801759Mitochondrial intermediate peptidase
PRO_0000338589Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi36630.CADNFIAP00004862.

Structurei

3D structure databases

ProteinModelPortaliA1DMR2.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000076521.
KOiK01410.
OMAiQMSTHEE.
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

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MKDQLLVPLR RRPWTCRKCL QRLQLLPQHQ TRRSFETAAS PFPRQLDSLP    50
ADYSRTKTVD DDTLRRVFDS QQFWREFSQQ RSAQPKPTGL VQNQYLTSPD 100
GFRTFANVSL QKCQAIVSKV LAASTLEEYR TMARDLDRLS DLLCRVIDLS 150
DFIRVIHPDP QVQEAATQAY ALMFEYMNVL NTTTGLNDQL KKAAANPEVT 200
SQWSDEEKIV AQILIKDFSN SAIHMPPHER QRFVNLSNDI SQLGSSFVNG 250
AEPAKSHVSV ATNNLRGLDP ILVQQIKRWN RTAAVPTTGM IPRLALRSVH 300
DENVRREVYL ASRTSSKRQL HRLEELLLKR AELAKLSGYE SFAHMTLSDK 350
MAKSPEAVSN FLTALVDSNR KLVREELSQL QAMKGAPLQP WDHAYYVHQR 400
VMQYSQARRS RELSAVPEFF SLGTVMQGLS RLFDRLYGVR LVPQEPAPGE 450
TWNPDVRRLD VVDESGRHIA VIYCDLFSRP NKHPNPAHFT LRCSREISTE 500
EVAECASLDQ SSHPNDGMAT AVDPVTKTLR QLPTIALVCD FSEPGTNGGG 550
RPSLLSEHSV RTLFHEMGHA VHSILGQTRL QSISGTRCAT DFAELPSVLM 600
EHFATAPSVL ALYARHWRTD EPLSEGMIRS MERDRTAHGS IYGAVENEAQ 650
ILMALVDQAY HSRPADGGRI DSTALYQQVS QQHSSLPEPA DVTPPTSWQG 700
FFGHLYGYGA TYYSYIFDRA IANKLWVDVF GAGRQAVDRA AGERYKNEVL 750
RWGGGRSGWE CVAGALGSAN ESNADGRLVE GGDEAMREVG RWGLGRDGVS 800
G 801
Length:801
Mass (Da):89,774
Last modified:January 23, 2007 - v1
Checksum:i906514456D11365F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
DS027698 Genomic DNA. Translation: EAW16083.1 .
RefSeqi XP_001257980.1. XM_001257979.1.

3D structure databases

ProteinModelPortali A1DMR2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 36630.CADNFIAP00004862.

Protein family/group databases

MEROPSi M03.006.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADNFIAT00004990 ; CADNFIAP00004862 ; CADNFIAG00004990 .
GeneIDi 4584495.
KEGGi nfi:NFIA_054290.

Phylogenomic databases

eggNOGi COG0339.
HOGENOMi HOG000076521.
KOi K01410.
OMAi QMSTHEE.
OrthoDBi EOG71GB4R.

Family and domain databases

Gene3Di 1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
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. 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: May 14, 2014
This is version 41 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

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

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