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P0CQ20

- PMIP2_CRYNJ

UniProt

P0CQ20 - PMIP2_CRYNJ

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Protein

Mitochondrial intermediate peptidase 2

Gene
OCT2, CNB02140
Organism
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
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 bindingi595 – 5951Zinc; catalytic By similarity
Active sitei596 – 5961 By similarity
Metal bindingi599 – 5991Zinc; catalytic By similarity
Metal bindingi602 – 6021Zinc; 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

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial intermediate peptidase 2 (EC:3.4.24.59)
Short name:
MIP 2
Alternative name(s):
Octapeptidyl aminopeptidase 2
Gene namesi
Name:OCT2
Ordered Locus Names:CNB02140
OrganismiCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Taxonomic identifieri214684 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex
ProteomesiUP000002149: Chromosome 2

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 – 3333Mitochondrion Reviewed predictionAdd
BLAST
Chaini34 – 823790Mitochondrial intermediate peptidase 2PRO_0000338582Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP0CQ20.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi528 – 5358Poly-Asp

Sequence similaritiesi

Belongs to the peptidase M3 family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK01410.
OrthoDBiEOG71GB4R.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 2 hits.
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.

P0CQ20-1 [UniParc]FASTAAdd to Basket

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MRRLQQSLRR RSARRCPFIL IPHRLLTTSY ASYKPAPQAT LEIEDTNSPT    50
FLLKTSPIQL PARATSDDSA IKAHFDLPHS IFGDMVGVRR EHVKGLFHYD 100
SLTQPESLMR LTDRTLIQAS AIVQRIVVAP QDPTGRELRL VVKNLDRLSD 150
ILCGVIDMCE LIRNVHPHQD WVNQSDRTHQ ILCSFMNELN ATRGLYESLA 200
KAIAHPFNDP LTTSELRVAR IFLTDFERSG IHLPPSVRER FVKHSDALLF 250
LGRSFLSSAS SGPSTVPHIE IPDPHRLLTG LGRQFVDSLP RTGRNGQAVI 300
EPGSWEAQMI LRYAREGRAR ELVYVGGMRA DKKRISVLEA MLKERAELAS 350
VLGKNNWAEV VLVDKMTKTP ENVMRFLTSL AQHHQPVARA EVDMLRRMKA 400
TALTGNYFDP RNSRTRHLPL FHAWDRDYYS DKYLTSLIPT GSPPSISPYL 450
STGTVMSGLS RIFSRLYGIS FKPAVVSPGE VWHPSVRRLD VVHEEEGLIG 500
VIYCDFFSRI GKSSGAAHYT VRCSRRVDDD DIDGDGLPED WDKPYGPGLE 550
ADKESLSGKP GKYQLPIIAL SMDVGTVNEG RPALLNWQEL ETLFHEMGHA 600
IHSMIGRTEY HNVSGTRCAT DFVELPSILM EHFVSSPEVL STLAFHHATG 650
EPLPIPVIEA HLALNQSLSA LETHGQIAMA LLDQKYHTLR HGQDSFDSTA 700
IWFQLQQEIG VIQPVPGTAW QMQFGHLYGY GATYYSYLFD RAIAGKIWST 750
LFHRSGTSQA YDRKAEGILS REGGELLKEK VLKWGGGRDP WEMVGDVIGG 800
VEGDELSKGD ERALALVGSW SVV 823
Length:823
Mass (Da):92,172
Last modified:June 28, 2011 - v1
Checksum:i4C30FAD763938997
GO

Sequence cautioni

The sequence AAW41837.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017342 Genomic DNA. Translation: AAW41837.1. Different initiation.
RefSeqiXP_569144.1. XM_569144.1.

Genome annotation databases

EnsemblFungiiAAW41837; AAW41837; CNB02140.
GeneIDi3255573.
KEGGicne:CNB02140.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017342 Genomic DNA. Translation: AAW41837.1 . Different initiation.
RefSeqi XP_569144.1. XM_569144.1.

3D structure databases

ProteinModelPortali P0CQ20.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii AAW41837 ; AAW41837 ; CNB02140 .
GeneIDi 3255573.
KEGGi cne:CNB02140.

Phylogenomic databases

KOi K01410.
OrthoDBi EOG71GB4R.

Family and domain databases

Gene3Di 1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 2 hits.
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. "The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans."
    Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S.
    , Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.
    Science 307:1321-1324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JEC21 / ATCC MYA-565.

Entry informationi

Entry nameiPMIP2_CRYNJ
AccessioniPrimary (citable) accession number: P0CQ20
Secondary accession number(s): Q55XK7, Q5KMC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 14, 2014
This is version 14 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

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