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Q4WMU9

- PMIP_ASPFU

UniProt

Q4WMU9 - PMIP_ASPFU

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Protein
Mitochondrial intermediate peptidase
Gene
oct1, AFUA_6G08640
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
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 bindingi564 – 5641Zinc; catalytic By similarity
Active sitei565 – 5651 By similarity
Metal bindingi568 – 5681Zinc; catalytic By similarity
Metal bindingi571 – 5711Zinc; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro
  3. metallopeptidase activity Source: ASPGD
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:AFUA_6G08640
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 6

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. intracellular Source: ASPGD
  2. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141Mitochondrion Reviewed prediction
Add
BLAST
Chaini42 – 801760Mitochondrial intermediate peptidase
PRO_0000338571Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00001931.

Structurei

3D structure databases

ProteinModelPortaliQ4WMU9.

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.

Q4WMU9-1 [UniParc]FASTAAdd to Basket

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MKDQLLVPLR RRPWTCQKCL QRLQLPRHQT RRSFETAASP FPRPLDSLPA    50
DYARTKTVDD DTLRRVFDSQ QFWREFSQQR AAQPKPTGLV QNQYLTSPDG 100
FRTFANVSLQ KCQAIVSKVL AASTLEEYRT MARDLDRLSD LLCRVIDLSD 150
FIRVIHPDPQ VQEAATQAYA LMFEYMNVLN TTTGLNDQLK KAAANPEVTS 200
QWSDEEKIVA QILIKDFSNS AIHMPPHERQ RFVNLSNDIS QLGSSFVNGA 250
EPAKSHVSVA TNNLRGLDPI LVQQIKRWNR TAAVPTTGMI PRLALRSVHD 300
ENVRREVYLA SRTSSKRQLH RLEELLLKRA ELAKLSGYES FAHMTLSDKM 350
AKSPEAVSNF LTALVESNRK LVREELSQLQ VMKGAPLQPW DHAYYVHQRV 400
LQYSQARRSR ELSAVPEFFS LGTVMQGLSR LFDRLYGVRL VPQEPAPGET 450
WNPDVRRLDV VDEAGRHIAV IYCDLFSRPN KHPNPAHFTL RCSREISAEE 500
VAECASLDQS SHPNDGMATA VDPVTQTLRQ LPTIALVCDF PEPGTNGGGR 550
PSLLSEHSVR TLFHEMGHAV HSILGQTRLQ SISGTRCATD FAELPSVLME 600
HFATVPSVLA LYARHWRTDE PLSEGMIRSM ERDRTAHGSI YGAVENEAQI 650
LMALVDQAYH SRPADGGRID STALYQQVSQ QHSSLPEPAD ATTPPTSWQG 700
FFGHLYGYGA TYYSYIFDRA IANKLWVDVF GAGRHAVDRA AGERYKNEVL 750
RWGGGRSGWE CVAGALGSAN ESNADGRLVE GGDQAMREVG RWGLGRDGVS 800
G 801
Length:801
Mass (Da):89,695
Last modified:July 5, 2005 - v1
Checksum:i93D0BDC76A499FE0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL88715.1.
RefSeqiXP_750753.1. XM_745660.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00001931; CADAFUAP00001931; CADAFUAG00001931.
GeneIDi3508040.
KEGGiafm:AFUA_6G08640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL88715.1 .
RefSeqi XP_750753.1. XM_745660.1.

3D structure databases

ProteinModelPortali Q4WMU9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00001931.

Protein family/group databases

MEROPSi M03.006.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00001931 ; CADAFUAP00001931 ; CADAFUAG00001931 .
GeneIDi 3508040.
KEGGi afm:AFUA_6G08640.

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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiPMIP_ASPFU
AccessioniPrimary (citable) accession number: Q4WMU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: July 5, 2005
Last modified: May 14, 2014
This is version 66 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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