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Q4WMU9 (PMIP_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial intermediate peptidase

Short name=MIP
EC=3.4.24.59
Alternative name(s):
Octapeptidyl aminopeptidase
Gene names
Name:oct1
ORF Names:AFUA_6G08640
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length801 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

Cofactor

Binds 1 zinc ion By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the peptidase M3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Mitochondrion Potential
Chain42 – 801760Mitochondrial intermediate peptidase
PRO_0000338571

Sites

Active site5651 By similarity
Metal binding5641Zinc; catalytic By similarity
Metal binding5681Zinc; catalytic By similarity
Metal binding5711Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WMU9 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 93D0BDC76A499FE0

FASTA80189,695
        10         20         30         40         50         60 
MKDQLLVPLR RRPWTCQKCL QRLQLPRHQT RRSFETAASP FPRPLDSLPA DYARTKTVDD 

        70         80         90        100        110        120 
DTLRRVFDSQ QFWREFSQQR AAQPKPTGLV QNQYLTSPDG FRTFANVSLQ KCQAIVSKVL 

       130        140        150        160        170        180 
AASTLEEYRT MARDLDRLSD LLCRVIDLSD FIRVIHPDPQ VQEAATQAYA LMFEYMNVLN 

       190        200        210        220        230        240 
TTTGLNDQLK KAAANPEVTS QWSDEEKIVA QILIKDFSNS AIHMPPHERQ RFVNLSNDIS 

       250        260        270        280        290        300 
QLGSSFVNGA EPAKSHVSVA TNNLRGLDPI LVQQIKRWNR TAAVPTTGMI PRLALRSVHD 

       310        320        330        340        350        360 
ENVRREVYLA SRTSSKRQLH RLEELLLKRA ELAKLSGYES FAHMTLSDKM AKSPEAVSNF 

       370        380        390        400        410        420 
LTALVESNRK LVREELSQLQ VMKGAPLQPW DHAYYVHQRV LQYSQARRSR ELSAVPEFFS 

       430        440        450        460        470        480 
LGTVMQGLSR LFDRLYGVRL VPQEPAPGET WNPDVRRLDV VDEAGRHIAV IYCDLFSRPN 

       490        500        510        520        530        540 
KHPNPAHFTL RCSREISAEE VAECASLDQS SHPNDGMATA VDPVTQTLRQ LPTIALVCDF 

       550        560        570        580        590        600 
PEPGTNGGGR PSLLSEHSVR TLFHEMGHAV HSILGQTRLQ SISGTRCATD FAELPSVLME 

       610        620        630        640        650        660 
HFATVPSVLA LYARHWRTDE PLSEGMIRSM ERDRTAHGSI YGAVENEAQI LMALVDQAYH 

       670        680        690        700        710        720 
SRPADGGRID STALYQQVSQ QHSSLPEPAD ATTPPTSWQG FFGHLYGYGA TYYSYIFDRA 

       730        740        750        760        770        780 
IANKLWVDVF GAGRHAVDRA AGERYKNEVL RWGGGRSGWE CVAGALGSAN ESNADGRLVE 

       790        800 
GGDQAMREVG RWGLGRDGVS G 

« Hide

References

[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000006 Genomic DNA. Translation: EAL88715.1.
RefSeqXP_750753.1. XM_745660.1.

3D structure databases

ProteinModelPortalQ4WMU9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00001931.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00001931; CADAFUAP00001931; CADAFUAG00001931.
GeneID3508040.
KEGGafm:AFUA_6G08640.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
KOK01410.
OMAQMSTHEE.
OrthoDBEOG71GB4R.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMIP_ASPFU
AccessionPrimary (citable) accession number: Q4WMU9
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries