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Q4WUD3 (AMPP1_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 60. 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:
Probable Xaa-Pro aminopeptidase P

Short name=AMPP
Short name=Aminopeptidase P
EC=3.4.11.9
Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase
Gene names
Name:ampp
ORF Names:AFUA_5G08050
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides By similarity.

Catalytic activity

Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Sequence similarities

Belongs to the peptidase M24B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 654654Probable Xaa-Pro aminopeptidase P
PRO_0000411781

Sites

Metal binding4491Manganese 2 By similarity
Metal binding4601Manganese 1 By similarity
Metal binding4601Manganese 2 By similarity
Metal binding5581Manganese 1 By similarity
Metal binding5721Manganese 1 By similarity
Metal binding5721Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WUD3 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 8884D6BCE899397C

FASTA65472,680
        10         20         30         40         50         60 
MLGFRSPIRL CKLSALGSTR LLPISRPKLF STAVARYAAD METVNTTKRL ARLRQLMQEH 

        70         80         90        100        110        120 
KIDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAIV SMTKAALSTD GRYFNQASKQ 

       130        140        150        160        170        180 
LDSNWELLKR GVENVPTWQE WTTEQAQGGK VVGVDPALIT ASGARSLEET LKRNGSSLVG 

       190        200        210        220        230        240 
ISQNLVDLVW GKDRPAPPRE KVRVHPDKFS GKTFQEKIAD LRKELEKKKT AGFVISMLDE 

       250        260        270        280        290        300 
IAWLFNLRGS DIPYNPVFFA YAIITPTKAE LYIDDDKITP EVVAHLGQDV VIKPYNSIFA 

       310        320        330        340        350        360 
DAKALSEARR KEAGETASKF LLSNKASWAL SLSLGGEEHV EETRSPIADA KAIKNEVELA 

       370        380        390        400        410        420 
GMRACHIRDG AALIEYFAWL ENELVNKKTV LDEVDAADKL EQIRTKHDLF AGLSFDTISS 

       430        440        450        460        470        480 
TGPNGAVIHY KPEKGTCSII DPDAIYLCDS GAQYLDGTTD VTRTFHFGKP TELEKKAFTL 

       490        500        510        520        530        540 
VLKGLIAIDT AVFPKGTSGF ALDALARQYL WKEGLDYLHG TGHGVGSYLN VHEGPIGIGT 

       550        560        570        580        590        600 
RVQYTEVPIA PGNVISDEPG FYEDGKFGIR IENVIMAREV QTTHKFGDKP WLGFEHVTMA 

       610        620        630        640        650 
PIGRNLIEPS LLSDLELKWV NDYHAEVWDK THHFFENDEF TRSWLQRETA PITK 

« 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
AAHF01000003 Genomic DNA. Translation: EAL91793.1.
RefSeqXP_753831.1. XM_748738.1.

3D structure databases

ProteinModelPortalQ4WUD3.
ModBaseSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00006272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00006272; CADAFUAP00006272; CADAFUAG00006272.
GeneID3511166.
KEGGafm:AFUA_5G08050.

Phylogenomic databases

HOGENOMHOG000255713.
KOK01262.
OMAISTARFP.
OrthoDBEOG45F0XX.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
InterProIPR000587. Creatinase.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamPF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
PROSITEPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPP1_ASPFU
AccessionPrimary (citable) accession number: Q4WUD3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 5, 2005
Last modified: April 3, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families