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Q4WRV9 (AMPP2_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable Xaa-Pro aminopeptidase AFUA_1G14920

EC=3.4.11.9
Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase
Gene names
ORF Names:AFUA_1G14920
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length487 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 – 487487Probable Xaa-Pro aminopeptidase AFUA_1G14920
PRO_0000411826

Sites

Metal binding2671Manganese 2 By similarity
Metal binding2781Manganese 1 By similarity
Metal binding2781Manganese 2 By similarity
Metal binding4161Manganese 1 By similarity
Metal binding4551Manganese 1 By similarity
Metal binding4551Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WRV9 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 762B5F710F5E5D53

FASTA48754,519
        10         20         30         40         50         60 
MRGSGRSDIV ISAVDALDIC ITLARNDCDK YPGSVAAKLG VSSGLIYLVG QPTINWGDSD 

        70         80         90        100        110        120 
QPRPFRQRRY FYYLSGVEEA DCYLTYDIKN DLLTLYVPDF DLHRAIWMGP TLTVKEARER 

       130        140        150        160        170        180 
YDVDQVRYHA SLKGDIQRWA DNYNKTSLLY ILHDTQKPQV LSNELRLDDE LLLPAMDAAR 

       190        200        210        220        230        240 
GIKDEHEIRM IREANRVSAL AHRKVLENVL RMSTEAEIEG LFLDTCISHG AKNQAYEIIA 

       250        260        270        280        290        300 
GSGENAAVLH YVKNNEPLQG RQLVCLDAGA EWNCYASDVT RTFPLAADWP TARARDIYQL 

       310        320        330        340        350        360 
VEEMQEECIK RIQKGVRFLD LQVLAHVIAI EGLMRLGILK GGSVEEIRES GASTVFFPHG 

       370        380        390        400        410        420 
LGHHVGLEVH DVSAKRLTAV EGDKEYYSSI LVPSMSHCPC TLSAPLLEEG MVVTVEPGIY 

       430        440        450        460        470        480 
FSRLALANAR KLAFAKYINF DEAEKYIPIG GVRIEDDILV TSSGHENLTT APKGEEMLEI 


IRRGIDS 

« 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
AAHF01000004 Genomic DNA. Translation: EAL90823.1.
RefSeqXP_752861.1. XM_747768.1.

3D structure databases

ProteinModelPortalQ4WRV9.
ModBaseSearch...

Protein family/group databases

MEROPSM24.A09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00007282; CADAFUAP00007282; CADAFUAG00007282.
GeneID3509884.
KEGGafm:AFUA_1G14920.

Phylogenomic databases

HOGENOMHOG000008763.
KOK14213.
OMAGHHVGLE.
OrthoDBEOG4897VR.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
InterProIPR007865. Aminopep_P_N.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamPF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SMARTSM01011. AMP_N. 1 hit.
[Graphical view]
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
PROSITEPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPP2_ASPFU
AccessionPrimary (citable) accession number: Q4WRV9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 5, 2005
Last modified: March 6, 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