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Q0UFY4 (AMPP1_PHANO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 52. 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 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:SNOG_09330
OrganismPhaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum) [Reference proteome]
Taxonomic identifier321614 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePhaeosphaeriaceaePhaeosphaeria

Protein attributes

Sequence length650 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 – 650650Probable Xaa-Pro aminopeptidase P
PRO_0000411805

Sites

Metal binding4471Manganese 2 By similarity
Metal binding4581Manganese 1 By similarity
Metal binding4581Manganese 2 By similarity
Metal binding5561Manganese 1 By similarity
Metal binding5701Manganese 1 By similarity
Metal binding5701Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0UFY4 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: E1C17EFDC9A294D1

FASTA65072,750
        10         20         30         40         50         60 
MPRDALSFEL QLSAGLEATE HKLDMLTRLL RRTHVAVKHP LLASRAFHTS PALRAIDMAK 

        70         80         90        100        110        120 
VDTTERLAEL RKLMKERKVD VYTYISGFTG SAGYAVVTHD KAALATDGRY FNQAEKQLDS 

       130        140        150        160        170        180 
NWELLKQGIQ DVPTIQEWTA DQVEGGKVVG VDPSVVTGAD ARKLAEKIKK KGGEYKAVDD 

       190        200        210        220        230        240 
NLVDLVWAAE RPARPSEKVI VQPMEYSGKS FDEKVEDLRK ELEKKKSLGF VVSMLDEVAW 

       250        260        270        280        290        300 
LFNLRGNDIP YNPVFFSYAV ITPTVVTLYV DESKLPKEVK DHLGDKVAIR PYEAIFGDIT 

       310        320        330        340        350        360 
ALSKDAFEAA DADATKKFLT SNRASWALNK ALGGDDKVEE IRSPIGDAKA VKNEVELEGM 

       370        380        390        400        410        420 
RQCHIRDGAA ISEYFAWLED QLLNKKATLD EVDGADKLEA IRKKHDKFMG LSFDTISSTG 

       430        440        450        460        470        480 
PNGAVIHYKP EKGACSIIDP NAIYLCDSGA QYHDGTTDTT RTLHFTKPTD MEKKAYTLVL 

       490        500        510        520        530        540 
KGNIALERVK FPKGTTGFAL DSIARQFLWA EGLDYRHGTG HGVGSFLNVH EGPIGIGTRV 

       550        560        570        580        590        600 
QYSEVSLAVG NVISDEPGYY EDGKFGIRIE NMIMVKEVET NHKFGDKPYL GFEHVTLTPH 

       610        620        630        640        650 
CRNLVDMTLL TEDEKKFIND YHKEVFEKTS KFFENDKLTM DWLKRETAPY 

« Hide

References

[1]"Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum."
Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P.
Plant Cell 19:3347-3368(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH445338 Genomic DNA. Translation: EAT83522.1.
RefSeqXP_001799625.1. XM_001799573.1.

3D structure databases

ProteinModelPortalQ0UFY4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSNOT_09330; SNOT_09330; SNOG_09330.
GeneID5976526.
KEGGpno:SNOG_09330.

Phylogenomic databases

KOK01262.
OMASRYWEQA.
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_PHANO
AccessionPrimary (citable) accession number: Q0UFY4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: September 5, 2006
Last modified: March 6, 2013
This is version 52 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