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B2VUU7 (AMPP1_PYRTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 28. 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:PTRG_01084
OrganismPyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis) [Complete proteome]
Taxonomic identifier426418 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaePyrenophora

Protein attributes

Sequence length594 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 – 594594Probable Xaa-Pro aminopeptidase P
PRO_0000411807

Sites

Metal binding3911Manganese 2 By similarity
Metal binding4021Manganese 1 By similarity
Metal binding4021Manganese 2 By similarity
Metal binding5001Manganese 1 By similarity
Metal binding5141Manganese 1 By similarity
Metal binding5141Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
B2VUU7 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: A1FAEF86BA116F09

FASTA59466,842
        10         20         30         40         50         60 
MAKVDTSHRL AELRKLMKER NVDIYTYISG FTGSAGYAVI THDKAALSTD GRYFNQAEKQ 

        70         80         90        100        110        120 
LDSNWELLKQ GIQDVPTIQE WTADQAEGGK VVGVDPSVVT AGDARKLAEK IKKKGGEYKA 

       130        140        150        160        170        180 
IDENLVDLVW SSERPARPSE KVIVQPERYA CKGFEDKIDD LRKELEKKKS LGFVVSMLDE 

       190        200        210        220        230        240 
VAWLFNLRGS DIPYNPVFFS YAVVTPTAAT LYVDENKLPE DVKEHLGNKI TIRPYEAIFG 

       250        260        270        280        290        300 
DVTALSKELF EASDKNETQK KFLTSNRASW ALNKALGGDD KVEETRSPVG DSKAVKNEVE 

       310        320        330        340        350        360 
LEGMRQCHIR DGAALSEYFA WLEDQLINKK ATLDEVDGAD KLEEIRKKHD MFMGLSFDTI 

       370        380        390        400        410        420 
SSTGANAAVI HYKPEKGECA TIDPKAIYLC DSGAQYRDGT TDTTRTLHFT EPTEMERKAY 

       430        440        450        460        470        480 
TLVLKGNMAL ERVKFPKGTT GFALDALARQ FLWAEGLDYR HGTGHGVGSF LNVHEGPIGI 

       490        500        510        520        530        540 
GTRVQYSEVS LAVGNVVSDE PGYYEDGKFG IRIENMVMVK EVETKHKFGD KPYLGFEHVT 

       550        560        570        580        590 
MTPHCRNLVD MSLLTEDEKK FINEYHKEVY EKTSKYFEND ALTLEWLKRE TAPY 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS231615 Genomic DNA. Translation: EDU40522.1.
RefSeqXP_001931417.1. XM_001931382.1.

3D structure databases

ProteinModelPortalB2VUU7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEDU40522; EDU40522; PTRG_01084.
GeneID6338674.

Phylogenomic databases

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_PYRTR
AccessionPrimary (citable) accession number: B2VUU7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 1, 2008
Last modified: May 29, 2013
This is version 28 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