Skip Header

Contribute Send feedback
Read comments (?) or add your own

E3S7K9 (AMPP1_PYRTT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 15. 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:PTT_18815
OrganismPyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) (Drechslera teres f. teres) [Complete proteome]
Taxonomic identifier861557 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaePyrenophora

Protein attributes

Sequence length656 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 – 656656Probable Xaa-Pro aminopeptidase P
PRO_0000411808

Sites

Metal binding4531Manganese 2 By similarity
Metal binding4641Manganese 1 By similarity
Metal binding4641Manganese 2 By similarity
Metal binding5621Manganese 1 By similarity
Metal binding5761Manganese 1 By similarity
Metal binding5761Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
E3S7K9 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: BAD2F9E88C9B38F6

FASTA65673,488
        10         20         30         40         50         60 
MLLPRIPQLS HATRAAYVAA KSPFSPVPVR PFHASAALRA IDMAKVDTTH RLAELRKLMK 

        70         80         90        100        110        120 
ERNVDIYMVP SEDSHQSEYI APCDARRAYI SGFTGSAGYA VITHEKAALS TDGRYFNQAE 

       130        140        150        160        170        180 
KQLDSNWELL KQGIQDVPTI QQWTADQAGG GKVVGVDPSV VTAGDARKLA EKIKKKGGEY 

       190        200        210        220        230        240 
KAIDENLVDL VWGSERPARP SEKVIVQPKK YAGKGFEDKI DDLRKELEKK KSLGFVVSML 

       250        260        270        280        290        300 
DEVAWLFNLR GSDIPYNPVF FSYAVVTPTT ATLYVDENKL PEDVKEHLGD KITIRPYEAI 

       310        320        330        340        350        360 
FGDVTALSKE LFEANDKNET QKKFLTSNTA SWALNKALGG DDKVEETRSP VGDSKAVKNE 

       370        380        390        400        410        420 
VELEGMRQCH IRDGAALSEY FAWLEDQLIN KKATLDEVDG ADKLEEIRKK HDMFMGLSFD 

       430        440        450        460        470        480 
TISSTGANAA VIHYKPEKGE CATIDSKAIY LCDSGAQYRD GTTDTTRTLH FTEPTEMERK 

       490        500        510        520        530        540 
AYTLVLKGNM ALERVKFPKG TTGFALDALA RQFLWAEGLD YRHGTGHGVG SFLNVHEGPI 

       550        560        570        580        590        600 
GIGTRVQYSE VSLAVGNVVS DEPGYYEDGK FGIRIENMVM VKEVETKHKF GDKPYLGFEH 

       610        620        630        640        650 
VTMTPYCRNL VDMKLLTEDE KKFINDYHKE VYEKTSKYFD KDALTLEWLK RETAPY 

« Hide

References

[1]"A first genome assembly of the barley fungal pathogen Pyrenophora teres f. teres."
Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S., Oliver R.P., Friesen T.L.
Genome Biol. 11:R109.1-R109.14(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 0-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GL537558 Genomic DNA. Translation: EFQ86051.1.
RefSeqXP_003305864.1. XM_003305816.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFQ86051; EFQ86051; PTT_18815.
GeneID10517360.
KEGGpte:PTT_18815.

Phylogenomic databases

KOK01262.

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_PYRTT
AccessionPrimary (citable) accession number: E3S7K9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: January 11, 2011
Last modified: April 3, 2013
This is version 15 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