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E9CTR7 (AMPP1_COCPS) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 11. 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:CPSG_00906
OrganismCoccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus) [Complete proteome]
Taxonomic identifier443226 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides

Protein attributes

Sequence length611 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 – 611611Probable Xaa-Pro aminopeptidase P
PRO_0000411788

Sites

Metal binding4081Manganese 2 By similarity
Metal binding4191Manganese 1 By similarity
Metal binding4191Manganese 2 By similarity
Metal binding5171Manganese 1 By similarity
Metal binding5311Manganese 1 By similarity
Metal binding5311Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
E9CTR7 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 3BE54F908636A4B8

FASTA61167,899
        10         20         30         40         50         60 
MPVDTSQRLA KLRELMKERH VDVYLIPSED SHQSEYIAPC DARRAFISGF TGSAGCAIVS 

        70         80         90        100        110        120 
MSKAALSTDG RYFNQAAKQL DENWLLLKRG MENVPTWQEW TAEQAEGGKV VGVDPSLITA 

       130        140        150        160        170        180 
AEARKLSDTI KDTGGSLVGV PDNLVDLVWG GDRPARPREK VMVHPIEFAG QSFEEKITDL 

       190        200        210        220        230        240 
RKELTKKKRA GMVISMLDEI AWLYNLRGAD IPFNPVFFAY AIVTHSTAEL FVDEAKLTQA 

       250        260        270        280        290        300 
VKEHLGDKVA LRPYESIFES LKLLSQAAAS NGDEGHQKFL LSDKASWSLN LALGGEEKVE 

       310        320        330        340        350        360 
EVRSPIADAK AVKNAVELEG TRACHIRDGA ALTEYFAWLE NELINKKTVL NEVNASDKLA 

       370        380        390        400        410        420 
QIRSKHKDFV GLSFDTISST GPNAAIIHYR AERGNCPNID PNAVYLCDSG AQYLDGTTDT 

       430        440        450        460        470        480 
TRTLHFGKPT EMEKKAYTLV LKGLISIDTA VFPKGTTGYA IDAFARQHLW RNGLDYLHGT 

       490        500        510        520        530        540 
GHGVGSYLNV HEGPMGIGTR VQYAETPITA GNVLSDEPGY YEDGNFGIRI ENIVVAKEVK 

       550        560        570        580        590        600 
TPHKFGDKPW IGFEHVTMTP LCQNLMDTSL LTAEEKKWVN DYHTEVWEKT KGFFNNDELT 

       610 
RNWLKRETQP I 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GL636486 Genomic DNA. Translation: EFW23007.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_COCPS
AccessionPrimary (citable) accession number: E9CTR7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: April 5, 2011
Last modified: March 6, 2013
This is version 11 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