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C6H7R7 (AMPP3_AJECH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 22. 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 PEPP

EC=3.4.11.9
Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase
Gene names
Name:PEPP
ORF Names:HCDG_01478
OrganismAjellomyces capsulata (strain H143) (Darling's disease fungus) (Histoplasma capsulatum) [Complete proteome]
Taxonomic identifier544712 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces

Protein attributes

Sequence length469 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 – 469469Probable Xaa-Pro aminopeptidase PEPP
PRO_0000411859

Sites

Metal binding2641Manganese 2 By similarity
Metal binding2751Manganese 1 By similarity
Metal binding2751Manganese 2 By similarity
Metal binding3981Manganese 1 By similarity
Metal binding4381Manganese 1 By similarity
Metal binding4381Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
C6H7R7 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 4A3328396BFBF22D

FASTA46952,439
        10         20         30         40         50         60 
MDESVDRVLA GKYPAKAHAK RVAARIRELG YGESGVIYLE GQKTQMIEDN DGSMPFRQRR 

        70         80         90        100        110        120 
NFFYLSGCPL PDSYLTYNIE EDHLTLFIPP IDEDSVIWSG LPLSPDEALE MYDVDAVLLT 

       130        140        150        160        170        180 
TDVNTSLAHF CSVKKGKKVF ALADQVSPHI TFLPFQETDF DVLKRAAEES RVVKDTYEIA 

       190        200        210        220        230        240 
LLRRANEIST KAHVAVIKAA RSAANERELE AIFIATCMSY GCREQSYHPI FASGTNAATL 

       250        260        270        280        290        300 
HYQNNNEDLV DKTTGEKRLN MLVDAGGEYR TYCADITRVV PLSGKFSAES RQIYDIVLDM 

       310        320        330        340        350        360 
QMTSLAMIRA GVMWEDVHSN SHRVAIRGLL KLGILRGTEE ELFDKGISVA FFPHGVGHYL 

       370        380        390        400        410        420 
GMDTHDTGGN PNYEDENPKF KYLRLRGTLA CGAVVTVEPG IYFCRFIIDP YLASPELGKY 

       430        440        450        460 
IDTNVLERYW NVGGVRIEDN VVVTQNGHDN LTAAPKIPEE IEKLVAATQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GG692420 Genomic DNA. Translation: EER43448.1.

3D structure databases

ProteinModelPortalC6H7R7.
ModBaseSearch...

Protein family/group databases

MEROPSM24.A09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.230.10. 1 hit.
InterProIPR007865. Aminopep_P_N.
IPR000994. Pept_M24_structural-domain.
[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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPP3_AJECH
AccessionPrimary (citable) accession number: C6H7R7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: September 1, 2009
Last modified: March 6, 2013
This is version 22 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