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C6HSY3 (AMPP1_AJECH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 21. 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:HCDG_09314
OrganismAjellomyces capsulata (strain H143) (Darling's disease fungus) (Histoplasma capsulatum) [Complete proteome]
Taxonomic identifier544712 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces

Protein attributes

Sequence length636 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 – 636636Probable Xaa-Pro aminopeptidase P
PRO_0000411771

Sites

Metal binding4141Manganese 2 By similarity
Metal binding4251Manganese 1 By similarity
Metal binding4251Manganese 2 By similarity
Metal binding5231Manganese 1 By similarity
Metal binding5371Manganese 1 By similarity
Metal binding5371Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
C6HSY3 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: B35B61DD67003A6A

FASTA63671,096
        10         20         30         40         50         60 
MGPIDTSQRL ARLRELMQER KVDVYVVPSE DSHQSEYIAH CDGRREFISG FTGSAGCAIV 

        70         80         90        100        110        120 
SMTKAALSTD GRYFNQAAKQ LDNNWILLKR GFENMPTWQE WTAEQAEGGK VVGVDPSLIT 

       130        140        150        160        170        180 
ASDARNLSET IKKCGGSLLG VQENLVDLVW GAERPARPSE KVALHPIEFA GKSFEEKISD 

       190        200        210        220        230        240 
LRKELQKKKC AGFVISMLDE IAWLFNLRGN DIPYNPVFFA YAIITQSTAD LYIDEEKLPA 

       250        260        270        280        290        300 
EVKNYLGDKV SLKPYSSIFE DAKVLGQSAQ NKSDGETSTK PPQKFLISTR ASWSLSLALG 

       310        320        330        340        350        360 
GEKNVEEVRS PITDAKAIKN EAELEGMRAC HIRDGAALSE YFAWLENELV NKKTVLNEVD 

       370        380        390        400        410        420 
ASDKLEQIRS KHQHFVGLSF DTISSTGPNA AVIHYKAERN NCSIIDPKAV YLCDSGAQYL 

       430        440        450        460        470        480 
DGTTDTTRTL HFGEPTEMEK KAYTLVLKGL ISIDTAVFPK GTTGFALDAF ARQYLWKEGL 

       490        500        510        520        530        540 
DYLHGTGHGV GSYLNVHEGP IGLGTRVQYS EVAIAPGNVI SDEPGYYEDG VFGIRIESPF 

       550        560        570        580        590        600 
FPHLLINLPF LLTPIIDIIM AKEVKTTHKF GEKPWLGFEH VTMTPLCQKL INPSLLSDVE 

       610        620        630 
KKWVNDYHTE IWEKTSKYFE NDELTRNWLK RETQPI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GG692439 Genomic DNA. Translation: EER36658.1.

3D structure databases

ProteinModelPortalC6HSY3.
ModBaseSearch...

Protein family/group databases

MEROPSM24.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.230.10. 2 hits.
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_AJECH
AccessionPrimary (citable) accession number: C6HSY3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: September 1, 2009
Last modified: March 6, 2013
This is version 21 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