Skip Header

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

C5GXZ9 (AMPP1_AJEDR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 20. 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:BDCG_09239
OrganismAjellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis) [Complete proteome]
Taxonomic identifier559297 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces

Protein attributes

Sequence length617 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 – 617617Probable Xaa-Pro aminopeptidase P
PRO_0000411773

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
C5GXZ9 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: FCE8AE5E32AF2D65

FASTA61768,559
        10         20         30         40         50         60 
MGPVDTSQRL ARLRELMQER KVDVYIVPSE DSHQSEYIAP CDGRREFISG FTGSAGCAIV 

        70         80         90        100        110        120 
SMSKAALSTD GRYFNQAAKQ LDNNWMLLKR GFENMPTWQE WTAEQAEGGK VVGVDPSLIT 

       130        140        150        160        170        180 
ASEARSLSET IEKSGGSLQG VQENLIDLVW GKERPARPSE KVALHPIEFA GKSFEEKISD 

       190        200        210        220        230        240 
LRKELQKKKS AGFVISMLDE IAWLFNLRGN DIPYNPVFFA YAIITPTTAD LYIDDEKLPA 

       250        260        270        280        290        300 
EVKKYLGDQV SVKPYGSIFE DAKALSQSAQ KKSDGDASTS PSEKFLISTK ASWSLSLALG 

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

       370        380        390        400        410        420 
GSDKLEQIRS KHKHFVGLSF DTISSTGPNA AVIHYKAERD TCSIIDPKAV YLCDSGAQYL 

       430        440        450        460        470        480 
DGTTDTTRTL HFGEPTEMER KAYTLVLKGL ISIDTAVFPK GTTGFALDAF ARQHLWKEGL 

       490        500        510        520        530        540 
DYLHGTGHGV GSYLNVHEGP IGLGTRVQYA EVAITPGNVI SDEPGFYEDG VFGIRIENII 

       550        560        570        580        590        600 
IAKEVKTTHG FGEKPWLGFE HVTMTPLCQK LINPSLLTDG EKKWVNDYHS KVWEKTSSYF 

       610 
ENDELTRNWL KRETQPI 

« Hide

References

[1]"The genome sequence of Blastomyces dermatitidis strain ER-3."
Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Klein B., Goldman B., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Heiman D.I., Hepburn T.A., Saif S., Shea T.D., Shenoy N., Sykes S. expand/collapse author list , Galagan J.E., Nusbaum C., Birren B.W.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ER-3 / ATCC MYA-2586.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EQ999986 Genomic DNA. Translation: EEQ85970.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM24.009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_AJEDR
AccessionPrimary (citable) accession number: C5GXZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 28, 2009
Last modified: March 6, 2013
This is version 20 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