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D1ZKF3 (AMPP1_SORMK) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 25. 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:SMAC_08089
OrganismSordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell) [Complete proteome]
Taxonomic identifier771870 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeSordaria

Protein attributes

Sequence length614 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 – 614614Probable Xaa-Pro aminopeptidase P
PRO_0000411810

Sites

Metal binding4111Manganese 2 By similarity
Metal binding4221Manganese 1 By similarity
Metal binding4221Manganese 2 By similarity
Metal binding5201Manganese 1 By similarity
Metal binding5341Manganese 1 By similarity
Metal binding5341Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
D1ZKF3 [UniParc].

Last modified February 9, 2010. Version 1.
Checksum: 719F8EB7E20C2AF8

FASTA61467,883
        10         20         30         40         50         60 
MTVNTTDRLA ALRSLMKERS VDIYVVPSED SHASEYITDC DARRTFISGF SGSAGTAVVT 

        70         80         90        100        110        120 
LDKAALATDG RYFNQASKQL DENWHLLKTG LQDVPTWQEW TADESAGGKT VGIDPTLISP 

       130        140        150        160        170        180 
AVAEKLNGDI KKHGGSGLKA VTENLVDLVW GESRPPRPSE PVFLLGAKYA GKGAAEKLTD 

       190        200        210        220        230        240 
LRKELEKKKA AAFVVSMLDE IAWLFNLRGN DITYNPVFFS YAIVTKDSAT LYVDESKLTD 

       250        260        270        280        290        300 
EVKQYLAENG TEIKPYTDLF KDTEVLANAA KSTSESEKPT KYLVSNKASW ALKLALGGEK 

       310        320        330        340        350        360 
HVDEVRSPIG DAKAIKNETE LEGMRKCHIR DGAALIKYFA WLEDQLVNKK AKLNEVEAAD 

       370        380        390        400        410        420 
QLEKFRSEQS DFVGLSFDTI SSTGPNGAII HYKPERGACS VIDPNAIYLC DSGAQFYDGT 

       430        440        450        460        470        480 
TDVTRTLHFG QPTAAEKKSY TLVLKGNIAL DTAVFPKGTS GFALDALARQ FLWKYGLDYR 

       490        500        510        520        530        540 
HGTGHGVGSF LNVHEGPIGI GTRKAYIDVP LAPGNVLSIE PGYYEDGNYG IRIENLAIVR 

       550        560        570        580        590        600 
EVKTEHQFGD KPYLGFEHIT MVPYCRKLID ESLLTQEEKD WLNKSNEEIR KNMAGYFDGD 

       610 
QLTTDWLLRE TSPF 

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References

[1]"De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: Sordaria macrospora, a model organism for fungal morphogenesis."
Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K., Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S., Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.
PLoS Genet. 6:E1000891-E1000891(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-333 / DSM 997 / K(L3346) / K-hell.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CABT02000052 Genomic DNA. Translation: CCC13968.1.
RefSeqXP_003347197.1. XM_003347149.1.

3D structure databases

ProteinModelPortalD1ZKF3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10804617.
KEGGsmp:SMAC_08089.

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_SORMK
AccessionPrimary (citable) accession number: D1ZKF3
Secondary accession number(s): F7W9H7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: February 9, 2010
Last modified: March 6, 2013
This is version 25 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