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D4D891 (AMPP1_TRIVH) 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 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:TRV_03327
OrganismTrichophyton verrucosum (strain HKI 0517) [Complete proteome]
Taxonomic identifier663202 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Protein attributes

Sequence length698 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 caution

The sequence EFE41910.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 698698Probable Xaa-Pro aminopeptidase P
PRO_0000411812

Sites

Metal binding5091Manganese 2 By similarity
Metal binding5201Manganese 1 By similarity
Metal binding5201Manganese 2 By similarity
Metal binding6041Manganese 1 By similarity
Metal binding6181Manganese 1 By similarity
Metal binding6181Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
D4D891 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: C74FC33E0CBA2CBD

FASTA69877,470
        10         20         30         40         50         60 
MTIFRPHLRF LFKPHFLYFQ SPAGQSSRPF STSQILRTAL DMPPPPVDTT QRLAKLRELM 

        70         80         90        100        110        120 
AQNKVDVYSM QFRYTIKAPL IITVVYSFFF FLLLALKLCL RKTAISQSTL LHVMGVETLI 

       130        140        150        160        170        180 
RITAAFISSF TGSAGCAIVS MSKAALSTDG RYFSQAAKQL DSNWTLLKRG VEGVPTWEEW 

       190        200        210        220        230        240 
TAEQAENGKV VGVDPSLITA GENLHYTPLT SVVVTNCSYV IADARKLSQT LKTTGGSLVG 

       250        260        270        280        290        300 
IDQNLIDAVW GNERPARPAN QITVQPVERA GKPFEEKVED LRKELAAKKR SAMVISTLDE 

       310        320        330        340        350        360 
IAWLFNLRGS DIPYNPVFFS YAIVTPSVAE LYVDESKLSP EARKHLEGKV VLKPYDSIFQ 

       370        380        390        400        410        420 
ASKVLAESKA SASSGSSGKF LLSNKASWSL SLALGGEQNV VEVRSPITDA KAIKNEVELE 

       430        440        450        460        470        480 
GFRKCHIRDG AALIEYFAWL ENALIKEGAQ LDEVDGADKL FEIRKKYDLF VGNSFDTISS 

       490        500        510        520        530        540 
TGANGATIHY KPEKSTCAVI DPKAMYLCDS GGQYLDGTTD TTRTLHFGEP TEFQKKAYAL 

       550        560        570        580        590        600 
VLKGHISIDN AIFPKGTTGY AIDSFARQHL WKEGLDYLHG TGHGVGSFLY AEVPLSASNV 

       610        620        630        640        650        660 
LSNEPGYYED GNFGIRLENL VICKEVQTAH KFGDKPFLGF ESITLVPFCQ KLLDASLLTE 

       670        680        690 
AERKWVNDYH ARVWEKTSPF FEKDELTTAW LKRETQPI 

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References

[1]"Comparative and functional genomics provide insights into the pathogenicity of dermatophytic fungi."
Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S., Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O., Schroeckh V. expand/collapse author list , Hertweck C., Hube B., White T.C., Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.
Genome Biol. 12:R7.1-R7.16(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HKI 0517.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACYE01000172 Genomic DNA. Translation: EFE41910.1. Sequence problems.
RefSeqXP_003022528.1. XM_003022482.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9581105.
KEGGtve:TRV_03327.

Phylogenomic databases

KOK01262.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
InterProIPR000587. Creatinase.
IPR000994. Pept_M24_structural-domain.
[Graphical view]
PfamPF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
PROSITEPS00491. PROLINE_PEPTIDASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPP1_TRIVH
AccessionPrimary (citable) accession number: D4D891
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 27, 2011
Last modified: March 6, 2013
This is version 22 of the entry and version 2 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