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Q5BF48 (AMPP2_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 60. 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 AN0832
EC=3.4.11.9
Alternative name(s):
Aminoacylproline aminopeptidase
Prolidase
Gene names
ORF Names:AN0832
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

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 AN0832
PRO_0000411835

Sites

Metal binding2601Manganese 2 By similarity
Metal binding2711Manganese 1 By similarity
Metal binding2711Manganese 2 By similarity
Metal binding3981Manganese 1 By similarity
Metal binding4371Manganese 1 By similarity
Metal binding4371Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5BF48 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 696B501930749EB7

FASTA46953,150
        10         20         30         40         50         60 
MRVSDPAKLD ILPDDACEIR LTIAASECDK YPAKQHARKV ASKLGVRDGL IYLVGKATIN 

        70         80         90        100        110        120 
WGDSDQPRPF RQRRYFYYLS GVDEADCYLT YDIRNDLLTI YVPNFSLQHA IWMGPTLTVE 

       130        140        150        160        170        180 
EARQRYDADR FRYYAALRSD LNSWVDQYNK DSPIYVLHSS QKPEISAKEL RSREVKDEYE 

       190        200        210        220        230        240 
IRMIRKANEI SALAHRNILQ NIHRMSNESE IEGLFLDTCV SHGAKNQSYE IIAGSGPNAA 

       250        260        270        280        290        300 
VLHYVKNDEP LNGRQLVCLD AGAEWNCYAS DVTRTIPLGK DWPSSHAKDI YAIVEEMQEE 

       310        320        330        340        350        360 
CIRRVKPGLR FRDLHELAHI IAIKGLQELG VLKAGTVEEI RRSGASSIFF PHGLGHHVGL 

       370        380        390        400        410        420 
EVHDVSEQPI TANGHLSREF VPQMSTPLLQ EGMVITIEPG VYFNKLALEN SRSLPLAKYI 

       430        440        450        460 
DFDKAEQYIP VGGVRIEDDL LVTSTGYENL TMAPKGKEML EILRGRSKQ

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000013 Genomic DNA. Translation: EAA65662.1.
BN001308 Genomic DNA. Translation: CBF88697.1.
RefSeqXP_658436.1. XM_653344.1.

3D structure databases

ProteinModelPortalQ5BF48.
ModBaseSearch...

Protein family/group databases

MEROPSM24.A09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00001828; CADANIAP00001828; CADANIAG00001828.
GeneID2876610.
KEGGani:AN0832.2.

Phylogenomic databases

eggNOGCOG0006.
HOGENOMHOG000008763.
KOK14213.
OMAGHHVGLE.
OrthoDBEOG4897VR.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
InterProIPR007865. Aminopep_P_N.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPP2_EMENI
AccessionPrimary (citable) accession number: Q5BF48
Secondary accession number(s): C8VQE3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: April 26, 2005
Last modified: March 6, 2013
This is version 60 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents