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B2AWD5 (CBPYA_PODAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 31. 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:
Carboxypeptidase Y homolog A

EC=3.4.16.5
Gene names
Name:CPYA
Ordered Locus Names:PODANS_7_6790
OrganismPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) [Complete proteome]
Taxonomic identifier515849 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate By similarity.

Catalytic activity

Release of a C-terminal amino acid with broad specificity.

Subcellular location

Vacuole By similarity.

Sequence similarities

Belongs to the peptidase S10 family.

Ontologies

Keywords
   Cellular componentVacuole
   DomainSignal
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type carboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 137120 By similarity
PRO_0000407472
Chain138 – 554417Carboxypeptidase Y homolog A
PRO_0000407473

Sites

Active site2781 By similarity
Active site4701 By similarity
Active site5291 By similarity

Amino acid modifications

Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation5181N-linked (GlcNAc...) Potential
Disulfide bond191 ↔ 431 By similarity
Disulfide bond325 ↔ 339 By similarity
Disulfide bond349 ↔ 372 By similarity
Disulfide bond356 ↔ 365 By similarity
Disulfide bond394 ↔ 401 By similarity

Sequences

Sequence LengthMass (Da)Tools
B2AWD5 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 7CD452763862547D

FASTA55461,984
        10         20         30         40         50         60 
MRVAASTVLL GVASAASFQQ QTQHVLSSGY ERAQAGMKPL AEQFVDAAGK PIANIEEAFH 

        70         80         90        100        110        120 
GMTAEVKALW DEIKLLVPES AFNHSNWFTK PKPARRRHDW DHVVKGADVQ KLWVQGESGE 

       130        140        150        160        170        180 
DHRQVDGKLA DFNLRVKAVD PSKLGVDKVK QYSGYLDDEA NDKHLFYWFF ESRNDPKNDP 

       190        200        210        220        230        240 
VVLWLNGGPG CSSLTGLFLE LGPSSIDKKL KVVNNEFSWN NNASVIFLDQ PVNVGYSYSG 

       250        260        270        280        290        300 
NSVSNTIAAG KDVYALLSLF FHQFPEYAKQ DFHIAGESYA GHYIPVFASE ILSHKNRNIN 

       310        320        330        340        350        360 
LKSILIGNGL TDGLTQYEHY RPMACGKGGY PAVLDESECR SMDNALPRCQ SLIQNCYDSG 

       370        380        390        400        410        420 
SVWSCVPASI YCNNALIGPY QRTGQNVYDI RGKCEDSSNL CYSALGWISD YLNQQDVMDA 

       430        440        450        460        470        480 
LGVEVSGYES CNFDINRNFL FQGDWMQPFH RLVPNILKEI PVLIYAGDAD YICNWLGNQA 

       490        500        510        520        530        540 
WTEALEWPGK KNFNKASIKD LKLAGAEKEY GKVKASGNFT FMQVYQAGHM VPMDQPENSL 

       550 
DFLNRWLGGE WFAK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU633900 Genomic DNA. Translation: CAP68709.1.
RefSeqXP_001908036.1. XM_001908001.1.

3D structure databases

ProteinModelPortalB2AWD5.
SMRB2AWD5. Positions 137-549.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6192366.
KEGGpan:PODANSg5071.

Phylogenomic databases

KOK13289.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBPYA_PODAN
AccessionPrimary (citable) accession number: B2AWD5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries