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A5AB21 (CBPYA_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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
Synonyms:cpy
ORF Names:An08g08750
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length557 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)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 138121 By similarity
PRO_0000407436
Chain139 – 557419Carboxypeptidase Y homolog A
PRO_5000242373

Sites

Active site2801 By similarity
Active site4721 By similarity
Active site5341 By similarity

Amino acid modifications

Glycosylation2241N-linked (GlcNAc...) Potential
Glycosylation5231N-linked (GlcNAc...) Potential
Disulfide bond193 ↔ 433 By similarity
Disulfide bond327 ↔ 341 By similarity
Disulfide bond351 ↔ 374 By similarity
Disulfide bond358 ↔ 367 By similarity
Disulfide bond396 ↔ 403 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5AB21 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 742FF0AE20371CEE

FASTA55762,093
        10         20         30         40         50         60 
MRVLPAAMLV GAATAAVPPF QQVLGGNGAK HGADHAAEVP ADHSADGFSK PLHAFQEELK 

        70         80         90        100        110        120 
SLSDEARKLW DEVASFFPES MDQNPLFSLP KKHNRRPDSH WDHIVRGSDV QSVWVTGENG 

       130        140        150        160        170        180 
EKEREVDGKL EAYDLRVKKT DPGSLGIDPG VKQYTGYLDD NENDKHLFYW FFESRNDPEN 

       190        200        210        220        230        240 
DPVVLWLNGG PGCSSLTGLF MELGPSSINK KIQPVYNDYA WNSNASVIFL DQPVNVGYSY 

       250        260        270        280        290        300 
SNSAVSDTVA AGKDVYALLT LFFKQFPEYA KQDFHIAGES YAGHYIPVFA SEILSHKKRN 

       310        320        330        340        350        360 
INLQSVLIGN GLTDGYTQYE YYRPMACGDG GYPAVLDESS CQSMDNALPR CQSMIESCYS 

       370        380        390        400        410        420 
SESAWVCVPA SIYCNNALLA PYQRTGQNVY DVRGKCEDSS NLCYSAMGYV SDYLNKPEVI 

       430        440        450        460        470        480 
EAVGAEVNGY DSCNFDINRN FLFHGDWMKP YHRLVPGLLE QIPVLIYAGD ADFICNWLGN 

       490        500        510        520        530        540 
KAWTEALEWP GQAEYASAEL EDLVIVDNEH TGKKIGQVKS HGNFTFMRLY GGGHMVPMDQ 

       550 
PESSLEFFNR WLGGEWF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM270178 Genomic DNA. Translation: CAK96655.1.
RefSeqXP_001392987.1. XM_001392950.2.

3D structure databases

ProteinModelPortalA5AB21.
SMRA5AB21. Positions 138-554.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00007065.

Protein family/group databases

MEROPSS10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANGAT00007198; CADANGAP00007065; CADANGAG00007198.
GeneID4983193.
KEGGang:ANI_1_1208074.

Phylogenomic databases

eggNOGCOG2939.
HOGENOMHOG000198296.
KOK13289.
OrthoDBEOG7XDBR1.

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
IPR008442. Propeptide_carboxypepY.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF05388. Carbpep_Y_N. 1 hit.
PF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBPYA_ASPNC
AccessionPrimary (citable) accession number: A5AB21
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 38 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