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A1CUJ5 (CBPYA_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 39. 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:ACLA_086840
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length543 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 – 124107 By similarity
PRO_0000407430
Chain125 – 543419Carboxypeptidase Y homolog A
PRO_0000407431

Sites

Active site2661 By similarity
Active site4581 By similarity
Active site5201 By similarity

Amino acid modifications

Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation5091N-linked (GlcNAc...) Potential
Disulfide bond179 ↔ 419 By similarity
Disulfide bond313 ↔ 327 By similarity
Disulfide bond337 ↔ 360 By similarity
Disulfide bond344 ↔ 353 By similarity
Disulfide bond382 ↔ 389 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1CUJ5 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: B3D2EB24E0FB5442

FASTA54360,925
        10         20         30         40         50         60 
MRVLPATLLV GAATAAVPPF QQILGLPKKG ADTLSKPLHD FQEQLKTLSD DARRLWDEVA 

        70         80         90        100        110        120 
KHFPDSMDHN PVFSLPKKHT RRPDSHWDHI VRGADVQSVW VTGANGEKER EVDGKLEAYD 

       130        140        150        160        170        180 
LRVKTTDPGA LGIDPGVKQY TGYLDDNEND KHLFYWFFES RNDPKNDPVV LWLNGGPGCS 

       190        200        210        220        230        240 
SLTGLFLELG PSSIDSKIKP VYNDFAWNSN ASVIFLDQPV NVGYSYSGSA VSDTVAAGKD 

       250        260        270        280        290        300 
VYALLTLFFK QFPEYAKQDF HIAGESYAGH YIPVFASEIL SHKKRNINLK SVLIGNGLTD 

       310        320        330        340        350        360 
PLTQYDHYRP MACGDGGYPA VLDEASCQSM DNALPRCKSM IESCYNTESS WVCVPASIYC 

       370        380        390        400        410        420 
NNALIGPYQR TGQNVYDVRG KCEDESNLCY KGMGYVSEYL NKREVREAVG AEVDGYDSCN 

       430        440        450        460        470        480 
FDINRNFLFH GDWMKPYHRL VPGLLEQIPV LIYAGDADFI CNWLGNKAWS EALEWPGQKE 

       490        500        510        520        530        540 
YASAELEDLV IEQNEHQGKK IGQIKSHGNF TFMRLYGGGH MVPMDQPEAS LEFFNRWIGG 


EWF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027060 Genomic DNA. Translation: EAW06982.1.
RefSeqXP_001268408.1. XM_001268407.1.

3D structure databases

ProteinModelPortalA1CUJ5.
SMRA1CUJ5. Positions 124-540.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00007909.

Protein family/group databases

MEROPSS10.001.

Proteomic databases

PRIDEA1CUJ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00008100; CADACLAP00007909; CADACLAG00008100.
GeneID4700272.
KEGGact:ACLA_086840.

Phylogenomic databases

eggNOGCOG2939.
HOGENOMHOG000198296.
KOK13289.
OMAWPGQKEY.
OrthoDBEOG7XDBR1.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR001563. 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.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBPYA_ASPCL
AccessionPrimary (citable) accession number: A1CUJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 39 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