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Q5J6J0 (CBPYA_TRIRU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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:ScpC
OrganismTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Taxonomic identifier5551 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Protein attributes

Sequence length536 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
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 – 124107 By similarity
PRO_0000407484
Chain125 – 536412Carboxypeptidase Y homolog A
PRO_0000407485

Sites

Active site2591 By similarity
Active site4511 By similarity
Active site5131 By similarity

Amino acid modifications

Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential
Disulfide bond172 ↔ 412 By similarity
Disulfide bond306 ↔ 320 By similarity
Disulfide bond330 ↔ 353 By similarity
Disulfide bond337 ↔ 346 By similarity
Disulfide bond375 ↔ 382 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5J6J0 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 0AFB2B9200435C27

FASTA53660,099
        10         20         30         40         50         60 
MKFFTTGLLA TAALAAAQEQ QVLQAEDGMG RAPLPDSSIF DETLQKFQSS LEDGISHFWS 

        70         80         90        100        110        120 
EMKTNFKDYL PLISLPKKHT RRPDSEWDHV VRGADIESVW VQGADGEKRR EIDGKLHNYD 

       130        140        150        160        170        180 
LRVKAVDPGV KQYSGYLDDN DADKHLFYWF FESRNDPKND PVVLWLNGGP GCSSLTGLFL 

       190        200        210        220        230        240 
ELGPATIDKN LKVVSNPYSW NSNASVIFLD QPVNVGFSYS GSSVSDTVAA GKDVYALLTL 

       250        260        270        280        290        300 
FFKQFPEYAT QDFHISGESY AGHYIPVFAA EILSHKNTNI NLKSALIGNG LTDPLTQYPQ 

       310        320        330        340        350        360 
YRPMACGEGG YPAVLDQGTC RSMDNSLERC LSLIETCYSS ESAWVCVPAA MYCNSAILAP 

       370        380        390        400        410        420 
YQQTGMNPYD VRTKCEDMAS LCYPQLNAIT EWLNQKPVMQ ALGVEVESYE SCNSGINRDF 

       430        440        450        460        470        480 
LFHGDWMKPY HRLVPSVLEK IPVLIYAGDA DFICNWLGNK AWTEALEWPG HKKFAETKLE 

       490        500        510        520        530 
DLKIVDNKNK GKKIGQVKSS GNFTFMRIFG AGHMVPLNQP EASLEFLNRW LRGEWH 

« Hide

References

[1]"Trichophyton rubrum secreted and membrane-associated carboxypeptidases."
Zaugg C., Jousson O., Lechenne B., Staib P., Monod M.
Int. J. Med. Microbiol. 298:669-682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY497024 Genomic DNA. Translation: AAS76668.1.

3D structure databases

ProteinModelPortalQ5J6J0.
SMRQ5J6J0. Positions 120-533.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBPYA_TRIRU
AccessionPrimary (citable) accession number: Q5J6J0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 15, 2005
Last modified: February 19, 2014
This is version 33 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