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C4JNM2 (CBPYA_UNCRE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 27. 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
ORF Names:UREG_03020
OrganismUncinocarpus reesii (strain UAMH 1704) [Complete proteome]
Taxonomic identifier336963 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesOnygenaceaeUncinocarpus

Protein attributes

Sequence length541 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 – 122105 By similarity
PRO_0000407490
Chain123 – 541419Carboxypeptidase Y homolog A
PRO_0000407491

Sites

Active site2641 By similarity
Active site4551 By similarity
Active site5171 By similarity

Amino acid modifications

Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Glycosylation5061N-linked (GlcNAc...) Potential
Disulfide bond177 ↔ 416 By similarity
Disulfide bond311 ↔ 325 By similarity
Disulfide bond335 ↔ 358 By similarity
Disulfide bond342 ↔ 351 By similarity
Disulfide bond380 ↔ 386 By similarity

Sequences

Sequence LengthMass (Da)Tools
C4JNM2 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 67D2CE6C1BB51FB4

FASTA54160,405
        10         20         30         40         50         60 
MKTFTAALLV GTALAAVPQQ QPLQTQVEDS AWAKPLEDLK DTIKSMGAEA KQAWDQLASA 

        70         80         90        100        110        120 
FPDALNEYTL FSAPKKHTRR PDSHWDHVVR GADVQGIWVD GVDGQKHREV DGKLENYDLR 

       130        140        150        160        170        180 
VKAVDPSKLG IDPGVKQFSG YLDDNENDKH LFYWFFESRN DPKNDPVVLW LNGGPGCSSL 

       190        200        210        220        230        240 
TGLFFELGPA SIDKNLKVIH NPYSWNSNAS VIFLDQPVNV GFSYSGSSVS DTIAAGKDVY 

       250        260        270        280        290        300 
ALLTLFFKQF PQYAKQDFHI AGESYAGHYI PAFASEILSH KNRNINLKSV LIGNGLTDPL 

       310        320        330        340        350        360 
TQYPHYRPMA CGEGGYPAVL DESSCRSMDN ALPRCQSMIE SCYSSESAWV CVPASIYCNN 

       370        380        390        400        410        420 
AMIGPYQRTG QNVYDVRTKC EDGSLCYTGL NYITQWLNQK PVMEALGAEV ESYDSCNMDI 

       430        440        450        460        470        480 
NRNFLFHGDW MKPYHRLVPG LIEKLPVLIY AGDADFICNW LGNKAWTETL EWSGRAEFAS 

       490        500        510        520        530        540 
AEMKNLTIVD NKSKGKNIGQ VKSHGNFTFM RLFGGGHMVP LDQPEASLEF FNRWLGGEWK 


A 

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References

[1]"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives."
Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. expand/collapse author list , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.
Genome Res. 19:1722-1731(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UAMH 1704.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476616 Genomic DNA. Translation: EEP78175.1.
RefSeqXP_002543504.1. XM_002543458.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8439365.
KEGGure:UREG_03020.

Phylogenomic databases

KOK13289.
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_UNCRE
AccessionPrimary (citable) accession number: C4JNM2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 7, 2009
Last modified: June 11, 2014
This is version 27 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