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A6RGA0 (CBPYA_AJECN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 36. 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:HCAG_08666
OrganismAjellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum) [Complete proteome]
Taxonomic identifier339724 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces

Protein attributes

Sequence length545 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 – 1818 Potential
Propeptide19 – 125107 By similarity
PRO_0000407418
Chain126 – 545420Carboxypeptidase Y homolog A
PRO_0000407419

Sites

Active site2661 By similarity
Active site4571 By similarity
Active site5181 By similarity

Amino acid modifications

Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation4871N-linked (GlcNAc...) Potential
Glycosylation5071N-linked (GlcNAc...) Potential
Disulfide bond179 ↔ 418 By similarity
Disulfide bond313 ↔ 327 By similarity
Disulfide bond337 ↔ 360 By similarity
Disulfide bond344 ↔ 353 By similarity
Disulfide bond382 ↔ 388 By similarity

Sequences

Sequence LengthMass (Da)Tools
A6RGA0 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 4E49F04D1C55BB8D

FASTA54560,747
        10         20         30         40         50         60 
MKSSLALALL VGGAIASGPQ QQVLREPVDH PQAAETPLQK ISDIFGHLSE QAGNVWEDVM 

        70         80         90        100        110        120 
DKFPDTLMDA ITQTPPPKKH NRRPDSEWDH IVRGSDVQAV WVEGDAGEKH RKVGGRLDTY 

       130        140        150        160        170        180 
DLRVKAVDPS NLGVDTVKQY SGYLDDNEND KHLFYWFFES RNDPKNDPVV LWLNGGPGCS 

       190        200        210        220        230        240 
SLTGLFLELG PSSITKQLKV EYNEFSWNSN ASVIFLDQPV NVGYSYSSSS VSNTQAAAKD 

       250        260        270        280        290        300 
VYALLTLFFE QFPEYSRQDF HIAGESYAGH YIPVFASEIM SHSHRNINLK SILVGNGLTD 

       310        320        330        340        350        360 
PLSQYPHYRP MACGEGGYPA VLSSSSCQAM DNALPRCLAM IQACYNTESR WSCVPASIYC 

       370        380        390        400        410        420 
NNALIGPYQR SGMNPYDVRS KCEGGSLCYT QLDDISKYLN RNAVMESLGA EVSSYESCNM 

       430        440        450        460        470        480 
DINRNFLFQG DWMQPYMRVV PTLLAQMPVL IYAGDADFIC NWLGNKAWTE ALEYPGHNEF 

       490        500        510        520        530        540 
AAAEMKNLTS QNHEDVRVIG QVKSAGNFTF MRLFGGGHMV PMDQPEASLE FFNRWLGGEW 


SDKSP 

« Hide

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: NAm1 / WU24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476666 Genomic DNA. Translation: EDN05012.1.
RefSeqXP_001536345.1. XM_001536295.1.

3D structure databases

ProteinModelPortalA6RGA0.
SMRA6RGA0. Positions 125-541.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5442623.
KEGGaje:HCAG_08666.

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_AJECN
AccessionPrimary (citable) accession number: A6RGA0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: August 21, 2007
Last modified: June 11, 2014
This is version 36 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