Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5VJG9 (CBPYA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. 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
Alternative name(s):
Carboxypeptidase 3
Gene names
Name:cpyA
ORF Names:AFUA_6G13540
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [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
Reference 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_0000407434
Chain125 – 543419Carboxypeptidase Y homolog A
PRO_0000407435

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
Q5VJG9 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 0B5B0D6D9A2DC16E

FASTA54360,917
        10         20         30         40         50         60 
MRVLPATLLV GAATAAAPPF QQILGLPKKS ADTLAKPLHD LQEQLKTLSG EARHLWDEVA 

        70         80         90        100        110        120 
SHFPNNMDHN PVFSLPKKHT RRPDSHWDHI VRGADVQSVW VAGASGEKER EIDGKLEAYD 

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

       190        200        210        220        230        240 
SLTGLFLELG PSSINEKIKP IYNDFAWNSN ASVIFLDQPV NVGYSYSGAA VSDTVAAGKD 

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

       310        320        330        340        350        360 
GLTQYDYYRP MACGEGGYPA VLDESSCQSM DNALPRCKSM IESCYNTESS WICVPASIYC 

       370        380        390        400        410        420 
NNALLGPYQR TGQNVYDIRG KCEDSSNLCY KGMGYVSEYL NKREVREAVG AEVDGYESCN 

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

       490        500        510        520        530        540 
YAPLPLKDLV IEENEHKGKK IGQIKSHGNF TFMRLYGAGH MVPMDQPEAS LEFFNRWLGG 


EWF 

« Hide

References

« Hide 'large scale' references
[1]"Genes encoding carboxypeptidases in Aspergillus fumigatus."
Jousson O., Monod M.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY436353 Genomic DNA. Translation: AAR96055.1.
AAHF01000006 Genomic DNA. Translation: EAL89192.1.
RefSeqXP_751230.1. XM_746137.1.

3D structure databases

ProteinModelPortalQ5VJG9.
SMRQ5VJG9. Positions 124-540.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00001729; CADAFUAP00001729; CADAFUAG00001729.
GeneID3508544.
KEGGafm:AFUA_6G13540.

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_ASPFU
AccessionPrimary (citable) accession number: Q5VJG9
Secondary accession number(s): E9RBK4, Q4WLH2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: December 7, 2004
Last modified: June 11, 2014
This is version 66 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