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Q96VC4 (CBPYA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. 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:AN5442.2
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length552 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 Ref.1.

Disruption phenotype

Decreases strongly intracellular carboxypeptidase activity. Ref.1

Sequence similarities

Belongs to the peptidase S10 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 133116 By similarity
PRO_0000407449
Chain134 – 552419Carboxypeptidase Y homolog A
PRO_0000407450

Sites

Active site2751 By similarity
Active site4671 By similarity
Active site5291 By similarity

Amino acid modifications

Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation5181N-linked (GlcNAc...) Potential
Disulfide bond188 ↔ 428 By similarity
Disulfide bond322 ↔ 336 By similarity
Disulfide bond346 ↔ 369 By similarity
Disulfide bond353 ↔ 362 By similarity
Disulfide bond391 ↔ 398 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q96VC4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F67CF39FDBF7D761

FASTA55262,066
        10         20         30         40         50         60 
MRVLPATLLV GAATAATPAQ QVLGGLQDFG NAVQDAMHEN LPKINKPLEA FQEQLKSLYE 

        70         80         90        100        110        120 
AREFWEEVAN AFPQNLDHNP VFSLPKKHTR RPDSHWDHIV RGADVQSVWV TGENGEKERE 

       130        140        150        160        170        180 
IEGKLEAYDL RIKKTDPSSL GIDPDVKQYT GYLDDNENDK HLFYWFFESR NDPKNDPVVL 

       190        200        210        220        230        240 
WLNGGPGCSS LTGLFMELGP SSIDENIKPV YNPYAWNSNA SVIFLDQPVN VGYSYSGSTV 

       250        260        270        280        290        300 
SDTVAAGKDV YALLTLFFKQ FPEYAEQDFH IAGESYAGHY IPVFTSEILS HQKRNINLKS 

       310        320        330        340        350        360 
VLIGNGLTDG LTQYEYYRPM ACGEGGYPAV LDESSCRSMD NALGRCQSMI ESCYNSESAW 

       370        380        390        400        410        420 
VCVPASIYCN NALLAPYQRT GQNVYDVRGK CEDESNLCYK GMGYVSEYLN KPEVRAAVGA 

       430        440        450        460        470        480 
EVDGYDSCNF DINRNFLFHG DWMKPYHRLV PGILEQIPVL IYAGDADFIC NWLGNKAWTE 

       490        500        510        520        530        540 
ALEWPGHKEF AAAPMEDLKI VDNEHTGKKI GQIKTHGNFT FMRLYGGGHM VPMDQPEASL 

       550 
EFFNRWLGGE WF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the cpyA gene encoding intracellular carboxypeptidase from Aspergillus nidulans."
Ohsumi K., Matsuda Y., Nakajima H., Kitamoto K.
Biosci. Biotechnol. Biochem. 65:1175-1180(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
Strain: A26.
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB051820 Genomic DNA. Translation: BAB56108.1.
AACD01000094 Genomic DNA. Translation: EAA62602.1.
BN001305 Genomic DNA. Translation: CBF81902.1.
PIRJC7666.
RefSeqXP_663046.1. XM_657954.1.

3D structure databases

ProteinModelPortalQ96VC4.
SMRQ96VC4. Positions 133-549.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00003647; CADANIAP00003647; CADANIAG00003647.
GeneID2871736.
KEGGani:AN5442.2.

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_EMENI
AccessionPrimary (citable) accession number: Q96VC4
Secondary accession number(s): C8VGH8, Q5B1Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 74 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