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Protein

Carboxypeptidase Y homolog A

Gene

cpyA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

Release of a C-terminal amino acid with broad specificity.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei275 – 2751PROSITE-ProRule annotation
Active sitei467 – 4671PROSITE-ProRule annotation
Active sitei529 – 5291PROSITE-ProRule annotation

GO - Molecular functioni

  • carboxypeptidase activity Source: ASPGD
  • serine-type carboxypeptidase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Protein family/group databases

ESTHERiemeni-CBPYA. Carboxypeptidase_S10.
MEROPSiS10.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Y homolog A (EC:3.4.16.5)
Gene namesi
Name:cpyA
ORF Names:AN5442.2
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome V

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: ASPGD
  • fungal-type vacuole lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Disruption phenotypei

Decreases strongly intracellular carboxypeptidase activity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 133116By similarityPRO_0000407449Add
BLAST
Chaini134 – 552419Carboxypeptidase Y homolog APRO_0000407450Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi188 ↔ 428By similarity
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi322 ↔ 336By similarity
Disulfide bondi346 ↔ 369By similarity
Disulfide bondi353 ↔ 362By similarity
Disulfide bondi391 ↔ 398By similarity
Glycosylationi518 – 5181N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00003647.

Structurei

3D structure databases

ProteinModelPortaliQ96VC4.
SMRiQ96VC4. Positions 133-549.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2939.
HOGENOMiHOG000198296.
InParanoidiQ96VC4.
KOiK13289.
OMAiGQKEYAS.
OrthoDBiEOG7XDBR1.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
IPR008442. Propeptide_carboxypepY.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF05388. Carbpep_Y_N. 1 hit.
PF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96VC4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLPATLLV GAATAATPAQ QVLGGLQDFG NAVQDAMHEN LPKINKPLEA
60 70 80 90 100
FQEQLKSLYE AREFWEEVAN AFPQNLDHNP VFSLPKKHTR RPDSHWDHIV
110 120 130 140 150
RGADVQSVWV TGENGEKERE IEGKLEAYDL RIKKTDPSSL GIDPDVKQYT
160 170 180 190 200
GYLDDNENDK HLFYWFFESR NDPKNDPVVL WLNGGPGCSS LTGLFMELGP
210 220 230 240 250
SSIDENIKPV YNPYAWNSNA SVIFLDQPVN VGYSYSGSTV SDTVAAGKDV
260 270 280 290 300
YALLTLFFKQ FPEYAEQDFH IAGESYAGHY IPVFTSEILS HQKRNINLKS
310 320 330 340 350
VLIGNGLTDG LTQYEYYRPM ACGEGGYPAV LDESSCRSMD NALGRCQSMI
360 370 380 390 400
ESCYNSESAW VCVPASIYCN NALLAPYQRT GQNVYDVRGK CEDESNLCYK
410 420 430 440 450
GMGYVSEYLN KPEVRAAVGA EVDGYDSCNF DINRNFLFHG DWMKPYHRLV
460 470 480 490 500
PGILEQIPVL IYAGDADFIC NWLGNKAWTE ALEWPGHKEF AAAPMEDLKI
510 520 530 540 550
VDNEHTGKKI GQIKTHGNFT FMRLYGGGHM VPMDQPEASL EFFNRWLGGE

WF
Length:552
Mass (Da):62,066
Last modified:December 1, 2001 - v1
Checksum:iF67CF39FDBF7D761
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051820 Genomic DNA. Translation: BAB56108.1.
AACD01000094 Genomic DNA. Translation: EAA62602.1.
BN001305 Genomic DNA. Translation: CBF81902.1.
PIRiJC7666.
RefSeqiXP_663046.1. XM_657954.1.

Genome annotation databases

EnsemblFungiiCADANIAT00003647; CADANIAP00003647; CADANIAG00003647.
GeneIDi2871736.
KEGGiani:AN5442.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051820 Genomic DNA. Translation: BAB56108.1.
AACD01000094 Genomic DNA. Translation: EAA62602.1.
BN001305 Genomic DNA. Translation: CBF81902.1.
PIRiJC7666.
RefSeqiXP_663046.1. XM_657954.1.

3D structure databases

ProteinModelPortaliQ96VC4.
SMRiQ96VC4. Positions 133-549.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00003647.

Protein family/group databases

ESTHERiemeni-CBPYA. Carboxypeptidase_S10.
MEROPSiS10.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00003647; CADANIAP00003647; CADANIAG00003647.
GeneIDi2871736.
KEGGiani:AN5442.2.

Phylogenomic databases

eggNOGiCOG2939.
HOGENOMiHOG000198296.
InParanoidiQ96VC4.
KOiK13289.
OMAiGQKEYAS.
OrthoDBiEOG7XDBR1.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
IPR008442. Propeptide_carboxypepY.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF05388. Carbpep_Y_N. 1 hit.
PF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.

Entry informationi

Entry nameiCBPYA_EMENI
AccessioniPrimary (citable) accession number: Q96VC4
Secondary accession number(s): C8VGH8, Q5B1Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.