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Protein

Carboxypeptidase Y homolog A

Gene

cpyA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei266 – 2661PROSITE-ProRule annotation
Active sitei458 – 4581PROSITE-ProRule annotation
Active sitei520 – 5201PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Protein family/group databases

ESTHERiaspfu-CBPYA. Carboxypeptidase_S10.
MEROPSiS10.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Y homolog A (EC:3.4.16.5)
Alternative name(s):
Carboxypeptidase 3
Gene namesi
Name:cpyA
ORF Names:AFUA_6G13540
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiFungiDB:Afu6g13540.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 124107By similarityPRO_0000407434Add
BLAST
Chaini125 – 543419Carboxypeptidase Y homolog APRO_0000407435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi179 ↔ 419By similarity
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi313 ↔ 327By similarity
Disulfide bondi337 ↔ 360By similarity
Disulfide bondi344 ↔ 353By similarity
Disulfide bondi382 ↔ 389By similarity
Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ5VJG9.
SMRiQ5VJG9. Positions 124-540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2939.
HOGENOMiHOG000198296.
InParanoidiQ5VJG9.
KOiK13289.
OMAiNTESSWI.
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.

Q5VJG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLPATLLV GAATAAAPPF QQILGLPKKS ADTLAKPLHD LQEQLKTLSG
60 70 80 90 100
EARHLWDEVA SHFPNNMDHN PVFSLPKKHT RRPDSHWDHI VRGADVQSVW
110 120 130 140 150
VAGASGEKER EIDGKLEAYD LRVKKTDPSA LGIDPGVKQY TGYLDDNEND
160 170 180 190 200
KHLFYWFFES RNDPKNDPVV LWLNGGPGCS SLTGLFLELG PSSINEKIKP
210 220 230 240 250
IYNDFAWNSN ASVIFLDQPV NVGYSYSGAA VSDTVAAGKD VYALLTLFFK
260 270 280 290 300
QFPEYAKQDF HIAGESYAGH YIPVFASEIL SHKKRNINLK SVLIGNGLTD
310 320 330 340 350
GLTQYDYYRP MACGEGGYPA VLDESSCQSM DNALPRCKSM IESCYNTESS
360 370 380 390 400
WICVPASIYC NNALLGPYQR TGQNVYDIRG KCEDSSNLCY KGMGYVSEYL
410 420 430 440 450
NKREVREAVG AEVDGYESCN FDINRNFLFH GDWMKPYHRL VPGLLEQIPV
460 470 480 490 500
LIYAGDADFI CNWLGNKAWT EALEWPGQKE YAPLPLKDLV IEENEHKGKK
510 520 530 540
IGQIKSHGNF TFMRLYGAGH MVPMDQPEAS LEFFNRWLGG EWF
Length:543
Mass (Da):60,917
Last modified:December 7, 2004 - v1
Checksum:i0B5B0D6D9A2DC16E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY436353 Genomic DNA. Translation: AAR96055.1.
AAHF01000006 Genomic DNA. Translation: EAL89192.1.
RefSeqiXP_751230.1. XM_746137.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00001729; CADAFUAP00001729; CADAFUAG00001729.
GeneIDi3508544.
KEGGiafm:AFUA_6G13540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY436353 Genomic DNA. Translation: AAR96055.1.
AAHF01000006 Genomic DNA. Translation: EAL89192.1.
RefSeqiXP_751230.1. XM_746137.1.

3D structure databases

ProteinModelPortaliQ5VJG9.
SMRiQ5VJG9. Positions 124-540.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiaspfu-CBPYA. Carboxypeptidase_S10.
MEROPSiS10.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00001729; CADAFUAP00001729; CADAFUAG00001729.
GeneIDi3508544.
KEGGiafm:AFUA_6G13540.

Organism-specific databases

EuPathDBiFungiDB:Afu6g13540.

Phylogenomic databases

eggNOGiCOG2939.
HOGENOMiHOG000198296.
InParanoidiQ5VJG9.
KOiK13289.
OMAiNTESSWI.
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. "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.
    , 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.

Entry informationi

Entry nameiCBPYA_ASPFU
AccessioniPrimary (citable) accession number: Q5VJG9
Secondary accession number(s): E9RBK4, Q4WLH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: December 7, 2004
Last modified: June 24, 2015
This is version 73 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.