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Q2TYA1

- CBPYA_ASPOR

UniProt

Q2TYA1 - CBPYA_ASPOR

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Protein

Carboxypeptidase Y homolog A

Gene

cpyA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - 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 sitei265 – 2651PROSITE-ProRule annotation
Active sitei457 – 4571PROSITE-ProRule annotation
Active sitei519 – 5191PROSITE-ProRule annotation

GO - Molecular functioni

  1. serine-type carboxypeptidase activity Source: ASPGD

GO - Biological processi

  1. proteolysis Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Protein family/group databases

MEROPSiS10.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Y homolog A (EC:3.4.16.5)
Gene namesi
Name:cpyA
ORF Names:AO090103000332
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 8

Subcellular locationi

Vacuole 3 Publications
Note: Requires vps10 for correct vacuolar localization.

GO - Cellular componenti

  1. fungal-type vacuole lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 123106By similarityPRO_0000407437Add
BLAST
Chaini124 – 542419Carboxypeptidase Y homolog APRO_0000407438Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi178 ↔ 418By similarity
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi312 ↔ 326By similarity
Disulfide bondi336 ↔ 359By similarity
Disulfide bondi343 ↔ 352By similarity
Disulfide bondi381 ↔ 388By similarity
Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00010017.

Structurei

3D structure databases

ProteinModelPortaliQ2TYA1.
SMRiQ2TYA1. Positions 123-539.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2939.
HOGENOMiHOG000198296.
KOiK13289.
OMAiWPGQKEY.
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.

Q2TYA1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRVLPATLLV GAASAAVPPL QQVLGRPEEG MSFSKPLHAF QEQLKTLSED
60 70 80 90 100
ARKLWDEVAN YFPDSMDHSP IFSLPKKHTR RPDSHWDHIV RGSDVQKIWV
110 120 130 140 150
NNADGEKERE IDGKLEAYDL RIKKADPSAL GIDPNVKQYT GYLDDNGNDK
160 170 180 190 200
HLFYWFFESR NDPKNDPVVL WLNGGPGCSS LTGLFMELGP SSIDENIKPV
210 220 230 240 250
YNDFSWNSNA SVIFLDQPVN VGYSYSGSAV SDTVAAGKDV YALLSLFFKQ
260 270 280 290 300
FPEYAEQDFH IAGESYAGHY IPVFASEILA HKNRNINLKS VLIGNGLTDG
310 320 330 340 350
LTQYGYYRPM GCGEGGYKAV LDEATCESMD NALPRCRSMI ESCYNSESAW
360 370 380 390 400
VCVPASIYCN NALIGPYQRT GQNVYDVRSK CEDESNLCYK GMGYVSEYLN
410 420 430 440 450
KAEVREAVGA EVGGYDSCNF DINRNFLFHG DWMKPYHRLV PGLLEQIPVL
460 470 480 490 500
IYAGDADYIC NWLGNKAWTE ALEWPGQKEY ASAELEDLKI EQNEHTGKKI
510 520 530 540
GQVKSHGNFT FMRLYGGGHM VPMDQPEASL EFFNRWLGGE WF
Length:542
Mass (Da):60,892
Last modified:January 24, 2006 - v1
Checksum:iBD339D3954E9EB3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007174 Genomic DNA. Translation: BAE65772.1.
RefSeqiXP_001826905.1. XM_001826853.2.

Genome annotation databases

EnsemblFungiiCADAORAT00010224; CADAORAP00010017; CADAORAG00010224.
GeneIDi5999027.
KEGGiaor:AOR_1_542034.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007174 Genomic DNA. Translation: BAE65772.1 .
RefSeqi XP_001826905.1. XM_001826853.2.

3D structure databases

ProteinModelPortali Q2TYA1.
SMRi Q2TYA1. Positions 123-539.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5062.CADAORAP00010017.

Protein family/group databases

MEROPSi S10.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00010224 ; CADAORAP00010017 ; CADAORAG00010224 .
GeneIDi 5999027.
KEGGi aor:AOR_1_542034.

Phylogenomic databases

eggNOGi COG2939.
HOGENOMi HOG000198296.
KOi K13289.
OMAi WPGQKEY.
OrthoDBi EOG7XDBR1.

Family and domain databases

Gene3Di 3.40.50.1820. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
IPR008442. Propeptide_carboxypepY.
[Graphical view ]
PANTHERi PTHR11802. PTHR11802. 1 hit.
Pfami PF05388. Carbpep_Y_N. 1 hit.
PF00450. Peptidase_S10. 1 hit.
[Graphical view ]
PRINTSi PR00724. CRBOXYPTASEC.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.
  2. "Visualization of vacuoles in Aspergillus oryzae by expression of CPY-EGFP."
    Ohneda M., Arioka M., Nakajima H., Kitamoto K.
    Fungal Genet. Biol. 37:29-38(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "Isolation and characterization of Aspergillus oryzae vacuolar protein sorting mutants."
    Ohneda M., Arioka M., Kitamoto K.
    Appl. Environ. Microbiol. 71:4856-4861(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Enhanced production and secretion of heterologous proteins by the filamentous fungus Aspergillus oryzae via disruption of vacuolar protein sorting receptor gene Aovps10."
    Yoon J., Aishan T., Maruyama J., Kitamoto K.
    Appl. Environ. Microbiol. 76:5718-5727(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCBPYA_ASPOR
AccessioniPrimary (citable) accession number: Q2TYA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 24, 2006
Last modified: October 1, 2014
This is version 50 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