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A5AB21

- CBPYA_ASPNC

UniProt

A5AB21 - CBPYA_ASPNC

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Protein

Carboxypeptidase Y homolog A

Gene

cpyA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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 sitei280 – 2801PROSITE-ProRule annotation
Active sitei472 – 4721PROSITE-ProRule annotation
Active sitei534 – 5341PROSITE-ProRule annotation

GO - Molecular functioni

  1. serine-type carboxypeptidase activity Source: InterPro
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
Synonyms:cpy
ORF Names:An08g08750
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 8R

Subcellular locationi

Vacuole By similarity

GO - Cellular componenti

  1. vacuole Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 138121By similarityPRO_0000407436Add
BLAST
Chaini139 – 557419Carboxypeptidase Y homolog APRO_5000242373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi193 ↔ 433By similarity
Glycosylationi224 – 2241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi327 ↔ 341By similarity
Disulfide bondi351 ↔ 374By similarity
Disulfide bondi358 ↔ 367By similarity
Disulfide bondi396 ↔ 403By similarity
Glycosylationi523 – 5231N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00007065.

Structurei

3D structure databases

ProteinModelPortaliA5AB21.
SMRiA5AB21. Positions 138-554.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2939.
HOGENOMiHOG000198296.
KOiK13289.
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.

A5AB21-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRVLPAAMLV GAATAAVPPF QQVLGGNGAK HGADHAAEVP ADHSADGFSK
60 70 80 90 100
PLHAFQEELK SLSDEARKLW DEVASFFPES MDQNPLFSLP KKHNRRPDSH
110 120 130 140 150
WDHIVRGSDV QSVWVTGENG EKEREVDGKL EAYDLRVKKT DPGSLGIDPG
160 170 180 190 200
VKQYTGYLDD NENDKHLFYW FFESRNDPEN DPVVLWLNGG PGCSSLTGLF
210 220 230 240 250
MELGPSSINK KIQPVYNDYA WNSNASVIFL DQPVNVGYSY SNSAVSDTVA
260 270 280 290 300
AGKDVYALLT LFFKQFPEYA KQDFHIAGES YAGHYIPVFA SEILSHKKRN
310 320 330 340 350
INLQSVLIGN GLTDGYTQYE YYRPMACGDG GYPAVLDESS CQSMDNALPR
360 370 380 390 400
CQSMIESCYS SESAWVCVPA SIYCNNALLA PYQRTGQNVY DVRGKCEDSS
410 420 430 440 450
NLCYSAMGYV SDYLNKPEVI EAVGAEVNGY DSCNFDINRN FLFHGDWMKP
460 470 480 490 500
YHRLVPGLLE QIPVLIYAGD ADFICNWLGN KAWTEALEWP GQAEYASAEL
510 520 530 540 550
EDLVIVDNEH TGKKIGQVKS HGNFTFMRLY GGGHMVPMDQ PESSLEFFNR

WLGGEWF
Length:557
Mass (Da):62,093
Last modified:June 12, 2007 - v1
Checksum:i742FF0AE20371CEE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270178 Genomic DNA. Translation: CAK96655.1.
RefSeqiXP_001392987.1. XM_001392950.2.

Genome annotation databases

EnsemblFungiiCADANGAT00007198; CADANGAP00007065; CADANGAG00007198.
GeneIDi4983193.
KEGGiang:ANI_1_1208074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270178 Genomic DNA. Translation: CAK96655.1 .
RefSeqi XP_001392987.1. XM_001392950.2.

3D structure databases

ProteinModelPortali A5AB21.
SMRi A5AB21. Positions 138-554.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00007065.

Protein family/group databases

MEROPSi S10.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00007198 ; CADANGAP00007065 ; CADANGAG00007198 .
GeneIDi 4983193.
KEGGi ang:ANI_1_1208074.

Phylogenomic databases

eggNOGi COG2939.
HOGENOMi HOG000198296.
KOi K13289.
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

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiCBPYA_ASPNC
AccessioniPrimary (citable) accession number: A5AB21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 12, 2007
Last modified: October 29, 2014
This is version 42 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