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A6RUD7

- CBPYA_BOTFB

UniProt

A6RUD7 - CBPYA_BOTFB

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Protein

Carboxypeptidase Y homolog A

Gene

CPYA

Organism
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
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 sitei273 – 2731By similarity
Active sitei465 – 4651By similarity
Active sitei523 – 5231By similarity

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
ORF Names:BC1G_03711
OrganismiBotryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Taxonomic identifieri332648 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotrytis

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 – 132115By similarityPRO_0000407441Add
BLAST
Chaini133 – 546414Carboxypeptidase Y homolog APRO_0000407442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi186 ↔ 426By similarity
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi320 ↔ 334By similarity
Disulfide bondi344 ↔ 367By similarity
Disulfide bondi351 ↔ 360By similarity
Disulfide bondi389 ↔ 396By similarity
Glycosylationi512 – 5121N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Interactioni

Protein-protein interaction databases

STRINGi332648.A6RUD7.

Structurei

3D structure databases

ProteinModelPortaliA6RUD7.
SMRiA6RUD7. Positions 135-542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2939.
KOiK13289.
OMAiWPGQKEY.

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.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A6RUD7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLASTVLV GAAAASITPQ QQVLQNPFKS ATKPVSDAWS KSMESLGHLT
60 70 80 90 100
GSMKGMTAEA KAIWDEVSML FPEAMEKAAF FSEPKPHTRK PDSTWDYIVK
110 120 130 140 150
GADIQSVWVE NSKGEKEREI DGKLEQYNLR AKKVDPSKLG VDTVKQYSGY
160 170 180 190 200
LDDEEDDKHL FYWFFESRND PKNDPVVLWL NGGPGCSSLT GLFLELGPSS
210 220 230 240 250
IDKNLKLHNN PYSWNANASV IFLDQPVNVG YSYSGSSVSN TVAAGKDVYA
260 270 280 290 300
LLTLFFKQFP EYAKQDFHIA GESYAGHYIP VFTSEILSHK KRNINLKSVL
310 320 330 340 350
IGNGLTDGLT QYEHYRPMAC GDGGWPAVLG ASECQAMDNA LPRCQSLIQN
360 370 380 390 400
CYDSESVWSC VPASIYCNNA MMGPYQRTGQ NVYDVRGKCE DTSNLCYSAL
410 420 430 440 450
GWISEFLNKA DVQKELGVEV SSYDSCNFDI NRNFLFQGDW MKPFHRLVPG
460 470 480 490 500
ILEQIPVLIY AGDADFICNW LGNQAWTDAL EWPGKKDFNA AKTKDLQLES
510 520 530 540
GHKTGTFKSS GNFTFARIFG AGHMVPMDQP EASLDFLNKW LNDYTL
Length:546
Mass (Da):60,852
Last modified:August 21, 2007 - v1
Checksum:i57286623880833A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476857 Genomic DNA. Translation: EDN21690.1.
RefSeqiXP_001557447.1. XM_001557397.1.

Genome annotation databases

GeneIDi5438040.
KEGGibfu:BC1G_03711.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476857 Genomic DNA. Translation: EDN21690.1 .
RefSeqi XP_001557447.1. XM_001557397.1.

3D structure databases

ProteinModelPortali A6RUD7.
SMRi A6RUD7. Positions 135-542.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 332648.A6RUD7.

Protein family/group databases

MEROPSi S10.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5438040.
KEGGi bfu:BC1G_03711.

Phylogenomic databases

eggNOGi COG2939.
KOi K13289.
OMAi WPGQKEY.

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 PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
    Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
    , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
    PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B05.10.

Entry informationi

Entry nameiCBPYA_BOTFB
AccessioniPrimary (citable) accession number: A6RUD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: August 21, 2007
Last modified: October 29, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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