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Q0V1R1 (CBPYA_PHANO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

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

Subcellular location

Vacuole By similarity.

Sequence similarities

Belongs to the peptidase S10 family.

Ontologies

Keywords
   Cellular componentVacuole
   DomainSignal
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphytochelatin biosynthetic process

Inferred from electronic annotation. Source: EnsemblFungi

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentfungal-type vacuole

Inferred from electronic annotation. Source: EnsemblFungi

   Molecular_functionserine-type carboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 128111 By similarity
PRO_0000407470
Chain129 – 543415Carboxypeptidase Y homolog A
PRO_0000407471

Sites

Active site2691 By similarity
Active site4601 By similarity
Active site5191 By similarity

Amino acid modifications

Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation5081N-linked (GlcNAc...) Potential
Disulfide bond182 ↔ 421 By similarity
Disulfide bond316 ↔ 330 By similarity
Disulfide bond340 ↔ 363 By similarity
Disulfide bond347 ↔ 356 By similarity
Disulfide bond385 ↔ 391 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0V1R1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 67C6C4D765B7D11B

FASTA54361,071
        10         20         30         40         50         60 
MRVAASALLA GAASAAVAPQ QQILKFPSSF SELKEDLWSK PLHNLEESLK SLTGEAKATW 

        70         80         90        100        110        120 
DEVATMYPES FDKAAFFSTP KPHTRKHDSE WDHIVKGADV QSVWVENAQG EKEREIDGKL 

       130        140        150        160        170        180 
EQFDLRVKKV DPSVLGVDKV KQYSGYLDDN EEDKHLFYWF FESRNDPKND PVVLWLNGGP 

       190        200        210        220        230        240 
GCSSLMGLFM ELGPASVMKD GKLKHNDYSW NANASVIFLD QPVNVGYSYS SGSVSNTVAA 

       250        260        270        280        290        300 
GKDIYALLTL FFKQFPEYSK QPFHISGESY AGHYIPVFAS EILSHKKRNI NLQSVLIGNG 

       310        320        330        340        350        360 
LTDGLTQYEY YRPMACGEGG WPAVLDESSC QAMDNAYPRC ASLIENCYKS ESVWSCVPAS 

       370        380        390        400        410        420 
IYCNNAMIGP YQRTGQNVYD VRRPCGDNQL CYDEIDYISA FLNKKEVMKA VGAEVSSYDS 

       430        440        450        460        470        480 
CNFDINRNFL LQGDWMKPYH RVVPGLLEEI PVLVYAGDAD YICNWLGNKA WTEALEWKGH 

       490        500        510        520        530        540 
EEYKKAEMKD FKIDGDGKKV GEVKSSGNFT FMKIHAGGHM VPFDQPEASL EMVNRWLSGE 


FWE 

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References

[1]"Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum."
Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P.
Plant Cell 19:3347-3368(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH445327 Genomic DNA. Translation: EAT90265.1.
RefSeqXP_001792672.1. XM_001792620.1.

3D structure databases

ProteinModelPortalQ0V1R1.
SMRQ0V1R1. Positions 131-541.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSNOT_02053; SNOT_02053; SNOG_02053.
GeneID5969522.
KEGGpno:SNOG_02053.

Phylogenomic databases

KOK13289.
OMAHYRPMAC.
OrthoDBEOG7XDBR1.

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
IPR008442. Propeptide_carboxypepY.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF05388. Carbpep_Y_N. 1 hit.
PF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBPYA_PHANO
AccessionPrimary (citable) accession number: Q0V1R1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries