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Q5J6J0

- CBPYA_TRIRU

UniProt

Q5J6J0 - CBPYA_TRIRU

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Protein

Carboxypeptidase Y homolog A

Gene

cpyA

Organism
Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
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 sitei259 – 2591PROSITE-ProRule annotation
Active sitei451 – 4511PROSITE-ProRule annotation
Active sitei513 – 5131PROSITE-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:ScpC
OrganismiTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Taxonomic identifieri5551 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeTrichophyton

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 – 124107By similarityPRO_0000407484Add
BLAST
Chaini125 – 536412Carboxypeptidase Y homolog APRO_0000407485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi172 ↔ 412By similarity
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi306 ↔ 320By similarity
Disulfide bondi330 ↔ 353By similarity
Disulfide bondi337 ↔ 346By similarity
Disulfide bondi375 ↔ 382By similarity
Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ5J6J0.
SMRiQ5J6J0. Positions 120-533.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. 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.

Q5J6J0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKFFTTGLLA TAALAAAQEQ QVLQAEDGMG RAPLPDSSIF DETLQKFQSS
60 70 80 90 100
LEDGISHFWS EMKTNFKDYL PLISLPKKHT RRPDSEWDHV VRGADIESVW
110 120 130 140 150
VQGADGEKRR EIDGKLHNYD LRVKAVDPGV KQYSGYLDDN DADKHLFYWF
160 170 180 190 200
FESRNDPKND PVVLWLNGGP GCSSLTGLFL ELGPATIDKN LKVVSNPYSW
210 220 230 240 250
NSNASVIFLD QPVNVGFSYS GSSVSDTVAA GKDVYALLTL FFKQFPEYAT
260 270 280 290 300
QDFHISGESY AGHYIPVFAA EILSHKNTNI NLKSALIGNG LTDPLTQYPQ
310 320 330 340 350
YRPMACGEGG YPAVLDQGTC RSMDNSLERC LSLIETCYSS ESAWVCVPAA
360 370 380 390 400
MYCNSAILAP YQQTGMNPYD VRTKCEDMAS LCYPQLNAIT EWLNQKPVMQ
410 420 430 440 450
ALGVEVESYE SCNSGINRDF LFHGDWMKPY HRLVPSVLEK IPVLIYAGDA
460 470 480 490 500
DFICNWLGNK AWTEALEWPG HKKFAETKLE DLKIVDNKNK GKKIGQVKSS
510 520 530
GNFTFMRIFG AGHMVPLNQP EASLEFLNRW LRGEWH
Length:536
Mass (Da):60,099
Last modified:February 15, 2005 - v1
Checksum:i0AFB2B9200435C27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497024 Genomic DNA. Translation: AAS76668.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497024 Genomic DNA. Translation: AAS76668.1 .

3D structure databases

ProteinModelPortali Q5J6J0.
SMRi Q5J6J0. Positions 120-533.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S10.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.1820. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view ]
PANTHERi PTHR11802. PTHR11802. 1 hit.
Pfami 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. "Trichophyton rubrum secreted and membrane-associated carboxypeptidases."
    Zaugg C., Jousson O., Lechenne B., Staib P., Monod M.
    Int. J. Med. Microbiol. 298:669-682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiCBPYA_TRIRU
AccessioniPrimary (citable) accession number: Q5J6J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 15, 2005
Last modified: October 29, 2014
This is version 37 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