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A5YCB8

- CBPYA_TRITO

UniProt

A5YCB8 - CBPYA_TRITO

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Protein

Carboxypeptidase Y homolog A

Gene

CPYA

Organism
Trichophyton tonsurans (Scalp ringworm fungus)
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 sitei266 – 2661PROSITE-ProRule annotation
Active sitei458 – 4581PROSITE-ProRule annotation
Active sitei520 – 5201PROSITE-ProRule annotation

GO - Molecular functioni

  1. serine-type carboxypeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Y homolog A (EC:3.4.16.5)
Gene namesi
Name:CPYA
Synonyms:CarbY
OrganismiTrichophyton tonsurans (Scalp ringworm fungus)
Taxonomic identifieri34387 [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_0000407486Add
BLAST
Chaini125 – 543419Carboxypeptidase Y homolog APRO_0000407487Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi179 ↔ 419By similarity
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi313 ↔ 327By similarity
Disulfide bondi337 ↔ 360By similarity
Disulfide bondi344 ↔ 353By similarity
Disulfide bondi382 ↔ 389By similarity
Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliA5YCB8.
SMRiA5YCB8. Positions 124-540.
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.

A5YCB8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKFLTTGLLA TAALAAAQEQ QVLQAEDGMG QAPQRGSSIF DETLQKFQSS
60 70 80 90 100
LEDGISHFWS EMKTNFKDYL PLISLPKKHT RRPDSEWDHV VRGADIESVW
110 120 130 140 150
VQGADGEKRR EIDGKLHNYD LRVKAVDPSK LGVDAGVKQY SGYLDDNDAD
160 170 180 190 200
KHLFYWFFES RNDPKNDPVV LWLNGGPGCS SLTGLFLELG PATIDKNLKV
210 220 230 240 250
VSNPYSWNSN ASVIFLDQPV NVGFSYSGSS VSDTVAAGKD IYALLTLFFK
260 270 280 290 300
QFPEYATQDF HISGESYAGH YIPVFAAEIL SHKNTNINLK SALIGNGLTD
310 320 330 340 350
PLTQYPQYRP MACGEGGYPA VLDQGTCRSM DNSLERCLSL IETCYSSESA
360 370 380 390 400
WICVPAAMYC NSAILAPYQQ TGMNPYDVRN KCEDMASLCY PQLNVITEWL
410 420 430 440 450
NQKSVMQALG VEVESYESCN SGINRDFLFH GDWMKPYHRL VPSVLEKIPV
460 470 480 490 500
LIYAGDADFI CNWLGNQAWT DALEWPGHKK FAEAKLEDLK IVDNKNKGKK
510 520 530 540
IGQVKSSGNF TFMRIFGAGH MVPLNQPEAS LEFLNRWLRG EWH
Length:543
Mass (Da):60,739
Last modified:July 10, 2007 - v1
Checksum:iEBBDFC83148B999F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF490685 Genomic DNA. Translation: ABQ96589.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF490685 Genomic DNA. Translation: ABQ96589.1 .

3D structure databases

ProteinModelPortali A5YCB8.
SMRi A5YCB8. Positions 124-540.
ModBasei Search...
MobiDBi Search...

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. "Multi-locus genotyping identifies infections with multiple strains of T. tonsurans."
    Abdel-Rahman S.M., Preuett B.L., Gaedigk A.
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiCBPYA_TRITO
AccessioniPrimary (citable) accession number: A5YCB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 10, 2007
Last modified: October 29, 2014
This is version 25 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