Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

D4DD24 (SCPA_TRIVH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 17. 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 namesRecommended name:
Carboxypeptidase S1 homolog A

EC=3.4.16.6
Alternative name(s):
Serine carboxypeptidase A
Short name=SCPA
Gene names
Name:SCPA
ORF Names:TRV_05031
OrganismTrichophyton verrucosum (strain HKI 0517) [Complete proteome]
Taxonomic identifier663202 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Extracellular serine carboxypeptidase that contributes to pathogenicity By similarity.

Catalytic activity

Preferential release of a C-terminal arginine or lysine residue.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Potential.

Sequence similarities

Belongs to the peptidase S10 family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 1919 Potential
Chain20 – 629610Carboxypeptidase S1 homolog A
PRO_0000397825
Propeptide630 – 65223Removed in mature form Potential
PRO_0000397826

Sites

Active site2381 By similarity
Active site4581 By similarity
Active site5161 By similarity
Binding site4611Substrate By similarity
Binding site5171Substrate By similarity

Amino acid modifications

Lipidation6291GPI-anchor amidated glycine Potential
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation1321N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation4741N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation5051N-linked (GlcNAc...) Potential
Glycosylation5941N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 121 By similarity
Disulfide bond325 ↔ 361 By similarity
Disulfide bond332 ↔ 354 By similarity

Sequences

Sequence LengthMass (Da)Tools
D4DD24 [UniParc].

Last modified May 18, 2010. Version 1.
Checksum: 09B03AAF0D8540FD

FASTA65271,675
        10         20         30         40         50         60 
MRLAASIAVA LPVIGAASAQ GFPPPVTGVT VVKSKYDENV KITYKENDIC ETTEGVRSFT 

        70         80         90        100        110        120 
GHVHLPPDND YFGVYQNYSI NTFFWFFEAR EDPKNAPLSI WLNGGPGSSS MIGLFQENGP 

       130        140        150        160        170        180 
CWINDDSKST TNNSFSWNNR VNMLYIDQPN QVGFSYDELT NITYSTINDT ISVADFSSGV 

       190        200        210        220        230        240 
PAQNLSTLVG TGSSQKPWAT ANNTVNAARS IWHFAQVWFQ EFPEHKPNNN KISIWTESYG 

       250        260        270        280        290        300 
GRYGPSFASY FQEQNEKIKN HTITKEGEMH ILNLDTLGVI NGCIDLMFQA ESYAEFPYNN 

       310        320        330        340        350        360 
TYGITAYTKE KRDAIIRDIH RPDGCFDKLA KCREAAKEGD PHFYSNNATV NAICAEANSD 

       370        380        390        400        410        420 
CDKYLMEPFQ EANLGYYDIA HPLQDPFPPP FFKGFLSQSS VLSDMGSPVN FSHYSQAVGK 

       430        440        450        460        470        480 
SFHGVGDYAR PDVRGFTGDI AYLLESGVKV ALVYGDRDYI CNWLGGEQVS LGLNYTGTEA 

       490        500        510        520        530        540 
FRKAGYADVK VNSSYVGGLV RQHGNFSFTR VFEAGHEVPG YQPETSLKIF ERIMFNKDIA 

       550        560        570        580        590        600 
TGELDIAQKQ DYGTTGTEST FQVKNEIPPS PEPTCYLLSA DGTCTPEQLN AIENGTAVVE 

       610        620        630        640        650 
NYIIKSPAAS KGNPPPTTTS SPTASPTAGS AMLKAPVAML AISALTVLAF YL 

« Hide

References

[1]"Comparative and functional genomics provide insights into the pathogenicity of dermatophytic fungi."
Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S., Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O., Schroeckh V. expand/collapse author list , Hertweck C., Hube B., White T.C., Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.
Genome Biol. 12:R7.1-R7.16(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HKI 0517.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACYE01000255 Genomic DNA. Translation: EFE40253.1.
RefSeqXP_003020871.1. XM_003020825.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9577701.
KEGGtve:TRV_05031.

Phylogenomic databases

OrthoDBEOG7FV40C.

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSCPA_TRIVH
AccessionPrimary (citable) accession number: D4DD24
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 18, 2010
Last modified: February 19, 2014
This is version 17 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