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Q5J6J1 (SPCA_TRIRU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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=SPCA
Gene names
Name:SCPA
OrganismTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Taxonomic identifier5551 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Extracellular serine carboxypeptidase that contributes to pathogenicity By similarity. Ref.1

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.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.5. Ref.1

Ontologies

Keywords
   Biological processVirulence
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
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_0000384117
Propeptide630 – 65223Removed in mature form Potential
PRO_0000384118

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
Disulfide bond50 ↔ 121 By similarity
Disulfide bond325 ↔ 361 By similarity
Disulfide bond332 ↔ 354 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5J6J1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: B5D3E435BAC0A9C5

FASTA65271,825
        10         20         30         40         50         60 
MRFAASIAVA LPVIHAASAQ GFPPPVKGVT VVKSKFDENV KITYKENDIC ETTQGVRSFT 

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

       130        140        150        160        170        180 
CWVNEDSKST TNNSFSWNNK VNMLYIDQPN QVGFSYDVPT NITYSTINDT ISVADFSNGV 

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

       250        260        270        280        290        300 
GRYGPSFASY FQEQNEKIKN HTITEEGEMH ILNLDTLGII NGCIDLMFQA ESYAEFPYNN 

       310        320        330        340        350        360 
TYGIKAYTKE KRDAILHDIH RPDGCFDKVT KCREAAKEGD PHFYSNNATV NTICADANSA 

       370        380        390        400        410        420 
CDKYLMDPFQ ETNLGYYDIA HPLQDPFPPP FYKGFLSQSS VLSDMGSPVN FSQYAQAVGK 

       430        440        450        460        470        480 
SFHGVGDYAR PDVRGFTGDI AYLLESGVKV ALVYGDRDYI CNWFGGEQVS LGLNYTGTQD 

       490        500        510        520        530        540 
FHRAKYADVK VNSSYVGGVV RQHGNFSFTR VFEAGHEVPG YQPETALKIF ERIMFNKDIS 

       550        560        570        580        590        600 
TGEIDIAQKP DYGTTGTEST FHIKNDIPPS PEPTCYLLSA DGTCTPEQLN AIKDGTAVVE 

       610        620        630        640        650 
NYIIKSPAAS KGNPPPTTTS SPTAAPTAGS AMLKAPVAML AISALTVLAF FL 

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References

[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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY497023 Genomic DNA. Translation: AAS76667.1.

3D structure databases

ProteinModelPortalQ5J6J1.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameSPCA_TRIRU
AccessionPrimary (citable) accession number: Q5J6J1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 15, 2005
Last modified: February 19, 2014
This is version 36 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