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

Q5J6J2 (SCPB_TRIRU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. 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 B

EC=3.4.16.6
Alternative name(s):
Serine carboxypeptidase B
Short name=SPCB
Gene names
Name:SCPB
OrganismTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Taxonomic identifier5551 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Protein attributes

Sequence length662 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. Ref.1

Catalytic activity

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

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Potential.

Induction

Expression is strongly increased during growth on protein-rich medium. Ref.2

Sequence similarities

Belongs to the peptidase S10 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0. 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

   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 – 2121 Potential
Chain22 – 633612Carboxypeptidase S1 homolog B
PRO_0000384123
Propeptide634 – 66229Removed in mature form Potential
PRO_0000384124

Sites

Active site2401 By similarity
Active site4591 By similarity
Active site5171 By similarity
Binding site4621Substrate By similarity
Binding site5181Substrate By similarity

Amino acid modifications

Lipidation6331GPI-anchor amidated glycine Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4751N-linked (GlcNAc...) Potential
Glycosylation4931N-linked (GlcNAc...) Potential
Glycosylation5061N-linked (GlcNAc...) Potential
Glycosylation5981N-linked (GlcNAc...) Potential
Glycosylation6121N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 123 By similarity
Disulfide bond328 ↔ 364 By similarity
Disulfide bond335 ↔ 357 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5J6J2 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: B47308AB5BB82CCB

FASTA66273,012
        10         20         30         40         50         60 
MVSFCGVAAC LLTVAGHLAQ AQFPPKPEGV TVLESKFGSG ARITYKEPGL CETTEGVKSY 

        70         80         90        100        110        120 
AGYVHLPPGT LRDFGVEQDY PINTFFWFFE ARKDPENAPL GIWMNGGPGS SSMFGMMTEN 

       130        140        150        160        170        180 
GPCFVNADSN STRLNPHSWN NEVNMLYIDQ PVQVGLSYDT LANFTRNLVT DEITKLKPGE 

       190        200        210        220        230        240 
PIPEQNATFL VGTYASRNMN TTAHGTRHAA MALWHFAQVW FQEFPGYHPR NNKISIATES 

       250        260        270        280        290        300 
YGGRYGPAFT AFFEEQNQKI KNGTWKGHEG TMHVLHLDTL MIVNGCIDRL VQWPAYPQMA 

       310        320        330        340        350        360 
YNNTYSIEAV NASIHAGMLD ALYRDGGCRD KINHCRSLSS VFDPENLGIN STVNDVCKDA 

       370        380        390        400        410        420 
ETFCSNDVRD PYLKFSGRNY YDIGQLDPSP FPAPFYMAWL NQPHVQAALG VPLNWTQSND 

       430        440        450        460        470        480 
VVSTAFRAIG DYPRPGWLEN LAYLLENGIK VSLVYGDRDY ACNWFGGELS SLGINYTDTH 

       490        500        510        520        530        540 
EFHNAGYAGI QINSSYIGGQ VRQYGNLSFA RVYEAGHEVP SYQPETALQI FHRSLFNKDI 

       550        560        570        580        590        600 
ATGTKDTSSR MDGGKFYGTS GPADSFGFKN KPPPQHVHFC HILDTSTCTK EQIQSVENGT 

       610        620        630        640        650        660 
AAVRSWIIVD SNSTSLFPEV VGSGEPTPTP MPGGATTLSA HGFLYGVTLW AVIVVAVIEL 


AM 

« Hide

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.
[2]"Gene expression profiling in the human pathogenic dermatophyte Trichophyton rubrum during growth on proteins."
Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J., Bueno M., Giddey K., Staib P.
Eukaryot. Cell 8:241-250(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY497022 Genomic DNA. Translation: AAS76666.1.

3D structure databases

ProteinModelPortalQ5J6J2.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
SUPFAMSSF53474. SSF53474. 2 hits.
PROSITEPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSCPB_TRIRU
AccessionPrimary (citable) accession number: Q5J6J2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 15, 2005
Last modified: June 11, 2014
This is version 37 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