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Protein

Carboxypeptidase S1 homolog B

Gene

SCPB

Organism
Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Extracellular serine carboxypeptidase that contributes to pathogenicity.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 8.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei240 – 2401PROSITE-ProRule annotation
Active sitei459 – 4591PROSITE-ProRule annotation
Binding sitei462 – 4621SubstrateBy similarity
Active sitei517 – 5171PROSITE-ProRule annotation
Binding sitei518 – 5181SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Keywords - Biological processi

Virulence

Protein family/group databases

ESTHERitriru-SCPB. Carboxypeptidase_S10.
MEROPSiS10.016.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase S1 homolog B (EC:3.4.16.6)
Alternative name(s):
Serine carboxypeptidase B
Short name:
SPCB
Gene namesi
Name:SCPB
OrganismiTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Taxonomic identifieri5551 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeTrichophyton

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 633612Carboxypeptidase S1 homolog BPRO_0000384123Add
BLAST
Propeptidei634 – 66229Removed in mature formSequence AnalysisPRO_0000384124Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 123By similarity
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi328 ↔ 364By similarity
Disulfide bondi335 ↔ 357By similarity
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi506 – 5061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence Analysis
Lipidationi633 – 6331GPI-anchor amidated glycineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Inductioni

Expression is strongly increased during growth on protein-rich medium.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi559305.XP_003230952.1.

Structurei

3D structure databases

ProteinModelPortaliQ5J6J2.
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. 2 hits.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5J6J2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFCGVAAC LLTVAGHLAQ AQFPPKPEGV TVLESKFGSG ARITYKEPGL
60 70 80 90 100
CETTEGVKSY AGYVHLPPGT LRDFGVEQDY PINTFFWFFE ARKDPENAPL
110 120 130 140 150
GIWMNGGPGS SSMFGMMTEN GPCFVNADSN STRLNPHSWN NEVNMLYIDQ
160 170 180 190 200
PVQVGLSYDT LANFTRNLVT DEITKLKPGE PIPEQNATFL VGTYASRNMN
210 220 230 240 250
TTAHGTRHAA MALWHFAQVW FQEFPGYHPR NNKISIATES YGGRYGPAFT
260 270 280 290 300
AFFEEQNQKI KNGTWKGHEG TMHVLHLDTL MIVNGCIDRL VQWPAYPQMA
310 320 330 340 350
YNNTYSIEAV NASIHAGMLD ALYRDGGCRD KINHCRSLSS VFDPENLGIN
360 370 380 390 400
STVNDVCKDA ETFCSNDVRD PYLKFSGRNY YDIGQLDPSP FPAPFYMAWL
410 420 430 440 450
NQPHVQAALG VPLNWTQSND VVSTAFRAIG DYPRPGWLEN LAYLLENGIK
460 470 480 490 500
VSLVYGDRDY ACNWFGGELS SLGINYTDTH EFHNAGYAGI QINSSYIGGQ
510 520 530 540 550
VRQYGNLSFA RVYEAGHEVP SYQPETALQI FHRSLFNKDI ATGTKDTSSR
560 570 580 590 600
MDGGKFYGTS GPADSFGFKN KPPPQHVHFC HILDTSTCTK EQIQSVENGT
610 620 630 640 650
AAVRSWIIVD SNSTSLFPEV VGSGEPTPTP MPGGATTLSA HGFLYGVTLW
660
AVIVVAVIEL AM
Length:662
Mass (Da):73,012
Last modified:February 15, 2005 - v1
Checksum:iB47308AB5BB82CCB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497022 Genomic DNA. Translation: AAS76666.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497022 Genomic DNA. Translation: AAS76666.1.

3D structure databases

ProteinModelPortaliQ5J6J2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi559305.XP_003230952.1.

Protein family/group databases

ESTHERitriru-SCPB. Carboxypeptidase_S10.
MEROPSiS10.016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. 2 hits.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

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], 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.

Entry informationi

Entry nameiSCPB_TRIRU
AccessioniPrimary (citable) accession number: Q5J6J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 15, 2005
Last modified: June 24, 2015
This is version 41 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.