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Protein

Carboxypeptidase S1 homolog A

Gene

SCPA

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.By similarity1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 4.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei238PROSITE-ProRule annotation1
Active sitei458PROSITE-ProRule annotation1
Binding sitei461SubstrateBy similarity1
Active sitei516PROSITE-ProRule annotation1
Binding sitei517SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Keywords - Biological processi

Virulence

Protein family/group databases

ESTHERitriru-SPCA. Carboxypeptidase_S10.
MEROPSiS10.016.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase S1 homolog A (EC:3.4.16.6)
Alternative name(s):
Serine carboxypeptidase A
Short name:
SPCA
Gene namesi
Name:SCPA
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000038411720 – 629Carboxypeptidase S1 homolog AAdd BLAST610
PropeptideiPRO_0000384118630 – 652Removed in mature formSequence analysisAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 121By similarity
Glycosylationi77N-linked (GlcNAc...)Sequence analysis1
Glycosylationi132N-linked (GlcNAc...)Sequence analysis1
Glycosylationi161N-linked (GlcNAc...)Sequence analysis1
Glycosylationi168N-linked (GlcNAc...)Sequence analysis1
Glycosylationi184N-linked (GlcNAc...)Sequence analysis1
Glycosylationi202N-linked (GlcNAc...)Sequence analysis1
Glycosylationi260N-linked (GlcNAc...)Sequence analysis1
Glycosylationi299N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi325 ↔ 361By similarity
Disulfide bondi332 ↔ 354By similarity
Glycosylationi347N-linked (GlcNAc...)Sequence analysis1
Glycosylationi410N-linked (GlcNAc...)Sequence analysis1
Glycosylationi474N-linked (GlcNAc...)Sequence analysis1
Glycosylationi492N-linked (GlcNAc...)Sequence analysis1
Glycosylationi505N-linked (GlcNAc...)Sequence analysis1
Lipidationi629GPI-anchor amidated glycineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Interactioni

Protein-protein interaction databases

STRINGi559305.XP_003234971.1.

Structurei

3D structure databases

ProteinModelPortaliQ5J6J1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1282. Eukaryota.
COG2939. LUCA.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Ser_caboxypep_ser_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 2 hits.
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.

Q5J6J1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFAASIAVA LPVIHAASAQ GFPPPVKGVT VVKSKFDENV KITYKENDIC
60 70 80 90 100
ETTQGVRSFT GHVHLPPDND DFGVYRNYSI NTFFWFFEAR EDPKNAPLSI
110 120 130 140 150
WLNGGPGSSS MIGLFQENGP CWVNEDSKST TNNSFSWNNK VNMLYIDQPN
160 170 180 190 200
QVGFSYDVPT NITYSTINDT ISVADFSNGV PAQNLSTLVG TGSSQNPWAT
210 220 230 240 250
ANNTVNAARS IWHFAQVWFQ EFPEHKPNNN KISIWTESYG GRYGPSFASY
260 270 280 290 300
FQEQNEKIKN HTITEEGEMH ILNLDTLGII NGCIDLMFQA ESYAEFPYNN
310 320 330 340 350
TYGIKAYTKE KRDAILHDIH RPDGCFDKVT KCREAAKEGD PHFYSNNATV
360 370 380 390 400
NTICADANSA CDKYLMDPFQ ETNLGYYDIA HPLQDPFPPP FYKGFLSQSS
410 420 430 440 450
VLSDMGSPVN FSQYAQAVGK SFHGVGDYAR PDVRGFTGDI AYLLESGVKV
460 470 480 490 500
ALVYGDRDYI CNWFGGEQVS LGLNYTGTQD FHRAKYADVK VNSSYVGGVV
510 520 530 540 550
RQHGNFSFTR VFEAGHEVPG YQPETALKIF ERIMFNKDIS TGEIDIAQKP
560 570 580 590 600
DYGTTGTEST FHIKNDIPPS PEPTCYLLSA DGTCTPEQLN AIKDGTAVVE
610 620 630 640 650
NYIIKSPAAS KGNPPPTTTS SPTAAPTAGS AMLKAPVAML AISALTVLAF

FL
Length:652
Mass (Da):71,825
Last modified:February 15, 2005 - v1
Checksum:iB5D3E435BAC0A9C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497023 Genomic DNA. Translation: AAS76667.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497023 Genomic DNA. Translation: AAS76667.1.

3D structure databases

ProteinModelPortaliQ5J6J1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi559305.XP_003234971.1.

Protein family/group databases

ESTHERitriru-SPCA. Carboxypeptidase_S10.
MEROPSiS10.016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1282. Eukaryota.
COG2939. LUCA.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Ser_caboxypep_ser_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 2 hits.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPCA_TRIRU
AccessioniPrimary (citable) accession number: Q5J6J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 15, 2005
Last modified: March 16, 2016
This is version 47 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

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 one 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.