SCPA_TRITO
ID SCPA_TRITO Reviewed; 651 AA.
AC B6V867;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Carboxypeptidase S1 homolog A;
DE EC=3.4.16.6;
DE AltName: Full=Serine carboxypeptidase A;
DE Short=SPCA;
DE Flags: Precursor;
GN Name=SCPA;
OS Trichophyton tonsurans (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=34387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Preuett B.L., Abdel-Rahman S.M.;
RT "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT and Trichophyton equinum.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular serine carboxypeptidase that contributes to
CC pathogenicity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal arginine or lysine
CC residue.; EC=3.4.16.6;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; FJ267690; ACJ06658.1; -; Genomic_DNA.
DR AlphaFoldDB; B6V867; -.
DR SMR; B6V867; -.
DR ESTHER; triru-SPCA; Carboxypeptidase_S10.
DR VEuPathDB; FungiDB:TESG_00118; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Protease; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..629
FT /note="Carboxypeptidase S1 homolog A"
FT /id="PRO_0000384119"
FT PROPEP 630..651
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000384120"
FT REGION 607..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT LIPID 629
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..121
FT /evidence="ECO:0000250"
FT DISULFID 325..361
FT /evidence="ECO:0000250"
FT DISULFID 332..354
FT /evidence="ECO:0000250"
SQ SEQUENCE 651 AA; 71592 MW; EE400CAC4FEE037A CRC64;
MRFAASIAVA LPVIGAASAQ GFPPPVEGVT VVKSKFDENV KITYKENDIC ETTEGVRSFT
GHVHLPPDDN DFGVYRNYSI NTFFWFFEAR EDPKNAPLSI WLNGGPGSSS MIGLFQENGP
CWINDDSKST TNNTFSWNNK VNMLYIDQPN QVGFSYDELT NITYSTINDT VYVADFSNGV
PAQNLSTLVG TGSSQNPWAT ANNTVNAARS IWHFAQVWFQ EFPEHKPNNN KISIWTESYG
GRYGPSFASY FQEQNEKIKN HTITEEGEMH ILNLDTLGII NGCIDLMFQA ESYAEFPYNN
TYGITAYTKE KYDAIIHDIH RPDGCFDKLA KCREAAKEGD PHFYSNNATV NAICADASSS
CDNYLMDPYQ ETNLGYYDIA HPLQDPFPPP FYKGFLSQSS VLSDMGSPVN FTQYAQAVGK
SFHGVGDYAR PDVRGFTGDI AYLLESGVKV ALVYGDRDYI CNWIGGEQVS LGLNYTGTAE
FHRAGYADVK VNSSYVGGLV RQHGNFSFTR VFEAGHEVPG YQPETSLKIF ERIMFNKDIA
TGELDIAQKP DYGTTGTEST FQVKNEIPPS PEPTCYLLSA DGTCTQEQLK AIKEGTAVVE
NYIIKSPAAS KGDPPPTTTT SPTAAPTAGS AMLQAPVAML AISVLTALAF L
