ID   SPCA_TRIEQ              Reviewed;         652 AA.
AC   A7UKV5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 53.
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 equinum (Horse ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=63418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Brown J.T., Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (JUL-2007) 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; EU076570; ABU50380.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7UKV5; -.
DR   SMR; A7UKV5; -.
DR   ESTHER; trieq-spca; Carboxypeptidase_S10.
DR   GlyCosmos; A7UKV5; 13 sites, No reported glycans.
DR   VEuPathDB; FungiDB:TEQG_03027; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.410; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF189; CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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_0000384115"
FT   PROPEP          630..652
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000384116"
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   652 AA;  71739 MW;  2840A00CAC4FEE03 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 FL
//