ID   SCPA_ARTBC              Reviewed;         652 AA.
AC   D4AIF1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Carboxypeptidase S1 homolog A;
DE            EC=3.4.16.6;
DE   AltName: Full=Serine carboxypeptidase A;
DE            Short=SCPA;
DE   Flags: Precursor;
GN   Name=SCPA; ORFNames=ARB_04046;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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; ABSU01000001; EFE36524.1; -; Genomic_DNA.
DR   RefSeq; XP_003017169.1; XM_003017123.1.
DR   AlphaFoldDB; D4AIF1; -.
DR   SMR; D4AIF1; -.
DR   ESTHER; triru-SPCA; Carboxypeptidase_S10.
DR   MEROPS; S10.016; -.
DR   GlyCosmos; D4AIF1; 14 sites, No reported glycans.
DR   GeneID; 9527135; -.
DR   KEGG; abe:ARB_04046; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_3_1; -.
DR   OMA; ESPEPTC; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
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; 3.40.50.1820; alpha/beta hydrolase; 1.
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; Reference proteome; Signal;
KW   Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..629
FT                   /note="Carboxypeptidase S1 homolog A"
FT                   /id="PRO_0000397823"
FT   PROPEP          630..652
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000397824"
FT   REGION          608..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..628
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   CARBOHYD        594
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;  71705 MW;  FFCA2819EAC39B97 CRC64;
     MRLAASIAVA LPVIGAASAQ GFPPPVMGVT VVKSKYDENV KITYKENDIC ETTEGVRSFT
     GHVHLPPDND YFGVYQNYSI NTFFWFFEAR EDPKNAPLSI WLNGGPGSSS MIGLFQENGP
     CWINDDSKST TNNSFSWNNR VNMLYIDQPN QVGFSYDELT NITYSTINDT ISVADFSSGV
     PAQNLSTLVG TGSSQKPWAT ANNTVNAARS IWHFAQVWFQ EFPEHKPNNN KISIWTESYG
     GRYGPSFASY FQEQNEKIKN HTITKEGEMH ILNLDTLGVI NGCIDLMFQA ESYAEFPYNN
     TYGITAYTKE KRDAIIRDIH RPDGCFDKLA KCREAAKEGD PHFYSNNATV NAICAEANSD
     CDKYLMEPFQ EANLGYYDIA HPLQDPFPPP FFKGFLSQSS VLSDMGSPVN FSHYSQAVGK
     SFHGVGDYAR PDVRGFTGDI AYLLESGVKV ALVYGDRDYI CNWLGGEQVS LGLNYTGTEA
     FRKAGYADVK VNSSYVGGLV RQHGNFSFTR VFEAGHEVPG YQPETSLKIF ERIMFNKDIA
     TGELDIAQKQ DYGTTGTEST FQVKNEIPPS PEPTCYLLSA DGTCTPEQLN AIENGTAVVE
     NYIIKSPAAS KGNPPPTTTS SPTASPTAGS AMLKAPVAML AISALTVLAF YL
//