SCPA_ARTBC
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 03-AUG-2022, entry version 51.
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 EnsemblFungi; EFE36524; EFE36524; ARB_04046.
DR GeneID; 9527135; -.
DR KEGG; abe:ARB_04046; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_3_1; -.
DR OMA; PEPTCYL; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
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; 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
