SPCA_ARTOC
ID SPCA_ARTOC Reviewed; 651 AA.
AC C5FW30;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
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; ORFNames=MCYG_06933;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995706; EEQ34114.1; -; Genomic_DNA.
DR RefSeq; XP_002844969.1; XM_002844923.1.
DR AlphaFoldDB; C5FW30; -.
DR SMR; C5FW30; -.
DR ESTHER; artoc-spca; Carboxypeptidase_S10.
DR MEROPS; S10.016; -.
DR EnsemblFungi; EEQ34114; EEQ34114; MCYG_06933.
DR GeneID; 9228194; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_3_1; -.
DR OMA; PEPTCYL; -.
DR OrthoDB; 625787at2759; -.
DR Proteomes; UP000002035; 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..625
FT /note="Carboxypeptidase S1 homolog A"
FT /id="PRO_0000384113"
FT PROPEP 626..651
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000384114"
FT REGION 604..631
FT /note="Disordered"
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 515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT LIPID 625
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
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 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 308
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 504
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; 72198 MW; 074F1DA49231EAE6 CRC64;
MHLATGLAVA LPFIGAASAQ YFPPPVEGVT VVESKFDKNV KITYKENDIC ETTEGVRSFT
GHVHLPPNNN DFGVNQNYSI NTFFWFFEAR EDPKNAPLSI WLNGGPGSSS MIGLFQENGP
CMVNNDSNST TNNPYSWNNK VNMLYIDQPN QVGFSYDVPT NVTVNPINDE VTVADFSNGV
PEQNNTLLVG TLGSQNPYAT ANNTQNAARS IWHFAQVWFQ EFPEYKPNND KVSIWTESYG
GRYGPAFTSY FQEQNEKIKN HTITEEGEMH ILHLDTVGII NGCVDLMEQA TSYPDFAYNN
TYGIKAYNQS QYDSMINEFY RTGGCRDQLI HCRDVAAESD PHFYSHNETV NKICNDAGDF
CGQKLEDAFE SANLGFYDIA HPLNDPFPPQ FYKGYLSQAH VLADMGMPVN FSQASDAVWK
AFHTVGDYGR GDVRGYIDDL AYLLENGIKV ALVYGDRDYI CNWFGGEKVS LALNYTGTEN
FHKAGYTDVK VNSQVGGQVR QYGNFSFTRV YEAGHEVPAY QPEVSLEIFH RIMFNKDIAT
GEIDIAQKPD YSTTGTADTF HIKNDIPPEP EPTCYVLSMG RTCSEEQVKA VKDGTAVVEN
YIVKSPAGKK QGPPPTSTSP PSPTSSSEGS VKEFSVSVLG VSVLAAITFF L
