SCPB_ARTBC
ID SCPB_ARTBC Reviewed; 656 AA.
AC D4AP52;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Carboxypeptidase S1 homolog B;
DE EC=3.4.16.6;
DE AltName: Full=Serine carboxypeptidase B;
DE Short=SPCB;
DE Flags: Precursor;
GN Name=SCPB; ORFNames=ARB_06019;
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; ABSU01000004; EFE35063.1; -; Genomic_DNA.
DR RefSeq; XP_003015708.1; XM_003015662.1.
DR AlphaFoldDB; D4AP52; -.
DR SMR; D4AP52; -.
DR ESTHER; triru-SCPB; Carboxypeptidase_S10.
DR MEROPS; S10.016; -.
DR EnsemblFungi; EFE35063; EFE35063; ARB_06019.
DR GeneID; 9525989; -.
DR KEGG; abe:ARB_06019; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_3_1; -.
DR OMA; IDRYVQW; -.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..627
FT /note="Carboxypeptidase S1 homolog B"
FT /id="PRO_0000397827"
FT PROPEP 628..656
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397828"
FT ACT_SITE 234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT LIPID 627
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..123
FT /evidence="ECO:0000250"
FT DISULFID 322..358
FT /evidence="ECO:0000250"
FT DISULFID 329..351
FT /evidence="ECO:0000250"
SQ SEQUENCE 656 AA; 72378 MW; A9DA1EA3F38BBD1B CRC64;
MVSFCGVAAC LLTVAGHLAQ AQFPPKPEGV TVLESKFGSG ARITYKEPGL CETTEGVKSY
AGYVHLPPGT LRDFGVEQDY PINTFFWFFE ARKDPENAPL GIWMNGGPGS SSMFGMMTEN
GPCFVNADSN STRLNPHSWN NEDQPVQVGL SYDTLANFTR NLVTDEITKL EPGEPIPEQN
ATFLVGTYAS RNMNTTAHGT RHAAMALWHF AQVWFQEFPG YHPRNNKISI ATESYGGRYG
PAFTAFFEEQ NQKIKNGTWK GHEGTMHVLH LDTLMIVNGC IDRLVQWPAY PQMAYNNTYG
IEAVNASIHA GMLDALYRDG GCRDKINHCR SLSSVSDPEN LGINSTVNDV CKDAETFCSN
DVRDPYTKLS GRNYYDIGQL DPSPFPAPFY MAWLNQPHVQ AALGVPLNWT QSNDVVSTAF
RAIGDYPRPG WLENLAFLLE NGIKVSLVYG DRDYACNWFG GELSSLGINY TDTQEFHNAG
YAGIQINSSY IGGQVRQYGN LSFARVYEAG HEVPSYQPET ALQIFHRALF NKDIATGTKD
TSSRMDRGKF YGTSGPADSF GFKNEPPPQH VHFCHILDTS TCTKEQIQSV ENGTATIRSW
IIVDSNSTSL FPEVVGSGEP TPTPMPGGAT TLSAHGYLYD VTLWVVLLVS AIELVM
