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 13-SEP-2023, entry version 54. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; D4AP52; 14 sites, No reported glycans. DR GeneID; 9525989; -. DR KEGG; abe:ARB_06019; -. DR eggNOG; KOG1282; Eukaryota. DR HOGENOM; CLU_008523_10_3_1; -. DR OMA; FQEFPGY; -. 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..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 //