ID SCPB_ARTOC Reviewed; 655 AA. AC C5FGX1; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 24-JAN-2024, entry version 63. 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=MCYG_02825; 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}. 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; DS995702; EEQ30006.1; -; Genomic_DNA. DR RefSeq; XP_002849891.1; XM_002849845.1. DR AlphaFoldDB; C5FGX1; -. DR SMR; C5FGX1; -. DR STRING; 554155.C5FGX1; -. DR ESTHER; artoc-scpb; Carboxypeptidase_S10. DR MEROPS; S10.016; -. DR GlyCosmos; C5FGX1; 12 sites, No reported glycans. DR GeneID; 9223265; -. DR VEuPathDB; FungiDB:MCYG_02825; -. DR eggNOG; KOG1282; Eukaryota. DR HOGENOM; CLU_008523_10_3_1; -. DR OMA; FQEFPGY; -. DR OrthoDB; 1647009at2759; -. DR Proteomes; UP000002035; 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..631 FT /note="Carboxypeptidase S1 homolog B" FT /id="PRO_0000384121" FT PROPEP 632..655 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000384122" FT ACT_SITE 240 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 459 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 517 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT BINDING 462 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 518 FT /ligand="substrate" FT /evidence="ECO:0000250" FT LIPID 631 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 163 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 186 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 266 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 302 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 311 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 414 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 475 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 493 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 506 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 598 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 612 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 51..123 FT /evidence="ECO:0000250" FT DISULFID 328..364 FT /evidence="ECO:0000250" FT DISULFID 335..357 FT /evidence="ECO:0000250" SQ SEQUENCE 655 AA; 72791 MW; 4E95D4568D454EB5 CRC64; MRPFARAALC LLAAAGHLAQ AQFPPRPEGV TVLESKFGGG ARISYKEPGL CETTEGVKSY AGYVHLPPGT LKDLGVEQDY PINTFFWFFE ARKDPENAPL SIWMNGGPGS SSMFGMMTEN GPCFVNPDSN STRLNPHSWN NEVNMLYLDQ PVQVGLSYDT LANFTRNLVT DEITKLEPGD PIPEQNATFL VGTYASRNMD TTAKGTRNAA IALWHFAQVW FQEFPGYHPR DSRISIATES YGGRYGPAFT AFFEEQNQKI KDGTWNGSEG NRHVLHLDTL MIVNGCIDRL VQWPAYPQMA YNNTYSIEAV NASIHEGMLD ALYREGGCRD KINHCRSISA VSDPENIGIN AMVNDVCKDA ETFCSTEVRD PYQEFSGRNY YDIGQLDPSP FPAPFYMAWL NQPHVQAALG VPLNWTQSND VVTTAFRAIG DYPRPGWLED LAYLLENGIK VSLVYGDRDY ACNWFGGELS SLAINYTDTQ NFHNAGYAGI QVNSSYIGGQ VRQYGNLSFS RVYEAGHEVP SYQPETALQI FHRALFNKDI ATGTIDTSSR REDGKFYGSS GPSDSFVFKN EPPPQHVHFC HILDTSTCTK EQIESVENGT AVVRSWIVVD SNSTSLFPEV VGSAEPTPMP GAALVSGRIK FHVHVIKSFD YYIFI //