SCPB_ARTOC
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 03-AUG-2022, entry version 57.
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}.
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DR EMBL; DS995702; EEQ30006.1; -; Genomic_DNA.
DR RefSeq; XP_002849891.1; XM_002849845.1.
DR AlphaFoldDB; C5FGX1; -.
DR SMR; C5FGX1; -.
DR ESTHER; artoc-scpb; Carboxypeptidase_S10.
DR MEROPS; S10.016; -.
DR EnsemblFungi; EEQ30006; EEQ30006; MCYG_02825.
DR GeneID; 9223265; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_3_1; -.
DR OMA; IDRYVQW; -.
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..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
