ID   CPS1_PENJA              Reviewed;         423 AA.
AC   P34946;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Carboxypeptidase S1;
DE            EC=3.4.16.6;
OS   Penicillium janthinellum (Penicillium vitale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5079;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8224168; DOI=10.1016/0014-5793(93)80371-z;
RA   Svendsen I., Hofmann T., Endrizzi J., Remington S.J., Breddam K.;
RT   "The primary structure of carboxypeptidase S1 from Penicillium
RT   janthinellum.";
RL   FEBS Lett. 333:39-43(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal arginine or lysine
CC         residue.; EC=3.4.16.6;
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   PIR; S38953; S38953.
DR   AlphaFoldDB; P34946; -.
DR   SMR; P34946; -.
DR   ESTHER; penja-cps1; Carboxypeptidase_S10.
DR   MEROPS; S10.008; -.
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; IPR033124; Ser_caboxypep_his_AS.
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; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease.
FT   CHAIN           1..423
FT                   /note="Carboxypeptidase S1"
FT                   /id="PRO_0000120564"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        340
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        397
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="substrate"
FT   BINDING         398
FT                   /ligand="substrate"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        8..68
FT   DISULFID        55..300
FT   DISULFID        223..246
FT   DISULFID        230..239
SQ   SEQUENCE   423 AA;  46496 MW;  55F3333608B12729 CRC64;
     FVKNSGICET TPGVNQYSGY LSVGSNMNMW FWFFEARNNP QQAPLAAWFN GGPGCSSMIG
     LFQENGPCHF VNGDSTPSLN ENSWNNYANM IYIDQPIGVG FSYGTDDVTS TVTAAPYVWN
     LLQAFYAQRP EYESRDFAIF TESYGGHYGP EFASYIEQQN AAIKAGSVTG QNVNIVALGV
     NNGWIDSTIQ EKAYIDFSYN NSYQQIIDSS TRDSLLDAYN NQCLPALQQC SQSGSTSDCT
     NADSVCYQNI EGPISSSGDF DVYDIREPSN DPYPPKTYST YLSDPTVVKA IGARTNYQEC
     PNGPYNKFAS TGDNPRSFLS TLSSVVQSGI NVLVWAGDAD WICNWLGNYE VANAVDFPGN
     AQFSALDLAP YTVNGVEKGQ FKTVDNFSFL KVYGAGHEVP YYQPDTALQA FKQIIQKKPI
     SST