ID   TRYP_SACER              Reviewed;         227 AA.
AC   P24664;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Trypsin;
DE            EC=3.4.21.4;
DE   AltName: Full=SET;
OS   Saccharopolyspora erythraea (Streptomyces erythraeus).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=1836;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Miyamoto K., Matsuo H., Narita K.;
RL   (In) Proceedings of Dai 30 kai tanpakushitsu kouzou touronkai kouen
RL   youshishuu, pp.77-80, Tokyo (1979).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND SEQUENCE REVISION.
RX   PubMed=1794983; DOI=10.1093/oxfordjournals.jbchem.a123694;
RA   Yamane T., Kobuke M., Tsutsui H., Toida T., Suzuki A., Ashida T.,
RA   Kawata Y., Sakiyama F.;
RT   "Crystal structure of Streptomyces erythraeus trypsin at 2.7-A
RT   resolution.";
RL   J. Biochem. 110:945-950(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC   -!- MISCELLANEOUS: Hardly autolyzes itself at all at its active pH range.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   PDB; 4M7G; X-ray; 0.81 A; A=1-227.
DR   PDB; 5DK1; X-ray; 0.94 A; A=1-227.
DR   PDBsum; 4M7G; -.
DR   PDBsum; 5DK1; -.
DR   AlphaFoldDB; P24664; -.
DR   SMR; P24664; -.
DR   IntAct; P24664; 1.
DR   MEROPS; S01.102; -.
DR   BRENDA; 3.4.21.4; 5518.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Protease; Serine protease.
FT   CHAIN           1..227
FT                   /note="Trypsin"
FT                   /id="PRO_0000088718"
FT   DOMAIN          1..223
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        42
FT                   /note="Charge relay system"
FT   ACT_SITE        88
FT                   /note="Charge relay system"
FT   ACT_SITE        179
FT                   /note="Charge relay system"
FT   SITE            173
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..43
FT   DISULFID        150..164
FT   DISULFID        175..199
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          15..19
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          25..33
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          66..76
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          118..128
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          138..144
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   HELIX           147..153
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          162..165
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          188..195
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   STRAND          206..210
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   HELIX           211..214
FT                   /evidence="ECO:0007829|PDB:4M7G"
FT   HELIX           215..222
FT                   /evidence="ECO:0007829|PDB:4M7G"
SQ   SEQUENCE   227 AA;  23308 MW;  D5AC5E47B227B418 CRC64;
     IVGGEDANVQ DHPFTVALVT PDGQQFCGGT LAAPNKVVTA AHCTVGSQPA DINVVSGRTV
     MSSNIGTVSK VTNVWVHPEY QDAAKGFDVS VLTLEAPVKE APIELAKADD AGYAPDTAAT
     ILGWGNTSEG GQQADHLQKA TVPVNSDDTC KQAYGEYTPN AMVCAGVPEG GVDTCQGDSG
     GPMVVNNKLI GVTSWGEGCA RPGKPGVYAR VGAYYDVLME QINAGAV