ID TRYP_STRGR Reviewed; 259 AA. AC P00775; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 2. DT 04-NOV-2026, entry version 133. DE RecName: Full=Trypsin; DE EC=3.4.21.4; DE AltName: Full=SGT; DE Flags: Precursor; GN Name=sprT; OS Streptomyces griseus. OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1911; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 10137 / DSM 40855 / NBRC 3430 / NCIMB 8232 / NCTC 6961 / RC IMRU 3496; RX PubMed=1755852; DOI=10.1016/0006-291x(91)91248-b; RA Kim J.C., Cha S.H., Jeong S.T., Oh S.K., Byun S.M.; RT "Molecular cloning and nucleotide sequence of Streptomyces griseus trypsin RT gene."; RL Biochem. Biophys. Res. Commun. 181:707-713(1991). RN [2] RP PROTEIN SEQUENCE OF 37-259. RX PubMed=804314; DOI=10.1021/bi00677a011; RA Olafson R.W., Jurasek L., Carpenter M.R., Smillie L.B.; RT "Amino acid sequence of Streptomyces griseus trypsin. Cyanogen bromide RT fragments and complete sequence."; RL Biochemistry 14:1168-1177(1975). RN [3] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=3135412; DOI=10.1016/0022-2836(88)90541-4; RA Read R.J., James M.N.G.; RT "Refined crystal structure of Streptomyces griseus trypsin at 1.7-A RT resolution."; RL J. Mol. Biol. 200:523-551(1988). CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. 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; M64471; AAA26820.1; ALT_SEQ; Genomic_DNA. DR PIR; JQ1302; TRSMG. DR RefSeq; WP_003965150.1; NZ_BAABSR010000068.1. DR PDB; 1OS8; X-ray; 1.55 A; A=37-259. DR PDB; 1OSS; X-ray; 1.93 A; A=37-259. DR PDB; 1SGT; X-ray; 1.70 A; A=37-259. DR PDB; 2FMJ; X-ray; 1.65 A; A=37-259. DR PDB; 3BEU; X-ray; 1.05 A; A/B=37-259. DR PDB; 3I77; X-ray; 2.10 A; A=37-259. DR PDB; 3I78; X-ray; 3.00 A; A=37-259. DR SMR; P00775; -. DR STRING; 1911.GCA_001715295_03561; -. DR DrugBank; DB03127; Benzamidine. DR MEROPS; S01.101; -. DR OMA; AAHCDKV; -. DR OrthoDB; 1496095at2; -. DR BRENDA; 3.4.21.4; 6035. DR EvolutionaryTrace; P00775; -. DR CDD; cd00190; Tryp_SPc; 1. DR FunFam; 2.40.10.10:FF:000011; Coagulation factor X; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24252; ACROSIN-RELATED; 1. DR PANTHER; PTHR24252:SF7; HYALIN; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR AlphaFoldDB; P00775; -. DR MDposit; P00775; -. DR MDRepo; P00775; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase; KW Protease; Serine protease; Signal; Zymogen. FT SIGNAL 1..32 FT PROPEP 33..36 FT /note="Activation peptide" FT /evidence="ECO:0000269|PubMed:804314" FT /id="PRO_0000028307" FT CHAIN 37..259 FT /note="Trypsin" FT /id="PRO_0000028308" FT DOMAIN 37..257 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 73 FT /note="Charge relay system" FT ACT_SITE 118 FT /note="Charge relay system" FT ACT_SITE 208 FT /note="Charge relay system" FT SITE 202 FT /note="Required for specificity" FT DISULFID 58..74 FT DISULFID 177..192 FT DISULFID 204..233 FT CONFLICT 95..96 FT /note="Missing (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:3BEU" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 58..64 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:3BEU" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 91..95 FT /evidence="ECO:0007829|PDB:3I78" FT STRAND 99..108 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:1OS8" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:1SGT" FT STRAND 142..152 FT /evidence="ECO:0007829|PDB:3BEU" FT HELIX 158..161 FT /evidence="ECO:0007829|PDB:1OS8" FT STRAND 165..172 FT /evidence="ECO:0007829|PDB:3BEU" FT HELIX 174..180 FT /evidence="ECO:0007829|PDB:3BEU" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:1OS8" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 190..193 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 197..200 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 211..215 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 221..234 FT /evidence="ECO:0007829|PDB:3BEU" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:3BEU" FT HELIX 245..256 FT /evidence="ECO:0007829|PDB:3BEU" SQ SEQUENCE 259 AA; 26776 MW; 050233AFF1F64823 CRC64; MKHFLRALKR CSVAVATVAI AVVGLQPVTA SAAPNPVVGG TRAAQGEFPF MVRLSMGCGG ALYAQDIVLT AAHCVSGSGN NTSITATGGV VDLQSSSAVK VRSTKVLQAP GYNGTGKDWA LIKLAQPINQ PTLKIATTTA YNQGTFTVAG WGANREGGSQ QRYLLKANVP FVSDAACRSA YGNELVANEE ICAGYPDTGG VDTCQGDSGG PMFRKDNADE WIQVGIVSWG YGCARPGYPG VYTEVSTFAS AIASAARTL //