ID TRYP_FUSOX Reviewed; 248 AA. AC P35049; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 117. DE RecName: Full=Trypsin; DE EC=3.4.21.4; DE Flags: Precursor; OS Fusarium oxysporum (Fusarium vascular wilt). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium oxysporum species complex. OX NCBI_TaxID=5507; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=8332590; DOI=10.1093/protein/6.4.341; RA Rypniewski W.R., Hastrup S., Betzel C., Dauter M., Dauter Z., Papendorf G., RA Branner S., Wilson K.S.; RT "The sequence and X-ray structure of the trypsin from Fusarium oxysporum."; RL Protein Eng. 6:341-348(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS). RX PubMed=15299338; DOI=10.1107/s0907444994009169; RA Rypniewski W.R., Dambmann C., von der Osten C., Dauter M., Wilson K.S.; RT "Structure of inhibited trypsin from Fusarium oxysporum at 1.55 A."; RL Acta Crystallogr. D 51:73-84(1995). RN [3] RP X-RAY CRYSTALLOGRAPHY (0.81 ANGSTROMS). RX PubMed=11134922; DOI=10.1107/s0907444900014116; RA Rypniewski W.R., Ostergaard P.R., Norregaard-Madsen M., Dauter M., RA Wilson K.S.; RT "Fusarium oxysporum trypsin at atomic resolution at 100 and 283 K: a study RT of ligand binding."; RL Acta Crystallogr. 57:8-19(2001). RN [4] RP X-RAY CRYSTALLOGRAPHY (0.80 ANGSTROMS). RX PubMed=12937176; DOI=10.1074/jbc.m306944200; RA Schmidt A., Jelsch C., Ostergaard P., Rypniewski W., Lamzin V.S.; RT "Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum RT chemistry revealing details of catalysis."; RL J. Biol. Chem. 278:43357-43362(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS). RX PubMed=19020355; DOI=10.1107/s0907444908030400; RA Leone P., Roussel A., Kellenberger C.; RT "Structure of Locusta migratoria protease inhibitor 3 (LMPI-3) in complex RT with Fusarium oxysporum trypsin."; RL Acta Crystallogr. 64:1165-1171(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; CC -!- SUBCELLULAR LOCATION: Secreted. 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; S63827; AAB27568.1; -; mRNA. DR PDB; 1FN8; X-ray; 0.81 A; A=25-248. DR PDB; 1FY4; X-ray; 0.81 A; A=25-248. DR PDB; 1FY5; X-ray; 0.81 A; A=25-248. DR PDB; 1GDN; X-ray; 0.81 A; A=25-248. DR PDB; 1GDQ; X-ray; 0.93 A; A=25-248. DR PDB; 1GDU; X-ray; 1.07 A; A=25-248. DR PDB; 1PPZ; X-ray; 1.23 A; A=25-248. DR PDB; 1PQ5; X-ray; 0.85 A; A=25-248. DR PDB; 1PQ7; X-ray; 0.80 A; A=25-248. DR PDB; 1PQ8; X-ray; 1.00 A; A=25-248. DR PDB; 1PQA; X-ray; 1.23 A; A=25-248. DR PDB; 1TRY; X-ray; 1.55 A; A=25-248. DR PDB; 1XVM; X-ray; 1.10 A; A=25-248. DR PDB; 1XVO; X-ray; 0.84 A; A=25-248. DR PDB; 2G51; X-ray; 1.84 A; A=25-248. DR PDB; 2G52; X-ray; 1.84 A; A=25-248. DR PDB; 2VU8; X-ray; 1.80 A; E=25-248. DR PDBsum; 1FN8; -. DR PDBsum; 1FY4; -. DR PDBsum; 1FY5; -. DR PDBsum; 1GDN; -. DR PDBsum; 1GDQ; -. DR PDBsum; 1GDU; -. DR PDBsum; 1PPZ; -. DR PDBsum; 1PQ5; -. DR PDBsum; 1PQ7; -. DR PDBsum; 1PQ8; -. DR PDBsum; 1PQA; -. DR PDBsum; 1TRY; -. DR PDBsum; 1XVM; -. DR PDBsum; 1XVO; -. DR PDBsum; 2G51; -. DR PDBsum; 2G52; -. DR PDBsum; 2VU8; -. DR AlphaFoldDB; P35049; -. DR SMR; P35049; -. DR MEROPS; S01.103; -. DR VEuPathDB; FungiDB:FOC1_g10004256; -. DR VEuPathDB; FungiDB:FOC4_g10005692; -. DR VEuPathDB; FungiDB:FOIG_10361; -. DR VEuPathDB; FungiDB:FOMG_09652; -. DR VEuPathDB; FungiDB:FOXG_13248; -. DR VEuPathDB; FungiDB:FOZG_15528; -. DR VEuPathDB; FungiDB:HZS61_010782; -. DR BRENDA; 3.4.21.4; 2351. DR EvolutionaryTrace; P35049; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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; Trypsin-like serine proteases; 2. 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 PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1. DR PANTHER; PTHR24276; POLYSERASE-RELATED; 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. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Hydrolase; Protease; Secreted; KW Serine protease; Signal; Zymogen. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT PROPEP 18..24 FT /note="Activation peptide" FT /id="PRO_0000028301" FT CHAIN 25..248 FT /note="Trypsin" FT /id="PRO_0000028302" FT DOMAIN 25..248 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 65 FT /note="Charge relay system" FT ACT_SITE 108 FT /note="Charge relay system" FT ACT_SITE 204 FT /note="Charge relay system" FT SITE 198 FT /note="Required for specificity" FT DISULFID 50..66 FT DISULFID 174..189 FT DISULFID 200..225 FT STRAND 39..44 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 47..56 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:1PQ7" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:1PQ7" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 82..91 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 93..98 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 110..116 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 141..147 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 162..169 FT /evidence="ECO:0007829|PDB:1PQ7" FT HELIX 171..178 FT /evidence="ECO:0007829|PDB:1PQ7" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 215..221 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 223..226 FT /evidence="ECO:0007829|PDB:1PQ7" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:1PQ7" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:1PQ7" FT HELIX 241..247 FT /evidence="ECO:0007829|PDB:1PQ7" SQ SEQUENCE 248 AA; 24576 MW; 1A0EBA88C3E70294 CRC64; MVKFASVVAL VAPLAAAAPQ EIPNIVGGTS ASAGDFPFIV SISRNGGPWC GGSLLNANTV LTAAHCVSGY AQSGFQIRAG SLSRTSGGIT SSLSSVRVHP SYSGNNNDLA ILKLSTSIPS GGNIGYARLA ASGSDPVAGS SATVAGWGAT SEGGSSTPVN LLKVTVPIVS RATCRAQYGT SAITNQMFCA GVSSGGKDSC QGDSGGPIVD SSNTLIGAVS WGNGCARPNY SGVYASVGAL RSFIDTYA //