TRYP_FUSOX
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 03-AUG-2022, entry version 114.
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}.
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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 PRIDE; P35049; -.
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; -; 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 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; 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
