ID   U4TWR6_DENPD            Unreviewed;       338 AA.
AC   U4TWR6;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=trypsin {ECO:0000256|ARBA:ARBA00038868};
DE            EC=3.4.21.4 {ECO:0000256|ARBA:ARBA00038868};
GN   ORFNames=D910_03448 {ECO:0000313|EMBL:ERL86034.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL86034.1, ECO:0000313|Proteomes:UP000030742};
RN   [1] {ECO:0000313|EMBL:ERL86034.1, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036320};
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DR   EMBL; KB631778; ERL86034.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4TWR6; -.
DR   STRING; 77166.U4TWR6; -.
DR   Proteomes; UP000030742; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; PTHR24264; TRYPSIN-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   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034}.
FT   DOMAIN          11..276
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   338 AA;  38159 MW;  87C82873E028CD8A CRC64;
     MFRFNRVSVY MVLWTINNAH ETHPYMASLH FFHTHLCGAS IISNRWLVTA AHCTTLDLRY
     SNNAIRGFTI RVGTGLLETG GQEVSVLKLY DHPLFLNSFP VGFDYDISLL YLEKDLTLST
     TVQPIRMLEI DENYPAATVV TVIGWGLQHE YGLFLAEILQ EVAVPLVSNE DCLTLYNTVG
     FSSWVTDRMI CAGHEEGEKD ACAGDSGGPL ITNNSLIGVV SWGYGCARAG FPGVYAISQN
     RKLRIAAKVP YFVRNSTLQR DLKTDDLLDH IRNLTSKFLD NARQSKNPTV RVTCKKTQFK
     KKTWTTCDDQ LLHHIEDHGL TLITWSVRHS NDVRFKNP
//