ID   T1DGK1_ANOAQ            Unreviewed;       257 AA.
AC   T1DGK1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative chymotrypsin-2 {ECO:0000313|EMBL:JAA98844.1};
OS   Anopheles aquasalis (Malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=42839 {ECO:0000313|EMBL:JAA98844.1};
RN   [1] {ECO:0000313|EMBL:JAA98844.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole body {ECO:0000313|EMBL:JAA98844.1};
RG   Brazilian Malaria Network (MCT/CNPq/MS/SCTIE/DECIT/PRONEX 555648/2009-5) and Research Network on Bioactive Molecules from Arthropod Vectors (NAP-MOBIARVE;
RG   University of Sao Paulo);
RA   Marinotti O., Ribeiro J.M.C., Costa-da-Silva A.L., Silva M.C.P.,
RA   Lopes A.R., Barros M.S., Sa-Nunes A., Konjin B.B., Carvalho E., Suesdek L.,
RA   Silva-Neto M.A.C., Capurro M.L.;
RT   "Transcriptome sequencing and developmental regulation of gene expression
RT   in Anopheles aquasalis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036320};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC       {ECO:0000256|ARBA:ARBA00024195}.
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DR   EMBL; GAMD01002746; JAA98844.1; -; mRNA.
DR   AlphaFoldDB; T1DGK1; -.
DR   MEROPS; S01.166; -.
DR   VEuPathDB; VectorBase:AAQUA_000873; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
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:SF100; AT20289P-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   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..257
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004574358"
FT   DOMAIN          33..255
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   257 AA;  27920 MW;  85B9152B46B4F8CF CRC64;
     MLRGITVLSA ICLMVGANNI PKLVLDDHYV NRVVGGQEAE EGSAPYQVSL QVSFWGHNCG
     GSIISERWVL TAAHCLVGND PEELEVLVGT NSLKEGGERY KVDKLFTHSR YNRPQFHNDI
     GLVRLATPIK FSSTVKSIEY SEHVVPVNAT VRLTGWGRTS AGGSVPTKLQ TIDLRTLSNE
     DCKKKSGDPR NVDIGHVCTL TRTGEGACNG DSGGPLVYDD KVIGVVNFGV PCALGYPDGF
     ARVSYYHDWI RTTVANN
//