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Database: UniProt
Entry: Q8T4T5_AEDAE
LinkDB: Q8T4T5_AEDAE
Original site: Q8T4T5_AEDAE 
ID   Q8T4T5_AEDAE            Unreviewed;       268 AA.
AC   Q8T4T5;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Chymotrypsin-like protein {ECO:0000313|EMBL:AAL85583.1};
GN   Name=CHYM {ECO:0000313|EMBL:AAL85583.1};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159 {ECO:0000313|EMBL:AAL85583.1};
RN   [1] {ECO:0000313|EMBL:AAL85583.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MOYO-R {ECO:0000313|EMBL:AAL85583.1};
RA   Morlais I., Severson D.W.;
RT   "Single nucleotide polymorphism and codon usage bias in Aedes aegypti.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC       {ECO:0000256|ARBA:ARBA00024195}.
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DR   EMBL; AY064082; AAL85583.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8T4T5; -.
DR   VEuPathDB; VectorBase:AAEL003060; -.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR   PANTHER; PTHR24250:SF65; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 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.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..268
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004314291"
FT   DOMAIN          26..267
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   268 AA;  29018 MW;  68F4886C732C732E CRC64;
     MAFKLTVAFL LVASLALASS RATHKIVGGD EAEAHEFPYQ ISLQWNFNDG QTETMHFCGA
     SVLNENFVLT AAHCKTAYSN TGFIEVVADE HDVAVAEGSE QRRLVAEFIV HEDYQGGVSP
     DDIAVIRVDK PFELNDKVKA VKLPKQLEQF EGDVTLSGWG SVSTTVFPDY PDKLRKVVLP
     LVDYEQCNAL WDNDSALAKS NVCAGPIDGS KSACSADSGG PLVKQSGEDV IQVGVVSWGA
     VPCGSPRRPT VFAGVSHYVD WIEQQLRA
//
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