ID   Q1M2L7_LEPDS            Unreviewed;       260 AA.
AC   Q1M2L7;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   10-FEB-2009, entry version 13.
DE   SubName: Full=Allergen Lep d 3;
OS   Lepidoglyphus destructor (Fodder mite).
OC   Eukaryota; Metazoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Glycyphagoidea; Glycyphagidae;
OC   Lepidoglyphus.
OX   NCBI_TaxID=36936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Chew F.T., Angus A.C., Lim S.H.;
RT   "Cloning of allergens from the storage mite Lepidoglyphus
RT   destructor.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
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DR   EMBL; AY291571; AAQ55487.1; -; mRNA.
DR   MEROPS; S01.234; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 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   Hydrolase; Protease; Serine protease.
SQ   SEQUENCE   260 AA;  26927 MW;  25579FAC4372CFA6 CRC64;
     MKFLVLLCLV SAAIAGPLSD LKPRYLVASK FGQTKDSKDG YIVGGSAVAS GEATYQVSLQ
     RSSHFCGGTI IDDYWVLTAA HCVSGTSASQ LKVRYNTVRH NSGGSLISVS EVIAHSGYSS
     WTLDNDIALL KTSSPMTGIK KADLPVSGSD VSGSVLVTGW GYTTEGGSLA SSLQKVSVPV
     VDRAQCNSSY SGDITPNMFC AGVSAGGKDS CQGDSGGPVV SGNTVVGAVS WGMGCARPNY
     PGVYTRVGNF REWIKTNSGL
//