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Database: UniProt
Entry: A0A232EUP1_9HYME
LinkDB: A0A232EUP1_9HYME
Original site: A0A232EUP1_9HYME 
ID   A0A232EUP1_9HYME        Unreviewed;       271 AA.
AC   A0A232EUP1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN   ORFNames=TSAR_000682 {ECO:0000313|EMBL:OXU22036.1};
OS   Trichomalopsis sarcophagae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC   Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX   NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU22036.1, ECO:0000313|Proteomes:UP000215335};
RN   [1] {ECO:0000313|EMBL:OXU22036.1, ECO:0000313|Proteomes:UP000215335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alberta {ECO:0000313|EMBL:OXU22036.1,
RC   ECO:0000313|Proteomes:UP000215335};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXU22036.1};
RX   PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA   Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT   "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL   Curr. Biol. 27:2007-2013(2017).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXU22036.1}.
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DR   EMBL; NNAY01002116; OXU22036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A232EUP1; -.
DR   STRING; 543379.A0A232EUP1; -.
DR   Proteomes; UP000215335; Unassembled WGS sequence.
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; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24276:SF97; GH13245P2-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.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..271
FT                   /note="Peptidase S1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012218119"
FT   DOMAIN          17..266
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   271 AA;  29421 MW;  A5545910D357D795 CRC64;
     MSKLLLVVLY ILWCETIAAG ISQPTLQRRK HVDIADFPYH VSVRRAGRHV CSGALVHESW
     IITAASCVYD SSVPRVSVAM GSSELQLPRH RFNVSKIVVH QTFDKDLLTG NIALLEIKPS
     VSFVDSNLLP IFLPSSENYH LKDGSVLRVS GWARLQRAQK EKPDAAAAKL HSGGFESQLS
     VTGASLVNQR TCIRSMPSYK AVSGKMLCAG NPNAKETCQG DIGAPLANHD ILVGILSLAD
     GCLASSYPAV YTKISSFLPW IAKILSLHTS E
//
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