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Database: UniProt
Entry: A4V9W6_DROSI
LinkDB: A4V9W6_DROSI
Original site: A4V9W6_DROSI 
ID   A4V9W6_DROSI            Unreviewed;       503 AA.
AC   A4V9W6;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=CG9649 protein {ECO:0000313|EMBL:CAL85489.1};
GN   Name=CG9649 {ECO:0000313|EMBL:CAL85489.1};
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000313|EMBL:CAL85489.1};
RN   [1] {ECO:0000313|EMBL:CAL85489.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KY215 {ECO:0000313|EMBL:CAL85489.1};
RX   PubMed=17465907; DOI=10.1111/j.1420-9101.2007.01305.x;
RA   Jiggins F.M., Kim K.W.;
RT   "A screen for immunity genes evolving under positive selection in
RT   Drosophila.";
RL   J. Evol. Biol. 20:965-970(2007).
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DR   EMBL; AM412866; CAL85489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4V9W6; -.
DR   MEROPS; S01.A44; -.
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; 1.
DR   InterPro; IPR031986; GD_N.
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; PTHR24260; -; 1.
DR   PANTHER; PTHR24260:SF153; GH19262P-RELATED; 1.
DR   Pfam; PF16030; GD_N; 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   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..503
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002673927"
FT   DOMAIN          256..502
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          170..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..208
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  56352 MW;  B9B86559924BF22D CRC64;
     MRQLQLLGFL IAVLQISYIS AQHLPYIQCP MIFRYLEYEN QFIGHLQLIL DSTNTDNVVR
     VELSQPGRNT PSTPGTLNFL EDEDSLRHRL TNNEPINYRI DFPTPGVVPK LTKVTVNGKV
     ACEAAPFRAP STRLTLSRTL RTTVPLAAIP PSQRTDHQWP QAPQTNYTVY EEEEEEPVQR
     RRPQQSPPRP RPQQPPSRPR PQPVPQLPQE PKFQTSARPS VLPSNPPAQV SKSYPQTIGQ
     LSGICGREKV IQTPFIHNGI EVERGQLPWM AALFEHVGRD YNFLCGGTLI SARTVISAAH
     CFRFGSRNLP GERTIVSLGR NSLDLFSSGA TVGVARLLIH EQYNPNVYTD ADLALLQLAN
     HVDIGDYIKP ICLWNENFLL ELPSGHKSYV AGWGEDEKGN RNTRLAKMTD TDIITQWECR
     GNLSEENAKF ITSHTICASN AQASGPCSGD SGGGLMLQEQ DIWMLRGVVS AGQRMTNRCN
     LTLPVIYTDV AKHIEWLVSS MWF
//
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