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Database: UniProt
Entry: F2X559_ANOQN
LinkDB: F2X559_ANOQN
Original site: F2X559_ANOQN 
ID   F2X559_ANOQN            Unreviewed;       200 AA.
AC   F2X559;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=AGAP005195-like protein {ECO:0000313|EMBL:ADP20266.1};
DE   Flags: Fragment;
OS   Anopheles quadriannulatus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34691 {ECO:0000313|EMBL:ADP20266.1};
RN   [1] {ECO:0000313|EMBL:ADP20266.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21418586; DOI=10.1186/1471-2148-11-72;
RA   Mancini E., Tammaro F., Baldini F., Via A., Raimondo D., George P.,
RA   Audisio P., Sharakhov I.V., Tramontano A., Catteruccia F., Della Torre A.;
RT   "Molecular evolution of a gene cluster of serine proteases expressed in the
RT   Anopheles gambiae female reproductive tract.";
RL   BMC Evol. Biol. 11:72-72(2011).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC       {ECO:0000256|ARBA:ARBA00024195}.
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DR   EMBL; HQ332690; ADP20266.1; -; Genomic_DNA.
DR   VEuPathDB; VectorBase:AQUA016640; -.
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; PTHR24276:SF101; FI18310P1-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.
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..200
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003292767"
FT   DOMAIN          28..200
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   NON_TER         200
FT                   /evidence="ECO:0000313|EMBL:ADP20266.1"
SQ   SEQUENCE   200 AA;  22139 MW;  AAC0F13C06303E66 CRC64;
     MFLSGIVPLV LLVVHSLEAS PVEPLAPIIG GSNVEDEKVP YLVSITVNSI VCGGSIIADR
     WILTAAHCIK RNMVKNAAVR VETNNLTASG TLYRIDRAIA HEKYFRGAFR DDVGLLRLRS
     PLKFGERVKK IELLSQIVPN NATLTLVGRG YISKDHKTTK ITQMIKAKNI ALKLCRKMQP
     BFIYXGHLCT FVKKGKGTCR
//
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