ID A0A182REW3_ANOFN Unreviewed; 309 AA.
AC A0A182REW3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase S1 domain-containing protein {ECO:0000313|EnsemblMetazoa:AFUN004741-PA};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN004741-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN004741-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN004741-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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DR AlphaFoldDB; A0A182REW3; -.
DR STRING; 62324.A0A182REW3; -.
DR EnsemblMetazoa; AFUN004741-RA; AFUN004741-PA; AFUN004741.
DR VEuPathDB; VectorBase:AFUN004741; -.
DR VEuPathDB; VectorBase:AFUN2_003944; -.
DR OrthoDB; 3430312at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF155; GH03360P-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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..309
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021500987"
FT DOMAIN 46..306
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 309 AA; 34916 MW; BA611CDD5D4FC0E0 CRC64;
MYNRVVVHIV LAVLLLLNLC DVRGLRLAEQ KCQEYRSTIA SFRSKMTGRT NNYETPPNGI
PATEGEFPHQ VRVGQWFYED EDTEHIFRCG GALISDRYVL VSGHCFWTMG DKMASLGRHD
YTRNSTLPEV LLKRDDLILH PAIDETVKAS YNDIGLLRLA EPVTFTSHIY PACLWTEDNL
PETQKFTVTG FTTGKLVNDT EDTRLVKVQM NRVSNDECTQ MYADSGYYPQ GVTDSFLCAA
SPVEWKASCD GDGGGLMQTL DDESGDVYRL IGLEAKGHDC DQPHQSYVYT YSLVQKHLDW
IESVVWSTS
//
