ID W5JAQ5_ANODA Unreviewed; 405 AA.
AC W5JAQ5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=CLIP-domain serine protease subfamily A {ECO:0000313|EMBL:ETN60483.1};
GN ORFNames=AND_007892 {ECO:0000313|EMBL:ETN60483.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN60483.1};
RN [1] {ECO:0000313|EMBL:ETN60483.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN60483.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN60483.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC007892-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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DR EMBL; ADMH02001924; ETN60483.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JAQ5; -.
DR STRING; 43151.W5JAQ5; -.
DR EnsemblMetazoa; ADAC007892-RA; ADAC007892-PA; ADAC007892.
DR VEuPathDB; VectorBase:ADAC007892; -.
DR VEuPathDB; VectorBase:ADAR2_000934; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_0_3_1; -.
DR OMA; VILRETM; -.
DR OrthoDB; 3436700at2759; -.
DR Proteomes; UP000000673; 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; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR041515; PPAF-2-like_Clip.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24256; TRYPTASE-RELATED; 1.
DR PANTHER; PTHR24256:SF565; ZGC:92313-RELATED; 1.
DR Pfam; PF18322; CLIP_1; 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:0000313|EMBL:ETN60483.1};
KW Protease {ECO:0000313|EMBL:ETN60483.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..405
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010155111"
FT DOMAIN 134..385
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 78..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 405 AA; 44993 MW; 264E08DEFA69BF10 CRC64;
MAKRSARTSS GLFYAALVLL ASVVLTRSED IETCIKASKP GVCVYKYRCK DGYIIEFGEG
LIDIRSSDVC GNPLMECCQE PEEPNENTTV DPSTNDTSTD RGTSTTVAPP GPIVPPYQQQ
QCGQRNPNGV IFKIENNVFS ESEYGEFPWV VAIFRLTGEP KPQFLCSGTL IDVAAVLTTA
SCFQRYRGAG NKFMVRMGEW DLSNDREPIP TVEREVETLH IHPRYSVRDK VNDIAVIILS
DSVQLTHTIG LACLPDASLR FNDIVGVGWG DAPSFLQPQK LPQTILKKSQ LTVIGAQQCQ
RTMRKLITPR YTLSDSFICA EGHAPEMLPC KGDSGSPYMV SIPTEQERYF VVGLSSWGFD
CNVQDAPTVL TNVGYHREWI DQIISTEGLS PFSYTYHQQE EDDDD
//
