GenomeNet

Database: UniProt
Entry: W5JCC9_ANODA
LinkDB: W5JCC9_ANODA
Original site: W5JCC9_ANODA 
ID   W5JCC9_ANODA            Unreviewed;       384 AA.
AC   W5JCC9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN   ORFNames=AND_007893 {ECO:0000313|EMBL:ETN60484.1};
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:ETN60484.1};
RN   [1] {ECO:0000313|EMBL:ETN60484.1, 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:ETN60484.1}
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:ETN60484.1}
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:ADAC007893-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; ETN60484.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5JCC9; -.
DR   STRING; 43151.W5JCC9; -.
DR   EnsemblMetazoa; ADAC007893-RA; ADAC007893-PA; ADAC007893.
DR   VEuPathDB; VectorBase:ADAC007893; -.
DR   VEuPathDB; VectorBase:ADAR2_006526; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_720070_0_0_1; -.
DR   OMA; CYVVGWS; -.
DR   OrthoDB; 3442002at2759; -.
DR   Proteomes; UP000000673; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR041515; PPAF-2-like_Clip.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR   Pfam; PF18322; CLIP_1; 1.
DR   Pfam; PF00089; Trypsin; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..384
FT                   /note="Peptidase S1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010155200"
FT   DOMAIN          118..367
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          91..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  43545 MW;  473AAC6F7C3833B2 CRC64;
     MDRFCWRRHV VVVLLSVLSV NRGAWADTRC LRENEICVPT ESCLYGIVNE AAAFIMVPRF
     GEDDECEDDD QVCCKKVPVT ANTYSVITTT ETPAVNSESE EEEEEHDWSE QCGKNANITE
     STGFLTNRRE FPWSVAIFRI ALVAGRTKNI FLCGGTLLED GTVLTSVECV RHQPKASLRV
     QFGRWDLGES NERGTKVLEV EEIVIHQDYK PSSKQDNIAL LFLADNVRFG PSVNRVCIGE
     KKHRYDTDYH CYTVGWGTRF INGANRLQKM KTFLAPTNEC QESIRRHTLL SRFELSPKDV
     CTDAVDAMGT DYPCARITGS ALVCAKNNQY FLVGIASYSL RKCSRTNVND VFVDVREYSA
     WIDGHIRSRF REPSTYRPVP VESD
//
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