GenomeNet

Database: UniProt
Entry: B0XE90_CULQU
LinkDB: B0XE90_CULQU
Original site: B0XE90_CULQU 
ID   B0XE90_CULQU            Unreviewed;       388 AA.
AC   B0XE90;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN   Name=6051539 {ECO:0000313|EnsemblMetazoa:CPIJ017564-PA};
GN   ORFNames=CpipJ_CPIJ017564 {ECO:0000313|EMBL:EDS25864.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS25864.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS25864.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ017564-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ017564-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   EMBL; DS232812; EDS25864.1; -; Genomic_DNA.
DR   RefSeq; XP_001867962.1; XM_001867927.1.
DR   AlphaFoldDB; B0XE90; -.
DR   STRING; 7176.B0XE90; -.
DR   MEROPS; S01.A67; -.
DR   EnsemblMetazoa; CPIJ017564-RA; CPIJ017564-PA; CPIJ017564.
DR   KEGG; cqu:CpipJ_CPIJ017564; -.
DR   VEuPathDB; VectorBase:CPIJ017564; -.
DR   VEuPathDB; VectorBase:CQUJHB002927; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; B0XE90; -.
DR   OMA; RQFETDC; -.
DR   OrthoDB; 4629979at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24256:SF575; MIP04821P; 1.
DR   PANTHER; PTHR24256; TRYPTASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 2.
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.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          15..386
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          150..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..177
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  43510 MW;  30266BFF4881E70D CRC64;
     MADTDPDGPN RNPKIMHGVP TLEGQYPWQV SLELMHPSYG FIGHWCGGVL IDRNWVLSAA
     HCVHNELFNL PLPALWTVVL GEYDRGRESG YEQRIPVDKI ILHEKYHNFK HDLVLLKLNR
     PANIAPNSRV KKICLPQLFY FDYLGRPPDK GGGRPVEEDG PTKEDVVDEE SELNAEDAST
     DFPDALPDRE DNYLRRLRLL GESGAPEYRR PRTARVVVNQ LVRKRLQQSP SSELVGNATR
     ARSESASRRS FRRGRRLDAE PISAIPDTSQ YVDCLATGWG KSTIDDELTD ILLQTKAPIQ
     NSKKCEEAYG DFIKLHRGHL CAGNLDGTGG TCVGDSGGPL QCRITKHGPW ILVGITSFGS
     GCAFKNYPDV YTKISFYRQW IVDTIQGN
//
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