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Database: UniProt
Entry: A0A182JGR8_9DIPT
LinkDB: A0A182JGR8_9DIPT
Original site: A0A182JGR8_9DIPT 
ID   A0A182JGR8_9DIPT        Unreviewed;       394 AA.
AC   A0A182JGR8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Anopheles atroparvus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=41427 {ECO:0000313|EnsemblMetazoa:AATE017795-PA.1, ECO:0000313|Proteomes:UP000075880};
RN   [1] {ECO:0000313|EnsemblMetazoa:AATE017795-PA.1}
RP   IDENTIFICATION.
RC   STRAIN=EBRO {ECO:0000313|EnsemblMetazoa:AATE017795-PA.1};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC       {ECO:0000256|ARBA:ARBA00024195}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   AlphaFoldDB; A0A182JGR8; -.
DR   STRING; 41427.A0A182JGR8; -.
DR   EnsemblMetazoa; AATE017795-RA; AATE017795-PA.1; AATE017795.
DR   VEuPathDB; VectorBase:AATE017795; -.
DR   OrthoDB; 2877984at2759; -.
DR   Proteomes; UP000075880; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   PANTHER; PTHR24256:SF549; -; 1.
DR   PANTHER; PTHR24256; TRYPTASE-RELATED; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01180; CUB; 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}.
SQ   SEQUENCE   394 AA;  43274 MW;  165806001FBE3CD8 CRC64;
     MWFNLVLVVL LVLGGSFVRQ VQGQCSFTLD MKFGSVYQLI SPRFPSNYPP NLQCTYVIRA
     PYGYRIALDC PTFQIPSSTN CRLDSFKVSR TGRLDLSDGY SYCGAGRLQE KSDANQMTIR
     LTSAATSSGG RFQCNLSVPA QSCECGRKKT QRIVNGVETV VNEFPMMAAL IDISRKNVIC
     GATIVTNNYA LTAAHCLLLR SINDTVLLVG DHNIRTGSDT SYAQVYVVAQ FLSHTGFTVK
     PVQNDIALVR TQQTIQYNPG VGPACLPWRY TTETFAGSTI EATGWGDLDF GGPRAEALNK
     VQLAVISNTD CSRRLETTVP YQQLCTFTPN RDTCQADSGG PLFYTNPSTG LLYNVGIVSF
     GFACATDRPS VNTRVTEFLD WITANSPTSF YCYQ
//
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