ID A0A182PPF0_9DIPT Unreviewed; 663 AA.
AC A0A182PPF0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI008829-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI008829-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI008829-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; A0A182PPF0; -.
DR STRING; 199890.A0A182PPF0; -.
DR EnsemblMetazoa; AEPI008829-RA; AEPI008829-PA; AEPI008829.
DR VEuPathDB; VectorBase:AEPI008829; -.
DR OrthoDB; 3431658at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF149; CLIP DOMAIN-CONTAINING SERINE PROTEASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..663
FT /note="Peptidase S1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008131688"
FT DOMAIN 236..491
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 663 AA; 73899 MW; A9021CBEC90C2608 CRC64;
MQSRVKLTLV AVVLWASVLH QPRTALGATD SGLPDFELDD GKDDADDEYY YVNDGTDQQM
QPSHKILSYA KPPPAPANGP AVPSAGQIDA SEPFLMEDDD TSFEVMDEVD FVEQGAEDFR
RKAERMKRIM LKAFANREFQ RKFGEVLPLL KVMSKTQKST LAALITAQVN SREGHTLSLE
QSCPRPDLFK FFYSQKTECM GIRVVPERFS LLVTVKQYNT RCLLTMGKCL LLCLLVLAGS
VGSLAQTPTL LRDTIWGEFP SVVLVKTPRE NQFCLGTVLN ANHVLTSAFC VLTDDRTRIF
TPRLVRVIAG DISVAPVAAT RQTRTAHHIF VHEAYRPHTF ENNIAVIRLA EPFHMPSNAI
EAAVIRLRIV PDNHPCDMVT WYRLVGTGNP PSLDIPRQQA FNVNIRNRDA CANERRAELT
IEESTLCTYT TITMAGIVQG DPMFCDGQLT AIQSFVFYPP GQQQQPPAQG QQNLVSTQVR
FYLHWINNQL NRTQPMPDGW NPASDSADIM VKLVLASFLL LGAVVTSSAQ TVIRSPVFGE
FPSVVFVSTP RHQRCIGTVI NANHVLTSAF CVMTDGATRV YPARLVRVIG GDLSATNPVD
TQQMRTGLHI FVHENYRVNS RDNNVAIIRL AEPFHLPSNG IEEAHVRMRI VPQGHQCYVT
RPA
//
