ID A0A182N933_9DIPT Unreviewed; 774 AA.
AC A0A182N933;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR004157-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., 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 dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR004157-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR004157-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; A0A182N933; -.
DR STRING; 7168.A0A182N933; -.
DR EnsemblMetazoa; ADIR004157-RA; ADIR004157-PA; ADIR004157.
DR VEuPathDB; VectorBase:ADIR004157; -.
DR OrthoDB; 3410499at2759; -.
DR Proteomes; UP000075884; 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; 4.
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; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF149; CLIP DOMAIN-CONTAINING SERINE PROTEASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 3.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
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 Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 46..260
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 293..529
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 774 AA; 87180 MW; B0BAD8AE822F856E CRC64;
CDVRFFKEQT ASFAAPVASQ PAYLREFAHI AAIGWTQPNG NVVWGCGGSL VWENFILTAA
HCSADDNDVP PDVARMGDIN IYSDEDDEFA QELKIVDIVR HPKHRFGRKY YDIALMKLER
NVSVHETVAP TCLWVDDEIR FPKLLAAGWG AIGIGEKHTE TLMKVEVAPV SNAECSRYHV
AGELGLKQGL QDDQMCAVDK EMDTCPGDSG GPLHVKLFKD KKMIPFLVGV TSFGKACGLS
VPSVYVKVSK FVDWIVETLQ QHGELATRFK FEPLVCTDRY YYLREYKEDI GKVINGIEYI
DLSILYVSLR MSDFIVDFRW KDTSFMRPDC FGTLIEPNIV VTLAQCVMDR RTNPTQVVLN
SSRAIDIVDI IVHPAYKPST DPYYNNIAVV KLESYAYIEP YCVWYGNHNP GMNVLLTGKR
LIPEEHTTIP HHITIMTRGN ERTSEQCHLA QRYISALREG LKEEHLCFEN QPFIVPESCE
LKLGGPIERK YGKVFIDGIN LFGRDCGYGE PAVGVRLSAH KAWLESVLLP QPLNTVLYID
SDLFAGDKCR YADGTAGLCV PQTQCSNIHE RIRTQKQIIF CKTGSVVCCP QTPTNLQTIE
REFNECEQRY LHLRTKEYDF KAHVVEIGWK NNVNTATNCL GYLISTRGVV TSASCLRAMS
VSQKIVKLGG DQFIGIEAVK FHPKYSQTTN WHNVAVVKLV SAVQPSVTAF PGCLWMNVTH
SPVLQFILNV DSAKYDPIHP MYKSDCEGLL KLSFDESETI CMNPDHPLQQ KKIL
//