ID A0A484B5L3_DRONA Unreviewed; 265 AA.
AC A0A484B5L3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN ORFNames=AWZ03_009636 {ECO:0000313|EMBL:TDG43939.1};
OS Drosophila navojoa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG43939.1, ECO:0000313|Proteomes:UP000295192};
RN [1] {ECO:0000313|EMBL:TDG43939.1, ECO:0000313|Proteomes:UP000295192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG43939.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:TDG43939.1};
RX PubMed=30423125; DOI=.1093/jhered/esy059;
RA Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT the mojavensis Cluster.";
RL J. Hered. 110:118-123(2019).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDG43939.1}.
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DR EMBL; LSRL02000124; TDG43939.1; -; Genomic_DNA.
DR RefSeq; XP_017959098.1; XM_018103609.1.
DR AlphaFoldDB; A0A484B5L3; -.
DR STRING; 7232.A0A484B5L3; -.
DR GeneID; 108653249; -.
DR KEGG; dnv:108653249; -.
DR OMA; GTGCARE; -.
DR OrthoDB; 2910936at2759; -.
DR Proteomes; UP000295192; 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; 1.
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; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
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:UP000295192};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..265
FT /note="Peptidase S1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019839261"
FT DOMAIN 31..254
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 265 AA; 28355 MW; E79D78959E68A130 CRC64;
MIRILIGCFI VGLSVAGTVF QSGVPMPDGR IVGGYDADIT SYPHQVSMRY RGNHRCGGSI
IAPNMILSAA HCVNTLKGVA NLTIIAGTTE TFFPTGQELP VREIIIHEKY KSLYQDYDAA
ILVLDGEFEY NKAVQPIELA SERPAHGTPV IVTGWGATTE GGALSNVLQQ VEVNVVENAK
CKSAYFIALT NRMLCAAVDG GGKDSCQGDS GGPLIYKNEL LGIVSWGSGC ARKGYPGVYA
AIPDLRQWII NTRASKASVG RIEFL
//
