ID Q58I79_BOMMO Unreviewed; 284 AA.
AC Q58I79;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:AAX39409.1, ECO:0000313|EMBL:ABC26003.1};
GN Name=sp-2 {ECO:0000313|EMBL:AAX39409.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:AAX39409.1};
RN [1] {ECO:0000313|EMBL:AAX39409.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Midgut {ECO:0000313|EMBL:AAX39409.1};
RA Wu X., Cao C., Xia Z., Zhou L., Lu X.;
RT "Cloning and molecular characterization of sp-2, an antiviral protein in
RT silkworm.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABC26003.1}
RP NUCLEOTIDE SEQUENCE.
RA Wu X., Yao H., Cao C., Zhao N., Lu X.;
RT "SP-2 isolated from the silkworm Bombyx mori.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; AY945211; AAX39409.1; -; mRNA.
DR EMBL; DQ310733; ABC26003.1; -; Genomic_DNA.
DR AlphaFoldDB; Q58I79; -.
DR MEROPS; S01.040; -.
DR HOGENOM; CLU_006842_7_6_1; -.
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 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:AAX39409.1};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..284
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010139851"
FT DOMAIN 51..284
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 284 AA; 29646 MW; 2D82B4B7112F31FE CRC64;
MKVFAAVLMA LAAVVVAEEA IELDYHTKIG IPRAESLKRA EEAADFDGTR IVGGSAANAG
AHPHLAGLVI ALTNGRTSIC GASLLTNTRS VTAAHCWRSR DAPARQFTLA FGTANIFSGG
TRATTSSVHM HGSYNMNNLH NDVAVINHNH VGFNNNIQRI NLASGSNNFA GTWAWAAGFG
RTSDAASGAN NQRKRQVSLQ VITNAVCART FGNTLIIGST LCVDGSNGRS TCRGDSGGPL
TIGSGGGRQL IGITSFGSAQ GCQRGFPAAF ARVTSFNSWI RARI
//
