ID   SCLXB_HELVI             Reviewed;         288 AA.
AC   C1JE15;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Scolexin B {ECO:0000312|EMBL:ACO55200.1};
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102;
RN   [1] {ECO:0000312|EMBL:ACO55200.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Larval hemolymph {ECO:0000269|PubMed:19442669};
RX   PubMed=19442669; DOI=10.1016/j.jip.2009.05.002;
RA   Shelby K.S., Popham H.J.R.;
RT   "Analysis of ESTs generated from immune-stimulated hemocytes of larval
RT   Heliothis virescens.";
RL   J. Invertebr. Pathol. 101:86-95(2009).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 237-249.
RC   TISSUE=Hemolymph;
RA   Shelby K.S.;
RL   Submitted (SEP-2009) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; FJ561484; ACO55200.1; -; mRNA.
DR   AlphaFoldDB; C1JE15; -.
DR   SMR; C1JE15; -.
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; -; 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   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Serine protease; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..288
FT                   /note="Scolexin B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000386591"
FT   DOMAIN          21..287
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          27..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        87
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UL52"
FT   ACT_SITE        145
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UL52"
FT   ACT_SITE        239
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UL52"
FT   DISULFID        72..88
FT                   /evidence="ECO:0000250|UniProtKB:Q9UL52,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        210..223
FT                   /evidence="ECO:0000250|UniProtKB:Q9UL52,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        235..264
FT                   /evidence="ECO:0000250|UniProtKB:Q9UL52,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   288 AA;  30561 MW;  907315D5EDB6C024 CRC64;
     MFASKLAVCS ALALLAVAHA APGGNDIQKI TKAPNVPTKA EGDAASKASA PAIPPKPVNE
     RFPHAVLFGG TCGGTIISPT WILTAGHCTL FTGGRYILAG TNNTDNPNAV TRHVKRQVIH
     PLFSVGPYWL DADDFNIKQV AARWDFLLAE LSEPLPLDGK LMAAAKLDDQ PSLPVGLNVG
     FGGYGTDHFG GTMRSEMHGM ELAVQSDEVC STLEQYNSKD MLCVKGRPPR FDSACNGDSG
     SGLVDETGRV IGVASWVEND AHSCFNGALV VFSRVASVRD WIKKVTNI