ID A0A0V0TL17_9BILA Unreviewed; 730 AA.
AC A0A0V0TL17;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Chymotrypsinogen B {ECO:0000313|EMBL:KRX39721.1};
GN Name=Ctrb1 {ECO:0000313|EMBL:KRX39721.1};
GN ORFNames=T05_13602 {ECO:0000313|EMBL:KRX39721.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX39721.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX39721.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX39721.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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:KRX39721.1}.
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DR EMBL; JYDJ01000224; KRX39721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TL17; -.
DR STRING; 144512.A0A0V0TL17; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048}.
FT DOMAIN 270..331
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 581..730
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 730 AA; 82475 MW; 8EE36D1AACC6A7E1 CRC64;
MSGRWRRMDF EHFKYFNTAW EENLLANDDN CHNSTASYFR CYLAELDPLL VSLTKTDNNT
EKASGCRHPD LSINTHLVSI SGPDAENFTH VLNCFIETSH QMVSAALDYV TKNMGIIGLN
YDTVKKIQLT DRNPITNARI SEIIHINTAL EDESLCTEEQ RRAAIDCIEM LEKSDEEERQ
KIQQSICKMK YECFSGIESP CQENVHFNRM SLSQLACGAL KFSKFNEQLS SCVGWSVTPE
VEPFIDHVLN DLAEPLCEMF ILFSDSCSSC GGNIELELGQ VVQIMSPNYY QTMTSPNCTW
NVHSKSKVVQ LHVDSLFTSS SSSSSEFSQY CVDVFRLKTR SNMHLVTSCK PVPFVDLIIG
EEVPFNFTLW YSNVYGQRPR AFSLRLSCAP VEPIFDNSQC TETFHLKNLS SSLTLRTPNW
PDKFPPQIHC NWTIYNELYQ NNCFFQVRFP RFNTLPVGQF IKIQNEIGMQ RQISGRTPST
HVEQFDGKVL NVEFVESFNT EGEAVSIEIN LITDEQFCYA NQIKCPNGGK CIEKSQICDE
QVDCEDASDE KLSLCRTKAQ CGVQNIPPTV ENKPKMAYLR IVNGTQARPG SWPWIASLQA
KFSNKHFCGA TLISARWLLT AKHCVIGADP EDLVVRLGAH DLASNTGVVM DVSNVYYIPE
HSFNPVLHDI ALLKLEQDVP TPFVNNINVA CLPDSNEKLL PETPCVAVGW GKTNWTRWCS
ASGSVARYKA
//
