ID A0A0V1CWY0_TRIBR Unreviewed; 1223 AA.
AC A0A0V1CWY0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Chymotrypsinogen B {ECO:0000313|EMBL:KRY53598.1};
GN Name=Ctrb1 {ECO:0000313|EMBL:KRY53598.1};
GN ORFNames=T03_2293 {ECO:0000313|EMBL:KRY53598.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY53598.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY53598.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY53598.1};
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:KRY53598.1}.
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DR EMBL; JYDI01000083; KRY53598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CWY0; -.
DR STRING; 45882.A0A0V1CWY0; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR007026; CC_domain.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR006150; Cys_repeat_1.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF04942; CC; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00089; Trypsin; 1.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SMART; SM00289; WR1; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
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:UP000054653}.
FT DOMAIN 53..177
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 187..301
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 325..604
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 865..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..994
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1082
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1223 AA; 139025 MW; E4F1C3EE46974236 CRC64;
MMCRLQMNAD SKHFFMASVC TAFAYLSQHL FVCSVTQVSI NCKIVQSEEF VNCGDIYTLV
DNSILRVVSP NYPEKGYPNN ANCLWQIRCK VNMVKMEMKF FELEQYDNYT CPDRLWLSWP
GDVQQEAELQ QQLNNHGCNS WPEKLIFKHQ APFSFNLTFQ SDEQFRYRGF ELEITGKDLG
PPVPADCGRT YRLKKRNTKF ALHTPNWPLN YPKNSKCKWT IENPLHDQGH YIKMEMIHFD
TLQPHHMLII HSKDDETRHQ FTGQINNKNK LYFFKTERLE ILFLSDNNYY DGKFHIEVST
TKQAECPRTK VRCPGTDICI PMKSICDGEI DCPGEHDENL SVCNVHKNCG KQQIPLNIEL
KESIATKAKP GSWPWAVSIH SYTFPKQVLC EATLISPKWI LTTAYCALKI SKNTAEYFVR
IGSYWSNEME ESWEFDSNIT NFYFHPDHQS DNKNDIALIL LQNEVPIPFN KRVNIACLPE
IDIPLGRRPK YANTGWGSTD LDNKKQPLYQ AITSPLSIYK CNSTLKWFQP ITNHMLCSFY
KKPENLDILN KGGPYMCKND ESSQWQLHGT IMNYTRAWDE EEEDEEKVGI LHILFTDGSE
RNETNLEPNG KTLTNRSMTS VKLTRRQQLR IMLGYCSNGN QVVAACFPNY RCGRGPVTGL
PYGIWKPTIP TSSLFCRDGS PAVSRCHLNS ACPVGFICTI DKLCCRSGTA ASCNFEAEPV
ALCDRGMCAP NHYCSRDGYC CPTTYGKNVC PNGATPIGLC EQGLCPLGHE CINGQICCPE
QPYTDNWQIS VCPNNREPVG ECINGLCPAD MVCINDVCCP TSDIMKLLHY KKRNLLHVTS
SNAIPGRSSS RLRLLERYDS LPSLRSHSED RYDDGVDRKW KKREGNSDDI CTEDETTVTE
GESEDGVDKE KPPSKEESGE KTSQEKESEE KTSQEKDEDK SEGETTEEKD VSQEQNSKEE
KGASEEDEDT PEEQNSKEEN GSSEEDDEDT SEAQASNEEK EASEEKDAVS EERKGASEEE
NEEKDDEHES EVESQASEEQ TTEEEEGASE EEDEENESKE QTSEEDEGAL EEKDEENASE
EQTSEGEEKG ASQEEEEDEE NEVESQASEE QTSEEEEEEG ASEEEDEENE SKEQTTEEEE
EEGASEEEDE ESASEEQTSE EEEENGASQE EEGDEENEQE SEVESQASEE KASEEEGASE
EGQDASEEED EDESEEEESD ESV
//
