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Database: UniProt
Entry: A0A077YX20_TRITR
LinkDB: A0A077YX20_TRITR
Original site: A0A077YX20_TRITR 
ID   A0A077YX20_TRITR        Unreviewed;       274 AA.
AC   A0A077YX20;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Trypsin and Ldl recept a domain containing protei n {ECO:0000313|EMBL:CDW52294.1};
GN   ORFNames=TTRE_0000055301 {ECO:0000313|EMBL:CDW52294.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW52294.1};
RN   [1] {ECO:0000313|EMBL:CDW52294.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW52294.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate host-
RT   pathogen interaction.";
RL   Submitted (MAR-2014) 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}.
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DR   EMBL; HG805819; CDW52294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077YX20; -.
DR   STRING; 36087.A0A077YX20; -.
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   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24256; TRYPTASE-RELATED; 1.
DR   PANTHER; PTHR24256:SF565; ZGC:92313-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}.
FT   DOMAIN          1..209
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        221..233
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        228..246
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   274 AA;  30773 MW;  3B52D5208B6C1650 CRC64;
     MGCTTANLFR TNEKTLTVRV SVQRNSSLSP YDQFSPVSHQ LKHSMYVGRP GGTNDIALLR
     LAIPLKSTPM AQPICFESLD TTAEDIWSAK EKTTSTFTLG MGRLRRKRIA ADYPDLAEIT
     ITNSSSCRQH RIVRLERLNI GTEQFCAFQQ PDTYRCQGES GSPVLKKHSD NLWHLIGLTS
     KPHSCLSVKY PSIYINITHY TKWIEHAADV LHAEKPYMRR CDNGMFACLL GDCIDASAVC
     DGVRNCAFGE DEKCEKTLTK DEVTFKVKRS SQLA
//
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