ID A0A0V0WN26_9BILA Unreviewed; 632 AA.
AC A0A0V0WN26;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Beta-glucuronidase {ECO:0000256|ARBA:ARBA00016205};
DE EC=3.2.1.31 {ECO:0000256|ARBA:ARBA00012761};
GN Name=Gusb {ECO:0000313|EMBL:KRX77174.1};
GN ORFNames=T06_13535 {ECO:0000313|EMBL:KRX77174.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX77174.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX77174.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX77174.1};
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 -!- FUNCTION: Plays an important role in the degradation of dermatan and
CC keratan sulfates. {ECO:0000256|ARBA:ARBA00003025}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:KRX77174.1}.
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DR EMBL; JYDK01000087; KRX77174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WN26; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR10066; BETA-GLUCURONIDASE; 1.
DR PANTHER; PTHR10066:SF67; BETA-GLUCURONIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..632
FT /note="Beta-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006871921"
FT DOMAIN 32..213
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 216..318
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 320..614
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 632 AA; 73720 MW; C0746FE6126C73F3 CRC64;
MLFFPVLLFE MVNLHRVGCI LYPYPTETRQ VQNLDGLWWF VAEERNSIGY GLLNKWFELD
LSLFRNASRI AVPASYNDQV ENGTFRRHVG YVWYQRSFFI DPNWEKQEKE LLLRFGSVNY
DAEVWINGVS VVHHIGGHLP FEVSIKKHVC SWKVNVITVA VNNTLSYWTI PQAEFSYKNN
SNLYPEGYFE QKMLFDFFNY AGIHRSVILY IVPCQYIRNI AIRTNFEGTT GYVNYSIDTM
IGVANSANLL SVDVSISSYF GDIVARGFNF RGTLQVQNVI LWWPRFMSSY AGYLYTLTVI
LRYNGSVADI YRIPFGIRTV EVSGSKFLIN HKPFYFFGFG MHEDSEIRGR GYDASVMVKD
FNLLLWSHAN SFRTSHYPYS EERMQEADRL GLVVIEEVPA VGLRYFDKGV LELHRQILQE
TSVVMWSLAN EPSIKNAAAV NHFIELINFA KTLDTTRPVT IVYGQSEWYS EETGRIYAKY
VDVLCLNRYY GWYRATSEPD LIQKQLSFEL KKWYETFSRP ILMTEYGAEA IDGLSHEPPV
MFSIQYQLEI LEAHHRVFDE LKEQFLIGEM VWNFADFMTD DSLTRVVGNH KGVFHRNRQP
KLSAYLMQKR YKKLAENFLN ATDVIIIDQQ II
//
