ID A0A8S1BWD1_ARCPL Unreviewed; 664 AA. AC A0A8S1BWD1; DT 12-OCT-2022, integrated into UniProtKB/TrEMBL. DT 12-OCT-2022, sequence version 1. DT 27-NOV-2024, entry version 8. DE RecName: Full=Beta-glucuronidase {ECO:0000256|ARBA:ARBA00016205, ECO:0000256|RuleBase:RU361154}; DE EC=3.2.1.31 {ECO:0000256|ARBA:ARBA00012761, ECO:0000256|RuleBase:RU361154}; GN ORFNames=APLA_LOCUS17996 {ECO:0000313|EMBL:CAB3261586.1}; OS Arctia plantaginis (Wood tiger moth) (Phalaena plantaginis). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea; OC Erebidae; Arctiinae; Arctia. OX NCBI_TaxID=874455 {ECO:0000313|EMBL:CAB3261586.1, ECO:0000313|Proteomes:UP000494106}; RN [1] {ECO:0000313|EMBL:CAB3261586.1, ECO:0000313|Proteomes:UP000494106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wallbank WR R., Pardo Diaz C., Kozak K., Martin S., Jiggins C., Moest M., RA Warren A I., Byers J.R.P. K., Montejo-Kovacevich G., Yen C E.; RL Submitted (APR-2020) 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 ECO:0000256|RuleBase:RU361154}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol; CC Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, CC ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31; CC Evidence={ECO:0000256|RuleBase:RU361154}; CC -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid. CC {ECO:0000256|RuleBase:RU361154}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361154}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}. 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:CAB3261586.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CADEBC010000858; CAB3261586.1; -; Genomic_DNA. DR Proteomes; UP000494106; Unassembled WGS sequence. DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:TreeGrafter. DR GO; GO:0030246; F:carbohydrate binding; IEA:TreeGrafter. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR FunFam; 2.60.120.260:FF:000027; Beta-glucuronidase; 1. DR FunFam; 2.60.40.10:FF:000628; Beta-glucuronidase; 1. DR FunFam; 3.20.20.80:FF:000029; Beta-glucuronidase; 1. 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; IPR023232; Glyco_hydro_2_AS. DR InterPro; IPR006103; Glyco_hydro_2_cat. DR InterPro; IPR023230; Glyco_hydro_2_CS. 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. DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1. DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1. PE 3: Inferred from homology; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}; KW Lysosome {ECO:0000256|RuleBase:RU361154}; KW Reference proteome {ECO:0000313|Proteomes:UP000494106}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..664 FT /note="Beta-glucuronidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5035856801" FT DOMAIN 57..234 FT /note="Glycosyl hydrolases family 2 sugar binding" FT /evidence="ECO:0000259|Pfam:PF02837" FT DOMAIN 236..337 FT /note="Glycoside hydrolase family 2 immunoglobulin-like FT beta-sandwich" FT /evidence="ECO:0000259|Pfam:PF00703" FT DOMAIN 343..638 FT /note="Glycoside hydrolase family 2 catalytic" FT /evidence="ECO:0000259|Pfam:PF02836" SQ SEQUENCE 664 AA; 75386 MW; 91DBD33A7D278F80 CRC64; MLTKELLVTL LTLSGIANVV VSESVSGNSI NEVPKKKTTT TGGALYPQAT ETRDLINLDG IWNFRKSPSD PEVGYRGGWY EQDLVKTGPV IPMPVPSSYN DVGEDITLRD HVGVVWYDRR FYVPYSWGAT GQRIWLRFSS VHYAAEVFVN GKSVLFHEIG HLPFEAEITD VVKYNTSNLL TVVVDNTLLS DTIPQGSIKD IYVGPKKIRQ EQSYTFDFFN YAGIHRSVYL YSTPETYIDD VIVNTDIQGL TGFVVYNVTY RGSNAEKVQC LVEVFDKNDT QVAGYNDCAG LLEIGNAKFW FPYLMHPEHG YLYTFKVSLI GSLGEILDTY SQKIGIRTIT WSNTTIFINE KPLYMKGFGM HEDSDLRGKG WDPVLWVKNF NLIKWLGANA FRTSHYPYAE EIYQLADEYG IMIINECPGV DIDIFTNNLL AKHKQSITEL IRRDKNHPSV IMWSIANEPR SGNKLADKYF GELVKHVKSM DLSRPVTIAI SVNALLDKSG RHLDVIMFNR YNGWYSNSGS TVQIAHNVIE EATNWYRLHS KPVIMSEYGA DTIAGLHLYP EFIWSEEYQC ALLSEHFKAF DHLRQVGFFA GEFIWNFADF KTAQSITRVG GNKKGIFTRN RQPKAAAHHI RARYHAIAAS DYGIPKIDTS YYVSDNLPAK HNEL //