ID A0A2J7QP26_9NEOP Unreviewed; 658 AA. AC A0A2J7QP26; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 12-AUG-2020, 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=B7P43_G13405 {ECO:0000313|EMBL:PNF30344.1}; OS Cryptotermes secundus. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae; OC Kalotermitidae; Cryptotermitinae; Cryptotermes. OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF30344.1, ECO:0000313|Proteomes:UP000235965}; RN [1] {ECO:0000313|EMBL:PNF30344.1, ECO:0000313|Proteomes:UP000235965} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Whole body {ECO:0000313|EMBL:PNF30344.1}; RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T., RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J., RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C., RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M., RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M., RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G., RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J., RA Bornberg-Bauer E.; RT "Hemimetabolous genomes reveal molecular basis of termite eusociality."; RL Submitted (DEC-2017) 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 = an alcohol + D-glucuronate; 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|ARBA:ARBA00001200, CC 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 -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}. 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:PNF30344.1}. 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; NEVH01012097; PNF30344.1; -; Genomic_DNA. DR EMBL; NEVH01012097; PNF30345.1; -; Genomic_DNA. DR Proteomes; UP000235965; Unassembled WGS sequence. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW. DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 2.60.40.10; -; 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 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; SSF49303; SSF49303; 1. DR SUPFAM; SSF49785; SSF49785; 1. DR SUPFAM; SSF51445; SSF51445; 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:UP000235965}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..658 FT /note="Beta-glucuronidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014559394" FT DOMAIN 36..215 FT /note="Glyco_hydro_2_N" FT /evidence="ECO:0000259|Pfam:PF02837" FT DOMAIN 217..319 FT /note="Glyco_hydro_2" FT /evidence="ECO:0000259|Pfam:PF00703" FT DOMAIN 325..621 FT /note="Glyco_hydro_2_C" FT /evidence="ECO:0000259|Pfam:PF02836" SQ SEQUENCE 658 AA; 74763 MW; 4F93A55E1D3F7AC7 CRC64; MGCVQWLSAP LVTMLMTSLV AADGILYPTE SESRIIHSLD GIWAFRLANE SESSVGHREG WYKQELRKTG RTIAMPVPAS YNDITQDKVV RDHVGVAWYD RTFYIPRKWN SSDTKIWLRF AGVHYAADVF VNGELVASHA GGHVPFQADV TSVLQYGQKN LISVAVNNTL TDITVPQGEV QQLQTDAGAR FVQYYKFDFF NYAGIHRPVV LYTTPSIYID DISVNTDVND DTGVIEYVVR VGGDTKTRAT VSVSLLDRDG NYVIRNVVGD QGNLQVPQAR LWWPYLMNPE PAYLYTLEVR TSTESAVPED VYRLPVGIRK LGWTNTSVTM NGKAIYIRGF GRHEDSAIRG KGHDYPLITR DYNLIKWIGA NAYRTSHYPY SEEIMDFADR EGIMIINECP GVDIGSYGFK DELLEAHKTA LTRLHRRDKN RPSVVMWSVA NEALTASPEA YGYFRDIADH MKALDISRPI TMALNKPCNL DLAGEFMDVI GFNRYNAWYV NSGRTDTIIQ NVKEEALNWH KKYNKPVLMT EYGGDTMAGL HLSPEYIWSE EYQVKLLSKH FEAFDQLRNE SFFIGEMIWN FADFNTAQTY VRVGGNKKGV FTRDRQPKAS AQLVRKRYWA LAEELDSVTP PDDLSEYVHE SHAKYLETGL PDVWVTSV //