ID   A0A3P9DC15_9CICH        Unreviewed;       640 AA.
AC   A0A3P9DC15;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   03-JUL-2019, entry version 4.
DE   RecName: Full=Beta-glucuronidase {ECO:0000256|RuleBase:RU361154};
DE            EC=3.2.1.31 {ECO:0000256|RuleBase:RU361154};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia;
OC   Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005031904, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005031904, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J.,
RA   Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J.,
RA   Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A.,
RA   Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O.,
RA   Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R.,
RA   Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T.,
RA   Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S.,
RA   Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D.,
RA   Rakotomanga M., Renn S.C.P., Ribeiro F.J., Ron M., Salzburger W.,
RA   Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R.,
RA   Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D.,
RA   Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A.,
RA   Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid
RT   fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005031904}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2018) to UniProtKB.
CC   -!- FUNCTION: Plays an important role in the degradation of dermatan
CC       and keratan sulfates. {ECO:0000256|RuleBase:RU361154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-
CC         glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411;
CC         EC=3.2.1.31; 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|RuleBase:RU361154}.
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DR   RefSeq; XP_004557499.1; XM_004557442.3.
DR   Ensembl; ENSMZET00005032938; ENSMZEP00005031904; ENSMZEG00005023801.
DR   GeneID; 101477863; -.
DR   GeneTree; ENSGT00390000001752; -.
DR   Proteomes; UP000265160; LG10.
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   Complete proteome {ECO:0000313|Proteomes:UP000265160};
KW   Glycosidase {ECO:0000256|RuleBase:RU361154};
KW   Hydrolase {ECO:0000256|RuleBase:RU361154};
KW   Lysosome {ECO:0000256|RuleBase:RU361154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    640       Beta-glucuronidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5017943126.
FT   DOMAIN       41    225       Glyco_hydro_2_N. {ECO:0000259|Pfam:
FT                                PF02837}.
FT   DOMAIN      227    328       Glyco_hydro_2. {ECO:0000259|Pfam:
FT                                PF00703}.
FT   DOMAIN      330    631       Glyco_hydro_2_C. {ECO:0000259|Pfam:
FT                                PF02836}.
SQ   SEQUENCE   640 AA;  73657 MW;  E23B0C5BF0D1CAD2 CRC64;
     MSVPGSFSVL RVLWLLSVFG TVLPLDGGML FPQESSFREV KELNGLWDFR ADGSPNRNEG
     FEKAWYKRRL TETGPVIEMP VPASYNDITQ DPTLRDFIGW VWYEREVFVP ARWISDEGTR
     VVLRVGSAHY YSIVWVNGEK VTEHEGGHLP FEAEISSLIR KEPTKPCRIT IAVNNTLTLE
     TLPPGTIQYM NDSSRYPDGF FVQNIDFDFF NYAGIHRSVL LYTTPKVHVD DISVETNFMD
     NTGLVRYKVS VQGGFNNTLN ITLMDKDGHF VASSNGSSGG LKVVDVKLWW PYLMHENPGY
     LYSMKVHLIA VSETSTYEDE YTLPVGIRTI NVTNTQFLIN NKPFYFHGVN KHEDSDIRGR
     GFDWPLIVKD FNLMKWLGVN SFRTSHYPYA EEILQMCDRH GIVVIDECPG VGIKDIRSFR
     NASLSHHLVV MDELVRRDKN HPSVVMWSVA NEPASEMPPA EFYFKTLIEH TKALDQTRPV
     TYVTIAAADM DKGGPYVDVV CANSYFAWYF DQGRLDIIPL QLSTHFENWY RKYQRPIIQS
     EYGADAVPGL HMDPPMMFTE EYQNALLQSY HDVFDQKRNQ YFVGELIWNF ADFMTSQGIY
     RVVGNKKGIF TRQRQPKAAA FLLRKRYWRL ANETGRLLPD
//