ID A0A158NEU1_ATTCE Unreviewed; 669 AA.
AC A0A158NEU1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Beta-glucuronidase {ECO:0008006|Google:ProtNLM};
GN Name=105619129 {ECO:0000313|EnsemblMetazoa:XP_012056049.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012056049.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012056049.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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; ADTU01013691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01013692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012056049.1; XM_012200659.1.
DR AlphaFoldDB; A0A158NEU1; -.
DR STRING; 12957.A0A158NEU1; -.
DR EnsemblMetazoa; XM_012200659.1; XP_012056049.1; LOC105619129.
DR GeneID; 105619129; -.
DR KEGG; acep:105619129; -.
DR eggNOG; KOG2024; Eukaryota.
DR InParanoid; A0A158NEU1; -.
DR OrthoDB; 1847696at2759; -.
DR Proteomes; UP000005205; 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; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
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; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..669
FT /note="Beta-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007629063"
FT DOMAIN 60..236
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 347..642
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 669 AA; 76851 MW; 3FA7D8864E815D0A CRC64;
MWHLIFLLIG SAMAGESGPE SPPEFSDTTI KIEALPYEEA FPTPLPGLLY PRESESREVK
SLDGLWDFTV SSEGDVLKHF SEAWFTDDLS RVGEMMKMPV PSSYNDVTTS RNLRDHLGAV
WYHRTFFVPY SWKDERVFVR FGSVHYLAQV WVNNVLMTNH EMGHLPFEAE ISSFVTYGSM
NHILVSVDNT LGQNSVPQGK IVQVNSDNGT KYLQTYSFDF FNYAGIHRSV LLYTTPRVYV
KDITVRTSLI GDMGIVKYTI EAGGMNEGEI PVCRVTLLNA EHTLAIKEPV YGISGTLKVP
LARLWWPRGM NPKPGYLYTL EIRLSVANLT KPDVYRLPIG IRTLTWTNTS LLLNNRPVYM
RGFGRHEDSA IRGRGFDLVT AVRDHELLQW VGANAYRTSH YPYSDEVLDL ADRLGFLIIG
ECPSVDTENY SSLLLMRHKD SLSELIRRDK NRPSVIMWSL ANEPRTQLPQ AEEYFMQIAH
HTKAIDPTRP VTIALARGVQ EDKAGQFLDV ISFNRYNAWY SNAGRLDMIV DRVQGEAEAW
HRKYNKPVLM SEYGADTMPG LHELPEYVWS EEYQKELFSK HFEAFDRLRH QGFFIGEFIW
NFADFRTAQT YTRVGGNKKG IFTRDRQPKM AAHHIRKRYH ALAVELDGAQ IPDDFEDYYY
SSQYSDLKL
//
