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Database: UniProt
Entry: A0A158NPS6_ATTCE
LinkDB: A0A158NPS6_ATTCE
Original site: A0A158NPS6_ATTCE 
ID   A0A158NPS6_ATTCE        Unreviewed;       625 AA.
AC   A0A158NPS6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-DEC-2018, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   Name=105622732 {ECO:0000313|EnsemblMetazoa:XP_012059534.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Formicoidea; Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012059534.1};
RN   [1] {ECO:0000313|EnsemblMetazoa:XP_012059534.1, 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.,
RA   Smith C.D., 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_012059534.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   RefSeq; XP_012059534.1; XM_012204144.1.
DR   EnsemblMetazoa; XM_012204144.1; XP_012059534.1; LOC105622732.
DR   GeneID; 105622732; -.
DR   KEGG; acep:105622732; -.
DR   KO; K12309; -.
DR   Proteomes; UP000005205; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005205};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    625       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007629425.
FT   DOMAIN       39    358       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      525    602       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    188    188       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    268    268       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   625 AA;  70400 MW;  5D3D014E81C029CF CRC64;
     MWSLMFVTIL ALSRAMSETI NLPNNEWQYS FHVDYENNQF LLDGKSFQYI SGSFHYFRTP
     RQYWRDRLRK IRAAGLNAIS TYVEWSLHEP EPGQFNWTGD ADLVNFLNIA QEEDLLVLLR
     PGPYICAERD MGGLPYWLLR EVPNINLRTK DADFVRYATL YLNEVLNKIR PLLRGNGGPI
     IMVQIENEYG SYYACDTEYM DMLKEIFIKK VGNKALLYTT DGAFASLLRC GFISGAYATV
     DFGTANNVTN SFLSMRLYQP RGPLVNSEFY PGWLTHWGEP FQRIKTEAVV KSLEEMLALG
     ASVNFYMFYG GTNFGFTSGA NGGTGVYSPQ LTSYDYDAPL TEAGDPTPKY FAIRDVIGRY
     LPLPNMSLPT ASPKGNYGPV LLEPVLKLLD NRSPFVVIRA TGDQPKTFEA LSVNQGFVLY
     ETNLPPSISD PAILHATTKD RALIYIDNQL RGILSRIDKI FTIPLESPYG HRLSLLVENQ
     GRLNFGNEIN DSKGISDVNI SGIPLTNWNM TGYTFSDVSS LRDITTIRID SGTLNKGPAF
     LRGKFTIVGQ PLDTYLDTTG WGKGVAFVNG HNLGRYWPLV GPQITLYVPA PYLREGENEL
     IILELEYVSQ TRKMKFQSVP NLGTL
//
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