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Database: UniProt
Entry: D8RK50_SELML
LinkDB: D8RK50_SELML
Original site: D8RK50_SELML 
ID   D8RK50_SELML            Unreviewed;       620 AA.
AC   D8RK50;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   16-JAN-2019, entry version 46.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
DE   Flags: Fragment;
GN   ORFNames=SELMODRAFT_61474 {ECO:0000313|EMBL:EFJ27173.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ27173.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A.,
RA   Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L.,
RA   Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M.,
RA   DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L.,
RA   Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L.,
RA   Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y.,
RA   Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U.,
RA   Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E.,
RA   Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S.,
RA   Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M.,
RA   Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P.,
RA   Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L.,
RA   Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R.,
RA   Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S.,
RA   Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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   EMBL; GL377582; EFJ27173.1; -; Genomic_DNA.
DR   RefSeq; XP_002971424.1; XM_002971378.1.
DR   ProteinModelPortal; D8RK50; -.
DR   STRING; 88036.EFJ27173; -.
DR   EnsemblPlants; EFJ27173; EFJ27173; SELMODRAFT_61474.
DR   Gramene; EFJ27173; EFJ27173; SELMODRAFT_61474.
DR   KEGG; smo:SELMODRAFT_61474; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   InParanoid; D8RK50; -.
DR   KO; K12309; -.
DR   OMA; GWGKGIV; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000001514; 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:UP000001514};
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:UP000001514}.
FT   DOMAIN       11    334       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      528    595       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    159    159       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    242    242       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:EFJ27173.1}.
FT   NON_TER     620    620       {ECO:0000313|EMBL:EFJ27173.1}.
SQ   SEQUENCE   620 AA;  69646 MW;  F2D365C1505915A8 CRC64;
     SRSFSIENDA FYKDGEPFRI LGGEIHYFRI VPEYWKDRIQ RAKAMGLNTI QTYVPWNVHE
     PSEGEFFFGD PVNLEAFLKL AQELEVLVML RMGPYVCGEW DLGGFPSWLL SKQPQLKLRT
     SDSSYLKLVD QWWNVLLPKL VPFLYSRGGP VIMLQVENEY GSFGSDKQYL HHLVSEAREY
     LGNEIILYTT DGATEDALQR GTISRDDVYA AVDFPTGWDP VAAFALQKNY NSPGKSPALS
     TEFYTGWLTH WGENLATTSP YVAAAELDKL LSANGSVVLY MAHGGSNFGF FSGANTGGKE
     TIYQPDITSY DYDAPIGEGG DLGEKFWRFR EVLSSYVNFP LPDPPQLPSR RNTGTVVLQK
     LANLFQVLQS LSHEFYLQQA PVTMELLNQS FGFIVYRSRL PSHAKPGSIL EIKKIHDRAQ
     VYVGKSSQSL RLVGTLQRWS NSSLQLPDGS SAGMEIYILV ENMGRINYGP FIFDQKGILS
     SVILDNVPML GWRAYTLSLA DVAENQEVLI NFAIHSKFFF LSLAAPHCDG PAFYAATFES
     EAQMDTFISF KGWSKGVAFV NGFNLGRFWP DAGPQCSLYV PGPLLRQGEN QLLILELENT
     LLHNKTLQFL GQHDWTCGKN
//
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