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Database: UniProt/TrEMBL
Entry: E6X917_CELAD
LinkDB: E6X917_CELAD
Original site: E6X917_CELAD 
ID   E6X917_CELAD            Unreviewed;       825 AA.
AC   E6X917;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   28-FEB-2018, entry version 43.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:ADV49788.1};
DE            EC=3.2.1.23 {ECO:0000313|EMBL:ADV49788.1};
GN   OrderedLocusNames=Celal_2500 {ECO:0000313|EMBL:ADV49788.1};
OS   Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV49788.1, ECO:0000313|Proteomes:UP000008634};
RN   [1] {ECO:0000313|EMBL:ADV49788.1, ECO:0000313|Proteomes:UP000008634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14237 / IC166 / ACAM 630
RC   {ECO:0000313|Proteomes:UP000008634};
RX   PubMed=21475589;
RA   Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Mavromatis K., Ovchinikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brambilla E., Rohde M., Tindall B.J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Cellulophaga algicola type strain
RT   (IC166).";
RL   Stand. Genomic Sci. 4:72-80(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|SAAS:SAAS00568376}.
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DR   EMBL; CP002453; ADV49788.1; -; Genomic_DNA.
DR   RefSeq; WP_013551260.1; NC_014934.1.
DR   ProteinModelPortal; E6X917; -.
DR   STRING; 688270.Celal_2500; -.
DR   EnsemblBacteria; ADV49788; ADV49788; Celal_2500.
DR   KEGG; cao:Celal_2500; -.
DR   eggNOG; ENOG4105CNT; Bacteria.
DR   eggNOG; COG3250; LUCA.
DR   HOGENOM; HOG000022809; -.
DR   KO; K01190; -.
DR   OMA; CLHHDQG; -.
DR   OrthoDB; POG091H0F66; -.
DR   BioCyc; CALG688270:G1GR0-2504-MONOMER; -.
DR   Proteomes; UP000008634; Chromosome.
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; -; 1.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
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; 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   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   Pfam; PF16355; DUF4982; 1.
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; SSF49373; SSF49373; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008634};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00013214,
KW   ECO:0000313|EMBL:ADV49788.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00013186,
KW   ECO:0000313|EMBL:ADV49788.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008634}.
FT   DOMAIN       36    178       Glyco_hydro_2_N. {ECO:0000259|Pfam:
FT                                PF02837}.
FT   DOMAIN      192    295       Glyco_hydro_2. {ECO:0000259|Pfam:
FT                                PF00703}.
FT   DOMAIN      297    453       Glyco_hydro_2_C. {ECO:0000259|Pfam:
FT                                PF02836}.
FT   DOMAIN      630    707       DUF4982. {ECO:0000259|Pfam:PF16355}.
SQ   SEQUENCE   825 AA;  92796 MW;  8B3BE732F4135737 CRC64;
     MKALKRTPLI ILFISIFISS CQENGVEVIA DQDFNKDWLF IKDTVPQGEA IHLDDSTWRK
     LNVPHDWAIE GPFDSKNNAR NGGLPIDGIA WYRKHFTIDA KNKNKQVAIE FDGVMDNSKI
     YVNGNFVGER HYGYSGFEFD ITPFIKFGED NIIAVQLAPE VLSERWYPGA GIYRNVRLKL
     NEKVHIPQWG TFISTPEVTS EKATVTIKTK LKNATDKPQE IFLETTIVDA SNKTMGIATE
     TIDVANNSEE QLTQHMTVVN PSLWDVGKPN LYKAISRVKI KDQIVDEFET EFGIRTIEFK
     KEGFFLNGKA VELNGVCMHH DLGPLGAAVN YRATERQMQI MQNMGANALR TSHNPPSPEM
     LQVCDRLGIV VIDEAFDEWK EPKVPNGYSN YFDQWAEKDL RDMIKRDRNH PSVIMWSIGN
     EILEQGKKDG WKIAKMLNDI CHDEDDSRPT TAGFNYYPAS FVNQLAAQID VVGVNYKPAY
     YGEIREQNPD MIFYGSETSS QTSTRGFYEV PQDYHVNKET NQVSSYDVTV GPPWAYAPDI
     EFDAQEKNPH SLGEFIWTGF DYLGEPTPYG GRDNSTNGYW NDDWPSHASY FAPVDLVGFP
     KDRFYLYQSQ WTSAPMVHVL PHWNWEGKEG QTIPVYAYTN ADEVELFVNG TSFGKKVKGK
     DLTDVFTEYN GFKKGIYKSK YRLSWQVAYQ PGSLKVVAYT NGKQVASKEI KTAGKPAKIS
     LVADRNTIKA DGKDLSFVSV SIEDKDGNLC PNAANLINFK VEGAGVLEAV GNGNSASLES
     FQENYIKSFF GKSLAIIKGT ENTGEVTITA TGENLATASL IIKTE
//
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