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Database: UniProt
Entry: I1HNC6_BRADI
LinkDB: I1HNC6_BRADI
Original site: I1HNC6_BRADI 
ID   I1HNC6_BRADI            Unreviewed;       829 AA.
AC   I1HNC6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   16-JAN-2019, entry version 39.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   Name=100839503 {ECO:0000313|EnsemblPlants:PNT72151};
GN   ORFNames=BRADI_2g40450v3 {ECO:0000313|EMBL:PNT72151.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:PNT72151.1};
RN   [1] {ECO:0000313|EMBL:PNT72151.1, ECO:0000313|EnsemblPlants:PNT72151, ECO:0000313|Proteomes:UP000008810}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:PNT72151.1,
RC   ECO:0000313|EnsemblPlants:PNT72151}, and cv. Bd21
RC   {ECO:0000313|Proteomes:UP000008810};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:PNT72151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:PNT72151.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:PNT72151}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:PNT72151};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) 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         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; CM000881; PNT72151.1; -; Genomic_DNA.
DR   RefSeq; XP_003566745.1; XM_003566697.2.
DR   EnsemblPlants; PNT72151; PNT72151; BRADI_2g40450v3.
DR   GeneID; 100839503; -.
DR   Gramene; PNT72151; PNT72151; BRADI_2g40450v3.
DR   KEGG; bdi:100839503; -.
DR   OMA; DPVWGKN; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000008810; Chromosome 2.
DR   GO; GO:0005618; C:cell wall; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 2.
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   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008810};
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:UP000008810};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    829       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003643704.
FT   DOMAIN      746    829       SUEL-type lectin. {ECO:0000259|PROSITE:
FT                                PS50228}.
SQ   SEQUENCE   829 AA;  91787 MW;  8750AE734321BAE8 CRC64;
     MATTTMARAS LALVLLLITA AVGAANCTTV AYNDRALVID GQRRIVLSGS IHYPRSTPEM
     WPDLIKKAKE GGLDAIETYV FWNGHEPRPR QYNFAGNYDI VRFFKEIQNA GMYAILRIGP
     YICGEWNYGG LPAWLRDIPG MQFRMHNQPF EHEMETFTTL IVNKLKDANM FAGQGGPIIL
     SQIENEYGNI MANLTDAQSA SEYIHWCAAM ANKQNVGVPW IMCQQDADVP PNVINTCNGF
     YCHDWFPKRT DIPKIWTENW TGWFKAWDKP DFHRSAQDIA FAVAMFFQKR GSLQNYYMYH
     GGTNFGRTAG GPYITTSYDY DAPLDEYGNI REPKYGHLKD LHAVLKSMEK ILVHGDFSDI
     NYGRNVTVTK YTLDGSSVCF ISNQFDDRDA NATIDGTTHV VPAWSVSVLP DCKAVAYNTA
     KIKAQTSVMV KKPNTVEQEP ENLKWSWMPE HLKPFMTDEK GSFRKNELLE QITTSTDQSD
     YLWYRTSFEH KGEAKYKLSV NTTGHQIYAF VNGKLAGRQH SPNGAFIFQL ESPVKLHDGK
     NYLSLLSATM GLKNYGALFE LMPAGIVGGP VKLVDNNGST IDLSNSSWSY KAGLAGEHRQ
     IHLDKPGYKW HGDNGTIPIN RAFTWYKATF QAPAGEEAVV ADLMGLNKGV AWVNGNNLGR
     YWPSYVAAEM GGCHHCDYRG AFKAEGDGLK CLTGCNEPAQ RFYHVPRVFL RAGEPNTVVL
     FEEAGGDPSR VGFHTVAVGP VCVEAAEKGD NVTLSCGQHK GRTISSVDLA SYGVTRGQCG
     AYQGGCESKA AYEAFAEACV GKESCTVQHT DAFSGAGCQS GVLTVQATC
//
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