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Database: UniProt
Entry: H0Z2A9_TAEGU
LinkDB: H0Z2A9_TAEGU
Original site: H0Z2A9_TAEGU 
ID   H0Z2A9_TAEGU            Unreviewed;       600 AA.
AC   H0Z2A9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   13-FEB-2019, entry version 49.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   Name=GLB1 {ECO:0000313|Ensembl:ENSTGUP00000004699};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea;
OC   Estrildidae; Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000004699, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000004699, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C.,
RA   London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B.,
RA   Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B.,
RA   Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M.,
RA   Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P.,
RA   Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T.,
RA   Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A.,
RA   Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E.,
RA   Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D.,
RA   Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H.,
RA   Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J.,
RA   Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000004699}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2012) 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   EMBL; ABQF01014141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABQF01014142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; H0Z2A9; -.
DR   STRING; 59729.ENSTGUP00000004699; -.
DR   Ensembl; ENSTGUT00000004748; ENSTGUP00000004699; ENSTGUG00000004528.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   GeneTree; ENSGT00390000006586; -.
DR   InParanoid; H0Z2A9; -.
DR   OMA; GWGKGIV; -.
DR   TreeFam; TF314816; -.
DR   Reactome; R-TGU-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-TGU-6798695; Neutrophil degranulation.
DR   Proteomes; UP000007754; Chromosome 2.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:Ensembl.
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:UP000007754};
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:UP000007754}.
FT   DOMAIN       18    333       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      522    591       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    165    165       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    245    245       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   600 AA;  67368 MW;  62658AA65C37E19B CRC64;
     VQNVPERSFG IDYDSNCFVK DGKPFRYISG SIHYSRVPPY YWKDRLLKMK MAGLDAIQTY
     VPWNYHEPQM GTYDFFGGKD LQYFLQLAND TGLLVILRAG PYICAEWDMG GLPAWLLEKK
     SIVLRSSDSD YLEAVERWMG VLLPKMRPYL YQNGGPIIMV QVENEYGSYF ACDYNYLRFL
     LKLFRLHLGD EVVLFTTDGA SQFHLKCGAL QGLYATVDFA PGANVTAAFL AQRSSEPKGP
     LVNSEFYTGW LDHWGHHHSV VPAQTIAKTL NEILASGANV NLYMFIGGTN FAYWNGANMP
     YMPQPTSYDY DAPLSEAGDL TEKYFALRKV IGMYKQLPEG LTPPTTPKFA YGKVRLQKAG
     TVLEVLDGLS RSGPVRSTYP LTFVELKQYF GYVLYRTTLP KNCVEPTPLS SPLNGVHDRA
     YVSVDGVPQG VLERDKSLKI NITGQAGASL DILVENMGRV NFGRYNNDFK GLVSNLTLAQ
     DVLVGWEIYP LDIDGAVNYD IIYLLHHPKR SAIKELSYEV PTFYTGTLSI PGGIPDLPQD
     TYVNFPGWTK GQIWINGFNL GRYWPARGPQ LTLYVPRNVL VASAPNNITV LELERSPCST
//
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