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Database: UniProt
Entry: M7ARL1_CHEMY
LinkDB: M7ARL1_CHEMY
Original site: M7ARL1_CHEMY 
ID   M7ARL1_CHEMY            Unreviewed;       721 AA.
AC   M7ARL1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   16-JAN-2019, entry version 29.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=UY3_17432 {ECO:0000313|EMBL:EMP25485.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudines; Cryptodira; Durocryptodira; Americhelydia;
OC   Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP25485.1};
RN   [1] {ECO:0000313|EMBL:EMP25485.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang G., Huang Z., Wang Z.;
RT   "Development and evolution of a turtle-specific body plan assessed by
RT   genome-wide analyses.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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; KB589327; EMP25485.1; -; Genomic_DNA.
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; -; 3.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
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; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR23421; PTHR23421; 2.
DR   Pfam; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF006336; B-gal; 2.
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   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869}.
FT   DOMAIN        4    209       Metallophos. {ECO:0000259|Pfam:PF00149}.
FT   DOMAIN      141    455       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      602    676       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    288    288       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    368    368       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   721 AA;  80750 MW;  1D8D1F0D4C0F4B3D CRC64;
     MDGLKVVLLS DIHLGPTVGK TKLAMVVQMV KALKPDITVI VGDLSDSEVM AIRPAVEPLS
     ELNSPLGTYF VTGNHEYYTS DVNSWFELLK SFNIHPLHNE NVKISSPRSS NDWFCLAGVD
     DIEAQNAPQR SFGIDYDNNY FLKDGKPFRY ISGSIHYSRV PRYYWKDRLV KMKMAGLDAI
     QTYVPWNYHE FKPGVYNFYG DRDIKYFLEL ANEIGLLVIL RAGPYICAEW DMGGLPAWLL
     EKESIVLRSS DLDYLEAVDR WMGVLLPKMK PHLYQNGGPV IMVQVENEYG SYFACDYDYL
     RHLQKLFHRH LGDEVVLFTT DGANKYYLRC GALQGLYATV DFAPGGNVTA AFLTQRGSEP
     RGPLVNSEFY TGWLDHWGHP HSVVPTNTIA KTLDEILARG ANVNMYMFIG GTNFAYWNGA
     NMPYSSQPTS YDYDAPLSEA GDLTDKYFAL REVIGRYKHL PEGPIPPTTP KYAYGQVAME
     KLGTVAELLD DLSPSGPIRS TYPLSFVQLQ QVPQGVLERG KSYMINITGK AGANLDVLVE
     NMGRVNYGKY NNDFKGLVSN LSLGQVTLVH WEIYPLDIDS VVGHGLNGKG GESKTSGGNP
     SSYAAPAFYT GRFSIPSGIP DLPQDTYIKF PGWTKGQIWI NGFNLGRYWP VRGPQVTLFV
     PSNILVSSSP NNITVLELER SPCGIQKCAI EFVDKPDINA TLQYESNTRK LFTKDLWLDP
     L
//
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