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Database: UniProt
Entry: L5M4L4_MYODS
LinkDB: L5M4L4_MYODS
Original site: L5M4L4_MYODS 
ID   L5M4L4_MYODS            Unreviewed;       739 AA.
AC   L5M4L4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   16-JAN-2019, entry version 27.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=MDA_GLEAN10018227 {ECO:0000313|EMBL:ELK33326.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK33326.1};
RN   [1] {ECO:0000313|EMBL:ELK33326.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spleen {ECO:0000313|EMBL:ELK33326.1};
RA   Zhang G., Cowled C., Wang L.;
RT   "Comparative analysis of bat genomes provides insight into the
RT   evolution of flight and immunity.";
RL   Science 0:0-0(2012).
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; KB104455; ELK33326.1; -; 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   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; 2.
DR   Pfam; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 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   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869}.
FT   DOMAIN       46    361       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      626    696       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
SQ   SEQUENCE   739 AA;  82962 MW;  2CDFC757147FB8E4 CRC64;
     MTSNTPHSRG RANADATPPL LPVPPPSPTQ NASQKTFEID YNHNCFRKDG QPFRYISGSI
     HYFRVPRFYW QDRLLKMKMA GLNAIQIYVP WNFHEPQPGQ YQFSEEHDVE HFIQLAHELG
     LLVILRPGPY ICAEWEMGGL PAWLLEKENI VLRSSDPDYL AAVDTWLGVI LPKMKPLLYQ
     NGGPIITVQV ENEYGSYFSC DYDYLRFLQK RFHYHLGNDV VLFTTDGEME KLMQCGALQG
     LYATVDFGPG ANITKAFLIQ RKYEPKGPLI NSEFYTGWLD HWGQPHSTVK TEVVASSLQD
     ILARGANVNL YMFIGGTNFG YWNGANMPYQ PQPTSYDYDA PLSEAGDLTE KYFAVRDVIR
     KFENVPEGPI PPSTPKFAYG KVALKKLKTV EEALNVLCPA GPVKSLYPLT FIQVKQYFGF
     VLYRTTLPED CSKPTPLSSP RRGVHDRAYV SVDGVLPLFL LPLNCAPHLL TWPPSCSICL
     IHPLTLLNLE APPQGPTLSE TFLAPPAQGH PMSSRLLEDG VRFVYNRGVP QGVLDRNYVT
     TLNITGKAGA TLDLLVENMG RVNYGYYIND YKGLISNLTL NSSILTDWMI FPLDIENAVY
     HLGAWHGNDR SYRSKACAHS SNYTLPAFYV GNFSIPSGIP DLPQDTFIQF PGWTKGQVWI
     NGFNLGRYWP ARGPQMTLFV PQHILVTSAP NTIAVLELER APCSANPPEP CTVEFVDKPV
     ISAAVTYSHL LQHQPDPDS
//
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