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Database: UniProt
Entry: A0A151P2K4_ALLMI
LinkDB: A0A151P2K4_ALLMI
Original site: A0A151P2K4_ALLMI 
ID   A0A151P2K4_ALLMI        Unreviewed;       651 AA.
AC   A0A151P2K4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-DEC-2018, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=Y1Q_0017586 {ECO:0000313|EMBL:KYO43296.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO43296.1};
RN   [1] {ECO:0000313|EMBL:KYO43296.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO43296.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y.,
RA   Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A.,
RA   Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D.,
RA   Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J.,
RA   Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y.,
RA   Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E.,
RA   Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J.,
RA   Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W.,
RA   Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D.,
RA   Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KYO43296.1}.
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DR   EMBL; AKHW03001210; KYO43296.1; -; Genomic_DNA.
DR   PhylomeDB; A0A151P2K4; -.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
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; -; 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:UP000050525};
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:UP000050525};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    651       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007586606.
FT   DOMAIN       33    348       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      537    606       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    180    180       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    260    260       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   651 AA;  73286 MW;  163B03A0D76BD977 CRC64;
     MPPLLLRLAA LLALLPASVP QRSFGIDYNC NCFVKDGKPF RYISGSIHYA RVPRYYWKDR
     LLKMKMAGLD AIQTYVPWNY HESEPGLYNF SGDRDVEYFL QLANETGLLV ILRAGPYICA
     EWDMGGLPAW LLEKESIILR SSDLDYLASV DKWMGVFLPK MKPLLYQNGG PIIMVQVENE
     YGSYFACDYN YLRYLQKLFR HHLGEDAVLF TTDGASRSYL RCGALQGLYA TVDFAPGCNV
     TAAFLSQRSS EPTGPLVNSE FYTGWLDHWG HRHSFVPAQL VAKSLSEILA RGANVNMYMF
     IGGTNFAYWN GANMPYTPQP TSYDYDAPLS EAGDLTEKYF ALREVIGMYK SLPEGPIPPT
     TPKFAYGQVQ MEKIGTLLEV LDDLSPSGPV KSIYPLTFVQ LKQYFGFVLY RTNLKKNYSE
     ETLLISPLSG VHDRAYISVD GIPQGVLERG KSLMINITGE AGANLDLLVE NMGRVNYGRY
     NNDFKGLVSN LTLDQDILVD WEIYPLDIDR AVGRGLKCDD DELKTPGNTP PSYELPAFYT
     GTLSIPSGIP DLPQDTYIRF PGWTKGQIWI NGFNLGRYWP ARGPQMTLFV PSNILVSSAP
     NNITVLELER SPCSIQECVV EFVDKPDINA TFQYEGNSEK LFSKDLWLSH L
//
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