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Database: UniProt
Entry: A0A251QR22_PRUPE
LinkDB: A0A251QR22_PRUPE
Original site: A0A251QR22_PRUPE 
ID   A0A251QR22_PRUPE        Unreviewed;       852 AA.
AC   A0A251QR22;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PRUPE_1G009200 {ECO:0000313|EMBL:ONI26203.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Rosales; Rosaceae; Amygdaloideae;
OC   Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI26203.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI26203.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G.,
RA   Dondini L., Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C.,
RA   Aramini V., Copetti D., Gonzalez S., Horner D.S., Falchi R., Lucas S.,
RA   Mica E., Maldonado J., Lazzari B., Bielenberg D., Pirona R.,
RA   Miculan M., Barakat A., Testolin R., Stella A., Tartarini S.,
RA   Tonutti P., Arus P., Orellana A., Wells C., Main D., Vizzotto G.,
RA   Silva H., Salamini F., Schmutz J., Morgante M., Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies
RT   unique patterns of genetic diversity, domestication and genome
RT   evolution.";
RL   Nat. Genet. 45:487-494(2013).
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; CM007651; ONI26203.1; -; Genomic_DNA.
DR   EnsemblPlants; ONI26203; ONI26203; PRUPE_1G009200.
DR   Gramene; ONI26203; ONI26203; PRUPE_1G009200.
DR   Proteomes; UP000006882; Chromosome g1.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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:UP000006882};
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:UP000006882};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    852       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5013146174.
FT   DOMAIN      764    851       SUEL-type lectin. {ECO:0000259|PROSITE:
FT                                PS50228}.
SQ   SEQUENCE   852 AA;  95637 MW;  42AB68308F979D19 CRC64;
     MAVSISRVLL ISLISIVISA AIVHAKGHGH HGHGGKHLHH QNRNQSVQGG PVTYDGRSLI
     INGKRELLFS GAIHYTRSTP EMWPYLIKKA KHGGLNMIET YVFWNIHEPV QGQYNFEGNY
     DLVRFIKLVQ EHGMYATIRL GPFIQAEWNH GGLPYWLREV PGIIFRSDNK AFKYHMEKYV
     QLIVNKLKEA KLFAPQGGPI VLAQIENEYN MVQLAYRELG SSYMRWAAAM AVQQNIGVPW
     IMCKQKDAPD PVINTCNGRQ CGDTFMGPNK PYKPTLWTEN WTAQYRVFGD PPSQRPVDDI
     AFAVARFFSK KGSLTNYYMY HGGTNFGRTS AIFTTTRYYD EAPLDEYGLP RDPKWSHLKD
     LHKALRLSRK ALLWGVPGVQ KMSANTEVYF YEMPATNICA AFLTNNNLTT EATVSWRGQD
     YYLPPHSISI LPDCKTVVFN TQTIVAQHNS RNFVQSTVAN NLKWKKYAEP IPSTLQVPVN
     NPTPLELYTL LKDTSDYAWY TTSLALNPQD LPRKASIQPV LRIASLGHAL HLFVNGKYIG
     FGHGSHDEKS FVLEKPVHFK AGVNQITLLA MTLGLPDGGA YMEHRYAGPN LIIVLGLNTG
     TLDITKNGWG HQVGLNGEKL QVFTEEGSKQ VQWDKTKGSA QGLTWYKTYF DAPEGNNPVA
     IRMTGMGKGM IWVNGRSIGR HWMSFLSPLG EPTQSEYHIP RSFIKPTQNI LVVLEEQPAK
     PKHIEILTVN RDTICSFITE YHPPNVKSWA RQDSVFRPVL DVIRSSADIK CPNKKKVVAV
     EFASFGDPPA GYCGSYVLGK CNSPVSKEVV EQHCLGKSSC SVPINRNLFL KNITDGCPGI
     KKTLAIQVKC AI
//
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