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Database: UniProt
Entry: A0A1Z5SYL3_HORWE
LinkDB: A0A1Z5SYL3_HORWE
Original site: A0A1Z5SYL3_HORWE 
ID   A0A1Z5SYL3_HORWE        Unreviewed;      1019 AA.
AC   A0A1Z5SYL3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   16-JAN-2019, entry version 8.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=BTJ68_11576 {ECO:0000313|EMBL:OTA26212.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Teratosphaeriaceae;
OC   Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA26212.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA26212.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA26212.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C.,
RA   Stajich J.E., Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea
RT   werneckii: insights from long-read sequencing.";
RL   Submitted (JAN-2017) 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         ECO:0000256|SAAS:SAAS01116863};
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:OTA26212.1}.
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DR   EMBL; MUNK01000190; OTA26212.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000194280; 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; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
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; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000194280};
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:UP000194280};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1019       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012328786.
FT   DOMAIN      399    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1019 AA;  111971 MW;  56D69C29ED2AA660 CRC64;
     MLFGKLCKAA LLSAAAVQSA TALAIGGKPN LMIRDSYKRE PLQDIVTWDE HSLFVHGERI
     IFYSGEFHPY RLPVPSLWLD VFQKIKALGY NGVSFYTDWA LLEGKPGVFN ASGVFDFQPF
     FDAAQEAGIY LLARPGPYIN AEVSGGGFPG WLQRIPGTLR TRDPSYLHAT DNYARNMNEI
     IAKAQITNGG PVILAQPENE YTGATDDVPE FPDPVYFGYV EKQMRDAGIV VPLISNDASP
     QGYFAPGSGS PAAVDIYGHD GYPLGFDCAN PYTWPDQSLP TNFLTLHRQQ SPSTPYSIIE
     FQGGAFDPWG GNGFEQCVKL LGPEFERVFY KNDFSFGLTI FNIYMTYGGT NWGNLGHPGG
     YTSYDYGAVI KEDRAVTREK YSEAKLEANF LQASPAYWTA WAQNNTNANG SYTGNDDLAV
     TALLGEQTNF FVLRHAAFNS LETTDYSITL PSKSQGNITI PQLGGSLSLH GRDSKWHVTD
     YDVGGINLVY STAEIFTWKQ YGHKRVLVVY GGPGEMHELA VEGGGHAKTV EGDGVKYGKK
     NGATVMQYSV SADRKVVELG CGLTVYLLDR NSAYNYWVLD LPSDNVWGNY THPSHAVSAP
     IVNGGYLLRT VEVKDDCVHL TGDINSTTTF EVIGGAPHHT REMTFNGEKV HFKQDHWSGV
     VTATVSYDEP SIDLPNLSTI GWKSVDTLPE LKSDYDDSLW TDAYLTYTNN TLRNLITPRS
     LYASDYGYNT GYLLFRGHFT AKGGESSLYL ATQGGSAFGH SVWINNTFVG SFDGADLYST
     WNATYDLPAL SAGSPYVITV LIDNMGLNED WTVGTDDMKN PRGILDYRLG GHSKDAVSWK
     LTGNLHGEDY EDKTRGPLNE GGLWVERNGY HLPGAPTSDW TSSALGPMEG LSEPGVKFYA
     TTFDLDMPEG YDTPLRFTFS NATMTSNGTA QAYRCQIYVN GYQFGKYVHN IGPQDDFPVP
     EGIFNYHGSN YVGVSFWSLE EEGARVGNFS LVAGHPVQSG FGPVALAPLT GWSKREGAY
//
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