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Database: UniProt
Entry: A0A1G4BH04_9PEZI
LinkDB: A0A1G4BH04_9PEZI
Original site: A0A1G4BH04_9PEZI 
ID   A0A1G4BH04_9PEZI        Unreviewed;       993 AA.
AC   A0A1G4BH04;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CORC01_03972 {ECO:0000313|EMBL:OHF00655.1};
OS   Colletotrichum orchidophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF00655.1, ECO:0000313|Proteomes:UP000176998};
RN   [1] {ECO:0000313|EMBL:OHF00655.1, ECO:0000313|Proteomes:UP000176998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF00655.1,
RC   ECO:0000313|Proteomes:UP000176998};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) 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:OHF00655.1}.
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DR   EMBL; MJBS01000025; OHF00655.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000176998; 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:UP000176998};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:OHF00655.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176998};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    993       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5009602880.
FT   DOMAIN      388    568       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   993 AA;  110246 MW;  20ECEF838C041BB2 CRC64;
     MLISRLKALS LLGLAWLNGV SARTIGTDLK LLNGRQQDIV TWDDKSLFIN GERLMIFSAE
     FHAFRMPVPS LWLDILQKIK AAGYNSVSFY VNWGLLEAKP GEVRPEGIFA LEPLFEAAKK
     AGLYLFARPG PYINAEVTGG GFPGWLQRVQ GALRTSDEAY LKATDNYTAA LGSTIAKAQI
     TNGGPVILFQ MENEYNAAVD PYPFPDYDYW KYVDHQFRSQ GVVVPYVNNE AWQLGAITAL
     TPAKVDIYGH DSYPLGFDCW NPTVWPENGL PIDWLATNNA IAPTTPYTIV EFQGGGFQPW
     GGAGFEYCAA LLNHEFERVL YKNNYAVGVT IFNIYMTWGG TNWGNLGYSD GYTSYDYGAQ
     ITEERLVNRE KYSETKLQSN FLHVSPAYLV ADRFNSSLEW TNNDAITVTP ATTNTTKFYI
     TRHTKYDALE TTAYKLKVKT VKYGEIEVPQ LSDSLYLTRR DSKIHVSDYP IGNKNLVYST
     AEIFTWKKYA DKTVLVVYGG ADEHHELAIE GEQADITDEN IIEGSDVTIQ QKDGYTVLGW
     AVSDERKVVR VHEDLYVYLL NRNEAYSFWV PPIVGDFGTS DVIVKAGYLI RNVAVNADSI
     SFTGDVNTTT TIEIIGGAPA PLKTLNFNGK SLDFKQNDHG AVTARVDFST PEIKLPCISQ
     LSWKYVDSLP EIKSDYSDEL WTAADLEKTY NTANPLKTPT SLYGGDYGYH TGSLLYRGHF
     TANGDESTFN ITTQGGNAYG ASVWLDDEFI GSWVGNAVSP AYNSTFTLPK LTKDKDYVFT
     VVVDHMGLNG NWVVGEEQQK NPRGILNYNL AGHEQSDIKW KITGNLGGED YADRVRGPLN
     EGGLFIERQG YHWPEPPSAS WEDSTGPAAG IKKAGIAYYS ATFDLDLPVG FDVPLSLTFA
     NTTVSAYRAQ IFVNGYQFGK FVHHIGPQAR FPIPEGILNY QGSNHLGITL WAMEKGGAKV
     EGLKWEVGMV SATGFGNVTP APQPKWVERK GAY
//
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