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Database: UniProt
Entry: A0A1G4B5L7_9PEZI
LinkDB: A0A1G4B5L7_9PEZI
Original site: A0A1G4B5L7_9PEZI 
ID   A0A1G4B5L7_9PEZI        Unreviewed;      1011 AA.
AC   A0A1G4B5L7;
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_08060 {ECO:0000313|EMBL:OHE96603.1};
OS   Colletotrichum orchidophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHE96603.1, ECO:0000313|Proteomes:UP000176998};
RN   [1] {ECO:0000313|EMBL:OHE96603.1, ECO:0000313|Proteomes:UP000176998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 309357 {ECO:0000313|EMBL:OHE96603.1,
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:OHE96603.1}.
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DR   EMBL; MJBS01000067; OHE96603.1; -; 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:OHE96603.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176998};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5009602487.
FT   DOMAIN      392    568       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  110452 MW;  12D7B0250CCAB7BC CRC64;
     MRLSLFSIAS LGIGFWTAVS AGLVGGRPPT VIIKDEKRDQ LQDIVTWDEH SLFVRGERVM
     IFSGEIHPFR LPVPSLYLDI FQKVKALGLN TVSFYVNWAL LEGKAGEFTA EGVYDLKPFF
     DAATKAGIYL IARPGPYINA EVSGGGFPGW LARLRAKLRT SDPEFLSATD NYMAKICGII
     AKAQITNGGP VILLQPENEY TNFENGSSPD GKYFQYVIDQ ARKAGVVVPL ISNDARPLGH
     NAPGTGTNIC IQGHDGYPLG FDCANPNTWP GGKLPTNYHA LHLQQSPSTP YSILEFQGGS
     FDPYGGPGFE KCAALLNHEF ERVFYKNNFG AGVTIFNVYM IFGGTNWGNL GHPGGYTSYD
     YGAAITEERS VAREKYSELK LEAQFLKVSP AYLTTTPGNL TVGVYSATPD ITVTPLLGNG
     NGSFFVVRHS NYSSLATTDY TLRLPTSQGT ITIPQSRDLL QLTRRDSKFV VTDYPVGETI
     LLYSTAEILT WKHFKNQTVL VVYSGLGETH EIAIKSTVTP FLIEGTSVDH NYVNKTLLLA
     WETSSTRRVV KVDNLVIYIL DRNSAYNYWV PDKPGGSQPA YGTSIMKPDS LIINGGYLIR
     SISIQGDTLR VQADFNRTVE LEIIGIEPEV TRLEVNGKQL DHTTNNLTNW IAKPSLADGT
     LSLPDLKSLN WSSIDSLPEI RAGYDDSAWP LADHKTTNNT IANLTTPVSL FASDYGFHAG
     TLVFRGYFTS KGTENMLNIT TQGGSAFASS IWLNETFLGS FANGPDASGD NNSNYTMTNL
     TAGATYVLTI LVDTTGLEEN FNIPADMMKN PRGIMDYIIT SPSGAQTNVT TWKVTGNLGG
     EDYADRFRGP LNEGGLFIER QGYHLPSPPE SALNTKRSPF DGADAPGVAF YAAKLDLHVP
     ATDLDVPLAF LFDDIVASSN GTGAYRAILY VNGFQYGRYV SNIGPQTRFP VPEGILRYQG
     TNYIGLAVWA LEKGGARVQN FRLDVGEVVT TGREEVKVVE APGWSRRAGA Y
//
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