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Database: UniProt
Entry: A0A2B7ZV48_9EURO
LinkDB: A0A2B7ZV48_9EURO
Original site: A0A2B7ZV48_9EURO 
ID   A0A2B7ZV48_9EURO        Unreviewed;      1011 AA.
AC   A0A2B7ZV48;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=GX50_00046 {ECO:0000313|EMBL:PGH37063.1};
OS   Emmonsia crescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH37063.1, ECO:0000313|Proteomes:UP000226031};
RN   [1] {ECO:0000313|EMBL:PGH37063.1, ECO:0000313|Proteomes:UP000226031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH37063.1,
RC   ECO:0000313|Proteomes:UP000226031};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from
RT   Ajellomycetaceae.";
RL   Submitted (OCT-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:PGH37063.1}.
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DR   EMBL; PDND01000001; PGH37063.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000226031; 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:UP000226031};
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:UP000226031};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012564048.
FT   DOMAIN      396    575       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  112209 MW;  92276D04754F2875 CRC64;
     MRFLSACAIA CLAFQSAAAV VDRKLGGFTV IEHPDPVKRD LLQDIVKWDN ESLFINGERI
     MIFSAEFHPF RLPVPSLWLD VFQKIKALGF NCVSFYTNWA LTEGKPGEYT AEGIFAWEPF
     FEAATEAGIY LLARPGPYIN AEVSGGGYPG WLQRVKGQFR TSAKDYLAAT DNYIAHIAAS
     VAKAQITNGG PVILYQPENE YTLSLRIHDF PDGKYMQYVI DQAREAGIVV PMISNDAWAA
     GNNAPGTGKG EVDIYGHDKY PPIRTSGLLG FCPPIGANSI SYKVLLHLIL LLRYVKLLDF
     QAGAYDPWGG VGLDKCSQLL NHEFERVFYK NNFSFGNVFL NLYMTFGGTN WGNLGHPGGY
     TSYDYGAPIS EDRNITREKY SELKLMGNFM KVSPSYLNAV PGHWSISRFT TTPALTVTPL
     IGRLSKSSFF VLRHSEYTSK ASTNYKLKLP TSVGRLTIPQ LNGTLTLNGR DSKIHVTDYD
     VAGTNILYST AEIFTWKKFG DRKVLVIYGG ENERHELAVS TNSMPSVVEG PSEDMQIKKV
     DDYVVLNWET IRERRIVDID DLSVFILDRN SAYNYWVPEV PRSGETPGFS TFENTASSII
     VKAGYLVRTA FVRGSELHIA ADFNTTTPIE VIGAPKTAST LHINGEKVEH NVDDNAIWTT
     SIEYAPPKID IPALENLEWK YIDSLPELQA DYDDSSWTTA DHKTTNNTLR PLTTPTSLHS
     SDYGYHAGYL IYRGHFVATG IETAISFETQ GGFGYGNSAW LNGRHIGSWK GKGYLGSSTN
     IYSFPKLKAG EKCVFTVLVD NMGLGQNYVI GADSAKNPRG IQHYVLFGRL QSSVTWKLAG
     NLGGEDYQDR FRGPLNEGGL YIERQGWHQS SPPSQSWKSA SPITDGIVGA GVGFFTAEFN
     LNIPRGWDVP LYFTFPGIKS SPSTYRVQLY VNGFQYGKYV SNLGPQTSFP VPQGILNYQG
     KNTIGITLWA LDGKGAKIER FVLEYREAVR TGMRDVALVD GPAWRKREGA C
//
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