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Database: UniProt
Entry: A0A0H1B1Z0_9EURO
LinkDB: A0A0H1B1Z0_9EURO
Original site: A0A0H1B1Z0_9EURO 
ID   A0A0H1B1Z0_9EURO        Unreviewed;      1011 AA.
AC   A0A0H1B1Z0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=EMPG_11070 {ECO:0000313|EMBL:KLJ05444.1};
OS   Emmonsia parva UAMH 139.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=1246674 {ECO:0000313|EMBL:KLJ05444.1};
RN   [1] {ECO:0000313|EMBL:KLJ05444.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 139 {ECO:0000313|EMBL:KLJ05444.1};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Munoz J.F., Gallo J.E., Misas E., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Priest M.E., Saif S., Young S., Zeng Q., Wortman J.,
RA   Birren B.;
RT   "The Genome Sequence of Emmonsia parva UAMH 139.";
RL   Submitted (MAY-2015) 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:KLJ05444.1}.
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DR   EMBL; LDEV01003634; KLJ05444.1; -; Genomic_DNA.
DR   EnsemblFungi; KLJ05444; KLJ05444; EMPG_11070.
DR   OrthoDB; 179316at2759; -.
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   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869}; 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_5005199349.
FT   DOMAIN      396    575       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  112196 MW;  6CE4182EC80F0015 CRC64;
     MRFLSACAIA CLALQSAAAA VVDRKLGGFT VIEHPDPAKR DLLQDIVKWD NESLFINGER
     IMIFSAEFHP FRLPVPSLWL DIFQKIKALG FNCVSFYTNW GLTEGKPGEY TAEGIFAWEP
     FFEAATEAGI YLLARPGPYI NAEVSGGGFP GWLQRVRGQF RTSDKDYLAA TDNYIAHIAS
     TVAKAQITNG GPVILYQPEN EYTLSLRLHD FPDGDYMQYV IDQARKAGIV VPMISNDAWA
     AGNNAPGSGK GEVDIYGHDK YPLGFNCADP DFWPPGFLPT HWRQLHLLQS PATPYSLVEF
     QAGAYDPWGG NGLDKCARLL NHEFQRVFYK NNFSFGNVFL NLYMTFGGTN WGNLGHPGGY
     TSYDYGAPIS EDRNITREKY SELKLMGNFM KASPSFMNAV PGHWSLSKFT NKPALTVTPL
     IGRLSDSSFF VLRHSEYSSK ASTNYKLKLP TSVGRLTIPQ LNGTLTLNGR DSKIHVTDYD
     VAGTNILYST AEIFTWKKFG DRKVLVVYGG ENERHELAVS TSSMPSVVEG PSHDMTIKKV
     DDYVVLNWET MPERRIVDIG DLSVFILDRN SAYNYWVPEV PRSGETPGFS TFENTASSII
     VKAGYLVRTA FVRGSELHIT ADFNTTTPIE VIGAPKKTST LHINGEKVGH KVNDHGIWTT
     SIEYAAPKIE LPDLESLEWK YIDSLPELQG DYDDSAWTVA DHKKTNNTLR PLTTPTSLHA
     SDYGYHAGYL IYRGHFVASG IETGISFETQ GGFGFGNSAW LNGSHIGSWK GKGHLGSSTN
     IYSFPKLKAG QKYIFTVLVD NMGLGQNYVI GADSAKNPRG IQHYELFGRL QSRVTWKLAG
     NLGGEDYQDR FRGPLNEGGL YIERQGWHQP KAPTQSWKSA SPITDGVDGA GVGFFTTEFN
     LDIPRGWDVP LYFTFPGINS SPSTYRVQLY VNGFQFGKYV SNLGPQTSFP VPQGILNYQG
     KNTVGITLWA LDGKGAKLER LVLEYREAVR TGMRDVTLVD GPAWKKREGA C
//
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