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Database: UniProt
Entry: A0A2B7XDZ9_9EURO
LinkDB: A0A2B7XDZ9_9EURO
Original site: A0A2B7XDZ9_9EURO 
ID   A0A2B7XDZ9_9EURO        Unreviewed;       997 AA.
AC   A0A2B7XDZ9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-FEB-2019, entry version 9.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=GX51_01927 {ECO:0000313|EMBL:PGH07140.1};
OS   Blastomyces parvus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH07140.1, ECO:0000313|Proteomes:UP000224080};
RN   [1] {ECO:0000313|EMBL:PGH07140.1, ECO:0000313|Proteomes:UP000224080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH130 {ECO:0000313|EMBL:PGH07140.1,
RC   ECO:0000313|Proteomes:UP000224080};
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:PGH07140.1}.
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DR   EMBL; PDNC01000016; PGH07140.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000224080; 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:UP000224080};
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:UP000224080};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    997       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012180029.
FT   DOMAIN      396    575       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   997 AA;  110469 MW;  C530726BED42E058 CRC64;
     MRFLSACAIA CLALQSAAAA VVDRKLGGFT VIEHPDPVKR DLLQDIVKWD NESLFINGER
     IMIFSAEFHP FRLPVPSLWL DIFQKIKALG FNCVSFYTYW ALTEGKPGDY TAEGIFAWEP
     FFEAATEAGI YLLARPGPYI NAEVSGGGFP GWLQRVKGQF RTSDKDYLAA TDNYIAHIAS
     TVAKAQITNG GPVILYQPEN EYTLSLRIHD FPDGDYMQYV IDQARNAGIV VPMISNDAWA
     AGNNAPGTGK GEVDIYGHDK YPLGFNCANP DFWPPGFLPT HWRQLHLIQS PTTPYSLVEF
     QAGAYDPWGG VGLDKCSQLL NHEFERVFYK NNFSFGNVFL NLYMTFGGTN WGNLGHPGGY
     TSYDYGAPIS EDRNITREKY SELKLMGNFM KVSPSFLNAV PGHWSISKFT TTPALTVTPL
     IGRMSNSSFF VLRHSEYTSK ASTNYKLKLP ASVGSLTIPQ LKGTLTLNGR DSKIHVTDYD
     VAGTNILYST AEIFTWKKFG DRKVLVVYGG ENERHELAVS TSSMPSVVEG PSEDMTIKKV
     DDYVVLNWET MRERRIVDIG ELSVYILGNG ETPGFSTFEN TASSIIVKAG YLVRTAFVRG
     SELHITADFN TTTPIEIIGA PKATSTLHIN GEKVGHKVDD NGIWTTSIEY AAPKIDLPDL
     GSLEWKYIDS LPELQEDYDD SSWTVADHKK TNNTLRPLTT PTSLHASDYG YHTGYLVYRG
     HFVASGIETG ISFETQGGFG FGNSAWLNGT HIGSWKGKGH LGSSTNIYSF PKLKAGEKYV
     FTVLVDNMGL GQNYVIGADS TKNPRGIQHY ELFGRLQSRV TWKLAGNLGG EDYQDRFRGP
     LNEGGLYIER QGWHQPSPPS QSWKSASPIT DGVDGAGVGF FTTEFNLNIP RGWDVPLYFT
     FPGINSSPST YRVQLYVNGF QFGKYVSNLG PQTSFPVPQG ILNYQGKNTV GITLWALDGK
     GAKLERFVLE YREAVRTGMR DVTLVDGPAW KEREGAC
//
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