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Database: UniProt
Entry: A0A1F8AA35_9EURO
LinkDB: A0A1F8AA35_9EURO
Original site: A0A1F8AA35_9EURO 
ID   A0A1F8AA35_9EURO        Unreviewed;       987 AA.
AC   A0A1F8AA35;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-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=ABOM_002518 {ECO:0000313|EMBL:OGM48583.1};
OS   Aspergillus bombycis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM48583.1, ECO:0000313|Proteomes:UP000179179};
RN   [1] {ECO:0000313|EMBL:OGM48583.1, ECO:0000313|Proteomes:UP000179179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX   PubMed=27664179;
RA   Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT   "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT   bombycis.";
RL   Genome Biol. Evol. 0:0-0(2016).
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:OGM48583.1}.
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DR   EMBL; LYCR01000015; OGM48583.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000179179; 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; -; 3.
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:UP000179179};
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:UP000179179};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    987       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5009534634.
FT   DOMAIN      395    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   987 AA;  107284 MW;  D5F9FDF849ACB5C9 CRC64;
     MKLLSVAAVA LLATQAAGAS IKHRLNGLTI LEHPDPAKRD LLQDIVTWDD KSLFINGERI
     MLFSGEVHPF RLPVPSLWLD IFQKIRALGF NCVSFYIDWA LLEGKPGDYR AEGIFALEPF
     FDAAKEAGIY LIARPGPYIN AESSGGGFPG WLQRVNGTLR SSDKPFLEAT DNYIANVAAT
     VAKAQITNGG PVILYQPENE YSGGCCGVTY PDGDYMQYVI DQALNAGIVV PLISNDASPS
     GHNAPGTGAG AVDIYGHDSY PLGFDCANPS VWPEGKLPDN FRQLHLEQSP STPYSLLEFQ
     AGAFDPWGGP GFENCYALVN HEFSRVFYRN DLSFGVSTFN LYMTFGGTNW GNLGHPGGYT
     SYDYGSPITE TRNVTREKYS DIKLLSNFVK VSPAYLTATP GNLSTGVYTD TSDLAVTPLI
     GDRPGSFFVV RHTDYSSQES TSYKLRLPTS AGNLTIPQLE GTLSLNGRDS KIHVVDYNVS
     GTNIIYSTAE VFTWKKFDDN KVLVLYGGPK EHHELAIASK SNATVIEGSD SGIVSKRKGS
     TVIISWDVSS TRRIVQVGDL RVVLLDRNSA YNYWVPELPT EGTSPGFNTA ETTASSIIVK
     AGYLLRGANL DGADLHLTAD FNATTPIEVI GAPASAKNLF VNGEKASHTV DKNGIWSSEV
     KYAAPEITLP SLKDLDWKYL DTLPEIKSSY DDSAWVSADL PTTKNTHRSL DTPTSLYSSD
     YGFHTGYLIY RGHFVANGKE SEFAIRTQGG SAFGSSVWLN EVYLGSWAGA DYAMDGNSTF
     KLSQLESGKN YVITVVIDNL GLDENWTVGE ETMKNPRGIL SYNLSGQDAS AITWKLTGNL
     GGEDYQDKVR GPLNEGGLYA ERQGFHQPQP PSDSWESGSP LEGLSKPGIG FYTAQLDLDI
     PKLGCAAVLQ LWQQHPGGPG TATSFPVPEG ILNYRGTNYL ALSLWALESD GAKLGSFELS
     YTTPVLTGYG DVESPEQPKY EQRKGAY
//
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