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Database: UniProt
Entry: A0A0F0IJN7_ASPPU
LinkDB: A0A0F0IJN7_ASPPU
Original site: A0A0F0IJN7_ASPPU 
ID   A0A0F0IJN7_ASPPU        Unreviewed;      1005 AA.
AC   A0A0F0IJN7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-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=P875_00021803 {ECO:0000313|EMBL:KJK66093.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 /
OS   SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK66093.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK66093.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R.,
RA   Ehrlich K.C., Bhatnagar D., Cleveland T.E., Bennett J.W.,
RA   Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-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:KJK66093.1}.
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DR   EMBL; JZEE01000322; KJK66093.1; -; Genomic_DNA.
DR   EnsemblFungi; KJK66093; KJK66093; P875_00021803.
DR   Proteomes; UP000033540; 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:UP000033540};
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:KJK66093.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1005       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002443313.
FT   DOMAIN      395    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1005 AA;  110081 MW;  BCEEBAA6E7E7AAE8 CRC64;
     MKLLSVAAVA LLAAQAAGAS IKHRLNGFTI LEHPDPAKRD LLQDIVTWDD KSLFINGERI
     MIFSGEVHPF RLPVPSLWLD IFHKIRALGF NCVSFYIDWA LLEGKPGDYR AEGIFALEPF
     FDAAKEAGIY LIARPGSYIN AEVSGGGFPG WLQRVNGTLR SSDEPFLKAT DNYIANAAAA
     VAKAQITNGG PVILYQPENE YSGGCCGVKY PDGDYMQYVM DQARKADIVV PFISNDASPS
     GHNVPGSGVG AVDIYGHDSY PLGFDCANPS VWPEGKLPDN FRTLHLEQSP STPYSLLEFQ
     AGAFDPWGGP GFEKCYALVN HEFSRVFYRN DLSFGVSTLN LYMIFGGTNW GNLGHPGGYT
     SYDYGSPITE TRNVTREKYS DIKLLSNFIK VSPSYLTATP RNLTTGVYTD TSDLAVTPLI
     GDRPGSFFIV RHTDYSSQES TSYKLKLPTS AGNLTIPQLD GTLSLNGRDS KIHVVDYNVS
     GTNIIYSTAE VFTWKKFNDN KVLVLYGGPK EHHELAIASK SNVTIIEGSD SGIVSTRKGS
     SVIIGWDVSS TRRIVQVGDL RVLLLDRNSA YNYWVPELPT EGTSPGFSTS KTTASSIIVK
     AGYLLRGAHL DGADLHLTAD FNATTPIEVI GAPTSAKNLF VNGEKASHTV DKNGIWSSEV
     KYAAPEIKLP GLKDLDWKYL DTLPEIKSSY DDSAWVSANL PKTKNTHRPL DTPTSLYSSD
     YGFHTGYLIY RGHFVANGKE SEFFIRTQGG SAFGSSVWLN ETYLGSWTGA DYAMDGNSTY
     KLSQLESGKN YVITVVIDNL GLDENWTVGE ETMKNPRGIL NYKLSGQDAS AITWKLTGNL
     GGEDYQDKVR GPLNEGGLYA ERQGFHQPQP PSESWESGSP LEGLSKPGIG FYTAQFDLDL
     PKGWDVPLYF NFGNNTQAAR AQLYVNGYQY GKFTGNVGPQ TSFPVPEGIL NYRGTNYLAL
     SLWALESDGA KLGSFELSYT TPVLTGYGDV ESPEQPKYEQ RKGAY
//
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