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Database: UniProt
Entry: A0A0L1J777_ASPNO
LinkDB: A0A0L1J777_ASPNO
Original site: A0A0L1J777_ASPNO 
ID   A0A0L1J777_ASPNO        Unreviewed;       997 AA.
AC   A0A0L1J777;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   13-FEB-2019, entry version 15.
DE   SubName: Full=Beta-galactosidase B {ECO:0000313|EMBL:KNG87268.1};
GN   ORFNames=ANOM_003563 {ECO:0000313|EMBL:KNG87268.1};
OS   Aspergillus nomius NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG87268.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG87268.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG87268.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus
RT   nomius.";
RL   Submitted (JUN-2014) 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|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:KNG87268.1}.
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DR   EMBL; JNOM01000087; KNG87268.1; -; Genomic_DNA.
DR   RefSeq; XP_015408191.1; XM_015548820.1.
DR   EnsemblFungi; KNG87268; KNG87268; ANOM_003563.
DR   GeneID; 26805367; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000037505};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      7     29       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      395    572       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   997 AA;  110233 MW;  4B11852005BDAB5D CRC64;
     MKEDLRAVSI VAGEGYAVIR IFYLVWLLLL TGKVSGLDNG KTTEVTWDKY SLSVKGERLF
     VFSGEFHYQR LPVPELWLDV FQKLRANGFN TISVYFFWSY HSASEDEFDF TTGAHDIQRL
     FDYAKQAGLY VIARAGPYCN AETSAGGFAL WAANGQMGSE RTSDEAYYKR WRPWIREVGK
     IIAANQITKG GPVILNQHEN ELQETTYDSN DTKVIYMEQI AKAFEEAGVV VPSSHNEKGM
     RTVSWSTDYK DVGGAVNVYG LDSYPGGLSC TNPNSGFNLV RTYYQWFQNY SYTQPEYLPE
     FEGGWFQPWG GSFYDTCASE LSPEFADVYY KNNIGSRVTL QNIYMTFGGT NWGHSAAPVV
     YTSYDYGSPL RETREIRDKL KQTKLLGLFT RVSKDLLKTY MEGNGTGYTS DDSIYTWALR
     NPETDAGFYV VTHETSSSRE VATFSLNVKT SAGTIAIPEI ELDGRQSKII VTDYRIGSES
     SLLYSSAEIL TYATLDVDVL VFYLNAGQKG VFVFKDAPAD LIYQTYGNSN LSSSETSQGT
     QYSYVQGEGI TAVKFSNGVL VYLLDKKTAW NFFAPPTISS PTVAPSEHIL VFGPYLVRGA
     SIKHDTVEVI GDNSNSSSIE VYTGDEHVKK VSWNGNLIDT RVTTYGSLIG TVPGAEDIEV
     SLPSLSSWKA QDTLPEISPD YDDSRWTICN KTTSVNSIAP LSLPVLYSGD YGYHAGTKIY
     RGRFDGQNVT GANVTVQNGA AAGWAAWLNG AYVGGFSGDP DKVTSWEVLQ FNISSLRPRD
     NVLTIIMDYT GHDQNSQKPI GTQNPRGIMG ATLIGGGNFT LWRIQGNAGG EKNIDPVRGP
     MNEGGLYGER MGWHLPGYQA PELALDSSPL EGVLGAEGRF YTTSFKLDLN ADLDVPIGLQ
     LSAPAGTTAV VQIFMNGYQF GHYLPHIGPQ DLFPFPPGVI NNQGQNSLAI SMWALTAAGA
     RLEQVELKAY AKYRSGFDFS RDWSYLQPGW KDRAEYA
//
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