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Database: UniProt
Entry: A0A229XDU5_9EURO
LinkDB: A0A229XDU5_9EURO
Original site: A0A229XDU5_9EURO 
ID   A0A229XDU5_9EURO        Unreviewed;      1005 AA.
AC   A0A229XDU5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   16-JAN-2019, entry version 8.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CFD26_03568 {ECO:0000313|EMBL:OXN18413.1};
OS   Aspergillus turcosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1245748 {ECO:0000313|EMBL:OXN18413.1, ECO:0000313|Proteomes:UP000215289};
RN   [1] {ECO:0000313|EMBL:OXN18413.1, ECO:0000313|Proteomes:UP000215289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 1038 {ECO:0000313|EMBL:OXN18413.1};
RA   Dufresne P.J., Fournier E., Martineau C., De Repentigny L.,
RA   Dufresne S.F.;
RT   "Draft genome of two Aspergillus turcosus strains, one azole-
RT   susceptible and the other azole-resistant, isolated from
RT   bronchoalveolarlavage fluid.";
RL   Submitted (OCT-2016) 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:OXN18413.1}.
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DR   EMBL; NIDN01000062; OXN18413.1; -; Genomic_DNA.
DR   Proteomes; UP000215289; 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:UP000215289};
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:UP000215289};
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_5012963440.
FT   DOMAIN      395    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1005 AA;  109637 MW;  470FF12C7295D4EB CRC64;
     MKLFSVCAVA LLAAQAAAAS IKHKLNGFSI TEHSDPEKRE LLQKYVTWDA KSLFVNGERI
     MIFSGEFHPF RLPVPPLWRD VFQKIKALGF NCVSFYVDWA LLEGKPGEYR AEGIFDLEAF
     FDAAKNAGIY LLARPGPYIN AEASGGGFPG WLQRVNGTLR TSAPAYLKST DNYVAHVAAT
     IAKGQITNGG PVILYQPENE YSGACCGVKF PDAAYMQYVE DQARNAGIIV PFINNDAYPG
     GHNAPGTGEG EVDIYGHDSY PLGFDCGHPS VWPAGGLPTN FRTLHMQQSP TTPYSLVEFQ
     AGSFDPWGGP GFAACAALVN HEFETVFYKN DLSFGAALLN LYMTYGGTNW GNLGHPGGYT
     SYDYGSALTE SRNLTRQKYS ELKLIGNFVK ASPSYLLATP GSSTTSGYAD TPDLTVTPLL
     GNGTGSYFVV RHTDYTSQAS TSYKLTLPTS AGNLTIPQLG GTLTLNGRDS KVHVVDYNVG
     GTNILYSTAE VFTWKKFGDS KVLILYGGPG EHHELAVSSK SNVQVVEGPM SGATSKKAGD
     VVVIAWDVSP SRRIVQIDDL KIFLLDRYSA YNYWVPQVDK DASSTGFSSE ETTASSIIVK
     AGYLVRTAYT KGSGLYLTAD FNATTSVEVI GAPSGVRNLY INGEKAQFKT DKNGIWSTEV
     KYSPPKMQIP NMKDLDWKYL DTLPEIQSTY DDSAWTAADL DKTYNTLRPL TTPKSLYGAD
     YGFNTGYLIF RGHFVADGSE TTLDIQTQGG QAFGSSVWLN GTFLGSWTGL NANMAYSSTY
     KLPQLEKGKH YVFTVVVDEM GLDENWTIGT ESMKNPRGIL SYKLSGRDDS VITWKLTGNL
     GGEDYWDKVR GPLNEGGLYA ERQGFHQPQP PSKNWKSASP LQGLSKPGIG FYSAQFDLDI
     PSGWDVPLYF TFGNGTSSAY RVQLYVNGYQ YGKLVSNIGP QTAFPVPQGI LNYQGTNWVA
     VTLWALESGA KLDDFELVNT TPVLSAIGKI GSSPQPKWRQ RKGAY
//
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