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Database: UniProt
Entry: A0A0S7DJI2_9EURO
LinkDB: A0A0S7DJI2_9EURO
Original site: A0A0S7DJI2_9EURO 
ID   A0A0S7DJI2_9EURO        Unreviewed;       983 AA.
AC   A0A0S7DJI2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-FEB-2019, entry version 13.
DE   SubName: Full=Probable beta-galactosidase C {ECO:0000313|EMBL:GAQ03470.1};
GN   ORFNames=ALT_0791 {ECO:0000313|EMBL:GAQ03470.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GAQ03470.1, ECO:0000313|Proteomes:UP000051487};
RN   [1] {ECO:0000313|EMBL:GAQ03470.1, ECO:0000313|Proteomes:UP000051487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GAQ03470.1,
RC   ECO:0000313|Proteomes:UP000051487};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Aspergillus lentulus strain IFM 54703T.";
RL   Submitted (NOV-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|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:GAQ03470.1}.
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DR   EMBL; BCLY01000001; GAQ03470.1; -; Genomic_DNA.
DR   EnsemblFungi; GAQ03470; GAQ03470; ALT_0791.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000051487; 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; 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:UP000051487};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051487};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    983       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006633851.
FT   DOMAIN      382    558       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   983 AA;  107930 MW;  E950855DC37ABEA2 CRC64;
     MRVFSFLFLL LLGILTGEGL VSGTDNGKTT DVTWDKYSLS VKGQRLFVFS GEFHYQRLPV
     PELWLDVFQK LRANGFNAIS VYFFWSFHSA SEGEYDFETG AHDIQRLFDY AKEAGLYVIA
     RAGPYCNAET SAGGFALWAA NGQMGNERTS DEAYYKKWRP WILEVGKIIA KNQITNGGPA
     ILNQHENELT ETTYDPNHTL VIYMKQIAQV FEEAGIVVPS SHNEKGMRGV SWSTDYNNVG
     GAVNIYGLDS YPGGLSCTNP NSGFRLVRTY YQWFQNYSFT QPSYMPEFEG GWFQPWGGSF
     YDTCAAELSP EFPDVYYKNN IGSRVTLHNI YMTFGGTNWG HSAAPVVYTS YDYAAPLRET
     REIRDKLKQT KLIGLFTRVS ADLLKTYMEG NGTGYTSDSS IYTWSLRNPD TNAGFYVLAH
     STSSSRDVTT FSLNVTTSAG AISIPDIELN GRQSKIIVTD YNFGNNSTLL FSSAEVLTYA
     NLDVNVLVFY LNVGQKGTFV FKEEPKLAFE TYGNSNITAS ESSYGTQYSY TQGEGATAVK
     FSNGVLVYLL DKESAWNFFA SPTTSSPQVA PNEHILVQGP YLVRGASINH GTVEITGDNA
     KTTSIEVYTG NSQVKKVKWN GKTVKTRETA YGSLIGTVPG AEDVTITLPS LDSWKAQDTL
     PEIQPDYDDS KWTVCNKTTS VNAIAPLSLP VLYSGDYGYH AGTKVYRGRF DGRNVTGANV
     TVQNGAAAGW AAWVNGQYAG GSVGSPSSAA TSAVLTFNSS ALKDRDNVLT VVTDYTGHDQ
     NSVRPKGTQN PRGILGATLI GGGNFTSWRI QGNAGGEKNI DPVRGPMNEG GLYGERMGWH
     LPGYKVPKSA SKSSPLDGVP GAEGRFYTTT FKLKFDKDLD VPIGLQLGAP EGTKAVVQVF
     MNGYQFGHYL PHTGPQSLFP FPPGVINNRG ENTLAISMWA LTDAGAKLDK VELVAYGKYR
     SGFDFNQDWG YLQPGWKDRS QYA
//
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