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Database: UniProt
Entry: A0A0F8X654_9EURO
LinkDB: A0A0F8X654_9EURO
Original site: A0A0F8X654_9EURO 
ID   A0A0F8X654_9EURO        Unreviewed;      1156 AA.
AC   A0A0F8X654;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ARAM_003474 {ECO:0000313|EMBL:KKK25120.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK25120.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK25120.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK25120.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic
RT   Aspergillus Species Obtained from the Cote d'Ivoire.";
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:KKK25120.1}.
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DR   EMBL; JZBS01000825; KKK25120.1; -; Genomic_DNA.
DR   EnsemblFungi; KKK25120; KKK25120; ARAM_003474.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
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   Gene3D; 3.90.190.10; -; 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   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR026893; Tyr/Ser_Pase_IphP-type.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; TYR_PHOSPHATASE_dom.
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   Pfam; PF13350; Y_phosphatase3; 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   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000034291};
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:UP000034291}.
FT   DOMAIN     1064   1115       TYR_PHOSPHATASE_2. {ECO:0000259|PROSITE:
FT                                PS50056}.
SQ   SEQUENCE   1156 AA;  126895 MW;  0B02875828F0D45E CRC64;
     MWLDVFQKLR ANGFNAVSVY FFWSWHSASE GEYDFTSGAH DIQRLFDYAK DAGLYVIARA
     GPYCNAETSA GGYALWAANG QMGSERTSDE AYYRLWKPWV LEVGKIIAAN QITNGGPVIL
     NQHENEYQET SYNSGATQVV YMEQIAEAFE EAGILVPSTH NEKGMRSVSW STDYHDVGGA
     VNVYGLDSYP GGLSCTNPNT GFNLVRNYYQ WFQNYSFTQP EFLPEFEGGW FQPWGGYVYD
     TCQAELSPEF ADVYYKNNVG SRVTLQSIYM VFGGTNWGHS AAPVVYTSYD YSAPLRETRE
     VRDKLKQTKL LGLFTRVSKD LLKTYMEGNG TGYTSDDSIF TWALRNPDTN AGFFVVAHES
     SPSRAVTNFT LTVNTTAGEL SIPDIQLAGR QSKIIVTDYT AGKQTSLLYS SAEVLTYATL
     DVDVLVFYLN VGQKGVFAFK DAPAHVSFKE YGSSRLIASK TSYGTQYSYV QTEGVTVVKF
     SNGVLAYLLD KASAWNFFAP PLTSNPDVAP GEQVLVQGPY LVRSASIHGD TIEVIGDNAN
     TTSLEVYTGK SHVQKVKWNN KLVKTKKTAY GSLIGTAPGV ENAKVSLPSL GPWKAQDTLP
     EIDPDYDDSN WTQCNKSTTV NGQPPVSLPV LYSGDYGYHA GTKLYRGRFD GKNATGVNVT
     VQNGIAAGWA AWLNGEYVGG ALGDPGLAST QAVLSLNPSS LRSRDNVLTI VADYTGHDED
     NVKPHGAQNA RGVLGATLVG GGDFTSWRIQ GNAGGEKNID PVRGPMNEGG LYGERMGWHL
     PGYRAPTTAS TSSPLDGVLG AEGRFYTTTF TLDLDSDLDV PIGLQLGAPE GTHAVVQIFM
     NGYQYGHYLP HIGPQSLFPF PPGVINQQGE NTLAISLWAL TDQGARLDQV ELTAYAKYRS
     GFEFGRDWSY LQPRWEDRSI IDLDSPDRPF DNIINFRDVG RTINRLMGRP VLKEGVFYRS
     ARLDEASERD KRRLVSEYHI STIIDLRSGK VLSYLASGNR IDAITLIGSE VMNPRGLVGL
     AKDTLDNSTA EMREVFEILG GGTAASLSTR GNENENETRT IPAPVLVHCT QGKDRTGLVV
     LLLLLLTGVV DDEAMAAEYV LSESELAVEG EERMKEIRAW GWMMSSRGVR GCLRGRSGRI
     WMSGMEACRA ERQPGI
//
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