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Database: UniProt
Entry: A0A0F4YKT2_TALEM
LinkDB: A0A0F4YKT2_TALEM
Original site: A0A0F4YKT2_TALEM 
ID   A0A0F4YKT2_TALEM        Unreviewed;       987 AA.
AC   A0A0F4YKT2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-FEB-2019, entry version 21.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:KKA18839.1};
GN   ORFNames=T310_7207 {ECO:0000313|EMBL:KKA18839.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA18839.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA18839.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA18839.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z.,
RA   Wu L., Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-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:KKA18839.1}.
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DR   EMBL; LASV01000412; KKA18839.1; -; Genomic_DNA.
DR   RefSeq; XP_013325451.1; XM_013469997.1.
DR   EnsemblFungi; KKA18839; KKA18839; T310_7207.
DR   GeneID; 25319483; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000053958; 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:UP000053958};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    987       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002481765.
FT   DOMAIN      381    558       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   987 AA;  107974 MW;  F0C077752C37638D CRC64;
     MRFLSLLLLL LPAVVLGTLL GRTDDGKTTA VTWDKYSLSV NGKRLFVFSG EFHYQRLPVP
     ELWLDVFQKL KANGFNAVSV YFFWSFHSAS EGHFDFETGA HNVQRLFDYA KQAGLYVIAR
     PGPYCNAETS AGGLALWAAN GQLGKERTSD ERYYSRWLPW MQEIGKILAA NQITNGGPVI
     LVQHENELQE TVYSPNNTLV VYMEQIAQAL DAAGVVVPST SNEKGMRSVS WSTDYHDVGG
     AVNIYGLDSY PGGLSCTDPN AGFNLVRTYY QWFQNYSFTQ PEFLPEFEGG WFSGWGGVFY
     DGCTSELSPE FADVYYKNNI GSRVTMQNLY MAFGGTNWGH SATPVVYTSY DYDAPLRETR
     EIRDKLKQTK LLGLFTRVSS DLLKTDMVGN GTGYTSDDGI YTWALRNPDT QAGFYVVAHN
     DSPSRAVTNF AINVNTSAGP VSIPNVQLDG RQSKIIVTDY RFGNSALLFS SAEVLTYANL
     DVDVLVLYLN AGQTGVFALK NPPPGLTYTV YGNSNFTASR SKNGTTTYSY TQGEGISAVK
     FSNGVLIYLL DKFTAWNFFA PPTTSDPAVG PDQHVFVIGP YLVRQASIQG DTIEIVGDNA
     NTTFIEVYAG DPKVNNVQWN GKHINVRRTP YGSLVGQVPG AEDVVISLPK LGPWKAQDTI
     PEIDPNYDDS RWTVCNKTVS VNAIAPLSLP VLYSGDYGYH AGVKVYRGRF DGQNVTGANI
     TVQNGVAAGW SAWLNGKYVG GSAGDVNLAA TWAELQFQNS TLRAKDNVLT VVTDYTGHDE
     DNVKPAGAQN PRGILGAVLT GGRNFTSWKI QGNAGGEKNI DPTRGPLNEG GLYGERMGWH
     LPGYEPPATA SDSSPLEGVS GAGGQFYITT FELNLDPDLD VPIGLRLSAP ADVPAVVYVF
     LNGYQFGHYL PHIGPQNTFP IPPGIINTNK NNNAKNTLAI SLWALTDKGA KLDAVELVAY
     GKYRTGFDLS HDWSYLQPGW VDRSEYA
//
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