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Database: UniProt
Entry: S8BHW2_DACHA
LinkDB: S8BHW2_DACHA
Original site: S8BHW2_DACHA 
ID   S8BHW2_DACHA            Unreviewed;      1092 AA.
AC   S8BHW2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   16-JAN-2019, entry version 30.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=H072_7445 {ECO:0000313|EMBL:EPS38833.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS38833.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS38833.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS38833.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A.,
RA   Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) 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:EPS38833.1}.
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DR   EMBL; AQGS01000526; EPS38833.1; -; Genomic_DNA.
DR   RefSeq; XP_011113201.1; XM_011114899.1.
DR   EnsemblFungi; EPS38833; EPS38833; H072_7445.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; 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   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; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000015100};
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:UP000015100};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1092       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004548389.
FT   DOMAIN     1054   1092       CBM1. {ECO:0000259|PROSITE:PS51164}.
SQ   SEQUENCE   1092 AA;  117658 MW;  8298206B96B1A817 CRC64;
     MVLFGRIAFA AAAAATTLVA AFPAQESPPG LKIRQSSSQT NVTWDKYSLS VNGKRVMLYS
     GEVHPFRNPV QSLHLDIFQK IKAMGFNCVS FYVHWGFIEY DRGTFNWNGI HDLQPFFDAA
     KKANIWLLAR PGPYINAEAT GGGFPGWGTR IEGPWRNSNP NYTNAWQPYW NSVSQIIAKN
     QVTNGGPIIL VQPENEYTSF PTGSSEDKSY ENNLLSILHN NGVIIPTICN DAWAAGNFKS
     VNIYGYDSYP AGQYTNGYSE IVVLMYKTAD FVTKGFDCSH PTTWPSVPNF WGSHEGTAPN
     TPHAIVEYQG GSFDGWGGAG WAACNQLLGP QFARVFYKDI YASAITIFNI YMTYGGTNWG
     RIGHPGVYTS YDYAAAIAED RTLREKYYEE KLQALFLKVS PAYLTSTPGT PATVGTSGSQ
     MTITTLKDNV GGKTRFNIIR QSNPNESSNS NWKLSLTTSA GTLSVPTLNN ANFALPSHDS
     KTIVTDYSAG GVNILYSTSE ILTWQVLDGK TIIVLYANKG ETGETAIITS ATLTPSVLSG
     SSGGISSKQS GSTFTIQYQH TGATVISLGS NILLYIVDHV EAYNFWVPDL SIPVIVKGGY
     LLRAATFSGN TLALSGDTNG TTTFEVFAGS AVSTITWNGK GLNLSKTAYG SFAGSYSPTL
     PSIAIPTLSS LTWKYADGLP EIQTSYDDSK WVSASNTYTP NSQKPSTPVI LYASDYGFHT
     GNIIWRGHFT ATGGETAFKV TVQGGSGFGY SVWDNGAFIG SWTGNGGTGS HSDTFSLSTW
     AKGSKHVITV VQDHSGLEQN WTANSDSFKA YRGIFAYSFN GATPTSNGWK VTGNLGGEKI
     LFAVAIMRAA YTENDKVLRI FHSLAEFRQP LNNMHHFSLG WHLPGFDDNN WAAKSPLQGP
     GGPAIEFYRA TFNLNIPSGV DYPMSIDLGN SIGGSSLRTQ IFVNGYHFGK YIDNIGPQVS
     FPIPQGILNY NGANTLVLSL WNLQKNPAGL KSLSLHIRAM IEGGVGTVSN APMPTWTARP
     NAYESTISGS SSTTTKATTT TSVAVTTTVS SPQSTATIYG QCGGIGYTGA TKCPSSSTCT
     YGNPLPPKLN VI
//
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