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Database: UniProt
Entry: A0A150UT40_9PEZI
LinkDB: A0A150UT40_9PEZI
Original site: A0A150UT40_9PEZI 
ID   A0A150UT40_9PEZI        Unreviewed;      1024 AA.
AC   A0A150UT40;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=M433DRAFT_7971 {ECO:0000313|EMBL:KYG41419.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales;
OC   Capnodiales incertae sedis; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG41419.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG41419.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG41419.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z.,
RA   LaButti K., Lapidus A., Lipzen A., Chen C., Johnson J.,
RA   Lindquist E.A., Pan C., Hettich R.L., Grigoriev I.V., Singer S.W.,
RA   Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG41419.1}.
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DR   EMBL; JPDO01000688; KYG41419.1; -; Genomic_DNA.
DR   EnsemblFungi; KYG41419; KYG41419; M433DRAFT_7971.
DR   Proteomes; UP000075602; 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:UP000075602};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:KYG41419.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1024       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007571224.
FT   DOMAIN      402    589       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1024 AA;  113157 MW;  E5797C45F8B5BF48 CRC64;
     MRLSKLPEAL VSAVLLGQTI ASTVPHGPAD IEIGIKNNPI ARNPNLQDIV TYDGESYFIY
     GERIFMFSGS FHPFRLPVAD LYIDVFQKIK ALGFNAVTFY TDWALVEAEP GHVRFDGIFD
     IEPFIQAAAD AGLYLLARPG PYINAEVSAG GIPAWVLQIP CVLRSNCTEW EDSTKLYMAA
     VGEIIAKYQI TNGGPIIFTQ VENEYTSWPN VTHFPAQLNR DYMAFLEREL RAAGIVVPLT
     FNDDAQAGIW APGTGLGSVD VYGIDSYPLG FDCADPLSWQ YASLPENWQI DQKSWSPTTP
     FTIFEFQGGS MEGWGDVSQT LCNAMVGPDA VRVFYKNNFS FGIKWFNLYM TYGGTNWGNL
     GYDGCYTSYD YGAAINEYRE VIREKYSAEK LEANFFKVSP GYLTAVAGNV TAGVYASTNA
     VSTTPLFGTR QNSNFYVVRQ TNWNSTGNVY YKITLPTSSG NISIPQLGGQ LSLIGRDSKI
     MVTDYAVGDF NLLYSSADIF SWGKSRAGKT VLIMYAAEGE TNEFAISPSS GRQSWNGAKP
     WCSDSSTEIS STDQKTWKIK WNTTEKSQMV KIGSDLDVYL LWRNDAYNYW LLELPAASPI
     NNYSHPGKEY VIVKAGYLMR TAQIIGTELQ LTGDFNKTTE LSLVFDPTDS VRSIRVNGKL
     LTVTDDQGVL KGTVQYTPPS LDLPDFSKIE WKTIDSLPEI KPSYDDSLWT KCDKTTSTND
     QMALKTPFSL FANEYGYDTG SFEYRGHFIA NGKESFVTLD VAGGTGFANS VWLDETFLGS
     WVGSGTNSSY QKTYTIPTNA TSKGKESILT VVIDMMGQTE EAPGTDTIKR PRGILDFELA
     GHSQKDVSWR MTGNLGGWAN YADKARGPRN EGAAWAVRQG YFQPDPPDSN WTVSSPMEGI
     SAPGLQFYTT EFDLNIAEGW DVPMGVAFTN NTASTGLYRL DFYVNGYQFG KFVPNLGPQF
     EFPVPQGILN YNGKNTLAMV FWALEEGGAK LGSIELKPKA IVLSALKTPA SSPQPKWTPR
     PNAY
//
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