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Database: UniProt
Entry: A0A150VFV6_9PEZI
LinkDB: A0A150VFV6_9PEZI
Original site: A0A150VFV6_9PEZI 
ID   A0A150VFV6_9PEZI        Unreviewed;      1019 AA.
AC   A0A150VFV6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-FEB-2019, entry version 15.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:KYG49409.1};
GN   ORFNames=M433DRAFT_140088 {ECO:0000313|EMBL:KYG49409.1};
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:KYG49409.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG49409.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG49409.1,
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|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:KYG49409.1}.
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DR   EMBL; JPDO01000024; KYG49409.1; -; Genomic_DNA.
DR   EnsemblFungi; KYG49409; KYG49409; M433DRAFT_140088.
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; 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:UP000075602};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:KYG49409.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   DOMAIN      388    571       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1019 AA;  111928 MW;  6DD76E3F223668EF CRC64;
     MKFLKVLLAA AQQWPLHNDG MNDVVQWDHY SLIVNGERLF FWSGEFHYWR IPVPELWIDI
     MQKIKAAGFN AFSIYAHWGF HSAAPNALDF ASGAHNFSRI FDIAKDLGLY ILMRPGPYIN
     AETTAGGFPG WLLTGDYGTL RNNDTRYTKA WTPYWEAISS MVGQHAVTHG GNVLLFQVEN
     EYGEQWLNVT ARTPNETAIA YMKLLEASAK NNGIDIPTIA NNPNLGSKCW SLDYDIHHVG
     GDTDLYGLDN YPSCWSCNLA ECTSVNGVLP EFTTLDYYTN FQQTAPTMPS ILAEFQGGSY
     NPWGGPQGGC INTTGPDWVN VFYRNNIGQK VAGQNLYMLF GGTNWGGLPM PTVGTSYDYS
     APISESRLLT SKYSETKLLS YFVRSAKDLT MVERAGNGTT NFTTNNPAVF AQALRNVDTG
     SHFYVTKHVN TTLTTYVTFK LNMTTSIGYI QVPQFAPDIA LNGRQAKILV ADFSAGDANL
     IYSTSEILTV SIQNGKPIIV FWVPTGESGE FYLSGAKYGN IIRCDGCSDV GFYDASHGLI
     VKFTQNEGMS VFVFDNGVKT VIVDRTVAYT MWQPTLSANP NVPLNETILV RGPYLLRTAA
     VDNNAITLTG DYNGTTELEI FAPVGNGNGD WSSDEGYQHE GWKTWSTRMI IFNDKPVAVH
     QTSYGSLIGV LDAPPKSSID SIQALIPQLT DWKVADGLPE RMPDYNDSGA GWVDANKIST
     LDPWQPETFP ILYADEYGFH TQNLLWRGRF TGEASGVYLN IIAGTSSGWS AWLNGNYLGS
     TLGNTSLSET DATLNFPSNS LVDGENVLFV IQDHMGHDET TSVLNPRGIL NATLLTNSNA
     KFTSWKVAGN AGGQANIDPI RGPYNEGGLH AERLGWILPG FDDSDWASGT PEQGLSEAGA
     KFYRTILPLD IPEGLDVSLA FELTAPTNSK LRAQLYVNGY MFGKFVPWVG NQISFPVFPG
     IFDYHGNNTI GLNVWSQDPS GSRMSVSINV LGVVASSLNP GAGTAYLRPG WSSERLQYY
//
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