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Database: UniProt
Entry: A0A0W0FXE0_9AGAR
LinkDB: A0A0W0FXE0_9AGAR
Original site: A0A0W0FXE0_9AGAR 
ID   A0A0W0FXE0_9AGAR        Unreviewed;      1042 AA.
AC   A0A0W0FXE0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   13-FEB-2019, entry version 15.
DE   SubName: Full=Putative glycoside hydrolase family 35 protein {ECO:0000313|EMBL:KTB41020.1};
GN   ORFNames=WG66_6407 {ECO:0000313|EMBL:KTB41020.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Marasmiaceae;
OC   Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB41020.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB41020.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB41020.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of
RT   frosty pod rot of cacao.";
RL   Submitted (DEC-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:KTB41020.1}.
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DR   EMBL; LATX01001522; KTB41020.1; -; Genomic_DNA.
DR   EnsemblFungi; KTB41020; KTB41020; WG66_6407.
DR   Proteomes; UP000054988; 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; 2.
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:UP000054988};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:KTB41020.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27   1042       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006902192.
FT   DOMAIN      404    598       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1042 AA;  115125 MW;  9B55F6894073CC41 CRC64;
     MATMRSTLLF LVQFVFLFTS LTLSVARGIA SRQEGPRPRT WTDQVDYDEY SLIIKGQRVF
     LHSGEFMTYR LPVPDLWPDI LEKFKAAGFN GLSLYTHMGS INPSRGVVDF ESYRALKPLF
     EAAKEIGVWV VLRPGAFVRL RGSFTFYKAN LQLYINAETS AGGLAHWTTT EVKGKLRSNA
     SDYREAWTPY ILGIIREAVD YQITQGGPII AVQVDNEYGQ DPGAGYFEDL KAVYRNESNG
     IVVPLTYNDP GMGRSFINGT GAVDLYGFDA YPNRYDCAHP NIWRPVPENY HEYHMEVNRW
     QPLYIPEYQG GSLQAWGPNT PDYSGCAALT GPDFESVFYK QLWADNVKLV NYYPLYGGTS
     WGGIPFQSTP RMTGEQLCIS EPRTLTTKYT ELKLQGIFLR SSPEFYKTDV IANSTEIPII
     DTLNSSSLGF ATLLRNPDTG AGFWIVRHNE STSTAISEFK LNVTTASGAS LQIPNIARAI
     TLDGRQSKVL VTDYAFGSSR ALYSTAEVFF AGVIDGRDVL FLHGYSNQEH EVVLSLTGTN
     TANATSEFII YTPEPALAGL APNSTLVSFR KGIQGLRTLH ASDTQLVVFA DTSTAETFWA
     PSIASNTSEH ASFWGIGTNQ SVLVGGPYLV RSAHIEGDTL ALRGDLNASN VKKESRLMII
     APRSITKVTW NEEIVLLDDS SVDDGYITGT IELAEKAEIT VPELDGWKYH DSLPEIGDEF
     DDSQWVVANH TETNVPFKMW YGDGRVLYGC DYGYCEGAVV WRGHFNAAGA EKSMNLSING
     GQGFAATVWL NDLFLDTSFG NSSNGANNIN ETDQVFTFPD GSVRLGQDNV VTVVQDNMGL
     NENWYTDDHM KSPRGIRGFQ LNSGNFSEWK VQGKIGGYTN FPDKVRGVMN EGGLFGERKG
     WHLPDFDTSS WENRSLSDGL PNAAAGVGFF VTKFILSIPG GYDVPISFNF DEPFGQPYRA
     LLFVNGWNMG KRIGNLGPQA KFPVHEGILN YQGENTVAVA LWSMTPNVTV SPTLSLAADG
     VFNGGVGRIR TNNPAWMQEG RE
//
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