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Database: UniProt
Entry: E3RXT9_PYRTT
LinkDB: E3RXT9_PYRTT
Original site: E3RXT9_PYRTT 
ID   E3RXT9_PYRTT            Unreviewed;      1010 AA.
AC   E3RXT9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   25-APR-2018, entry version 40.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PTT_14249 {ECO:0000313|EMBL:EFQ89454.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ89454.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ89454.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F.,
RA   Moffat C.S., Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora
RT   teres f. teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000256|RuleBase:RU000675, ECO:0000256|SAAS:SAAS00108875}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; GL535709; EFQ89454.1; -; Genomic_DNA.
DR   RefSeq; XP_003302444.1; XM_003302396.1.
DR   STRING; 861557.XP_003302444.1; -.
DR   EnsemblFungi; EFQ89454; EFQ89454; PTT_14249.
DR   KEGG; pte:PTT_14249; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   OrthoDB; EOG092C0SLI; -.
DR   Proteomes; UP000001067; 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; -; 3.
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:UP000001067};
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:UP000001067};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1010       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003180939.
FT   DOMAIN      395    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1010 AA;  110473 MW;  BE02A3724D03EFBB CRC64;
     MKSFKKLGSA LALSCLAIGT AARAVGYSSP KDWIKPYKRE ALQDIVTWDE DSLFVHGERI
     FLYSGEVHPY RLPVPTLYLD IFQKIKALGY NGVSFYVDWA LLEGTPGVYR EEGVFDLQPF
     FDAAKEAGIY LLARPGPYIN AEVSGGGFPG WLQRVEGMLR TRAEDYLNST DNYMKNVGAK
     IASAQITNGG PIILVQPENE YTQATSAIKP FPDPVYMEYV ENQIRSAGII VPLISNDASA
     QGNNAPNQPA AVDIYGHDGY PLGFDCANPT TWPDRNLPTN WHQLHEKQSP STPYSIIEFQ
     SGSFDPWGGP GFDKCGILVG AEFNRVFYKQ LYSFGVTILN LYMTYGGTNW GNLGHPGGYT
     SYDYAAPIRE DRQVDREKYS ELKLQASFLK VSPAYLTASR GNASTTAWTT NSALSVTPAT
     NKNTKFYFLR HNKYNSLDST TYKLKIQTST FGNITVPQMN GTSLTLNGRD SKVHVSDYDI
     GGANLIYSTA EIFTWHKYED KTVLVVYGGP GETHELALAV TGLDVLEGDV NSIATRRVTL
     LNFVADGTRK VAKVGVDSFI YVYMLDRNQA FNYWSVDQAP YDSSSPVMLK AGYLMRTAKV
     TGDTIALTGD LNATTPVEII GGAPSSVSTI TFNGKALDFT KSEAGTLVAN VEFTKPELSI
     PKLSSLEWKY VDSLPEIQPG YDDSKWTVAD LKKTYNSKRP LNTPVSLYSS DYGFHTGTLL
     FRGTFTARGN ESTFYLSTQG GSAFGSSAWI GDQFLGSWRG YDRAMSGNAT FTMPNLTKGK
     TYTITVVIDN QGLEENWTIG TETMKNPRGI LNYKLAGHDA SDIAWKLTGN LGGEDYKDIS
     RGPLNEGGLF VERQGLHLPG ALSASTAGWK ASPGPVAAGI TAPGIGFFAT EFDLNMPAGY
     DIPLSFTFTN GTASSGNGSS VPAYRVQLYV NGWQYGKYVS NVGPQLKFPV TEGILNYNGT
     NYLGISLWNL DGGAAKVEGL ELTVDAMVWS EMQTVKKVEG QVYEPRTGAY
//
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