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Database: UniProt
Entry: A0A1X7S3W2_ZYMTR
LinkDB: A0A1X7S3W2_ZYMTR
Original site: A0A1X7S3W2_ZYMTR 
ID   A0A1X7S3W2_ZYMTR        Unreviewed;      1022 AA.
AC   A0A1X7S3W2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ZT3D7_G9543 {ECO:0000313|EMBL:SMQ54388.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ54388.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ54388.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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}.
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DR   EMBL; LT853700; SMQ54388.1; -; Genomic_DNA.
DR   EnsemblFungi; SMQ54388; SMQ54388; ZT3D7_G9543.
DR   Proteomes; UP000215127; Chromosome 9.
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:UP000215127};
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:UP000215127};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1022       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5013321898.
FT   DOMAIN      398    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1022 AA;  111856 MW;  666EA922E5BABA4E CRC64;
     MLFRTLCRAA LLSLTALQVA GLAISGKPNL MIKPYKREVL QDIVTWDEHS IFIRGDRVML
     YSAEFHPFRL PVPSLWLDVF QKIKSMGYNT VSVYFDWALV EGKPGNYTAE GIFALEPFFE
     AAKTAGIYIL ARPGPYINAE VSGGGFPGWL QRTPGRLRTT DKGYIDATNN YIANIGKSIA
     AAQITNGGPV ILVQPENEYS GAAKNVPEFP DPVYWSKVED QLRKSGIVVP FISNDNHNHG
     YFAPGPPPQN PAVSVDIYGH DGYPLGFDCA NPETWPDNHL PTNFGEQHLN QSSSTPFSLV
     EFQGGSFDPW GGPGFTKCGQ LLGPEFQRVF YKNDFSFGVT FFSIYMTYGG TNWGNLGHPG
     GYTSYDYGAV ISEERLVGQE KYSQAKLLAN FLQASPAYLT AAYQNNTYAN GSYTGNSAIA
     TTALFGEVTK FFVVRHAFFN TLESTDYTIT LPTSQGNITI PQLGGSLTLH GRDSKVYATD
     YDVGGANLLY TTAEIFTWKQ YGDTKVLILY GGPDETNEFA VSGCGGAKIA EGEDVKIEAK
     NEAIVVQYSS SSTRKVVEFD NGLWVYLLDR QSAYNYWVVD LPNDDVTANF TNHKHAISAP
     IIQFGYLVRT VTVDGNNLHL TGDLNATSSL EVIGAPHCLE QLTFNGESLD FEEGDSGIVT
     ATVVYNEPAL VVPDLAKVQW KVLDSLPEVK ADYDDSAWTA ADLTQTPNDY RNLTTPTSLY
     SSDYGYHTGS LIYRGHFTAN GQESSLYLAT QGGSAFGHSI WLDDTLVGSF YGADLYMTWN
     ETYTLPPITS GKTYVLTILV DNMGLDENYN TGENQMKAPR GILDYNLSGH SKSDITWKLT
     GNLGGEDYLD AARGPLNEGG LYAERQGYHL PNAPTSSWRD SAGPMEGIAN AGVAFYTTTF
     DLDMPSGYDI PLSFSFSNAT DGVQDAVPTD GQISKYRCQI YVNGYQFGKY VHNIGPQDVF
     PVPEGIWNYH GSNYVAVSLW ALEASGAKVA NLSLVTGPVI QSGFGPVELS PVPAWEQRKG
     AY
//
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