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Database: UniProt
Entry: A0A0F4GN40_9PEZI
LinkDB: A0A0F4GN40_9PEZI
Original site: A0A0F4GN40_9PEZI 
ID   A0A0F4GN40_9PEZI        Unreviewed;      1022 AA.
AC   A0A0F4GN40;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=TI39_contig477g00003 {ECO:0000313|EMBL:KJX97605.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX97605.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX97605.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX97605.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related
RT   genes and transposable element activity.";
RL   Submitted (MAR-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|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:KJX97605.1}.
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DR   EMBL; LAFY01000469; KJX97605.1; -; Genomic_DNA.
DR   EnsemblFungi; KJX97605; KJX97605; TI39_contig477g00003.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000033647; 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:UP000033647};
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:UP000033647};
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_5002468840.
FT   DOMAIN      398    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1022 AA;  111804 MW;  9FE685F7E0BC0226 CRC64;
     MLFRTLCRAA LLSLTALQVA GLAISGKPNL MIKPYKREVL QDIVTWDEHS IFIRGDRVML
     YSAEFHPFRL PVPSLWLDVF QKIKSMGYNT VSVYFDWALV EGKPGNYTAE GIFALEPFFE
     AAKTAGIYIL ARPGPYINAE VSGGGFPGWL QRTPGRLRTT DKGYIDATNN YIANIGKSIA
     AAQITNGGPV ILVQPENEYS GAAKNVPEFP DPVYWSKVEE QLRNSGIVVP FISNDNHNHG
     YFAPGPPPQN PAVSVDIYGH DGYPLGFDCA NPETWPDNSL PTDFGEQHLN QSSSTPFSLV
     EFQGGSFDPW GGPGFTKCGQ LLGPEFQRVF YKNDFSFGVT FFSIYMTYGG TNWGNLGHPG
     GYTSYDYGAV ISEERLVDQE KYSQAKLLAN FLQASPAYLT AAYQNNTYAN GSYTGNSAIA
     TTALFGEVTK FFVVRHAFFN TLDSTDYTIT LPTSQENITI PQLGGSLTLY GRDSKVFATD
     YDVGGANLLY TTAEIFTWKQ YGDTKVLILY GGPDETNEFA VSGCGGANIA EGEDVKIEAK
     NEAIVVQYSS SSTRKVVEFD NGLWVYLLDR QSAYNYWVVD LPNDDVTANF TNHKHAISTP
     IIQFGYLVRT VKVDGNNLHL TGDLNATSSL EVIGAPHCLE QLTFNGESLD FEESELGIVT
     ATVVYNEPAL AVPDLARVQW KVLDSLPEIK ADYDDSAWTS ADLTQTPNDY RDLTTPTSLY
     SSDYGYHTGS LIYRGHFTAN GQESSLYLAT QGGSAFGHSV WLDDTLVGSF YGADLFMTWN
     ETYTLPPTTS GKAYVLTILV DNMGLDENYD TGENQMKAPR GILDYNLSGH SKSDITWKLT
     GNLGGEDYLD AARGPLNEGG LYAERQGYHL PNAPTSSWKD SAGPMEGIAN AGVAFYATTF
     ELDMPAGYDI PLSFSFSNST DGVQDAAPTN GEVAKYRCQI YVNGYQFGKY VHNIGPQDVF
     PVPEGIWNYR GSNYVAVSLW ALEASGAKVA NLSLVPGPVI QSGFGPVELS PAPAWGQRNG
     AY
//
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