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Database: UniProt
Entry: A0A178AN08_9PLEO
LinkDB: A0A178AN08_9PLEO
Original site: A0A178AN08_9PLEO 
ID   A0A178AN08_9PLEO        Unreviewed;      1001 AA.
AC   A0A178AN08;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=IQ06DRAFT_277882 {ECO:0000313|EMBL:OAK98558.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Massarineae;
OC   Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK98558.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK98558.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK98558.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L.,
RA   Chaput D.L., Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-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; KV441715; OAK98558.1; -; Genomic_DNA.
DR   EnsemblFungi; OAK98558; OAK98558; IQ06DRAFT_277882.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077206; 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:UP000077206};
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:UP000077206};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1001       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008081986.
FT   DOMAIN      391    570       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1001 AA;  109016 MW;  705DEF42C74E8510 CRC64;
     MRNLLSAIAL STCAVVAAAR AVAGSPKDWI IPYKREALQD IVTWDEDSIK INGERIFLYS
     GEVHPFRLPV PSLYIDIFQK IKSLGYNCVS FYVDWALLEG KPGEYREEGI FDLQPFYDAA
     SEAGIYLIAR PGPYINAEAS GGGFPGWLQR INGTLRTSAK DFLDATDNYM KNIGASIAKA
     QITNGGPIIL VQPENEYTQA TSAIKPFPDP VYMEYIFDQI RDAGIIVPLI SNDASAKGNN
     APGQPAAVDI YGHDGYPLGF DCANPDVWPD NNLPTNWKTL HEQQSPSTPY SIVEFQAGSF
     DPWGGPSFEK CYTLVGAAFE RVFYKNLYSF GVTILNLYMT WGGTNWGNLG HPGGYTSYDY
     ASPIREDRRV DREKYSEQKV QANFFKVSPA YLTASRGNAS NTAWTTTSAL TVTPAFEGST
     AFYFLRHAKY NTLDSTSYKL KISTTAFGNI TVPQTNGTSL TLNGRDSKVH VSDYDVGGAT
     LVYSTAEIFT WHKYEDKTVL VVYGGPGETH ELVLAVTGLE MIEGEVQSIS TRGYTLLNFK
     ADGTRKVAKV GVGSNFIYVH MLDRYQAYNY WSIDTAPHSN ANPVILQAGY LVRTAKVDGS
     TLALTGDLNA TTTLEIFGGA PSSLSKLTFN GKDIEFTTSK EGVIGATAEY TAPQIDVPKL
     QDLEWKYIDS LPEVQNDYDD SAWTVANLKK TYNSLRPLNT PVSLYSSDYG YHTGTLIYRG
     TFTATGNEST IWLSTQGGSA FGSSAFIGTH FIGSWRGYDA ALYGNNTWSL PNLTAGKKYT
     ITVVVDNQGL DENWTIGTET MKNPRGIMDY VISGHDKSDV SWKLTGNLGG EDYVDKSRGP
     LNEGGLYVER QGLHLPGALA SNSSAKWTAS KGPVTDGIPA PGIGFFATEF TLNVPAGYDA
     PMSFTFTNGT SGAALRAQLY VNGFQYGKYV SNVGPQTKYP VPQGILNYQG VNYVGVSLWG
     LDGGATKLDG LELEVDGVVA SGLGEVETVE GSRYGVRKGA Y
//
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