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Database: UniProt
Entry: A0A0C3QCI9_9HOMO
LinkDB: A0A0C3QCI9_9HOMO
Original site: A0A0C3QCI9_9HOMO 
ID   A0A0C3QCI9_9HOMO        Unreviewed;      1005 AA.
AC   A0A0C3QCI9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=M407DRAFT_15607 {ECO:0000313|EMBL:KIO23116.1};
OS   Tulasnella calospora MUT 4182.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Cantharellales; Tulasnellaceae; Tulasnella.
OX   NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO23116.1, ECO:0000313|Proteomes:UP000054248};
RN   [1] {ECO:0000313|EMBL:KIO23116.1, ECO:0000313|Proteomes:UP000054248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO23116.1,
RC   ECO:0000313|Proteomes:UP000054248};
RG   DOE Joint Genome Institute;
RA   Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA   Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN823092; KIO23116.1; -; Genomic_DNA.
DR   EnsemblFungi; KIO23116; KIO23116; M407DRAFT_15607.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000054248; 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:UP000054248};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:KIO23116.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054248};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1005       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002168728.
FT   DOMAIN      366    564       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1005 AA;  112180 MW;  8177C1FA26D62A82 CRC64;
     MKLILGYIIS SVIACAAGTV TWDGYSLSIN DQRIFLWSGE FHPWRLPVVH KWRDVLVKVK
     AAGMNAISVY IHWGLTNPAP GVFDFNEYRA LEPLFKMAME IGIWIVLRPG PYINAETTAG
     GIPHWVTSHV SGHLRTNDTA YYNAWRPYID KVAELAAPHQ ITRGGPIIAV QLENEYVDRD
     DVGYPGKREM MEELKAAIRS GGIEVPLTIN DAYMGANYVN GTGSGDIYGF DSYPQGFDCA
     HPGHWQPVIE TYAKFHKHAN PHQPLYIPEF QGGAYDAWPG YEACATLTNG EFESVFHLAL
     LASNAKMINI YMIYGGTSWG HLPFPGVYTS YDYGAAISEN RDIRVEKYAE IKRQGLFLRS
     VPDFYKTDIM PDTTWEISPT PGSSPVAATL LQNSDTNSSF LIARHQDSTL SGSSSFHLRI
     HANSHVRAQW QIAGELQIPQ IANSIQLEGR QSKIVTTFLA SPPAVEPRRN TLLYSTAAIL
     YFGWMGGREV LVLTGHGNQE HEFAVFLQTS VMAAVHPFLN MSPCPTSSLY TIFHVLPGLT
     GLVPIHESKN QAIYFVDTAT SRTFWAPMLE VMEPKTPPFQ TFWSVGSNSS IIISGPALVR
     SASFHPHLHQ LSITGDLDPS ASVYLTIIGM PLTTKSIHWN GQEIIPLKSL SVDANFRAMF
     HLVPNPALLN SDHWPQQLDN WEYANSLPEA SFHYDDSNWV RANHTSTNLS QKPYCGKHVL
     YGCDYGFCEG VVIWRGHFVS SPKIDGVTLT INGGQGFAAS VYVNDVFIRT TYGNSTSNKN
     IISETTEWYS FPNGVLTEGE NVLTIVQDNM GLDETRNHWD TDGSRSPRGI RGYDLHNGDF
     TYWKVQGKSG GFNNYPDRKR GIFNEGGLYG ERMGWHRPEV PKDGQEWTTR SLTQGLTGGY
     SGIGFFRTHF QLKLFPGRDV MQSFHFVDCT SMTPTLQPYR AWIFVNGWMM GKRVANLGPQ
     TRFPVHEGIL VNGTNLVVIA VWGMDATVAP CFKLELATDR VYDQS
//
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