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Database: UniProt
Entry: B0DSN5_LACBS
LinkDB: B0DSN5_LACBS
Original site: B0DSN5_LACBS 
ID   B0DSN5_LACBS            Unreviewed;      1092 AA.
AC   B0DSN5;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   13-FEB-2019, entry version 62.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:EDR02353.1};
GN   ORFNames=LACBIDRAFT_309612 {ECO:0000313|EMBL:EDR02353.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured
OS   deceiver) (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Tricholomataceae;
OC   Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR02353.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A.,
RA   Shapiro H.J., Wuyts J., Blaudez D., Buee M., Brokstein P.,
RA   Canbaeck B., Cohen D., Courty P.E., Coutinho P.M., Delaruelle C.,
RA   Detter J.C., Deveau A., DiFazio S., Duplessis S.,
RA   Fraissinet-Tachet L., Lucic E., Frey-Klett P., Fourrey C.,
RA   Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P., Kilaru S.,
RA   Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R., Melayah D.,
RA   Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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|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; DS547131; EDR02353.1; -; Genomic_DNA.
DR   RefSeq; XP_001887030.1; XM_001886995.1.
DR   ProteinModelPortal; B0DSN5; -.
DR   STRING; 486041.XP_001887030.1; -.
DR   EnsemblFungi; EDR02353; EDR02353; LACBIDRAFT_309612.
DR   GeneID; 6082670; -.
DR   KEGG; lbc:LACBIDRAFT_309612; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   InParanoid; B0DSN5; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000001194; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001194};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:EDR02353.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001194};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     62     82       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      459    646       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1092 AA;  119691 MW;  5FD0EBB86CB0B14A CRC64;
     MLEIASRTSP KQAFSHQSTP TTAWKQDIQP FSMKTSFSGY GDDNNLEAKP PICRYQAKRR
     LFWLRICAIS ILLMLVNCWL PGVKFFRAFR DIITQGNTQI PQPVISTART DQVQFDNYTL
     ILKGQRIFLH SGEFHTFRLP VPSLWPDILE KFKAAGLNAV SVYTHMGLIN PAPGVVDLGG
     FRALQPLFDA AKAIGIWVVL RPGPYINAET SAGGIAHWAT SEVSCTLRTN ASDWKAAWKD
     YIQAIIDVTV PNQITNEGPV IAIQIDNEYD QAVGAQAEYF VDLENAYHES AIVVPLTYND
     PGPKRNFING TGAVDLYGVD AYPQRFDCSA PTTWNPVETY YHEYHSEVNP LQPLYIPEFQ
     GGAFDAWGPT ASGYAPCRVL TGPDFQSVFN LQLWASNAKL INYYMLYGGT SWGGIPFHGV
     YTSYDYGAPI TESRELTIKY DELKRQGLFL RSSPDFYKTD WIADSSTGLQ ASTNSAAFVT
     LLRNPDTRSS FYIARQADST SSATITFKLN VTTSAGTLQL PQVAPSITLG GRQSKVIVAD
     CTFGVLSKLL YSTAQIFYAS TIGGRDVLFL FGDSTQEHEA ALLLTGTPNK LQNLSPLVSF
     TAYGSPLHQQ GVSLVNFLPG IEGLVTVWDS DTQLVLFADT DTAATFWSPS IAGKAGDPFR
     NFWGLGTNDS ILVGGPYLVR SATVSGSKLA LRGDLKTDVR LTVIAPRGIR SITWNDEYVS
     GDLVATSALT AVGGFIGQLR MRPSLAGISV PRLTGWKFKD SLPEIKRDFD DASWRTANHT
     STNIPLKPYY GDGRVLYGCD YGFCENVVLW RGHFNASGAE KSVDLSINGG QAFAASVWLN
     DVFLNTSFGN STNNHNILEE TDDTFVFPEG ALLPGQDNVI TVVQDNMGLN QTEWPNPDTS
     KSPRGVRGFK LEGGSFSEWK VQGKIGGYVN FPDKVRGVLN EGGLFGERKG WHLPGFPTSD
     WDSRPISSGL PNGASGFGFF VTTFKLDMPR GLDIMMSFFF GEAQGQPYRA LLFVNGWMMG
     KRVANLGPQS KFPVHEGILN YHGENTVAVA LWVMTPNKTA APDLQLVLDA VYDGGVGDVV
     SDNPPWSSQG RG
//
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