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Database: UniProt
Entry: G2R540_THITE
LinkDB: G2R540_THITE
Original site: G2R540_THITE 
ID   G2R540_THITE            Unreviewed;      1053 AA.
AC   G2R540;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   13-FEB-2019, entry version 43.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:AEO65317.1};
GN   ORFNames=THITE_2045005 {ECO:0000313|EMBL:AEO65317.1};
OS   Thielavia terrestris (strain ATCC 38088 / NRRL 8126) (Acremonium
OS   alabamense).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Thielavia.
OX   NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO65317.1, ECO:0000313|Proteomes:UP000008181};
RN   [1] {ECO:0000313|EMBL:AEO65317.1, ECO:0000313|Proteomes:UP000008181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J.,
RA   Reid I., Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B.,
RA   Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J.,
RA   Lucas S., Harris P., Powlowski J., Bellemare A., Taylor D., Butler G.,
RA   de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R.,
RA   Powell A.J., Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J.,
RA   LaBoissiere S., Clutterbuck A.J., Martinez D., Wogulis M.,
RA   de Leon A.L., Rey M.W., Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading
RT   fungi Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
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; CP003010; AEO65317.1; -; Genomic_DNA.
DR   RefSeq; XP_003651653.1; XM_003651605.1.
DR   SMR; G2R540; -.
DR   STRING; 578455.XP_003651653.1; -.
DR   EnsemblFungi; AEO65317; AEO65317; THITE_2045005.
DR   GeneID; 11518891; -.
DR   KEGG; ttt:THITE_2045005; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000008181; Chromosome 2.
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:UP000008181};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:AEO65317.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008181};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1053       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003436904.
FT   DOMAIN      438    621       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1053 AA;  113295 MW;  D71869BCC45ECB44 CRC64;
     MRLRLALLLL TSTAVVLCRH IFSSSSSSSP SSSSSHLPSS EFNPLSILPR LISRPSTPPS
     ANPQPNPEPN PNQNRNEKLP PRADATYAPP TWDNATLVLL GQRAMLFGGE FHPFRLPVPA
     LWSDVLEKMR AAGLNAVSFY VPWALLEGRP GEVRAEGVFD VAAFCRAAAE VGLWLVARPG
     PYINGEVTGG GLPGWIQRLR GHPRTSDADY LAATNNYAAN VGAIIAKAQI NNGGKVILYQ
     PENEYSVSRT LIGFNFPDPG YMQYVEDQAR RAGVVVPFMN NDAWSAGHNA PGTGVGQVDI
     YGHDLAPLDP DCDDMAWEKG ALRETQYANH LNVSASTPYA IPDGGVLDYW GGTGFARCAE
     RFNAEQARVF NKNNFAAGVK IFSLYMMYGG TNWGNLGYDS GYTSYDYAAA IAEDRTLTRE
     KYSEIKLQAN FFKVSPGYLV ATPDLKPTTG VYSPGHEDIT VTAVVGPQGS FYVARKTAYR
     DASPVNFTLR LPTASKGAVT IPHLGGALTM PGRDSRIYVT DYPVGAMTLV YCTAEIFTWQ
     KFDNGQTVAV LYGGVVGETH ELLLQRGGAD LQATVTRSPE VRTSLEGQFV YAQWTTTGDR
     QFVRVGNTYI YLVDRNAAYN YWVADTPGQP PLIVNGGYLI RSAALANGTL TIRGDFNRTT
     TLELIGVPQA ATSLVINTTP TPHRADDDGH WLAQIAYSPP SITLPDLSAV AWSYIDTLPE
     RQSSFSDAAW PSANHTFTNN TYLQAPQTPT SLYASDYTFH AGGALLFRGH FTATGGESAV
     TLHTQGGRAY AAAVWLDDEF LGGWAGNSSA SSHRDTFAVR LVPGRAYALT VLLDNMGNAQ
     NALVGGDDMK APRGILQFNF TMGGGGAAPA VDWKVTGNLG GEDYVDKARG PLNEGGLWAE
     RQGFHLPGAP TSSGGWTAGS SPMKGIGEPG VGFWRAEAEL DIPGEQWDVP LSFEFPPIDT
     TGAQGRYRAV LWVNGFQFGR YISHIGPQTS VPVPEGILNY HGTNTIAVAL WALQPGGARI
     PSLSLRAGTP VLTGRRPVVG VAAPAWTQRP GAY
//
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