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Database: UniProt
Entry: G9NPC7_HYPAI
LinkDB: G9NPC7_HYPAI
Original site: G9NPC7_HYPAI 
ID   G9NPC7_HYPAI            Unreviewed;      1020 AA.
AC   G9NPC7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   16-JAN-2019, entry version 39.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=TRIATDRAFT_52125 {ECO:0000313|EMBL:EHK47399.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK47399.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK47399.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A.,
RA   Antal Z., Atanasova L., Cervantes-Badillo M.G., Challacombe J.,
RA   Chertkov O., McCluskey K., Coulpier F., Deshpande N., von Doehren H.,
RA   Ebbole D.J., Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as
RT   the ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(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|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:EHK47399.1}.
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DR   EMBL; ABDG02000020; EHK47399.1; -; Genomic_DNA.
DR   RefSeq; XP_013945605.1; XM_014090130.1.
DR   EnsemblFungi; EHK47399; EHK47399; TRIATDRAFT_52125.
DR   GeneID; 25785051; -.
DR   OMA; GGEDYVD; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000005426; 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:UP000005426};
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:EHK47399.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005426};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1020       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003524441.
FT   DOMAIN      396    579       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1020 AA;  111134 MW;  21A0155681241B82 CRC64;
     MRSDTLLTAA SALLLAGTNA LNSGANGGRP REVVMDSSTS PLLQDIVTWD EDSLYIHGER
     VVIFSGEVHP FRLPVPSLYL DVFQKIKALG FNMVSFYVDW ALLEGKPGHF RADGIFDLEP
     FFEAATQAGI YLLARPGPYI NAEASGGGFP GWLARVKGIL RTNATDYLDA TDNYAANVAR
     IIAKAQITNG GPVILYQPEN EYSAGNAGVV FPNKPYMQYV IDQAREGGIT VPLINNDAFA
     GGTSAPGTGL GSVDIYGWDA YPVGFDCAHP YTWPDNGLPT GQHDTHQRIS PNTPFSLIEF
     QGGAFDPYGG WGFDQCSTLV NHEFERVFYK NNFASGVTIF SIYMIFGGTN WGNLGHSGGY
     TSYDYGASIR EDRTVDREKY SEVKLQAQFL KVSPGYITTT PGNLTQGVYS DNKDISITPL
     LAEENGNFFV VRHTNYSSLD TTSYTVKLPT SAGELTIPQQ GGTLTLSGRD SKFHVTDYPV
     GNFTLLYSTA EIFTWKQFDN RTVLVLYGGA GEVHEFAVKN PFGSTKAGKI NKVQGKDVVV
     HTAQDLTLVL QFTASTDRQV IQLGDLVIYM VDRNAAYNYW VPTLPGSGSH PAYGSSLMNP
     AAVIVNGGYL VRSVAVDGPT LSIQADFNVT TPLEIIGAPQ GVSKLVVNGK ELSYTVSELG
     DWTANPDTVL PVVQVPDLTK LTWYQLDSLP EVQNYYDDSH WPSANHKTSN NSVAPLKTPV
     SLYGSDYGFH TGTLVFRGRF TAQTSQQQLS LTTQGGNAFA SSVWLNDKFI GSFHGFDAGV
     SANSSYKLTN LIRGKRYVLT VVVDSTGLSE NWNIGLDEMK APRGILDYSL VSSRGAHVPI
     SSWKITGNLG GEDYRDTFRG PLNEGGLFFE RQGYHLPSPP LHAFDSRHGV SPYKGISHAG
     IAFYAAKLTL DLPSDSYDIP LSFVFDNTTA AAPYRSLLYV NGFQYGKYVS NVGPQTEFPV
     PEGILNYNGD NWIGVALWAL DSHGAKVPGL ELKAKSPILT SRQKVELVQG PAYKKRWGAY
//
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