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Database: UniProt
Entry: A0A2H2ZLF1_9HYPO
LinkDB: A0A2H2ZLF1_9HYPO
Original site: A0A2H2ZLF1_9HYPO 
ID   A0A2H2ZLF1_9HYPO        Unreviewed;      1023 AA.
AC   A0A2H2ZLF1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   16-JAN-2019, entry version 6.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=A9Z42_0084350 {ECO:0000313|EMBL:OTA07539.1};
OS   Trichoderma parareesei.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Trichoderma.
OX   NCBI_TaxID=858221 {ECO:0000313|EMBL:OTA07539.1, ECO:0000313|Proteomes:UP000219286};
RN   [1] {ECO:0000313|EMBL:OTA07539.1, ECO:0000313|Proteomes:UP000219286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 125925 {ECO:0000313|EMBL:OTA07539.1};
RX   PubMed=26272569;
RA   Yang D., Pomraning K., Kopchinskiy A., Karimi Aghcheh R.,
RA   Atanasova L., Chenthamara K., Baker S.E., Zhang R., Shen Q.,
RA   Freitag M., Kubicek C.P., Druzhinina I.S.;
RT   "Genome Sequence and Annotation of Trichoderma parareesei, the
RT   Ancestor of the Cellulase Producer Trichoderma reesei.";
RL   Genome Announc. 3:e00885-15(2015).
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:OTA07539.1}.
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DR   EMBL; LFMI01000780; OTA07539.1; -; Genomic_DNA.
DR   Proteomes; UP000219286; 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:UP000219286};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1023       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5013655511.
FT   DOMAIN      394    577       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1023 AA;  111374 MW;  6698941566AAC6AB CRC64;
     MRPVSLLSAA VLLLSGIDAS GIGIHGGRPR DIILDDAKGP LQNIVTWDEH SLFVHGERVV
     IFSGEVHPFR LPVPSLYLDV FHKIKALGFN TVSFYVDWAL LEGKPGRFRA DGIFSLEPFF
     EAATKAGIYL LARPGPYINA EVSGGGFPGW LQRVKGKLRT DAPDYLHATD NYAAHIASII
     AKAQITNGGP VILYQPENEY SGAAEGVLFP NKPYMQYVID QARNAGIVVP LINNDAFPGG
     TGAPGTGLGS VDIYGHDGYP LGFDCAHPSA WPDNGLPTTW RQDHLNISPS TPFSLVEFQG
     GAFDPFGGWG FEQCSALVNH EFERVFYKNN MAAGVTIFNI YMTFGGTNWG NLGHPGGYTS
     YDYGASIRED RRIDREKYSE LKLQGQFLKV SPGYITATPE NATQGVYSDS QNIVITPLLA
     KESGNFLVVR HTNYSSTDTA SYTVKLPTSA GDLTVPQLGG SLTLTGRDSK IHVTDYPVGK
     FTLLYSTAEI FTWKEFADKT VLILYGGAQE LHELAVKNPF GSSKTAKAKK IEGSDVTIHS
     TSNLTVVLQW TASSVRQVVQ LGPLVIYMVD RNSAYNYWVP TLPGSGKQSA YGSSLMNPDS
     VIINGGYLIR SVAIKGNALL VQADFNITTP LEIIGIPKGI AKLAVNGKEL DYSVSELGDW
     IAHPAIKIPH LQVPDLSKLK WYKVDSLPEI RSNYDDSRWP FANLRTSNNT YAPLKTPVSL
     YGSDYGFHAG TLLFRGRFTA RTERQQLFLS TQGGSAFASS VWLNDRFIGS FTGFDAASAA
     NSSYTLDKLV RGRRYILTVV VDSTGLDENW TTGDDSMKAP RGILDYALTS SSGAKVSISW
     KLTGNLGGED YRDAFRGPLN EGGLFFERQG FHLPSPPLSD FTHGPSSSSS SPLDGIPHAG
     IAFYAAKLPL RLPAQEYDIP LSFVFDNATA AAAVAPYRAL LYVNGFQYGK YVSNIGPQTE
     FPVPEGILDY NGDNWIGVAL WALESRGAKV PSLVLKSKSP ILTGRERVEV VKGPHFKKRQ
     GAY
//
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