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Database: UniProt
Entry: A0A161WGK1_9PEZI
LinkDB: A0A161WGK1_9PEZI
Original site: A0A161WGK1_9PEZI 
ID   A0A161WGK1_9PEZI        Unreviewed;       984 AA.
AC   A0A161WGK1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CI238_06015 {ECO:0000313|EMBL:KZL83618.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL83618.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL83618.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL83618.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P.,
RA   Garrido Oter R., Ver Loren van Themaat E., Dallerey J.-F., Damm U.,
RA   Henrissat B., Lespinet O., Thon M., Kemen E., McHardy A.C.,
RA   Schulze-Lefert P., O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely
RT   related pathogenic and mutualistic fungi.";
RL   Submitted (JUN-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}.
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:KZL83618.1}.
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DR   EMBL; LFIW01001090; KZL83618.1; -; Genomic_DNA.
DR   EnsemblFungi; KZL83618; KZL83618; CI238_06015.
DR   Proteomes; UP000076584; 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; 2.
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:UP000076584};
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:KZL83618.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    984       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007829049.
FT   DOMAIN      361    537       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   984 AA;  107681 MW;  4ACC615AAA0741D2 CRC64;
     MRPSLFLIVS LALRICSASL TGAIGGRPPT LIIDVHKRDQ LQDVVTWDEH SLFVRGERVM
     IFSGEIHPFR LPVPSLWLDL FQKVKALGLN TVSFYVDWAL LEGKAGDFSA EGVFDLQPFF
     EAATKAGVYL IARPGPYINA EVSGGGFPGW LAKIRGKLRT SDPEFLSATD NYMAKICSII
     AKAQITNGGP VILFQPENEY TNFKNGSSVD GQYFQYVIDQ ARNAGIVVPL ISNDARPSGN
     NAPGTGVGAV DIYGHDAYPL GFDCFQGGSF DPFGGPGFEK CAALVNHEFE RVFYKNNYAA
     GVTIFNIYML FGGTNWGNLG HPGGYTSYDY GAAVTEERGV GREKFSELKL EAQFLKVSPT
     YLIATPYNLT VGVYSRTTDV TVTPLLGNGT GSFFVVRHSN YSSLVTTDYT LRLPTSEGNI
     TIPQFRELLQ LGRRDSKVIV TDYRVGNTTL LYLTAEIFTW KEYNNQTVLV VYSGPDESHE
     MAIKTNATPL FLEGTSIDHH YVNNTLVLSW ATLTTRRVVQ VDHLLIYILD RNSAYNYWVT
     DKPGGSSRPS YGTSIMSPES LIINGGYLIR SVTIQGDTLR VQADFNRTTE LEILGVDAEV
     TKLEVNGKPL VHTTNNLTNW IAHPTFMDSA FTVPDLKTLN WTFLDSLPEI RPGYDDSAWP
     LANHTTTNNT IANLTTPVSL FASDYGFHTS TLVFRGYFTA TGAEDTLKIT TQGGSAFASS
     VWLNDTFLGS FANNHDDAAG DNTSNYTLEN LTASMTYVLT VVVDTTGLEE NFVIPAEVMK
     NPRGIMDYSI TSPSGVLTNV TTWKITGNLG GEDYADRFRG PLNEGGLFFE RQGYHLPSPP
     AAAFTTQRSP FDGVDAPGVA FYAATLDLSL PASDLDIPLA FVLDNITPTN DTDGAGAYRA
     ILYVNGFQFG KYISNIGPQT RFPVPEGILR YQGANWVGLA VWALGKGGAR VRDLRLDVGE
     VVTTGREEVK IVDGPAWSQR AGAY
//
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