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Database: UniProt
Entry: A0A1Q8RN56_9PEZI
LinkDB: A0A1Q8RN56_9PEZI
Original site: A0A1Q8RN56_9PEZI 
ID   A0A1Q8RN56_9PEZI        Unreviewed;      1011 AA.
AC   A0A1Q8RN56;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CCHL11_07779 {ECO:0000313|EMBL:OLN85748.1};
OS   Colletotrichum chlorophyti.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN85748.1, ECO:0000313|Proteomes:UP000186583};
RN   [1] {ECO:0000313|EMBL:OLN85748.1, ECO:0000313|Proteomes:UP000186583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTL11 {ECO:0000313|EMBL:OLN85748.1,
RC   ECO:0000313|Proteomes:UP000186583};
RA   Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT   "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT   herbaceous plants.";
RL   Submitted (NOV-2016) 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:OLN85748.1}.
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DR   EMBL; MPGH01000155; OLN85748.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000186583; 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:UP000186583};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186583};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5013248979.
FT   DOMAIN      393    569       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  110832 MW;  C428B10D0186D152 CRC64;
     MILSLLCIGL LGLCIRTVVY QGAIAGHPPT FAVKIEKRDR NQDVVTWDQH SLFVRGERVM
     IFSGEIHPFR LPVPSLYLDL FQKVKALGLN TVSFYADWAL MEGRAGSFSA GGVFDLQPFF
     DAATKAGIYL IARPGPYINA EVSGGGFPGW LMRTRARLRT SDPEFLSATD NYMSHICSII
     AKAQITNGGP VILFQPENEY TNFERNRSPD GDYFQYVIDQ ARKAGIVVPL ISNDARPLGH
     NAPGTGIGAA EIYGHDAYPL GFDCGNPTFW PPDQLPTNYR SLHLSQSPNT PFSLIEFQGG
     SFDPPGGSGF EQCAALTNHE FERVFYKNNI AAGVTIFSVY MIFGGTNWGN LGHPGGYTSY
     DYGAAITEER GLARVKYSEL KLEAQFLKVS PTYLTATPGN VTVGVYSRTT DLAITPIIGN
     GTGSYFVVRH TNYSSLATTD YTLRLPTSEG NITIPQSRGR LQLGRRDSKV IVTDYEVGNM
     TVLYLTAEIL TWKRYKNKTV LVVYGGPEET HEMAIKTTAT PQTLEGSTVE HNYANETLLL
     NWMTSASRRV VQVEQLFVYI IDRSSAYNYW VPDLPGKGSQ PSYGTSTMNP DALIINGGYL
     IRSISIQDDT LKMKADFNRT TELEIIGLED HVLKLEMNGR QINHTLNNLS NWIAQPPLTA
     TKLDIPDLRT LSWAYVDSLP ELRPTYDDSV WPIANHTTSN NTAANVTTPV SLFASDYGFH
     TGTILYRAHF TAGGAEGNLT LKTQGGSGYA SSVWLNDTFL GSFANGPDAA GDNSANYTLP
     EMTPNASYVL TILVDTTGLE ENFIIATDMM KNPRGIMEYG IASPGGSTNV TTWRITGNLG
     GEDFADRFRG PLNEGGLFFE RQGYHVPSPP PEAFAPRSPF DGTEGPGVAF YAATMELDLP
     SRDLDVPLAF VFDDITTDGG GAAAYRALLF VNGFQYGRYA SNIGPQTRFP VPEGVLRYRG
     TNWIGLAVWA LGREGARVRN FRLGVGEVVT TGREEAGVVE GPGWRRREGA Y
//
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