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Database: UniProt
Entry: A0A168KPU0_CORDF
LinkDB: A0A168KPU0_CORDF
Original site: A0A168KPU0_CORDF 
ID   A0A168KPU0_CORDF        Unreviewed;       629 AA.
AC   A0A168KPU0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=LEL_01528 {ECO:0000313|EMBL:OAA81983.1};
OS   Cordyceps confragosa RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA81983.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA81983.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA81983.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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   -!- 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:OAA81983.1}.
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DR   EMBL; AZHF01000001; OAA81983.1; -; Genomic_DNA.
DR   EnsemblFungi; OAA81983; OAA81983; LEL_01528.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000076881; 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; 2.60.120.260; -; 2.
DR   InterPro; IPR026283; B-gal_1-like.
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; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076881};
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:OAA81983.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    629       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007898531.
FT   DOMAIN       33    356       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      529    598       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    181    181       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    258    258       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   629 AA;  69248 MW;  31BF18D6FE488EDC CRC64;
     MKFFVGALAT LSALSATVVA SSAPGNFSYN RNQFLLNGEP YQIIGGQMDP QRISPEYWTH
     RLKMARAMGL NTIFSYLYWN LHEPSPGEWD FQGRNDVAKF FRLAQDEGLK VVLRPGPYIC
     GERDWGGFPA WLSQVPGMAV RQNNGPFLDA AKTYLDRVGK EVGQLQITQG GPILMTQLEN
     EYGSFGTDKK YLAALAAILR DNFDVFLYTN DGGGKSYLEG GQLHGVLAVI DGDSKSGFEA
     RDKYVTDPTS LGPQLNGEYY ITWIDQWGSD YAHQQISGSD TDIAKAVGDL DWTLAGNYSF
     SIYMFHGGTN FGFENGGIRD DGPLAAMTTS YDYGAPLDES GRPTDVYYKL REMISKYVPA
     GSIPDVPTTP DRAVVPEFEL KPAAALFDLQ DKPTQQANDP VSMDALGQSY GYVLYEHTVT
     KNVSGNVTIG DGARDRAMIY VNGERVGVVD TIYKTPTTVK VALKKGDILQ ILVENLGRVD
     VRQRLRDQVK GIVGHVAVGC HVLRKWSMHS IPLSTLPSNL NKEHTIKKDD SPVFYTGTFN
     MPKGTSADPS GDTFISVPKG VKGVLWVNGV NIGRYWTVGP QQSLYVPGSF LKEKNEVVLL
     ELEPQPDTKL SAEGISERKW FNNADPDAP
//
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