ID W3WVB9_PESFW Unreviewed; 877 AA.
AC W3WVB9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Beta-galactosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFICI_09852 {ECO:0000313|EMBL:ETS77790.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS77790.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; KI912115; ETS77790.1; -; Genomic_DNA.
DR RefSeq; XP_007836624.1; XM_007838433.1.
DR AlphaFoldDB; W3WVB9; -.
DR STRING; 1229662.W3WVB9; -.
DR GeneID; 19274865; -.
DR KEGG; pfy:PFICI_09852; -.
DR eggNOG; KOG2024; Eukaryota.
DR HOGENOM; CLU_006501_0_1_1; -.
DR InParanoid; W3WVB9; -.
DR OMA; WYDTITR; -.
DR OrthoDB; 1847696at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048229; GalB-like.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR NCBIfam; NF041463; GalB; 1.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..877
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004835103"
FT DOMAIN 112..234
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 245..355
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 362..535
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 698..757
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 770..873
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 877 AA; 95978 MW; F8B709418DC12810 CRC64;
MANFNRIELL LGLLLVSFSL LAANAHPTDL HLAHKRATTS PRERISINKD WKFSRFTSNP
DGLSYNETLK PWILPSANDF VIDGTQYQRP NGTSPGQDVE YTQASFDDST WEALDLPHDW
AIKGPFNAPG ISGGMGRLPS NGIGWYRHNL TFTEEDVGKS IFIDIDGAMS YSAVWLNGEL
VGGWPYGYTS FQLDLTPYIT VGEENLLAVR LDNPLDFSRW YPGAGLYRNV WLVKVDPVHV
AKFGTHITTP VVTAEEATVD IVVNVENKGE NAQGVIVQTD IRPSGSDEAV ASFDPASVLI
NGGSKQSVNG SVTLTNPQLW GPPPTQQPNL YVAVTTITSS NGTVLDQYET TFGVRSVVYD
PDEGIIVNGE KIPIRGTDNH HDLGSIGAAF NHRAAERQLE LLQEMGGNAL RMSHNPPAPE
LLDLADIKGF LVMDEAFDVW NEEKVTNDYH LLFADWHEPD LRTLIRRDVN HPSVIAWSIG
NEIPEQRTDE GAATGQILYD IVHEEDSTRP VTSALNNGQP GDGLADLLDV ISLNYQGEGR
GNSWTSTFPA FHETYPEKLL WTSESASTVS TRGTYFFPVI GNMSQVVSDA PGDGGNSTLL
EVSAYDLYAP SWATSPDKVF KQQDTYPYVA GEFVWTGWDY IGEPTPYDDY DAARSSYFGI
IDLAGFKKDR FYLYQSRWRP DVQFAHILPH WTWPDRVGEV TPVHVFSSAD EAELFINGES
AGKITKEELT YRFRWDNVTY TPGELHVVTY KNGSVWAEAS KKTAESAAAL NITADRTTIT
ADGYDLSFVS VAVVDEAGTV VPEASNNITF SVTGPGEIVS TDNGKPTDLT PFPSLTRSAF
SGLALAVVRS QSGQAGSITV SAVADGLAGA EITVEAS
//
