ID A0A2V1BFV8_9HELO Unreviewed; 1032 AA.
AC A0A2V1BFV8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN ORFNames=DL98DRAFT_470669 {ECO:0000313|EMBL:PVH72306.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH72306.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH72306.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH72306.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; KZ804275; PVH72306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1BFV8; -.
DR STRING; 1485229.A0A2V1BFV8; -.
DR Proteomes; UP000244409; 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; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 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:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1032
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016118949"
FT DOMAIN 413..591
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1032 AA; 114576 MW; 140E48AA10676EBB CRC64;
MHLSKILIHI QLMMWISPFL RCLLILVPFT LASAELIRAD SSHIQYYRGE KQQDLVTWDK
YSIYVRGERI LFLSGEFHPF RLPSPGLWLD VFQKIRALGY SGVSFYLMWG LLEGKPGHFQ
SNGVFDLQAF FDAATQAGIY LLARPGPYIN SEVSGGGYPG WLQRIEGNVR TNTPIFLNAT
GNYVSRVGKI ISEAQITNGG PVILFQPENE YTMCSGFSSI EDISACLEED YMASVEQQWR
DSGIRVPFVN NDAVPIGNFA PGTGPGAIDI YGFDSYPLGW GTGCQDPHNW TRLLDPLSIY
NSTTHQKISP TTPFSIIEYQ GGSADPWGGE GVDTCSAMIN HEFARIFYKV NFGFRATVMN
LYMMFGGTNW GNLGHPGGYT SYDVGAAISE DRLVTREKYS EIKLQAQFQQ ASPAFMTSQP
LESTFEYTNA SRLVTTLLRG ASTNFYTVRH FDYGSLNSTP YLLHVETSIG NLTLPRLGGS
LMLNGRDSKV HVTDYNAGGV TLIYSTAEIY TWKKVGRKVI LILYGGEGET NEFAISSRSD
HLMKIEGHGI THQKTGNVGT FQWKVERCRR IISFGDELEV YLLWRNDAYN YWILDLPLPQ
PLGLHVSPPR SGSSVIVRGG YLMRNATISD KTLFLTGDLN ATTEVEVIAT PAGCCSALAF
NGKNVNTRVK DGRLSGTLKY QAPKTHLPRL SSLEWKYLDS LPELEHSYND SRWVLCDHET
SNSSRNLTTP TSLYASDYGY HSGSILYRGH FVANGEETSF YLSSQGGFAY AHSVWLNSTF
LGSWAGSPTI ATYNHMLNLP KQLVMGTPYV LTILIDHMGL DQQFLVNAQT MKSPRGLLDY
NLSSHESKSD IVWKITGNFE GEQHRDLSRG PLNEGSMFAE RQGFHLPGAP VQNWASRSPI
EGLSAPGVGF YATTFNLDYP SGYDIPTSIV FTNSSAVGGQ AGPAVFRIQL FVNGWQFGKY
VNNIGPQTEY SIPEGILNHH GENFLALTFW SLQSKGAKLG GVKLKNNAIV KTGYAAPEMV
LGAKYVPRER SY
//
