ID A0A8H6K0R1_9PEZI Unreviewed; 1087 AA.
AC A0A8H6K0R1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=CMUS01_11126 {ECO:0000313|EMBL:KAF6822321.1};
OS Colletotrichum musicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orchidearum species complex.
OX NCBI_TaxID=2175873 {ECO:0000313|EMBL:KAF6822321.1, ECO:0000313|Proteomes:UP000639643};
RN [1] {ECO:0000313|EMBL:KAF6822321.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LFN0074 {ECO:0000313|EMBL:KAF6822321.1};
RX PubMed=32352862;
RA Rogerio F., Boufleur T.R., Ciampi-Guillardi M., Sukno S.A., Thon M.R.,
RA Massola Junior N.S., Baroncelli R.;
RT "Genome Sequence Resources of Colletotrichum truncatum, C. plurivorum, C.
RT musicola, and C. sojae: Four Species Pathogenic to Soybean (Glycine max).";
RL Phytopathology 110:1497-1499(2020).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6822321.1}.
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DR EMBL; WIGM01000547; KAF6822321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H6K0R1; -.
DR OrthoDB; 408320at2759; -.
DR Proteomes; UP000639643; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005990; P:lactose catabolic process; IEA:TreeGrafter.
DR FunFam; 3.20.20.80:FF:000018; Beta-galactosidase; 1.
DR Gene3D; 2.70.98.10; -; 1.
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; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR050347; Bact_Beta-galactosidase.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; GH.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006102; Ig-like_GH2.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 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 Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KAF6822321.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000639643}.
FT DOMAIN 800..1087
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 26..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 124149 MW; 78C6BF46934E8B1A CRC64;
MSDISDDYVT ISPQTDLHMS VYMEKMARHG RPGSSSSSEG SSAAGPAEEE ERATTPTTTV
VAPTHVLPKK IPDWSNLKVL HRNTLPPRSY FFLYNNEEDA LTRDTSKSKS LLLSGKWKFH
LTTSPFAGPR DFYKRDFDTS EWDDIVVPGM WQCQGHGKGP QYTNLNFPWP VEPPNIPYDD
NECGRHVTKF HVGKDFAEHQ LRLRFEGVDS GFAVWVNGHE VGYSQGARNP SEFDVTDFIE
LDAENTLAVE VYQRCDGTYL EDQDQWWLSG IFRDVYLHAF PKFHPEDYHV HTILDDDYKD
ATLRVEVTMN RGAYVDMKLL DADGKLIAKG MEIFDRTNRF EVRVKNPHKW TAETPYLYTL
VLNFQKCSLV QRIGFRRTEL IKGVFCINGE PVKFRGVNRH EHHPDSGRAV PYEFLKRDLL
IMKHFNINGI RTSHYINDPR LYDLADELGI WILDEADLEC HGLGVLGTDG NSLASDNPDW
REAYEDRARQ MVMRDKNHAS IVLWSLGNES FYGRNHQHMY DVIKSIDKSR LVHYEGDWGA
NTADIYSRMY TSVDEIVSMS AERDWKKPLV MCEYIHAMGN GPGGIKEYID AFYEHPRLMG
GFVWEWANHG LRTKNDEGEE YMGYGGDFGD EPNDYNFVFD GLCFGNHSPT PGLREYGKAI
EPVQTLEIKG NEVTIINRYD FITLDHLTAT WHIVGDGVVI GSDQEVEIPK GIKPHTKGHL
KIKGLPKDLT SEAYLHIDFA LAKDTNWAKA GHRVAFGQAA LSKPPSMAAV LSTLFHPWVD
PVPTITQTSP NLLSITSSSG LNTWGFDFTL GTLTSWRRSS RPHLELLTEP FVMDFYRALT
DNDRGGRFGQ NWEDRRLHQT RHHVKRVEWR KEKHGLTVHV HSRIAPPVLA WAVDTWTTFT
FHGEAVYIKI KGKPNGPLLP DTFARIGLTG GVKGVEKVAW WGRGPGESYS DKKQAQAFGN
WEETVDDLFV DYEFPQDGGN RTDVRWVELR GRLPDEEGVV DDDQPLKRIL RARFGDLEGA
SFSAMHYTTK DLDECKHPYE LHRRKREDTV VRLDWKHHGL GTGSCGPATL PQYELKSRDF
DVEIVLD
//
