ID A0A1E1K715_9HELO Unreviewed; 981 AA.
AC A0A1E1K715;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Probable beta-galactosidase C {ECO:0000256|ARBA:ARBA00040694};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase C {ECO:0000256|ARBA:ARBA00042635};
GN ORFNames=RCO7_08048 {ECO:0000313|EMBL:CZS93879.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZS93879.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZS93879.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZS93879.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
CC {ECO:0000256|ARBA:ARBA00002691}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; FJUW01000007; CZS93879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E1K715; -.
DR STRING; 914237.A0A1E1K715; -.
DR InParanoid; A0A1E1K715; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000178129; 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; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF125; BETA-GALACTOSIDASE C-RELATED; 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.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000178129};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..981
FT /note="Probable beta-galactosidase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009445624"
FT DOMAIN 378..554
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 981 AA; 107497 MW; CC65DAC998C45516 CRC64;
MRLLNFFLVI STLFWGGFAT DNGQTTAVTW DPYSLTVNGS RVFIFSAEFH YQRMPVPELW
LDIFQKFKAN GINTISVYFF WSYHSSSKGV YDFQTSGKNA QKVFDYAKEA GIWVITRAGP
YCNAETNGGG LALWGSDGSL GNLRTSDATY YQAWLPWITQ IGEIIARNEI TKGGPVILNQ
HENELQETTH AADNTLVVYM EQVKKTFRDA GVTVPSTHNE KGMRSQSWST DYQNVGGAVD
IYGLDSYPGG FSCTNINSGF NINRKYYQWF QNNSYTQPSY LAEFEAGYFT PWGGSFYDDC
AAEHDPAYAD VYYKNNLAQR VTLLSLYMAW GGTNWGHSAA PVVYTSYDYS APLRETRQIQ
DKFYQTKLIS LFTRVSTDML KTDMIGNGTG YAVSSPLIWT WELRNPDTRA AFYTVQQNTS
KSRDSVTFSA SLNTSEGVIT VPNINLDGRQ SKILVTDYTF GKNLLLYSSA DVLSYGVFDV
DVLVLYLKPG QVGQFALKTG FASAAHIIEG SAAVNVTSTN NTTTFTYTQG SGKTTVKFGS
VLVYLLDQES AWKFWAPPTT TNPNVKPDEQ IFVLGPYLVR SASVSHGVVH VSGDNDNATT
IEVYTGNPSI QTITWNEIRL SATKTSYGSV IAQIPGAKER AISLPVLGNW RSADSLPEKS
ASYDDKNWAV CNKSSTLSPI APLTKPVLFS SDYGFYSGAK IYRGYFTGAN FNSVKITCSG
GLAFGWSAWL NGVLIGGNVG NASLTTTAAV LPLPAASLKS GDNLLTVVVD YHGHDETSTA
KGVGNPRGIL GASLLPANGT GFTLWKVQGN AGGSKNLDPV RGPMNEGGLY AERVGWHLPG
FKPDSTFDRA GPSTGLTTSG IRFYTTTFHL DIDSDLDVPL GIELAAPVGT VARVMIWVNG
YQYGKYVPHI GPQTRFPVPP GVINNRGLNT VALSLWAMTD AGAKLDTVKL ISYGAYQTDF
DFNRDWAELQ PQYDTSRLQY A
//
