ID A0A319CK03_9EURO Unreviewed; 993 AA.
AC A0A319CK03;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=BO82DRAFT_316012 {ECO:0000313|EMBL:PYH78993.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH78993.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH78993.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH78993.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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; KZ821723; PYH78993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CK03; -.
DR STRING; 1448315.A0A319CK03; -.
DR VEuPathDB; FungiDB:BO82DRAFT_316012; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000248340; 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:UP000248340};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..993
FT /note="Probable beta-galactosidase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016459297"
FT DOMAIN 379..557
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 993 AA; 107557 MW; 6A9834AB09E57D0F CRC64;
MKLWSSLLLG ASLLTGSRAT TDGLTDLVSW DPYSLSVNGN RLFVFSGEFA YPRLPVPELW
LDIFQKMRAN GFNAASVYLF WNFHSPVNGT FDFETGAHNI QRLFDYAQEA GIYLIARPGP
YDNAEISGGG LALHLSDGSG GSLRTGDATY TAAWQPWVEE IGKIIAANSI TNGGPVILNQ
IENELQETTH SASNTLVQYM IKLEDAFRAA GVDVPFTHNE KGMRSESWST DYEDVGGAVN
VYGLDSYPGG LSCTNEATGF NVVRTYYQWF QNYSYTQPSY IPEFEGGWFS AWGASSFYDT
CTSELSPQFA DVYYKNNIGQ KITLQSIYMT YGGTNWGHLA APVVYTSYDY SAPLSESRVV
RDKMSQTKLI GLYTRVSTGL LTADMEGNGT GYTSSTSAYT WVLRDSQSDG GFYVVQQATT
SSRSSLTFDL DVTTSAGNIT LTDINLDGRQ SKIISTDYPL GHSTLLYVST DIATYGTFGD
TDVVVLYSRV GQTASFAFKN PGRLNFTEYG SSVNLTQSSG NSTTPSYTYT QASGTSVVQF
SNKTIFYLLD TDTAFRFWAP PTTNDPYVTA DQHIFVIGPY LVRNASVDGS VVNLIGDNDN
TTTIEVFAGS SVNTVKWNGK RISVTKTAYG SLVGSIDGAS STISLPALSG WKVKNSLPEL
ESDYDDSNWT VCNKTTTLSP VQPSTLPVLY ASDYGYYTGI KIYRGRFDGA NVTGASLTAQ
GGVGFGWNVW LNGDLVATLP GDASATSSIA TLDFSNQTLK DTDNLLTVVI DYTGHDETST
AKGVENPRGL LAATLTGGNF TSWKIQGNAG GAAGAYELDP VRAPMNEGGL LAERQGWHLP
GYKAQSSDGW TSGSPLDGLN KSGVAFYLTT FTLNLPKSYD VPLGIRFTSP STVNPVRIQL
FINGYQYGKY VPYLGPQTTF PVPPGIINNR DKNTIGLSVW AQTDEGAALE NIELVTYGAY
ASGFDAGSGT SFDMNGAKLG YQPEWTEARL KYT
//
