ID A0A2K1QV22_9PEZI Unreviewed; 1014 AA.
AC A0A2K1QV22;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CAC42_5441 {ECO:0000313|EMBL:PNS18902.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS18902.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS18902.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS18902.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PNS18902.1}.
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DR EMBL; NKHZ01000039; PNS18902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1QV22; -.
DR STRING; 2082308.A0A2K1QV22; -.
DR InParanoid; A0A2K1QV22; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000243797; 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:SF122; BETA-GALACTOSIDASE A-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.
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:UP000243797};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1014
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014423593"
FT DOMAIN 395..573
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1014 AA; 111002 MW; F7F48F9C95D692A8 CRC64;
MLGLNSLKAL LLVGLAGLAS ARSIGAKPGQ MWIQNDKRQE LQDLVTFDNS SLFVRGERVL
FYSGEVHPYR LPVPGLWLDL FQKIKSLGFN GVSFYTSWAS LEGKPGEFIA EGIFNFEDFF
KAASDAGIYL LARPGPYINA EATGGGFPGW LQRNPGILRT PDPEYLRATD NYIANMAGII
AKAQITNGGP VILYQPENEY SQADPNVVFP DSDYFSYVIK QARDAGIVVP LISNDNAPRG
LFSPDGQQAA KVDIYGHDNY PLGFDCANPD VWPNNNLPTN YRRLHLQQAP STPYSLVEYQ
GGAFDPWGGN GFDKCLSLVN YEFERVFYKN MYAAAVTIFN IYMTFGGTNW GNQGHPGGYT
SYDYGASIAE DLTVSREKFS EIKLQANFLH ASPAYLVATP QNNEQNVGAF TNNGDIAVIQ
STTDTTNFYI VRHSQYNSLA TREYQLTVPT SQGNVTVPQL GGSLVLTRRD SKFHVTDYDV
GGVNLLYSSA EIFTWKKYED KTVLVVYGGP NELHEFAVQT NKTAETLEGD GLKIETRNGN
SIVQFPVSST RRVLRYGSDF YVYILDRNSA YNFWTLDLPT GLPKGDPNAG IKAAAIVKAG
YLMRTAAVDG TTLSLVGDVN ATTPIEVIGG APRNLQTLNF NGQALDFEQD ADTGVVTATV
EFTEPELTLP DLATAEWRTV DSLPEIQENY DDSLWTVASL TQSNNTARNL TTPTSLYASD
YGYHTGPLVY RGRFTAGGNE STLSLTTQGG SAFGYSAWLG SSFLQSFVGN DKTSTITQTI
TLPSLTAGQE YVIVVVVDHM GINQNYNPGS EDMKEPRGVL DFNLAGRDKT AVTWKLTGNL
GGEDYRDRAR GPINEGGLFF ERQGWHLPSA PTESFAVGSP LTGIDKAGVQ FYSTSFDLAI
PEGYIIPLAL SFGNSTEDTG ADGLSRAYRA QIYVNGYQYG KYVHNVGPQD VYPVPQGIWN
YQGPNYLGVA LWALEADGAK LSDFKIVVGE KVQSGYGKFP NSPQDGYVER EGAY
//
