ID W5J5L0_ANODA Unreviewed; 656 AA.
AC W5J5L0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=AND_009692 {ECO:0000313|EMBL:ETN58683.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN58683.1};
RN [1] {ECO:0000313|EMBL:ETN58683.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN58683.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN58683.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC009692-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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|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; ADMH02002125; ETN58683.1; -; Genomic_DNA.
DR AlphaFoldDB; W5J5L0; -.
DR STRING; 43151.W5J5L0; -.
DR EnsemblMetazoa; ADAC009692-RA; ADAC009692-PA; ADAC009692.
DR VEuPathDB; VectorBase:ADAC009692; -.
DR VEuPathDB; VectorBase:ADAR2_007160; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_7_2_1; -.
DR OMA; HERQYLH; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000000673; 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; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
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:SF65; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
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:UP000000673};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..656
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014109495"
FT DOMAIN 49..372
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 422..519
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 572..629
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 280
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 656 AA; 73370 MW; 43F8552F93B5AD4E CRC64;
MRRPKLLGIC AIVLVAIVGL TLGLVLGLQS DDDGDDAQRS FTIDYERDTF VMDGKDFRYV
AGSFHYFRAL PQTWRTKLRT LRAGGLNAVD LYVQWSLHNP RDGVYSWEGI ANVTDIIEAA
IEEDLYVILR PGPYICAEID NGGLPYWLFN KYPGIQVRTS DANYLAEVKK WYGELMSRME
PYMYGNGGPI IMVQIENEYG AFGKCDKPYL NFLKEETNRY VQDKAVLFTV DRPYDDEIGC
GQIDGVFITT DFGLMTDEEV DTHAAKVRSY QPKGPLVNTE FYTGWLTHWQ ESNQRRPAGP
LAATLRKMLK DGWNVDFYMY FGGTNFGFWA GANDWGLGKY MADITSYDYD APMDEAGDPT
MKYIAFRDII GEYLPLAIMP VPEATPKMVL ESVQLTTIGS ILSESGRQLL GTKQTNPSGK
LLTFEEINQN SGFVLYETTL PKLTRDPSLL TINGLHDRAQ VYQDEFYVGT LARENAIDAL
PLTAGFGSKL SLLVENQGRI NFDILDDYKG ILGNVTIQTY DEPHELSLEG EWSVTGYPFD
DYAKLQQFVN SAPGGPGANG RGMAVHGPIV LSAVFDVSTA DIHDTYLNMA GWGKGFIFVN
GFNLGRYWPV VGPQVTTYLP KDLLKPTGNT VVVVELQKLP TDRMLHFASK AILDEA
//
