ID A0A084VG17_ANOSI Unreviewed; 1060 AA.
AC A0A084VG17;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=ZHAS_00004081 {ECO:0000313|EMBL:KFB36911.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB36911.1};
RN [1] {ECO:0000313|EMBL:KFB36911.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC004081-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; ATLV01012598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE524806; KFB36911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084VG17; -.
DR STRING; 74873.A0A084VG17; -.
DR EnsemblMetazoa; ASIC004081-RA; ASIC004081-PA; ASIC004081.
DR VEuPathDB; VectorBase:ASIC004081; -.
DR VEuPathDB; VectorBase:ASIS016193; -.
DR OMA; YWRVKDS; -.
DR Proteomes; UP000030765; 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; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 3.
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:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 2.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 3.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
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:UP000030765};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1060
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010759818"
FT DOMAIN 34..206
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 207..317
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 367..477
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 499..786
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 836..947
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 977..1035
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
SQ SEQUENCE 1060 AA; 121202 MW; 802640BC9B4A3781 CRC64;
MAHKLSGFVY LVLILLTPSV VEMRSFSIDY DNNTFLMDGV PFQYVAGSFH YFRALPQMWQ
PILRSMRAAG LTAVTTYVEW SLHNPKENVY TWDGMADIEH FIELAAQEDL YVILRPGPYI
CAERDMGGFP AWLLHKYPGI QLRTNDVAYL REVRSWYAQL LSRLERFMYG HGGPILLVQV
ENEYGSYFAC DHKYLNWLRD ETEDEISGFW SQLRKTQPKG PLVNAEYYPG WLTHWQEPHM
ARTDIKSVVD SLDYMLRNKV NVNIYMFYGG TNYGYTAGAN AIGAGKYAAD ITSYDYDAPL
SECGEPTDKY FAIRDTILKY FPTPNVSTPT KEIKMELPSI NVTRLGSLLD PPVLQHLSQQ
IVTNKEPMTF EALNQVSGLV LYETLLPEDI KTDPYKLTVE EVHDRGYVFV DRKFIGVLSR
ENLINTLPIG LDAGRTLQIV VENQGRINFG ISNDFKGIVG KVFINTRELV NWTMYAMPLE
QFHPIKQLIM EHQKVASRKK IADVGKGVTP IYIEWSLHEP FPGQYRWDGI ADLEKFIETA
QSENLYVILR PGPYICAERD MGGFPHWLLT KYPAVKLRTY DIDYLKEVQK WYSTLMPRVE
RFLYGNGGPV IMVSIENEYG SFHACDRLYM QYMKNLTVHF VEDKAVLFTN DGPELLECGS
IPGILPTLDF GITNNPDVFW KRLRKYLPKG PLVNAEYYPG WLTHWMEPTA RVDADMVVSS
LRLMLNQKAN VNFYMFFGGT NFGFTAGAND VGPGKYSADI TSYDYDAPLD EAGDPTPKYF
AIRKALIEYF GDPGVPAPEK LPKMSLDTVW LERRGSLISK HGRKMLAKRM VAAPKPVSFE
ALNQHSGFLL YETSLPEGLN RDPYTLTVEH LHDRAYVHVD DVFQGILSRE TNVSSLPLSV
GLGTKLQLLV ESQGRINYNI PNDFKGILGS VTVDGKPLNN WTITCFPLDS YQYMENFLNQ
LSNAEDDDLS DAAAQIYYGT FMLSNETIYD TYLYPSEWGK GLVFINGFNL GRYWPLAGPQ
ITLYVPRHIL TKGSNHIVMI EYQKKIQYPY VQFIDKPIFN
//