ID A0A2H3HA44_FUSOX Unreviewed; 1024 AA.
AC A0A2H3HA44;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=AU210_007071 {ECO:0000313|EMBL:PCD38600.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD38600.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD38600.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD38600.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD38600.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD38600.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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:PCD38600.1}.
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DR EMBL; MABQ02000004; PCD38600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3HA44; -.
DR STRING; 327505.A0A2H3HA44; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000219602; Chromosome 5.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF1; LACTASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602}.
FT DOMAIN 742..1022
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1024 AA; 116095 MW; 88F5361CEFAE0D2D CRC64;
MDKPDYENLE VIQRNRLTPR AYWLPPTHLL LNGTWDFQYA PTPLEASEYP PKDGSSEETW
SAINVPGHWQ LQGHGHPHYT NVQFPFPSNP PYIPTENPTG TYRRHFKVPT EWDSTSQLRL
RFDGVDSAYH VWLNGSFVGY SQGSRNAAEF DITGIAKKDN ENELVVRVYQ WCEASYIEDQ
DQWWLSGIFR DVTLLALPGQ DRIEDFFVKT NLDDTYENAV LQVDVTLNQP DPSTPELLLI
LRDGGIEVGS TRKTVDANRK VKFELPVSNP KKWTAESPYL YQLEISLQTQ GGESIQTIAQ
NVGFRKIELK EGLITVNGSP ILLRGTNRHD HHPIHGRAVP YEFLKQDLLL MKQHNINALR
TSHYPGQPWL YDLADELGFW VMDEADLECH GFYDVVTQHV TPAPYLDYEG SKEEFFPKAA
QFTSDNPEWR ESYLDRMVQM VQRDKNHPCI FSWSLGNESF YGVNHVAMIE YARSIDDRLI
HYEGDIKAQE TDMYSYMYPD QDRLKRHVEI DGIKDGQWEK PVILCEYAHA MGNGPGGLDD
YQDAFRKYKR LQGGFIWEWA NHGLLHKDGY YAYGGDFGDE PNDSTFVMDG LCNSEHKPTP
GLIELKRVFQ PINFKYEDGK VFITNEYDFI GLDHLEAKYA IKAYGDKVSL LESGKLAVPS
AQPWNTVKLD LPIDLTQYSD HGEEVFLSVS FALKESTSWA PASHEVACFQ HKISANRQPS
IPASLSASSG SVKVVETRTK VEVSCSDWNI HFDRVRGYIT KWSRGSDILE VDPVTRAAIY
PCFWRAPTDN DKDSAVSVWK DYGVHRMTSQ LRSFKVEKSE DGSGVSIETK TYFAPPVLGW
GYDIHTVYHI SSKGFLSINL DLKPKGVFPV DVPRVGLNIR LPKSLSQASW FGRGPGESYP
DKKHSQAIGI WSSAVDDLEV PYDVPQGNGN RMETRWVRLV DADGHGIKAS RLDASTFNWT
GGRLSDQTIE NAKHPCDLVR EDATLLNLSP RVAGVGSATC GPGVRDDLLV KVKPESYGFV
LESI
//
