ID A0A2H3GJZ8_FUSOX Unreviewed; 1049 AA.
AC A0A2H3GJZ8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=AU210_013294 {ECO:0000313|EMBL:PCD26874.1};
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:PCD26874.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD26874.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD26874.1,
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:PCD26874.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD26874.1,
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}.
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:PCD26874.1}.
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DR EMBL; MABQ02000009; PCD26874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3GJZ8; -.
DR STRING; 327505.A0A2H3GJZ8; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000219602; Chromosome 11.
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; 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; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602}.
FT DOMAIN 763..1047
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 118285 MW; 68BBFEB75694621B CRC64;
MGDSIQQEPK GIPLQEDPSQ PDYINEAVFR RNTLPTRSYH IPDTSISLNG TWDFSLAGTV
LEAPEPGAKD VAYGQIQVPG HWQLQGHGKP WYTNVQYPIP VCPPYVPTEN PTGTYRREFH
VPTGWAADSQ LRLRFDGVDS AYHIWVNGTL IGYAQGSRNP SEFDVSSFVN REGANELFVR
VYQWSDATYI EDQDQWWLSG IFRDVYLISF PAARVDDFFL TPHLDTDYKN ARLNASVDVS
AQKGVIVELI VSELAKNGGA VIGSTETSFD GQSKVTLSLY VEDPKKWTAE TPYLYSAEIT
LKSEDKQTVL HKVQQRVGFR TVELKDGLMK VNGKRIRLRG VNRHEHHPLL GRSVPLEFAK
RDLFIMKKHN INALRCAHQP HDPRVLDLCD EYGLWVMAEA DLECHGFYDA VARPLDIPES
MDYGERKKLA FGKAAEFTSN NPKWKDAYLD RIRAVLNRDK NHASVIMWSF GNEAFYGDNH
REMFKYATEA DPSRLIHYEG DMEAETTHMY SYMYPTVDRL IKYAEEEGVK DGKYEKPIVL
CEYGHAMGNG PGWLEDYEQA FRDYPRLQGG FIWEWANHGL WKDDHEGAGY YAYGGDFGDT
PNDGTFVMDG LLNSQHEPTP GLTEFKKVIQ PVGFSFKDGE LKIENWHDFA GLDHLTASYK
VEQFGQESTL IHSGSFDIPE IPAGETRSVS LPVDAKRYNK DNEVYLTVTL SLKHSTAWAP
AGHEIAWYQQ QLQAPQTDAK AALAASNTLT SKLSVTEKGA TVSVFGKNFE FVFDRAYGAL
KSWVSNNVTL LTFDPKTQAA IIPSFWRPKT DNDVPGAVPY WERFGVEQLQ SQLRSFSVDA
SNSDKVVVKS HTFITPPVLF WGWDCEIEYT VYLTGALSVN VTRLSPTGSF PEHVPRIGLN
LYGSKTLEHV KWLGRGPGES YPDKKDSQRV GIWNAESVSE LQTPYDVPQE NGNREDTRWV
SLRDSKSPSI GLRATRLDGK NFSFLASHHR DATIHEARHP PDLKEDDAVF IRLDSKVAGV
GSGACGPAVR EDLMVKTEET TFGFLLEPL
//
