ID   C9SNK3_VERA1            Unreviewed;      1020 AA.
AC   C9SNK3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN   ORFNames=VDBG_06478 {ECO:0000313|EMBL:EEY20368.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR   EMBL; DS985221; EEY20368.1; -; Genomic_DNA.
DR   RefSeq; XP_003002916.1; XM_003002870.1.
DR   AlphaFoldDB; C9SNK3; -.
DR   STRING; 526221.C9SNK3; -.
DR   GeneID; 9536189; -.
DR   KEGG; val:VDBG_06478; -.
DR   eggNOG; KOG2024; Eukaryota.
DR   HOGENOM; CLU_002346_0_0_1; -.
DR   OMA; EITDFCH; -.
DR   OrthoDB; 276651at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
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; -; 2.
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:UP000008698}.
FT   DOMAIN          754..1016
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1020 AA;  114263 MW;  E51950EC4EE81391 CRC64;
     MSPKSIPPQE IEGTPDWQHQ AVFRRNTLPA RSYHIPETSL LLNGQWEFSY TSCPEESPQP
     GDEDVPEDNW GTIEVPGHWQ LQGHGRPHYT NTVFPIPVCP PFAPTDNPTG VYRRTFNVPS
     TWDASSQLRL RFDGVDSAYH IYVNGALVGY AEGSRNASEF DVTEFVKHDA PNDLFVKVYQ
     WSSATYIEDQ DQWWLSGIFR DVHLLAFPKT DRIDDWFLRT DLDAKYENAT LQATVDVTAS
     TSDTLKITLK ELAKNGGAVI TTQDAPVKSG DTKIDLDLAV SNPKKWTAET PYLYQVEITL
     GAHTIQQNIG FRKVELKGGL IRVNGVPIRI YGVNRHEHHP KFGRAVPLDF IKRDLLLMKT
     HNINSLRCSH YPPHPKLFDM CDELGLWVMD EADLETHGFY DCIARPLDIP EEWDYEERKK
     QTFPPAGKYT SQNPDWKEAY VDRMVQLVQR DKNHSSIIMW SLGNEAFYGD NHKAMYEYGK
     AFDPTRPIHY EGDVDAVTAD MFSYMYPPID RLLHLMKTAG VKEDGSWDKP IVLCEYAHAM
     GNGPGALDDY VETFEANERL QGGYIWEWAN HGIWKEDSDG KKYYAYGGDF DDFPNDGTFV
     MDGLLHSTHE PTLGLVQLKK SYQPLLLSVE GGKLVIKNKY DFVGVQHLSA TYKVEELGES
     TSHIAAGSLE IPAIAAGETL SVDLPASLSN IKSTKDVFLT VSFRLKESTN WAEPSHEIAW
     IQHQLSSAEA PTSAAALNTL TSKLTVEKTR ARATISGLDF SFVFDTARGL LVSWTAGDKT
     LLEKDPATGA ALIPNFWRPP TDNDVPVACV YWKRFGVHEL TSQLRSLEIV ESADKVEIST
     KTFLSPPVLA WGFETTSKYT ISATGKLTAL SQVKYLGLGP DESYPDKQTS QRVGVYSATV
     PELQTHYEVP QENGNRMATR YVTLTEGGHG RGFRATPSDA SAWTDESWRD FSFRASHYSA
     DTLHFAKHPC DLVEADATLL RLDARVAGVG SAACGPGPRE DLLVKTEPLK FGFVLERVGF
//