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BGALA_ASPNC
ID   BGALA_ASPNC             Reviewed;        1007 AA.
AC   A2QAN3;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Beta-galactosidase A {ECO:0000305};
DE            Short=An-beta-gal {ECO:0000303|PubMed:28391618};
DE            EC=3.2.1.23 {ECO:0000269|PubMed:28391618};
DE   AltName: Full=Lactase A;
DE   Flags: Precursor;
GN   Name=lacA; ORFNames=An01g12150;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF WILD-TYPE AND MUTANT GLN-298 IN
RP   COMPLEXES WITH ALLOLACTOSE; 3-GALACTOSYL-GLUCOSE; 6-GALACTOSYL-GALACTOSE;
RP   4-GALACTOSYL-LACTOSE AND 6-GALACTOSYL-LACTOSE, FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MISCELLANEOUS, REGIONS, ACTIVE
RP   SITE, GLYCOSYLATION AT ASN-156; ASN-402; ASN-478; ASN-522; ASN-622;
RP   ASN-739; ASN-760; ASN-777 AND ASN-914, DISULFIDE BONDS, AND MUTAGENESIS OF
RP   GLU-298; TYR-304; TYR-355; ASN-357 AND TRP-806.
RX   PubMed=28391618; DOI=10.1111/febs.14083;
RA   Rico-Diaz A., Ramirez-Escudero M., Vizoso-Vazquez A., Cerdan M.E.,
RA   Becerra M., Sanz-Aparicio J.;
RT   "Structural features of Aspergillus niger beta-galactosidase define its
RT   activity against glycoside linkages.";
RL   FEBS J. 284:1815-1829(2017).
CC   -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000269|PubMed:28391618}.
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:0000269|PubMed:28391618};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=92.5 mM for lactose {ECO:0000269|PubMed:28391618};
CC         Note=kcat is 214.9 sec(-1). {ECO:0000269|PubMed:28391618};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- MISCELLANEOUS: Mutants of this enzyme have improved
CC       transgalactosylation activity and can be used for galacto-
CC       oligosaccharides (GOS) production in vitro.
CC       {ECO:0000269|PubMed:28391618}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; AM269982; CAK44114.1; -; Genomic_DNA.
DR   RefSeq; XP_001389622.1; XM_001389585.2.
DR   PDB; 5IFP; X-ray; 1.71 A; A=1-1007.
DR   PDB; 5IFT; X-ray; 2.45 A; A=1-1007.
DR   PDB; 5IHR; X-ray; 2.40 A; A=1-1007.
DR   PDB; 5JUV; X-ray; 2.27 A; A=1-1007.
DR   PDB; 5MGC; X-ray; 2.30 A; A=1-1007.
DR   PDB; 5MGD; X-ray; 2.15 A; A=1-1007.
DR   PDBsum; 5IFP; -.
DR   PDBsum; 5IFT; -.
DR   PDBsum; 5IHR; -.
DR   PDBsum; 5JUV; -.
DR   PDBsum; 5MGC; -.
DR   PDBsum; 5MGD; -.
DR   AlphaFoldDB; A2QAN3; -.
DR   SMR; A2QAN3; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   iPTMnet; A2QAN3; -.
DR   PaxDb; A2QAN3; -.
DR   EnsemblFungi; CAK44114; CAK44114; An01g12150.
DR   GeneID; 4977988; -.
DR   KEGG; ang:ANI_1_1636014; -.
DR   VEuPathDB; FungiDB:An01g12150; -.
DR   HOGENOM; CLU_005732_2_0_1; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IMP:AspGD.
DR   GO; GO:0005990; P:lactose catabolic process; IDA:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
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; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1007
FT                   /note="Beta-galactosidase A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000219458"
FT   ACT_SITE        200
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:28391618"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:28391618"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:28391618,
FT                   ECO:0007744|PDB:5JUV"
FT   BINDING         140..142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:28391618,
FT                   ECO:0007744|PDB:5JUV"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:28391618,
FT                   ECO:0007744|PDB:5JUV"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:28391618,
FT                   ECO:0007744|PDB:5JUV"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT   CARBOHYD        622
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT   CARBOHYD        739
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT   CARBOHYD        760
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT   CARBOHYD        777
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT   CARBOHYD        805
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        914
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT   DISULFID        205..206
FT                   /evidence="ECO:0000269|PubMed:28391618,
FT                   ECO:0007744|PDB:5IFP"
FT   DISULFID        266..315
FT                   /evidence="ECO:0000269|PubMed:28391618,
FT                   ECO:0007744|PDB:5IFP"
FT   MUTAGEN         298
FT                   /note="E->Q: Loss of hydrolytic activity."
FT                   /evidence="ECO:0000269|PubMed:28391618"
FT   MUTAGEN         304
FT                   /note="Y->A: Nearly complete loss of hydrolytic activity
FT                   against lactose compared to wild-type due to decreased
FT                   substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:28391618"
FT   MUTAGEN         304
FT                   /note="Y->F: Over 33% increase of hydrolytic activity
FT                   against lactose compared to wild-type. No effect on
FT                   hydrolytic activity compared to wild-type; when associated
FT                   with H-355 and G-357. 58% reduction in hydrolytic activity
FT                   compared to wild-type; when associated with H-355, G-357
FT                   and F-806."
FT                   /evidence="ECO:0000269|PubMed:28391618"
FT   MUTAGEN         355
FT                   /note="Y->H: No effect on hydrolytic activity compared to
FT                   wild-type; when associated with F-304 and G-357. 58%
FT                   reduction in hydrolytic activity compared to wild-type;
FT                   when associated with F-304, G-357 and F-806."
FT                   /evidence="ECO:0000269|PubMed:28391618"
FT   MUTAGEN         357
FT                   /note="N->G: No effect on hydrolytic activity compared to
FT                   wild-type; when associated with F-304 and H-355. 58%
FT                   reduction in hydrolytic activity compared to wild-type;
FT                   when associated with F-304, H-355 and F-806."
FT                   /evidence="ECO:0000269|PubMed:28391618"
FT   MUTAGEN         806
FT                   /note="W->F: 43% loss of hydrolytic activity against
FT                   lactose compared to wild-type. 58% reduction in hydrolytic
FT                   activity compared to wild-type; when associated with F-304,
FT                   H-355 and G-357."
FT                   /evidence="ECO:0000269|PubMed:28391618"
FT   MUTAGEN         806
FT                   /note="W->S: 90% loss of hydrolytic activity against
FT                   lactose compared to wild-type."
FT                   /evidence="ECO:0000269|PubMed:28391618"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           75..86
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           99..102
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           118..127
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          130..137
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           144..147
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           150..154
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           164..183
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          190..199
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           213..225
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          236..239
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          257..259
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           281..288
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          295..302
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           312..318
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           321..332
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   TURN            333..335
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          337..342
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           350..352
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           377..390
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           394..397
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          398..400
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          404..410
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          414..420
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          422..424
FT                   /evidence="ECO:0007829|PDB:5MGD"
FT   STRAND          426..434
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          440..443
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          445..447
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          454..456
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          458..460
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          463..468
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          471..479
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          482..497
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          500..507
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          512..518
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          523..528
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          534..537
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          539..547
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          553..557
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          560..566
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           567..570
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          578..583
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           590..594
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          598..600
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          602..611
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          614..623
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          625..631
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          638..641
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          644..646
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          656..660
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           672..674
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          678..682
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           684..686
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          706..708
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          711..714
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           718..721
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          728..735
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          742..748
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          755..759
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          762..767
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          774..781
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          790..797
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           812..814
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          818..824
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           829..831
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          833..839
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   TURN            840..843
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   TURN            848..850
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          852..854
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   HELIX           859..862
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   TURN            863..866
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          867..869
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          875..877
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   TURN            880..882
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          884..899
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          908..912
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          921..927
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          930..936
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   TURN            937..939
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          944..947
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          955..966
FT                   /evidence="ECO:0007829|PDB:5IFP"
FT   STRAND          977..981
FT                   /evidence="ECO:0007829|PDB:5IFP"
SQ   SEQUENCE   1007 AA;  109712 MW;  CD1E91854D7A8A0A CRC64;
     MKLSSACAIA LLAAQAAGAS IKHRINGFTL TEHSDPAKRE LLQKYVTWDD KSLFINGERI
     MIFSGEFHPF RLPVKELQLD IFQKVKALGF NCVSFYVDWA LVEGKPGEYR ADGIFDLEPF
     FDAASEAGIY LLARPGPYIN AESSGGGFPG WLQRVNGTLR SSDKAYLDAT DNYVSHVAAT
     IAKYQITNGG PIILYQPENE YTSGCCGVEF PDPVYMQYVE DQARNAGVVI PLINNDASAS
     GNNAPGTGKG AVDIYGHDSY PLGFDCANPT VWPSGDLPTN FRTLHLEQSP TTPYAIVEFQ
     GGSYDPWGGP GFAACSELLN NEFERVFYKN DFSFQIAIMN LYMIFGGTNW GNLGYPNGYT
     SYDYGSAVTE SRNITREKYS ELKLLGNFAK VSPGYLTASP GNLTTSGYAD TTDLTVTPLL
     GNSTGSFFVV RHSDYSSEES TSYKLRLPTS AGSVTIPQLG GTLTLNGRDS KIHVTDYNVS
     GTNIIYSTAE VFTWKKFADG KVLVLYGGAG EHHELAISTK SNVTVIEGSE SGISSKQTSS
     SVVVGWDVST TRRIIQVGDL KILLLDRNSA YNYWVPQLAT DGTSPGFSTP EKVASSIIVK
     AGYLVRTAYL KGSGLYLTAD FNATTSVEVI GVPSTAKNLF INGDKTSHTV DKNGIWSATV
     DYNAPDISLP SLKDLDWKYV DTLPEIQSSY DDSLWPAADL KQTKNTLRSL TTPTSLYSSD
     YGFHTGYLLY RGHFTATGNE STFAIDTQGG SAFGSSVWLN GTYLGSWTGL YANSDYNATY
     NLPQLQAGKT YVITVVIDNM GLEENWTVGE DLMKTPRGIL NFLLAGRPSS AISWKLTGNL
     GGEDYEDKVR GPLNEGGLYA ERQGFHQPEP PSQNWKSSSP LEGLSEAGIG FYSASFDLDL
     PKGWDVPLFL NIGNSTTPSP YRVQVYVNGY QYAKYISNIG PQTSFPVPEG ILNYRGTNWL
     AVTLWALDSA GGKLESLELS YTTPVLTALG EVESVDQPKY KKRKGAY
 
 
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