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Database: UniProt
Entry: Q75I93
LinkDB: Q75I93
Original site: Q75I93 
ID   BGL07_ORYSJ             Reviewed;         504 AA.
AC   Q75I93; Q10EB0; Q10EB1; Q10EB2; Q42975; Q75I92;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   26-NOV-2014, entry version 75.
DE   RecName: Full=Beta-glucosidase 7;
DE            Short=Os3bglu7;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=BGLU7; Synonyms=BGLU1;
GN   OrderedLocusNames=Os03g0703000, LOC_Os03g49600;
GN   ORFNames=OSJNBa0004L11.16;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nipponbare; TISSUE=Root;
RA   Esen A., Opassiri R., Ketudat Cairns J.R., Akiyama T.;
RT   "Oryza sativa beta-glucosidase mRNA.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R.,
RA   Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L.,
RA   Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S.,
RA   Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S.,
RA   Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J.,
RA   de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H.,
RA   Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F.,
RA   Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A.,
RA   Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J.,
RA   Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L.,
RA   Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A.,
RA   Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W.,
RA   Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome
RT   3 and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14692878; DOI=10.1042/BJ20031485;
RA   Opassiri R., Hua Y., Wara-Aswapati O., Akiyama T., Svasti J., Esen A.,
RA   Ketudat Cairns J.R.;
RT   "Beta-glucosidase, exo-beta-glucanase and pyridoxine transglucosylase
RT   activities of rice BGlu1.";
RL   Biochem. J. 379:125-131(2004).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17196101; DOI=10.1186/1471-2229-6-33;
RA   Opassiri R., Pomthong B., Onkoksoong T., Akiyama T., Esen A.,
RA   Ketudat Cairns J.R.;
RT   "Analysis of rice glycosyl hydrolase family 1 and expression of
RT   Os4bglu12 beta-glucosidase.";
RL   BMC Plant Biol. 6:33-33(2006).
RN   [8]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19766588; DOI=10.1016/j.abb.2009.09.004;
RA   Kuntothom T., Luang S., Harvey A.J., Fincher G.B., Opassiri R.,
RA   Hrmova M., Ketudat Cairns J.R.;
RT   "Rice family GH1 glycoside hydrolases with beta-D-glucosidase and
RT   beta-D-mannosidase activities.";
RL   Arch. Biochem. Biophys. 491:85-95(2009).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 29-504 IN COMPLEX WITH ZINC
RP   IONS AND SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND MUTAGENESIS OF ILE-207; ASN-218; ASN-273 AND LEU-470.
RX   PubMed=18308333; DOI=10.1016/j.jmb.2008.01.076;
RA   Chuenchor W., Pengthaisong S., Robinson R.C., Yuvaniyama J.,
RA   Oonanant W., Bevan D.R., Esen A., Chen C.J., Opassiri R., Svasti J.,
RA   Cairns J.R.;
RT   "Structural insights into rice BGlu1 beta-glucosidase oligosaccharide
RT   hydrolysis and transglycosylation.";
RL   J. Mol. Biol. 377:1200-1215(2008).
CC   -!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl
CC       beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl
CC       beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl
CC       beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside
CC       and the cyanogenic glucosides amygdalin, prunasin and dhurrin.
CC       Possesses pyridoxine transglucosylation activity.
CC       {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC       ECO:0000269|PubMed:19766588}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
CC       glucosyl residues with release of beta-D-glucose.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=0.23 mM for p-nitrophenyl beta-D-fucoside (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=3.2 mM for p-nitrophenyl beta-D-galactoside (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=1.3 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=1.3 mM for p-nitrophenyl beta-D-xyloside (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=1.2 mM for p-nitrophenyl beta-L-arabinoside (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=0.78 mM for p-nitrophenyl beta-D-cellobioside (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=22 mM for cellobiose (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=0.22 mM for cellotriose (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=0.28 mM for cellotetraose (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=0.24 mM for cellopentaose (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=0.22 mM for cellohexaose (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=2.05 mM for laminaribiose (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=1.92 mM for laminaritriose (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=13.9 mM for sophorose (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC         KM=38.3 mM for gentiobiose (at pH 5.0)
CC         {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC         ECO:0000269|PubMed:19766588};
CC   -!- SUBUNIT: Homodimer. Formation of the homodimer is zinc-dependent.
CC       Dimerization does not increase activity.
CC       {ECO:0000269|PubMed:18308333}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS07255.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABF98424.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABF98425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABF98426.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U28047; AAA84906.3; -; mRNA.
DR   EMBL; AC091670; AAX95519.1; -; Genomic_DNA.
DR   EMBL; AC133334; AAS07254.1; -; Genomic_DNA.
DR   EMBL; AC133334; AAS07255.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000009; ABF98423.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF98424.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000009; ABF98425.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000009; ABF98426.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008209; BAF12927.1; -; Genomic_DNA.
DR   EMBL; AK100165; BAG94472.1; -; mRNA.
DR   PIR; T03296; T03296.
DR   RefSeq; NP_001051013.1; NM_001057548.1.
DR   UniGene; Os.5072; -.
DR   PDB; 2RGL; X-ray; 2.20 A; A/B=29-504.
DR   PDB; 2RGM; X-ray; 1.55 A; A/B=29-504.
DR   PDB; 3AHT; X-ray; 2.80 A; A/B=29-504.
DR   PDB; 3AHV; X-ray; 1.75 A; A/B=29-504.
DR   PDB; 3F4V; X-ray; 1.65 A; A/B=29-504.
DR   PDB; 3F5J; X-ray; 1.95 A; A/B=29-504.
DR   PDB; 3F5K; X-ray; 1.80 A; A/B=29-504.
DR   PDB; 3F5L; X-ray; 1.37 A; A/B=29-504.
DR   PDB; 3SCN; X-ray; 2.20 A; A/B=29-504.
DR   PDB; 3SCO; X-ray; 1.95 A; A/B=29-504.
DR   PDB; 3SCP; X-ray; 2.10 A; A/B=29-504.
DR   PDB; 3SCQ; X-ray; 2.10 A; A/B=29-504.
DR   PDB; 3SCR; X-ray; 1.80 A; A/B=29-504.
DR   PDB; 3SCS; X-ray; 1.85 A; A/B=29-504.
DR   PDB; 3SCT; X-ray; 1.60 A; A/B=29-504.
DR   PDB; 3SCU; X-ray; 1.58 A; A/B=29-504.
DR   PDB; 3SCV; X-ray; 2.11 A; A/B=29-504.
DR   PDB; 3SCW; X-ray; 1.90 A; A/B=29-504.
DR   PDBsum; 2RGL; -.
DR   PDBsum; 2RGM; -.
DR   PDBsum; 3AHT; -.
DR   PDBsum; 3AHV; -.
DR   PDBsum; 3F4V; -.
DR   PDBsum; 3F5J; -.
DR   PDBsum; 3F5K; -.
DR   PDBsum; 3F5L; -.
DR   PDBsum; 3SCN; -.
DR   PDBsum; 3SCO; -.
DR   PDBsum; 3SCP; -.
DR   PDBsum; 3SCQ; -.
DR   PDBsum; 3SCR; -.
DR   PDBsum; 3SCS; -.
DR   PDBsum; 3SCT; -.
DR   PDBsum; 3SCU; -.
DR   PDBsum; 3SCV; -.
DR   PDBsum; 3SCW; -.
DR   ProteinModelPortal; Q75I93; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PRIDE; Q75I93; -.
DR   EnsemblPlants; OS03T0703000-01; OS03T0703000-01; OS03G0703000.
DR   GeneID; 4333841; -.
DR   KEGG; osa:4333841; -.
DR   Gramene; Q75I93; -.
DR   eggNOG; COG2723; -.
DR   HOGENOM; HOG000088630; -.
DR   InParanoid; Q75I93; -.
DR   KO; K05350; -.
DR   OMA; RDENISC; -.
DR   SABIO-RK; Q75I93; -.
DR   EvolutionaryTrace; Q75I93; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0047668; F:amygdalin beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0033907; F:beta-D-fucosidase activity; IDA:UniProtKB.
DR   GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0080083; F:beta-gentiobiose beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0047701; F:beta-L-arabinosidase activity; IDA:UniProtKB.
DR   GO; GO:0004567; F:beta-mannosidase activity; IDA:UniProtKB.
DR   GO; GO:0080079; F:cellobiose glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0050224; F:prunasin beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; -; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Metal-binding; Reference proteome; Secreted;
KW   Signal; Zinc.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    504       Beta-glucosidase 7.
FT                                /FTId=PRO_0000383461.
FT   REGION      468    469       Substrate binding.
FT   ACT_SITE    204    204       Proton donor. {ECO:0000250}.
FT   ACT_SITE    414    414       Nucleophile. {ECO:0000250}.
FT   METAL        93     93       Zinc; shared with dimeric partner.
FT   METAL        96     96       Zinc; shared with dimeric partner.
FT   BINDING      57     57       Substrate.
FT   BINDING     158    158       Substrate.
FT   BINDING     203    203       Substrate.
FT   BINDING     343    343       Substrate.
FT   BINDING     461    461       Substrate.
FT   CARBOHYD    280    280       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    422    422       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    223    226       {ECO:0000250}.
FT   MUTAGEN     207    207       I->V: Increases KM for substrate about 5-
FT                                fold. {ECO:0000269|PubMed:18308333}.
FT   MUTAGEN     218    218       N->H: Decreases KM for substrate about 2-
FT                                fold. {ECO:0000269|PubMed:18308333}.
FT   MUTAGEN     273    273       N->V: Increases KM for substrate about 5-
FT                                fold. {ECO:0000269|PubMed:18308333}.
FT   MUTAGEN     470    470       L->R: No effect on KM.
FT                                {ECO:0000269|PubMed:18308333}.
FT   CONFLICT     52     52       A -> V (in Ref. 1; AAA84906).
FT                                {ECO:0000305}.
FT   TURN         34     37       {ECO:0000244|PDB:3F5L}.
FT   HELIX        40     42       {ECO:0000244|PDB:3F5L}.
FT   STRAND       48     52       {ECO:0000244|PDB:3F5L}.
FT   HELIX        55     58       {ECO:0000244|PDB:3F5L}.
FT   HELIX        71     76       {ECO:0000244|PDB:3F5L}.
FT   HELIX        83     85       {ECO:0000244|PDB:3F5L}.
FT   STRAND       88     90       {ECO:0000244|PDB:3F5L}.
FT   HELIX        94    107       {ECO:0000244|PDB:3F5L}.
FT   STRAND      112    116       {ECO:0000244|PDB:3F5L}.
FT   HELIX       119    122       {ECO:0000244|PDB:3F5L}.
FT   STRAND      126    128       {ECO:0000244|PDB:3F5L}.
FT   HELIX       132    147       {ECO:0000244|PDB:3F5L}.
FT   STRAND      151    156       {ECO:0000244|PDB:3F5L}.
FT   HELIX       163    169       {ECO:0000244|PDB:3F5L}.
FT   HELIX       171    173       {ECO:0000244|PDB:3F5L}.
FT   HELIX       177    192       {ECO:0000244|PDB:3F5L}.
FT   TURN        193    195       {ECO:0000244|PDB:3F5L}.
FT   STRAND      198    203       {ECO:0000244|PDB:3F5L}.
FT   HELIX       205    213       {ECO:0000244|PDB:3F5L}.
FT   TURN        232    234       {ECO:0000244|PDB:3F5L}.
FT   HELIX       235    257       {ECO:0000244|PDB:3F5L}.
FT   HELIX       259    262       {ECO:0000244|PDB:3F5L}.
FT   STRAND      265    271       {ECO:0000244|PDB:3F5L}.
FT   STRAND      274    281       {ECO:0000244|PDB:3F5L}.
FT   HELIX       282    295       {ECO:0000244|PDB:3F5L}.
FT   HELIX       297    305       {ECO:0000244|PDB:3F5L}.
FT   HELIX       310    316       {ECO:0000244|PDB:3F5L}.
FT   HELIX       317    319       {ECO:0000244|PDB:3F5L}.
FT   HELIX       325    331       {ECO:0000244|PDB:3F5L}.
FT   STRAND      336    341       {ECO:0000244|PDB:3F5L}.
FT   STRAND      345    349       {ECO:0000244|PDB:3F5L}.
FT   HELIX       361    364       {ECO:0000244|PDB:3F5L}.
FT   STRAND      368    373       {ECO:0000244|PDB:3F5L}.
FT   STRAND      376    379       {ECO:0000244|PDB:3F5L}.
FT   HELIX       392    404       {ECO:0000244|PDB:3F5L}.
FT   STRAND      410    414       {ECO:0000244|PDB:3F5L}.
FT   STRAND      419    422       {ECO:0000244|PDB:3F5L}.
FT   HELIX       425    429       {ECO:0000244|PDB:3F5L}.
FT   HELIX       432    450       {ECO:0000244|PDB:3F5L}.
FT   STRAND      455    461       {ECO:0000244|PDB:3F5L}.
FT   HELIX       469    474       {ECO:0000244|PDB:3F5L}.
FT   STRAND      479    482       {ECO:0000244|PDB:3F5L}.
FT   TURN        484    486       {ECO:0000244|PDB:3F5L}.
FT   STRAND      489    491       {ECO:0000244|PDB:3F5L}.
FT   HELIX       493    501       {ECO:0000244|PDB:3F5L}.
SQ   SEQUENCE   504 AA;  56872 MW;  4C36D2A5AF452CE9 CRC64;
     MAARRANCAL VLVLALALLA ARDAGAAAVP KPNWLGGLSR AAFPKRFVFG TATSAYQVEG
     MAASGGRGPS IWDAFAHTPG NVAGNQNGDV ATDQYHRYKE DVNLMKSLNF DAYRFSISWS
     RIFPDGEGRV NQEGVAYYNN LINYLLQKGI TPYVNLYHYD LPLALEKKYG GWLNAKMADL
     FTEYADFCFK TFGNRVKHWF TFNEPRIVAL LGYDQGTNPP KRCTKCAAGG NSATEPYIVA
     HNFLLSHAAA VARYRTKYQA AQQGKVGIVL DFNWYEALSN STEDQAAAQR ARDFHIGWYL
     DPLINGHYPQ IMQDLVKDRL PKFTPEQARL VKGSADYIGI NQYTASYMKG QQLMQQTPTS
     YSADWQVTYV FAKNGKPIGP QANSNWLYIV PWGMYGCVNY IKQKYGNPTV VITENGMDQP
     ANLSRDQYLR DTTRVHFYRS YLTQLKKAID EGANVAGYFA WSLLDNFEWL SGYTSKFGIV
     YVDFNTLERH PKASAYWFRD MLKH
//
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