GenomeNet

Database: UniProt/SWISS-PROT
Entry: PFKA_DROME
LinkDB: PFKA_DROME
Original site: PFKA_DROME 
ID   PFKA_DROME              Reviewed;         788 AA.
AC   P52034; Q8IH94; Q8MKV4; Q9V5G7; Q9Y100;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   16-JAN-2019, entry version 144.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03184};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN   Name=Pfk; ORFNames=CG4001;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), AND FUNCTION.
RC   STRAIN=Oregon-R;
RX   PubMed=7929140;
RA   Currie P.D., Sullivan D.T.;
RT   "Structure and expression of the gene encoding phosphofructokinase
RT   (PFK) in Drosophila melanogaster.";
RL   J. Biol. Chem. 269:24679-24687(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA   Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E.,
RA   Stapleton M., Harvey D.A.;
RT   "A Drosophila complementary DNA resource.";
RL   Science 287:2222-2224(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-788 (ISOFORM C).
RC   STRAIN=Berkeley; TISSUE=Testis;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=2935142; DOI=10.1007/BF00499933;
RA   Munneke L.R., Collier G.E.;
RT   "Genetic and biochemical characterization of phosphofructokinase from
RT   Drosophila melanogaster.";
RL   Biochem. Genet. 23:847-857(1985).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184,
CC       ECO:0000269|PubMed:2935142, ECO:0000269|PubMed:7929140}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=B;
CC         IsoId=P52034-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=P52034-2; Sequence=VSP_014950;
CC         Note=No experimental confirmation available.;
CC       Name=C;
CC         IsoId=P52034-3; Sequence=VSP_014951;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Nearly 90% of the PFK activity in adults is
CC       localized to the thorax. {ECO:0000269|PubMed:2935142}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN71109.1; Type=Frameshift; Positions=218; Evidence={ECO:0000305};
DR   EMBL; L27653; AAA62385.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF58840.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF58841.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM71065.2; -; Genomic_DNA.
DR   EMBL; AF145673; AAD38648.1; -; mRNA.
DR   EMBL; BT001354; AAN71109.1; ALT_FRAME; mRNA.
DR   PIR; A55034; A55034.
DR   RefSeq; NP_523676.1; NM_078952.3. [P52034-2]
DR   RefSeq; NP_724890.1; NM_165746.3. [P52034-1]
DR   RefSeq; NP_724891.2; NM_165747.4. [P52034-3]
DR   UniGene; Dm.7095; -.
DR   ProteinModelPortal; P52034; -.
DR   SMR; P52034; -.
DR   BioGrid; 61888; 4.
DR   IntAct; P52034; 2.
DR   MINT; P52034; -.
DR   STRING; 7227.FBpp0087506; -.
DR   PaxDb; P52034; -.
DR   PRIDE; P52034; -.
DR   EnsemblMetazoa; FBtr0088420; FBpp0087506; FBgn0003071. [P52034-2]
DR   EnsemblMetazoa; FBtr0088421; FBpp0087507; FBgn0003071. [P52034-3]
DR   EnsemblMetazoa; FBtr0088422; FBpp0087508; FBgn0003071. [P52034-1]
DR   GeneID; 36060; -.
DR   KEGG; dme:Dmel_CG4001; -.
DR   UCSC; CG4001-RA; d. melanogaster. [P52034-1]
DR   CTD; 36060; -.
DR   FlyBase; FBgn0003071; Pfk.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   GeneTree; ENSGT00940000171778; -.
DR   HOGENOM; HOG000148827; -.
DR   InParanoid; P52034; -.
DR   KO; K00850; -.
DR   OMA; KQYDELC; -.
DR   PhylomeDB; P52034; -.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-70171; Glycolysis.
DR   UniPathway; UPA00109; UER00182.
DR   GenomeRNAi; 36060; -.
DR   PRO; PR:P52034; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0003071; Expressed in 35 organ(s), highest expression level in head.
DR   ExpressionAtlas; P52034; baseline and differential.
DR   Genevisible; P52034; DM.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IMP:FlyBase.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
DR   GO; GO:0006096; P:glycolytic process; IMP:FlyBase.
DR   GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
DR   GO; GO:0051259; P:protein complex oligomerization; IBA:GO_Central.
DR   GO; GO:0009744; P:response to sucrose; IMP:FlyBase.
DR   GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 2.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Alternative splicing; ATP-binding;
KW   Complete proteome; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    788       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_0000112031.
FT   NP_BIND      90     91       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     120    123       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        1    392       N-terminal catalytic PFK domain 1.
FT   REGION      166    168       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      210    212       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      300    303       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      393    410       Interdomain linker.
FT   REGION      411    788       C-terminal regulatory PFK domain 2.
FT   REGION      537    541       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      582    584       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      670    673       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    168    168       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       121    121       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      27     27       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     203    203       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     266    266       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     294    294       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     480    480       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     575    575       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     638    638       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     664    664       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     745    745       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   VAR_SEQ       1     15       MNSEINQRFLARGSQ -> MHSIKFRVFTKLKPIFLEINGR
FT                                IPICRHFHGPTTFRLEISNKTPPIRQKLTFPNIGIQCTRSH
FT                                HLCCPRDISGNTLLSVKFNCKRHCIKLRSDSGDQKNDSPGE
FT                                KNIQKDKSAQRCGKPINNLHNGFLNAVNYSEKNAVKKKKSA
FT                                PKRKCGKSVDELRKCLRTMQDVIDFVHPVKPF (in
FT                                isoform A).
FT                                {ECO:0000303|PubMed:10731138}.
FT                                /FTId=VSP_014950.
FT   VAR_SEQ     219    250       LVGGLACEADFIFIPEMPPKVDWPDRLCSQLA -> ISAAI
FT                                ATEADFMFIPEEPVSVNWKDEICVKLH (in isoform
FT                                C). {ECO:0000303|PubMed:12537569}.
FT                                /FTId=VSP_014951.
FT   CONFLICT     68     70       QEA -> RKS (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT     80     92       HRGGTIIGSARCQ -> PFVGWHHPLLRPLP (in Ref.
FT                                1). {ECO:0000305}.
FT   CONFLICT    130    131       FR -> LP (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    160    161       IV -> ML (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    190    199       AIDAISSTAY -> QSKAKVQSPVQPN (in Ref. 1;
FT                                AAA62385). {ECO:0000305}.
FT   CONFLICT    209    212       VMGR -> GQVS (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    228    252       DFIFIPEMPPKVDWPDRLCSQLAQE -> IHIHPNAPGRLG
FT                                QTGSALSWTQ (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    313    313       I -> F (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    322    325       ATLA -> PLWP (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    360    361       VA -> G (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    374    375       KL -> NV (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    455    455       G -> R (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    478    478       T -> S (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    522    526       DNYPQ -> TTTHS (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    590    591       AT -> PP (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    613    613       D -> E (in Ref. 1; AAA62385).
FT                                {ECO:0000305}.
FT   CONFLICT    622    636       ASKMAEGVSRGLILR -> PPRWPRRLPRSNPA (in
FT                                Ref. 1; AAA62385). {ECO:0000305}.
FT   CONFLICT    695    705       WLAAQIKANID -> CWPPRSRRTST (in Ref. 1;
FT                                AAA62385). {ECO:0000305}.
SQ   SEQUENCE   788 AA;  86648 MW;  BE45A03013299B75 CRC64;
     MNSEINQRFL ARGSQKDKGL AVFTSGGDSQ GMNAAVRACV RMAIYLGCKV YFIREGYQGM
     VDGGDCIQEA NWASVSSIIH RGGTIIGSAR CQDFRERQGR LKAANNLIQR GITNLVVIGG
     DGSLTGANLF RQEWSSLLDE LVKNKTITTE QQEKFNVLHI VGLVGSIDND FCGTDMTIGT
     DTALHRIIEA IDAISSTAYS HQRTFIMEVM GRHCGYLALV GGLACEADFI FIPEMPPKVD
     WPDRLCSQLA QERSAGQRLN IVIVAEGAMD REGHPITAED VKKVIDERLK HDARITVLGH
     VQRGGNPSAF DRILACRMGA EATLALMEAT KDSVPVVISL DGNQAVRVPL MECVERTQAV
     AKAMAEKRWA DAVKLRGRSF ERNLETYKML TRLKPPKENF DADGKGIEGY RLAVMHIGAP
     ACGMNAAVRS FVRNAIYRGD VVYGINDGVE GLIAGNVREL GWSDVSGWVG QGGAYLGTKR
     TLPEGKFKEI AARLKEFKIQ GLLIIGGFES YHAAGQIADQ RDNYPQFCIP IVVIPSTISN
     NVPGTEFSLG CDTGLNEITE ICDRIRQSAQ GTKRRVFVIE TMGGYCGYLA TLAGLAGGAD
     AAYIYEEKFS IKDLQQDVYH MASKMAEGVS RGLILRNEKA SENYSTDFIY RLYSEEGKGL
     FTCRMNILGH MQQGGSPTPF DRNMGTKMAA KCVDWLAAQI KANIDANGVV NCKSPDTATL
     LGIVSRQYRF SPLVDLIAET NFDQRIPKKQ WWLRLRPLLR ILAKHDSAYE EEGMYITVEE
     ECDTDAVA
//
DBGET integrated database retrieval system