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   27-MAR-2024, entry version 170.
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; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   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; DOI=10.1016/s0021-9258(17)31444-8;
RA   Currie P.D., Sullivan D.T.;
RT   "Structure and expression of the gene encoding phosphofructokinase (PFK) in
RT   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., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., 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., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., 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., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   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., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   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., Stapleton M.,
RA   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., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   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 to
CC       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 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03184};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC       2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC       {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       Name=C;
CC         IsoId=P52034-3; Sequence=VSP_014951;
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) family.
CC       ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC       sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN71109.1; Type=Frameshift; Evidence={ECO:0000305};
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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   AlphaFoldDB; P52034; -.
DR   SMR; P52034; -.
DR   BioGRID; 61888; 4.
DR   IntAct; P52034; 3.
DR   MINT; P52034; -.
DR   STRING; 7227.FBpp0087506; -.
DR   PaxDb; 7227-FBpp0087506; -.
DR   DNASU; 36060; -.
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   AGR; FB:FBgn0003071; -.
DR   CTD; 36060; -.
DR   FlyBase; FBgn0003071; Pfk.
DR   VEuPathDB; VectorBase:FBgn0003071; -.
DR   eggNOG; KOG2440; Eukaryota.
DR   GeneTree; ENSGT00940000171778; -.
DR   HOGENOM; CLU_011053_1_0_1; -.
DR   InParanoid; P52034; -.
DR   OMA; EWQDQMC; -.
DR   PhylomeDB; P52034; -.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-70171; Glycolysis.
DR   SignaLink; P52034; -.
DR   UniPathway; UPA00109; UER00182.
DR   BioGRID-ORCS; 36060; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 36060; -.
DR   PRO; PR:P52034; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0003071; Expressed in adult hindgut (Drosophila) and 29 other cell types or tissues.
DR   ExpressionAtlas; P52034; baseline and differential.
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:0042593; P:glucose homeostasis; IMP:FlyBase.
DR   GO; GO:0006096; P:glycolytic process; IMP:FlyBase.
DR   GO; GO:0009744; P:response to sucrose; IMP:FlyBase.
DR   Gene3D; 3.40.50.450; -; 2.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
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   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
DR   Genevisible; P52034; DM.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Alternative splicing; ATP-binding; Cytoplasm;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..788
FT                   /note="ATP-dependent 6-phosphofructokinase"
FT                   /id="PRO_0000112031"
FT   REGION          1..392
FT                   /note="N-terminal catalytic PFK domain 1"
FT   REGION          393..410
FT                   /note="Interdomain linker"
FT   REGION          411..788
FT                   /note="C-terminal regulatory PFK domain 2"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         90..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         120..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         166..168
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         210..212
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         300..303
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         480
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         537..541
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         575
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         582..584
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         638
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         664
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         670..673
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         745
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   VAR_SEQ         1..15
FT                   /note="MNSEINQRFLARGSQ -> MHSIKFRVFTKLKPIFLEINGRIPICRHFHGPT
FT                   TFRLEISNKTPPIRQKLTFPNIGIQCTRSHHLCCPRDISGNTLLSVKFNCKRHCIKLRS
FT                   DSGDQKNDSPGEKNIQKDKSAQRCGKPINNLHNGFLNAVNYSEKNAVKKKKSAPKRKCG
FT                   KSVDELRKCLRTMQDVIDFVHPVKPF (in isoform A)"
FT                   /evidence="ECO:0000303|PubMed:10731138"
FT                   /id="VSP_014950"
FT   VAR_SEQ         219..250
FT                   /note="LVGGLACEADFIFIPEMPPKVDWPDRLCSQLA -> ISAAIATEADFMFIPE
FT                   EPVSVNWKDEICVKLH (in isoform C)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_014951"
FT   CONFLICT        68..70
FT                   /note="QEA -> RKS (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80..92
FT                   /note="HRGGTIIGSARCQ -> PFVGWHHPLLRPLP (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130..131
FT                   /note="FR -> LP (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        160..161
FT                   /note="IV -> ML (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190..199
FT                   /note="AIDAISSTAY -> QSKAKVQSPVQPN (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209..212
FT                   /note="VMGR -> GQVS (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        228..252
FT                   /note="DFIFIPEMPPKVDWPDRLCSQLAQE -> IHIHPNAPGRLGQTGSALSWTQ
FT                   (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        313
FT                   /note="I -> F (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322..325
FT                   /note="ATLA -> PLWP (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360..361
FT                   /note="VA -> G (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374..375
FT                   /note="KL -> NV (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="G -> R (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        478
FT                   /note="T -> S (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        522..526
FT                   /note="DNYPQ -> TTTHS (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        590..591
FT                   /note="AT -> PP (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        613
FT                   /note="D -> E (in Ref. 1; AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        622..636
FT                   /note="ASKMAEGVSRGLILR -> PPRWPRRLPRSNPA (in Ref. 1;
FT                   AAA62385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        695..705
FT                   /note="WLAAQIKANID -> CWPPRSRRTST (in Ref. 1; AAA62385)"
FT                   /evidence="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
//