ID   SYEP_DROME              Reviewed;        1714 AA.
AC   P28668; Q8IGR4; Q8IMX9; Q95TL3; Q9VCF5;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Bifunctional glutamate/proline--tRNA ligase {ECO:0000305|PubMed:1756734};
DE   AltName: Full=Bifunctional aminoacyl-tRNA synthetase;
DE   Includes:
DE     RecName: Full=Glutamate--tRNA ligase {ECO:0000305|PubMed:1756734};
DE              EC=6.1.1.17 {ECO:0000269|PubMed:1756734};
DE     AltName: Full=Glutamyl-tRNA synthetase {ECO:0000303|PubMed:1756734};
DE   Includes:
DE     RecName: Full=Proline--tRNA ligase {ECO:0000305|PubMed:1756734};
DE              EC=6.1.1.15 {ECO:0000269|PubMed:1756734};
DE     AltName: Full=Prolyl-tRNA synthetase;
DE              Short=ProRS;
GN   Name=GluProRS {ECO:0000303|PubMed:9063462,
GN   ECO:0000312|FlyBase:FBgn0005674};
GN   Synonyms=Aats-glupro {ECO:0000312|FlyBase:FBgn0005674};
GN   ORFNames=CG5394 {ECO:0000312|FlyBase:FBgn0005674};
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 [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY,
RP   MOTIF, AND REGION.
RX   PubMed=1756734; DOI=10.1002/j.1460-2075.1991.tb05005.x;
RA   Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M.;
RT   "A component of the multisynthetase complex is a multifunctional aminoacyl-
RT   tRNA synthetase.";
RL   EMBO J. 10:4267-4277(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RC   STRAIN=Oregon-R;
RX   PubMed=9063462; DOI=10.1111/j.1432-1033.1997.00176.x;
RA   Cerini C., Semeriva M., Gratecos D.;
RT   "Evolution of the aminoacyl-tRNA synthetase family and the organization of
RT   the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure
RT   of the gene, control of expression of the two mRNAs, selective advantage of
RT   the multienzyme complex.";
RL   Eur. J. Biochem. 244:176-185(1997).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1110, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Catalyzes the attachment of both L-glutamate and L-proline to
CC       their cognate tRNAs in a two-step reaction where the amino acid is
CC       first activated by ATP to form a covalent intermediate with AMP.
CC       Subsequently, the activated amino acid is transferred to the acceptor
CC       end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-
CC       tRNA(Pro). {ECO:0000269|PubMed:1756734}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.17;
CC         Evidence={ECO:0000269|PubMed:1756734};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23541;
CC         Evidence={ECO:0000305|PubMed:1756734};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC         tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC         COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC         EC=6.1.1.15; Evidence={ECO:0000269|PubMed:1756734};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14306;
CC         Evidence={ECO:0000305|PubMed:1756734};
CC   -!- SUBUNIT: Component of the multisynthetase complex which is comprised of
CC       a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific
CC       isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-
CC       tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43.
CC       {ECO:0000250|UniProtKB:P07814}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P28668-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P28668-2; Sequence=VSP_009609, VSP_009610;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class-I
CC       aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC       aminoacyl-tRNA synthetase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN71400.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M74104; AAA28594.1; -; mRNA.
DR   EMBL; U59923; AAC47469.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF56211.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13964.1; -; Genomic_DNA.
DR   EMBL; AY058703; AAL13932.1; -; mRNA.
DR   EMBL; BT001645; AAN71400.1; ALT_INIT; mRNA.
DR   PIR; S18644; S18644.
DR   RefSeq; NP_524471.2; NM_079747.3. [P28668-1]
DR   RefSeq; NP_732925.1; NM_170103.2. [P28668-2]
DR   AlphaFoldDB; P28668; -.
DR   SMR; P28668; -.
DR   BioGRID; 67770; 47.
DR   IntAct; P28668; 15.
DR   STRING; 7227.FBpp0083898; -.
DR   iPTMnet; P28668; -.
DR   PaxDb; 7227-FBpp0083898; -.
DR   DNASU; 42834; -.
DR   EnsemblMetazoa; FBtr0084511; FBpp0083898; FBgn0005674. [P28668-1]
DR   EnsemblMetazoa; FBtr0084512; FBpp0083899; FBgn0005674. [P28668-2]
DR   GeneID; 42834; -.
DR   KEGG; dme:Dmel_CG5394; -.
DR   AGR; FB:FBgn0005674; -.
DR   CTD; 42834; -.
DR   FlyBase; FBgn0005674; GluProRS.
DR   VEuPathDB; VectorBase:FBgn0005674; -.
DR   eggNOG; KOG1147; Eukaryota.
DR   eggNOG; KOG4163; Eukaryota.
DR   GeneTree; ENSGT00550000074815; -.
DR   HOGENOM; CLU_001882_0_0_1; -.
DR   InParanoid; P28668; -.
DR   OMA; WDPKGNN; -.
DR   OrthoDB; 2733051at2759; -.
DR   PhylomeDB; P28668; -.
DR   BioGRID-ORCS; 42834; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 42834; -.
DR   PRO; PR:P28668; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0005674; Expressed in eye disc (Drosophila) and 24 other cell types or tissues.
DR   ExpressionAtlas; P28668; baseline and differential.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; TAS:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IDA:UniProtKB.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IDA:UniProtKB.
DR   CDD; cd00807; GlnRS_core; 1.
DR   CDD; cd10309; GST_C_GluProRS_N; 1.
DR   CDD; cd00862; ProRS_anticodon_zinc; 1.
DR   CDD; cd00778; ProRS_core_arch_euk; 1.
DR   CDD; cd00936; WEPRS_RNA; 6.
DR   Gene3D; 1.20.1050.130; -; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 6.
DR   HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR   InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR   InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR   InterPro; IPR017449; Pro-tRNA_synth_II.
DR   InterPro; IPR033721; ProRS_core_arch_euk.
DR   InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   InterPro; IPR000738; WHEP-TRS_dom.
DR   NCBIfam; TIGR00463; gltX_arch; 1.
DR   NCBIfam; TIGR00408; proS_fam_I; 1.
DR   PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF00458; WHEP-TRS; 6.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   SMART; SM00991; WHEP-TRS; 6.
DR   SUPFAM; SSF64586; C-terminal domain of ProRS; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 6.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS00762; WHEP_TRS_1; 6.
DR   PROSITE; PS51185; WHEP_TRS_2; 6.
DR   Genevisible; P28668; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW   Magnesium; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
KW   RNA-binding; Zinc.
FT   CHAIN           1..1714
FT                   /note="Bifunctional glutamate/proline--tRNA ligase"
FT                   /id="PRO_0000119741"
FT   DOMAIN          744..800
FT                   /note="WHEP-TRS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT   DOMAIN          816..872
FT                   /note="WHEP-TRS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT   DOMAIN          890..946
FT                   /note="WHEP-TRS 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT   DOMAIN          969..1025
FT                   /note="WHEP-TRS 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT   DOMAIN          1044..1100
FT                   /note="WHEP-TRS 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT   DOMAIN          1118..1174
FT                   /note="WHEP-TRS 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT   REGION          166..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..754
FT                   /note="Glutamate--tRNA ligase"
FT                   /evidence="ECO:0000269|PubMed:1756734"
FT   REGION          718..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          755..1201
FT                   /note="6 X 57 AA approximate repeats"
FT                   /evidence="ECO:0000303|PubMed:1756734"
FT   REGION          791..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          943..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1093..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1168..1210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1714
FT                   /note="Proline--tRNA ligase"
FT                   /evidence="ECO:0000269|PubMed:1756734"
FT   MOTIF           209..220
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000303|PubMed:1756734"
FT   MOTIF           438..442
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000303|PubMed:1756734"
FT   COMPBIAS        734..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1322..1324
FT                   /ligand="L-proline"
FT                   /ligand_id="ChEBI:CHEBI:60039"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1353
FT                   /ligand="L-proline"
FT                   /ligand_id="ChEBI:CHEBI:60039"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1365
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1438
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1438
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1441
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1443
FT                   /ligand="L-proline"
FT                   /ligand_id="ChEBI:CHEBI:60039"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1476
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1648
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1653
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   BINDING         1695
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P07814"
FT   MOD_RES         1110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         1..718
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_009609"
FT   VAR_SEQ         719..732
FT                   /note="TSGLKVNAPDAKAT -> MLNYLACGSLSSTS (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_009610"
FT   CONFLICT        102..106
FT                   /note="DKSIA -> TSPLP (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        233..234
FT                   /note="AF -> VC (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341..345
FT                   /note="KYCVR -> NTACA (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        583
FT                   /note="R -> K (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        692
FT                   /note="A -> L (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        753
FT                   /note="S -> T (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        802
FT                   /note="S -> T (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        873
FT                   /note="T -> P (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        887
FT                   /note="V -> G (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1035
FT                   /note="D -> G (in Ref. 5; AAN71400)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1202
FT                   /note="Missing (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1461
FT                   /note="E -> EK (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1587
FT                   /note="V -> G (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1714 AA;  189412 MW;  3F8CF3DB128765A8 CRC64;
     MSIKLKANLN NPPISGLATA HLINGTVPVE IVWSKEETSL QFPDNRLLVC HSNNDVLRAL
     ARAAPDYKLY GETAIERTQI DHWLSFSLTC EDDISWALSF LDKSIAPVTY LVANKLTIAD
     FALFNEMHSR YEFLAAKGIP QHVQRWYDLI TAQPLIQKVL QSLPEDAKVK RSPQSSKEQT
     PAKTGERKQE GKFVDLPGAE MGKVVVRFPP EASGYLHIGH AKAALLNQYY ALAFQGTLIM
     RFDDTNPAKE TVEFENVILG DLEQLQIKPD VFTHTSNYFD LMLDYCVRLI KESKAYVDDT
     PPEQMKLERE QRVESANRSN SVEKNLSLWE EMVKGSEKGQ KYCVRAKIDM SSPNGCMRDP
     TIYRCKNEPH PRTGTKYKVY PTYDFACPIV DAIENVTHTL RTTEYHDRDD QFYWFIDALK
     LRKPYIWSYS RLNMTNTVLS KRKLTWFVDS GLVDGWDDPR FPTVRGIIRR GMTVEGLKEF
     IIAQGSSKSV VFMNWDKIWA FNKKVIDPIA PRYTALEKEK RVIVNVAGAK VERIQVSVHP
     KDESLGKKTV LLGPRIYIDY VDAEALKEGE NATFINWGNI LIRKVNKDAS GNITSVDAAL
     NLENKDFKKT LKLTWLAVED DPSAYPPTFC VYFDNIISKA VLGKDEDFKQ FIGHKTRDEV
     PMLGDPELKK CKKGDIIQLQ RRGFFKVDVA YAPPSGYTNV PSPIVLFSIP DGHTKDVPTS
     GLKVNAPDAK ATKKASSPVS SSGQASELDS QISQQGDLVR DLKSKKAAKD QIDVAVKKLL
     ALKADYKSAT GKDWKPGQTS ASSAPVPAAS SSSANDAVSV NASIVKQGDL VRDLKGKKAS
     KPEIDAAVKT LLELKAQYKT LTGQDWKPGT VPTTAAPSAS AAPSVGVNDS VAQILSQITA
     QGDKVRELKS AKADKATVDA AVKTLLSLKA DYKAATGSDW KPGTTAPAPA AAPVKVKQEK
     NPDPASVLTV NTLLNKIAQQ GDKIRQLKSA KSEKSLVEAE VKLLLALKTD YKSLTGQEWK
     PGTVAPAPTT VNVIDLTGGD SGSDVGSVLS KIQAQGDKIR KLKSEKAAKN VIDPEVKTLL
     ALKGEYKTLS GKDWTPDAKS EPAVVKKEAS PVSMASPAKD ELTQEINAQG EKVRAAKGNK
     AAKEVIDAEV AKLLALKAKY KEVTGTDFPV AGRGGGGGGG SAKKAPKEAQ PKPAKPVKKE
     PAADASGAVK KQTRLGLEAT KEDNLPDWYS QVITKGEMIE YYDVSGCYIL RQWSFAIWKA
     IKTWFDAEIT RMGVKECYFP IFVSKAVLEK EKTHIADFAP EVAWVTKSGD SDLAEPIAVR
     PTSETVMYPA YAKWVQSYRD LPIRLNQWNN VVRWEFKQPT PFLRTREFLW QEGHTAFADK
     EEAAKEVLDI LDLYALVYTH LLAIPVVKGR KTEKEKFAGG DYTTTVEAFI SASGRAIQGA
     TSHHLGQNFS KMFEIVYEDP ETQQKKYVYQ NSWGITTRTI GVMIMVHADN QGLVLPPHVA
     CIQAIVVPCG ITVNTKDDER AQLLDACKAL EKRLVGGGVR CEGDYRDNYS PGWKFNHWEL
     KGVPLRLEVG PKDLKAQQLV AVRRDTVEKI TIPLADVEKK IPALLETIHE SMLNKAQEDM
     TSHTKKVTNW TDFCGFLEQK NILLAPFCGE ISCEDKIKAD SARGEEAEPG APAMGAKSLC
     IPFDQPAPIA ASDKCINPSC TNKPKFYTLF GRSY
//