SYEP_DROME
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 03-AUG-2022, entry version 185.
DE RecName: Full=Bifunctional glutamate/proline--tRNA ligase;
DE AltName: Full=Bifunctional aminoacyl-tRNA synthetase;
DE Includes:
DE RecName: Full=Glutamate--tRNA ligase;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000303|PubMed:1756734};
DE Includes:
DE RecName: Full=Proline--tRNA ligase;
DE EC=6.1.1.15 {ECO:0000250|UniProtKB:P07814};
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).
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 the cognate amino acid to the
CC corresponding tRNA in a two-step reaction: the amino acid is first
CC activated by ATP to form a covalent intermediate with AMP and is then
CC transferred to the acceptor end of the cognate tRNA.
CC {ECO:0000250|UniProtKB:P07814}.
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 -!- 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:0000250|UniProtKB:P07814};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; P28668; -.
DR PRIDE; P28668; -.
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 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 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 tissues.
DR ExpressionAtlas; P28668; baseline and differential.
DR Genevisible; P28668; DM.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; TAS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; TAS:FlyBase.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 1.10.1160.10; -; 1.
DR Gene3D; 2.40.240.10; -; 1.
DR Gene3D; 3.30.110.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
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_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR PANTHER; PTHR43382; PTHR43382; 3.
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; 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; SSF47060; SSF47060; 6.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50715; SSF50715; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF64586; SSF64586; 1.
DR TIGRFAMs; TIGR00463; gltX_arch; 1.
DR TIGRFAMs; TIGR00408; proS_fam_I; 1.
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.
PE 1: Evidence at protein level;
KW Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; 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 DOMAIN 816..872
FT /note="WHEP-TRS 2"
FT DOMAIN 890..946
FT /note="WHEP-TRS 3"
FT DOMAIN 969..1025
FT /note="WHEP-TRS 4"
FT DOMAIN 1044..1100
FT /note="WHEP-TRS 5"
FT DOMAIN 1118..1174
FT /note="WHEP-TRS 6"
FT REGION 166..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..754
FT /note="Glutamate--tRNA ligase"
FT REGION 718..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 MOTIF 209..220
FT /note="'HIGH' region"
FT MOTIF 438..442
FT /note="'KMSKS' region"
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 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 438..442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1322..1324
FT /ligand="L-proline"
FT /ligand_id="ChEBI:CHEBI:60039"
FT /evidence="ECO:0000250|UniProtKB:P07814"
FT BINDING 1353..1355
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 1364..1365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07814"
FT BINDING 1438..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 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
