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Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)]

 SYEP_HUMAN              Reviewed;        1512 AA.
P07814; A0AVA9; B9EGH3; Q05BP6; Q05DF8; Q5DSM1; Q5H9S5; Q6PD57;
Q86X73;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 5.
22-NOV-2017, entry version 209.
RecName: Full=Bifunctional glutamate/proline--tRNA ligase;
AltName: Full=Bifunctional aminoacyl-tRNA synthetase;
AltName: Full=Cell proliferation-inducing gene 32 protein;
AltName: Full=Glutamatyl-prolyl-tRNA synthetase;
Includes:
RecName: Full=Glutamate--tRNA ligase;
EC=6.1.1.17;
AltName: Full=Glutamyl-tRNA synthetase;
Short=GluRS;
Includes:
RecName: Full=Proline--tRNA ligase;
EC=6.1.1.15 {ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331};
AltName: Full=Prolyl-tRNA synthetase;
Name=EPRS; Synonyms=GLNS, PARS, QARS, QPRS; ORFNames=PIG32;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-308 AND
VAL-1043.
TISSUE=Bone marrow;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-308.
TISSUE=Brain, Duodenum, Eye, Lung, Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 54-1512, AND VARIANTS GLU-308 AND
HIS-334.
PubMed=1988429;
Fett R., Knippers R.;
"The primary structure of human glutaminyl-tRNA synthetase. A highly
conserved core, amino acid repeat regions, and homologies with
translation elongation factors.";
J. Biol. Chem. 266:1448-1455(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-1512, AND VARIANTS
GLU-308 AND HIS-334.
Kim J.W.;
"Identification of a proliferation inducing gene.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[6]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 168-959, AND VARIANTS
GLU-308 AND HIS-334.
TISSUE=Cervix carcinoma;
PubMed=3290852; DOI=10.1093/nar/16.12.5391;
Thoemmes P., Fett R., Schray B., Kunze N., Knippers R.;
"The core region of human glutaminyl-tRNA synthetase homologies with
the Escherichia coli and yeast enzymes.";
Nucleic Acids Res. 16:5391-5406(1988).
[7]
FUNCTION.
PubMed=1756734;
Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M.;
"A component of the multisynthetase complex is a multifunctional
aminoacyl-tRNA synthetase.";
EMBO J. 10:4267-4277(1991).
[8]
GENE STRUCTURE.
PubMed=1556743; DOI=10.1007/BF00163851;
Kaiser E., Eberhard D., Knippers R.;
"Exons encoding the highly conserved part of human glutaminyl-tRNA
synthetase.";
J. Mol. Evol. 34:45-53(1992).
[9]
FUNCTION, AND IDENTIFICATION IN THE GAIT COMPLEX.
PubMed=15479637; DOI=10.1016/j.cell.2004.09.030;
Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L.,
Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
"Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-
specific silencing of translation.";
Cell 119:195-208(2004).
[10]
INTERACTION WITH DUS2L.
PubMed=15994936; DOI=10.1158/0008-5472.CAN-05-0600;
Kato T., Daigo Y., Hayama S., Ishikawa N., Yamabuki T., Ito T.,
Miyamoto M., Kondo S., Nakamura Y.;
"A novel human tRNA-dihydrouridine synthase involved in pulmonary
carcinogenesis.";
Cancer Res. 65:5638-5646(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-898, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-872; SER-882; SER-885;
SER-886 AND THR-898, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19131329; DOI=10.1074/jbc.M809636200;
Kaminska M., Havrylenko S., Decottignies P., Gillet S.,
Le Marechal P., Negrutskii B., Mirande M.;
"Dissection of the structural organization of the aminoacyl-tRNA
synthetase complex.";
J. Biol. Chem. 284:6053-6060(2009).
[18]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=19289464; DOI=10.1074/jbc.M900480200;
Kaminska M., Havrylenko S., Decottignies P., Le Marechal P.,
Negrutskii B., Mirande M.;
"Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the
Cytoplasm of Human Cells.";
J. Biol. Chem. 284:13746-13754(2009).
[19]
PHOSPHORYLATION AT SER-886 AND SER-999, AND INTERACTION WITH SYNCRIP.
PubMed=19647514; DOI=10.1016/j.molcel.2009.05.028;
Arif A., Jia J., Mukhopadhyay R., Willard B., Kinter M., Fox P.L.;
"Two-site phosphorylation of EPRS coordinates multimodal regulation of
noncanonical translational control activity.";
Mol. Cell 35:164-180(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-886 AND
SER-891, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-300; LYS-417; LYS-498;
LYS-535; LYS-542; LYS-637; LYS-788 AND LYS-1503, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
MALONYLATION AT LYS-300.
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[25]
PHOSPHORYLATION AT SER-886.
PubMed=21220307; DOI=10.1073/pnas.1011275108;
Arif A., Jia J., Moodt R.A., DiCorleto P.E., Fox P.L.;
"Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-
dependent kinase 5 dictates transcript-selective translational
control.";
Proc. Natl. Acad. Sci. U.S.A. 108:1415-1420(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
FUNCTION, RECONSTITUTION OF THE GAIT COMPLEX, AND MUTAGENESIS OF
SER-886 AND SER-999.
PubMed=23071094; DOI=10.1128/MCB.01168-12;
Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
"Heterotrimeric GAIT complex drives transcript-selective translation
inhibition in murine macrophages.";
Mol. Cell. Biol. 32:5046-5055(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-355; SER-434; SER-747;
SER-882; SER-886; THR-898; SER-998 AND SER-1350, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1152, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
STRUCTURE BY NMR OF 749-805, AND RNA-BINDING.
PubMed=11123902; DOI=10.1021/bi001393h;
Jeong E.-J., Hwang G.-S., Kim K.H., Kim M.J., Kim S., Kim K.-S.;
"Structural analysis of multifunctional peptide motifs in human
bifunctional tRNA synthetase: identification of RNA-binding residues
and functional implications for tandem repeats.";
Biochemistry 39:15775-15782(2000).
[33] {ECO:0000244|PDB:4K86, ECO:0000244|PDB:4K87, ECO:0000244|PDB:4K88}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1000-1512 IN COMPLEXES WITH
SYNTHETIC INHIBITOR HALOFUGINONE; L-PROLINE; ZINC AND ADENOSINE,
CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND MUTAGENESIS OF PHE-1097 AND
ARG-1152.
PubMed=24100331; DOI=10.1107/S0907444913020556;
Son J., Lee E.H., Park M., Kim J.H., Kim J., Kim S., Jeon Y.H.,
Hwang K.Y.;
"Conformational changes in human prolyl-tRNA synthetase upon binding
of the substrates proline and ATP and the inhibitor halofuginone.";
Acta Crystallogr. D 69:2136-2145(2013).
[34] {ECO:0000244|PDB:4HVC}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1003-1512 IN COMPLEX WITH
SYNTHETIC INHIBITOR; ZINC AND ATP ANALOG, CATALYTIC ACTIVITY,
FUNCTION, AND SUBUNIT.
PubMed=23263184; DOI=10.1038/nature11774;
Zhou H., Sun L., Yang X.L., Schimmel P.;
"ATP-directed capture of bioactive herbal-based medicine on human tRNA
synthetase.";
Nature 494:121-124(2013).
[35] {ECO:0000244|PDB:5A34, ECO:0000244|PDB:5BMU}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-175, AND SUBUNIT.
PubMed=26472928; DOI=10.1074/JBC.M115.690867;
Cho H.Y., Maeng S.J., Cho H.J., Choi Y.S., Chung J.M., Lee S.,
Kim H.K., Kim J.H., Eom C.Y., Kim Y.G., Guo M., Jung H.S., Kang B.S.,
Kim S.;
"Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric
Glutathione Transferase-homology Domains.";
J. Biol. Chem. 290:29313-29328(2015).
-!- FUNCTION: Catalyzes the attachment of the cognate amino acid to
the corresponding tRNA in a two-step reaction: the amino acid is
first activated by ATP to form a covalent intermediate with AMP
and is then transferred to the acceptor end of the cognate tRNA
(PubMed:1756734, PubMed:24100331, PubMed:23263184). Component of
the GAIT (gamma interferon-activated inhibitor of translation)
complex which mediates interferon-gamma-induced transcript-
selective translation inhibition in inflammation processes. Upon
interferon-gamma activation and subsequent phosphorylation
dissociates from the multisynthetase complex and assembles into
the GAIT complex which binds to stem loop-containing GAIT elements
in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin)
and suppresses their translation. {ECO:0000269|PubMed:15479637,
ECO:0000269|PubMed:1756734, ECO:0000269|PubMed:23071094,
ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331}.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
diphosphate + L-glutamyl-tRNA(Glu).
-!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
diphosphate + L-prolyl-tRNA(Pro). {ECO:0000269|PubMed:23263184,
ECO:0000269|PubMed:24100331}.
-!- ENZYME REGULATION: Inhibited by halofuginone.
{ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331}.
-!- SUBUNIT: Homodimer (PubMed:24100331, PubMed:23263184). Part of a
multisubunit complex that groups tRNA ligases for Arg (RARS), Asp
(DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS)
the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary
subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:19131329,
PubMed:19289464). Forms a linear complex that contains MARS,
EEF1E1, EPRS and AIMP2 that is at the core of the multisubunit
complex (PubMed:26472928). Interacts with DUS2L (PubMed:15994936).
Component of the GAIT complex; in humans the complex assembly
seems to be a two-step process in which EPRS first associates with
SYNCRIP to form a pre-GAIT complex which is deficient in GAIT
element binding (PubMed:15479637). {ECO:0000269|PubMed:15479637,
ECO:0000269|PubMed:15994936, ECO:0000269|PubMed:19131329,
ECO:0000269|PubMed:19289464, ECO:0000269|PubMed:19647514,
ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331,
ECO:0000269|PubMed:26472928}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-355315, EBI-355315;
Q8IWL3:HSCB; NbExp=4; IntAct=EBI-355315, EBI-1805738;
P41252:IARS; NbExp=5; IntAct=EBI-355315, EBI-355303;
Q15046:KARS; NbExp=4; IntAct=EBI-355315, EBI-356367;
O60506:SYNCRIP; NbExp=3; IntAct=EBI-355315, EBI-1024357;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:19289464}.
-!- DOMAIN: The WHEP-TRS domain is involved in RNA binding.
-!- PTM: Phosphorylated at Ser-886 by CDK5 and at Ser-999 by an
unknown kinase in a IFN-gamma-dependent manner in monocytes; these
sequential phosphorylations are causing release from the
multisynthetase complex, association with the GAIT complex and
subsequent involvement in transcript-selective translation
inhibition. Phosphorylation at Ser-999 is specifically required
for the interaction of GAIT complex-associated RPL13A with eIF4G.
{ECO:0000269|PubMed:19647514, ECO:0000269|PubMed:21220307}.
-!- SIMILARITY: In the N-terminal section; belongs to the class-I
aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2
subfamily. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the class-II
aminoacyl-tRNA synthetase family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be a glutaminyl-tRNA
synthetase. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH15494.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH34797.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH46156.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH58921.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAS72877.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA30354.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
Sequence=CAA38224.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; CR933648; CAI45949.1; -; mRNA.
EMBL; AC103590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015494; AAH15494.1; ALT_SEQ; mRNA.
EMBL; BC034797; AAH34797.1; ALT_SEQ; mRNA.
EMBL; BC046156; AAH46156.1; ALT_SEQ; mRNA.
EMBL; BC058921; AAH58921.1; ALT_SEQ; mRNA.
EMBL; BC126275; AAI26276.1; -; mRNA.
EMBL; BC136465; AAI36466.1; -; mRNA.
EMBL; X54326; CAA38224.1; ALT_INIT; mRNA.
EMBL; AY493416; AAS72877.1; ALT_INIT; mRNA.
EMBL; X07466; CAA30354.1; ALT_SEQ; mRNA.
CCDS; CCDS31027.1; -.
PIR; A38663; SYHUQT.
RefSeq; NP_004437.2; NM_004446.2.
UniGene; Hs.497788; -.
PDB; 1FYJ; NMR; -; A=749-805.
PDB; 4HVC; X-ray; 2.00 A; A/B=1003-1512.
PDB; 4K86; X-ray; 2.40 A; A=1000-1512.
PDB; 4K87; X-ray; 2.30 A; A=1000-1512.
PDB; 4K88; X-ray; 2.62 A; A=1000-1512.
PDB; 5A1N; X-ray; 2.10 A; A=1-175.
PDB; 5A34; X-ray; 2.60 A; A/C/E/G=1-175.
PDB; 5A5H; X-ray; 2.32 A; A/C/E/G=1-175.
PDB; 5BMU; X-ray; 2.60 A; B/D/F/H=1-175.
PDB; 5VAD; X-ray; 2.36 A; A/B=998-1512.
PDBsum; 1FYJ; -.
PDBsum; 4HVC; -.
PDBsum; 4K86; -.
PDBsum; 4K87; -.
PDBsum; 4K88; -.
PDBsum; 5A1N; -.
PDBsum; 5A34; -.
PDBsum; 5A5H; -.
PDBsum; 5BMU; -.
PDBsum; 5VAD; -.
ProteinModelPortal; P07814; -.
SMR; P07814; -.
BioGrid; 108372; 114.
CORUM; P07814; -.
DIP; DIP-40825N; -.
IntAct; P07814; 37.
MINT; MINT-141120; -.
STRING; 9606.ENSP00000355890; -.
BindingDB; P07814; -.
ChEMBL; CHEMBL3873; -.
DrugBank; DB03376; '5'-O-(N-(L-Alanyl)-Sulfamoyl)Adenosine.
DrugBank; DB02510; '5'-O-(N-(L-Prolyl)-Sulfamoyl)Adenosine.
DrugBank; DB02684; 5'-O-(N-(L-Cysteinyl)-Sulfamoyl)Adenosine.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB00172; L-Proline.
iPTMnet; P07814; -.
PhosphoSitePlus; P07814; -.
SwissPalm; P07814; -.
BioMuta; EPRS; -.
DMDM; 288558855; -.
EPD; P07814; -.
MaxQB; P07814; -.
PaxDb; P07814; -.
PeptideAtlas; P07814; -.
PRIDE; P07814; -.
Ensembl; ENST00000366923; ENSP00000355890; ENSG00000136628.
GeneID; 2058; -.
KEGG; hsa:2058; -.
UCSC; uc001hly.2; human.
CTD; 2058; -.
DisGeNET; 2058; -.
EuPathDB; HostDB:ENSG00000136628.17; -.
GeneCards; EPRS; -.
HGNC; HGNC:3418; EPRS.
HPA; HPA026490; -.
HPA; HPA030052; -.
MIM; 138295; gene.
neXtProt; NX_P07814; -.
OpenTargets; ENSG00000136628; -.
PharmGKB; PA27837; -.
eggNOG; KOG1147; Eukaryota.
eggNOG; KOG4163; Eukaryota.
eggNOG; COG0008; LUCA.
eggNOG; COG0442; LUCA.
GeneTree; ENSGT00550000074815; -.
HOVERGEN; HBG017875; -.
InParanoid; P07814; -.
KO; K14163; -.
OMA; VAMLHIK; -.
OrthoDB; EOG091G04TK; -.
PhylomeDB; P07814; -.
TreeFam; TF300380; -.
BRENDA; 6.1.1.15; 2681.
Reactome; R-HSA-2408517; SeMet incorporation into proteins.
Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
SIGNOR; P07814; -.
EvolutionaryTrace; P07814; -.
GeneWiki; EPRS; -.
GenomeRNAi; 2058; -.
PRO; PR:P07814; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000136628; -.
CleanEx; HS_EPRS; -.
CleanEx; HS_QARS; -.
ExpressionAtlas; P07814; baseline and differential.
Genevisible; P07814; HS.
GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004827; F:proline-tRNA ligase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IBA:GO_Central.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0006433; P:prolyl-tRNA aminoacylation; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
CDD; cd00778; ProRS_core_arch_euk; 1.
Gene3D; 1.10.1160.10; -; 1.
Gene3D; 1.10.287.10; -; 3.
Gene3D; 2.40.240.10; -; 2.
Gene3D; 3.30.110.30; -; 1.
Gene3D; 3.40.50.620; -; 2.
Gene3D; 3.40.50.800; -; 1.
HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR001412; aa-tRNA-synth_I_CS.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004154; Anticodon-bd.
InterPro; IPR036621; Anticodon-bd_dom_sf.
InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
InterPro; IPR000924; Glu/Gln-tRNA-synth.
InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004046; GST_C.
InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
InterPro; IPR016061; Pro-tRNA_ligase_II_C.
InterPro; IPR017449; Pro-tRNA_synth_II.
InterPro; IPR033721; ProRS_core_arch_euk.
InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR009068; S15_NS1_RNA-bd.
InterPro; IPR000738; WHEP-TRS_dom.
Pfam; PF00043; GST_C; 1.
Pfam; PF03129; HGTP_anticodon; 1.
Pfam; PF09180; ProRS-C_1; 1.
Pfam; PF00749; tRNA-synt_1c; 1.
Pfam; PF03950; tRNA-synt_1c_C; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
Pfam; PF00458; WHEP-TRS; 3.
PRINTS; PR00987; TRNASYNTHGLU.
SMART; SM00946; ProRS-C_1; 1.
SMART; SM00991; WHEP-TRS; 3.
SUPFAM; SSF47060; SSF47060; 3.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF50715; SSF50715; 1.
SUPFAM; SSF52954; SSF52954; 1.
SUPFAM; SSF64586; SSF64586; 1.
TIGRFAMs; TIGR00463; gltX_arch; 1.
TIGRFAMs; TIGR00408; proS_fam_I; 1.
PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE; PS00762; WHEP_TRS_1; 3.
PROSITE; PS51185; WHEP_TRS_2; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
Complete proteome; Cytoplasm; Ligase; Metal-binding; Methylation;
Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Polymorphism; Protein biosynthesis; Reference proteome; Repeat;
RNA-binding; Translation regulation; Zinc.
CHAIN 1 1512 Bifunctional glutamate/proline--tRNA
ligase.
/FTId=PRO_0000119743.
DOMAIN 749 805 WHEP-TRS 1.
DOMAIN 822 878 WHEP-TRS 2.
DOMAIN 900 956 WHEP-TRS 3.
NP_BIND 432 436 ATP. {ECO:0000250}.
NP_BIND 1152 1154 ATP. {ECO:0000244|PDB:4HVC,
ECO:0000244|PDB:4K87,
ECO:0000269|PubMed:23263184,
ECO:0000269|PubMed:24100331}.
NP_BIND 1163 1164 ATP. {ECO:0000244|PDB:4HVC,
ECO:0000244|PDB:4K87,
ECO:0000269|PubMed:23263184,
ECO:0000269|PubMed:24100331}.
NP_BIND 1237 1240 ATP. {ECO:0000244|PDB:4HVC,
ECO:0000244|PDB:4K87,
ECO:0000269|PubMed:23263184,
ECO:0000269|PubMed:24100331}.
REGION 164 759 Glutamate--tRNA ligase.
REGION 760 956 3 X 57 AA approximate repeats.
REGION 959 991 Charged.
REGION 1007 1512 Proline--tRNA ligase.
REGION 1121 1123 L-proline binding. {ECO:0000244|PDB:4K87,
ECO:0000269|PubMed:24100331}.
MOTIF 204 214 "HIGH" region.
MOTIF 432 436 "KMSKS" region.
METAL 1448 1448 Zinc. {ECO:0000244|PDB:4HVC,
ECO:0000244|PDB:4K86,
ECO:0000244|PDB:4K87,
ECO:0000269|PubMed:23263184,
ECO:0000269|PubMed:24100331}.
METAL 1453 1453 Zinc. {ECO:0000244|PDB:4HVC,
ECO:0000244|PDB:4K86,
ECO:0000244|PDB:4K87,
ECO:0000244|PDB:4K88,
ECO:0000269|PubMed:23263184,
ECO:0000269|PubMed:24100331}.
METAL 1495 1495 Zinc. {ECO:0000244|PDB:4HVC,
ECO:0000244|PDB:4K86,
ECO:0000244|PDB:4K87,
ECO:0000244|PDB:4K88,
ECO:0000269|PubMed:23263184,
ECO:0000269|PubMed:24100331}.
METAL 1497 1497 Zinc. {ECO:0000244|PDB:4HVC,
ECO:0000244|PDB:4K86,
ECO:0000244|PDB:4K87,
ECO:0000244|PDB:4K88,
ECO:0000269|PubMed:23263184,
ECO:0000269|PubMed:24100331}.
BINDING 211 211 ATP. {ECO:0000250}.
BINDING 398 398 ATP. {ECO:0000250}.
BINDING 1152 1152 L-proline. {ECO:0000244|PDB:4K87,
ECO:0000269|PubMed:24100331}.
BINDING 1242 1242 L-proline. {ECO:0000244|PDB:4K87,
ECO:0000269|PubMed:24100331}.
BINDING 1276 1276 ATP. {ECO:0000244|PDB:4HVC,
ECO:0000244|PDB:4K87,
ECO:0000269|PubMed:23263184,
ECO:0000269|PubMed:24100331}.
MOD_RES 300 300 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 300 300 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:21908771}.
MOD_RES 355 355 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 417 417 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 498 498 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 535 535 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 542 542 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 637 637 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 788 788 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 861 861 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8CGC7}.
MOD_RES 872 872 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 885 885 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 886 886 Phosphoserine; by CDK5.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19647514,
ECO:0000269|PubMed:21220307}.
MOD_RES 891 891 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 898 898 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 998 998 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 999 999 Phosphoserine.
{ECO:0000269|PubMed:19647514}.
MOD_RES 1000 1000 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1152 1152 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1350 1350 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1503 1503 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 296 296 A -> P (in dbSNP:rs35999099).
/FTId=VAR_037288.
VARIANT 308 308 D -> E (in dbSNP:rs2230301).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:1988429,
ECO:0000269|PubMed:3290852,
ECO:0000269|Ref.5}.
/FTId=VAR_037289.
VARIANT 334 334 Q -> H (in dbSNP:rs1063236).
{ECO:0000269|PubMed:1988429,
ECO:0000269|PubMed:3290852,
ECO:0000269|Ref.5}.
/FTId=VAR_037290.
VARIANT 893 893 P -> H (in dbSNP:rs5030751).
/FTId=VAR_037291.
VARIANT 913 913 E -> G (in dbSNP:rs2230302).
/FTId=VAR_057358.
VARIANT 1043 1043 I -> V (in dbSNP:rs5030752).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_037292.
VARIANT 1107 1107 S -> F (in dbSNP:rs12144752).
/FTId=VAR_037293.
VARIANT 1399 1399 T -> N (in dbSNP:rs34559775).
/FTId=VAR_037294.
MUTAGEN 886 886 S->A: Abolishes release from
multisynthetase complex and association
with GAIT complex assembly upon
interferon-gamma treatment. Abolishes
interaction with SYNCRIP.
{ECO:0000269|PubMed:23071094}.
MUTAGEN 886 886 S->D: Not active in translation
inhibition (phosphomimetic) and abolishes
GAIT complex association with eiF4G. No
effect on interaction with SYNCRIP.
{ECO:0000269|PubMed:23071094}.
MUTAGEN 999 999 S->A: Not active in translation
inhibition, and abolishes release from
multisynthetase complex and association
with GAIT complex assembly upon
interferon-gamma treatment.
{ECO:0000269|PubMed:23071094}.
MUTAGEN 999 999 S->D: Active in translation inhibition
(phosphomimetic). No effect on GAIT
complex association with eiF4G.
{ECO:0000269|PubMed:23071094}.
MUTAGEN 1097 1097 F->A: Almost complete loss of prolyl-tRNA
ligase activity.
{ECO:0000269|PubMed:24100331}.
MUTAGEN 1097 1097 F->W: No effect on prolyl-tRNA ligase
activity. Decreases inhibition by
halofuginone.
{ECO:0000269|PubMed:24100331}.
MUTAGEN 1152 1152 R->K: No effect on prolyl-tRNA ligase
activity. Decreases inhibition by
halofuginone.
{ECO:0000269|PubMed:24100331}.
MUTAGEN 1152 1152 R->L: Almost complete loss of prolyl-tRNA
ligase activity.
{ECO:0000269|PubMed:24100331}.
CONFLICT 532 532 K -> R (in Ref. 1; CAI45949).
{ECO:0000305}.
CONFLICT 594 594 L -> F (in Ref. 4; CAA38224 and 5;
AAS72877). {ECO:0000305}.
CONFLICT 943 943 K -> E (in Ref. 1; CAI45949).
{ECO:0000305}.
CONFLICT 1177 1179 ATM -> VTV (in Ref. 1; CAI45949).
{ECO:0000305}.
CONFLICT 1441 1441 K -> R (in Ref. 1; CAI45949).
{ECO:0000305}.
STRAND 4 7 {ECO:0000244|PDB:5A1N}.
STRAND 10 12 {ECO:0000244|PDB:5A34}.
HELIX 15 24 {ECO:0000244|PDB:5A1N}.
TURN 25 27 {ECO:0000244|PDB:5A1N}.
STRAND 30 33 {ECO:0000244|PDB:5A1N}.
STRAND 39 43 {ECO:0000244|PDB:5A1N}.
STRAND 46 48 {ECO:0000244|PDB:5A1N}.
HELIX 51 61 {ECO:0000244|PDB:5A1N}.
HELIX 63 65 {ECO:0000244|PDB:5A1N}.
HELIX 72 87 {ECO:0000244|PDB:5A1N}.
TURN 88 90 {ECO:0000244|PDB:5A1N}.
HELIX 95 106 {ECO:0000244|PDB:5A1N}.
STRAND 110 113 {ECO:0000244|PDB:5A1N}.
STRAND 114 116 {ECO:0000244|PDB:5BMU}.
HELIX 119 129 {ECO:0000244|PDB:5A1N}.
HELIX 132 139 {ECO:0000244|PDB:5A1N}.
HELIX 145 155 {ECO:0000244|PDB:5A1N}.
HELIX 158 167 {ECO:0000244|PDB:5A1N}.
HELIX 750 769 {ECO:0000244|PDB:1FYJ}.
HELIX 774 795 {ECO:0000244|PDB:1FYJ}.
TURN 1020 1022 {ECO:0000244|PDB:4HVC}.
HELIX 1024 1034 {ECO:0000244|PDB:4HVC}.
STRAND 1038 1040 {ECO:0000244|PDB:4HVC}.
STRAND 1042 1045 {ECO:0000244|PDB:4K86}.
STRAND 1047 1049 {ECO:0000244|PDB:4HVC}.
HELIX 1051 1070 {ECO:0000244|PDB:4HVC}.
STRAND 1080 1083 {ECO:0000244|PDB:4HVC}.
HELIX 1084 1087 {ECO:0000244|PDB:4HVC}.
TURN 1088 1090 {ECO:0000244|PDB:4K86}.
HELIX 1095 1100 {ECO:0000244|PDB:4HVC}.
STRAND 1102 1107 {ECO:0000244|PDB:4HVC}.
STRAND 1110 1118 {ECO:0000244|PDB:4HVC}.
STRAND 1120 1122 {ECO:0000244|PDB:4HVC}.
HELIX 1123 1133 {ECO:0000244|PDB:4HVC}.
HELIX 1137 1139 {ECO:0000244|PDB:4HVC}.
STRAND 1142 1151 {ECO:0000244|PDB:4HVC}.
TURN 1160 1162 {ECO:0000244|PDB:4HVC}.
STRAND 1165 1178 {ECO:0000244|PDB:4HVC}.
HELIX 1179 1198 {ECO:0000244|PDB:4HVC}.
STRAND 1206 1209 {ECO:0000244|PDB:4HVC}.
TURN 1212 1214 {ECO:0000244|PDB:4HVC}.
STRAND 1219 1229 {ECO:0000244|PDB:4HVC}.
TURN 1230 1233 {ECO:0000244|PDB:4HVC}.
STRAND 1234 1245 {ECO:0000244|PDB:4HVC}.
HELIX 1247 1252 {ECO:0000244|PDB:4HVC}.
STRAND 1255 1257 {ECO:0000244|PDB:4HVC}.
STRAND 1259 1261 {ECO:0000244|PDB:5VAD}.
STRAND 1265 1267 {ECO:0000244|PDB:4HVC}.
STRAND 1269 1276 {ECO:0000244|PDB:4HVC}.
HELIX 1278 1287 {ECO:0000244|PDB:4HVC}.
TURN 1297 1299 {ECO:0000244|PDB:4HVC}.
STRAND 1303 1308 {ECO:0000244|PDB:4HVC}.
STRAND 1313 1315 {ECO:0000244|PDB:4K87}.
HELIX 1317 1336 {ECO:0000244|PDB:4HVC}.
STRAND 1341 1343 {ECO:0000244|PDB:4HVC}.
STRAND 1347 1349 {ECO:0000244|PDB:4HVC}.
HELIX 1351 1360 {ECO:0000244|PDB:4HVC}.
STRAND 1364 1369 {ECO:0000244|PDB:4HVC}.
HELIX 1371 1376 {ECO:0000244|PDB:4HVC}.
STRAND 1378 1383 {ECO:0000244|PDB:4HVC}.
TURN 1384 1386 {ECO:0000244|PDB:4HVC}.
STRAND 1389 1393 {ECO:0000244|PDB:4HVC}.
HELIX 1394 1396 {ECO:0000244|PDB:4HVC}.
HELIX 1397 1423 {ECO:0000244|PDB:4HVC}.
STRAND 1424 1426 {ECO:0000244|PDB:4HVC}.
HELIX 1430 1438 {ECO:0000244|PDB:4HVC}.
STRAND 1442 1447 {ECO:0000244|PDB:4HVC}.
HELIX 1451 1462 {ECO:0000244|PDB:4HVC}.
STRAND 1477 1484 {ECO:0000244|PDB:4HVC}.
STRAND 1498 1501 {ECO:0000244|PDB:4K87}.
STRAND 1504 1509 {ECO:0000244|PDB:4HVC}.
SEQUENCE 1512 AA; 170591 MW; 2CE4311076719403 CRC64;
MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD VNSILRYLAR
VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSTIN ELNHCLSLRT YLVGNSLSLA
DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW FGFLEAQQAF QSVGTKWDVS TTKARVAPEK
KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN
PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
AEREQRIDSK HRKNPIEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC MRDPTLYRCK
IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI
WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS
SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG
LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKLNLENKD
YKKTTKVTWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK HEELMLGDPC
LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCVLI YIPDGHTKEM PTSGSKEKTK
VEATKNETSA PFKERPTPSL NNNCTTSEDS LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA
VKQLLSLKAE YKEKTGQEYK PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL
KAEKSPKAKI NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE
AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY KPVSATGAED
KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS GAGEGQGPKK QTRLGLEAKK
EENLADWYSQ VITKSEMIEY HDISGCYILR PWAYAIWEAI KDFFDAEIKK LGVENCYFPM
FVSQSALEKE KTHVADFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL
PIKLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL
LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK MFEIVFEDPK
IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA CVQVVIIPCG ITNALSEEDK
EALIAKCNDY RRRLLSVNIR VRADLRDNYS PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV
AVRRDTGEKL TVAENEAETK LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG
KIVQIPFCGE IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN
PAKYYTLFGR SY


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