PIR:S21236 >P1;S21236 glutamate--tRNA ligase (EC 6.1.1.17) - Thermus aquaticus C;Species: Thermus aquaticus C;Date: 22-Nov-1993 #sequence_revision 22-Nov-1993 #text_change 22-Nov-1993 C;Accession: S21236 R;Nureki, O.; Suzuki, K.; Hara-Yokoyama, M.; Kohno, T.; Matsuzawa, H.; Ohta, T.; Shimizu, T.; Morikawa, K.; Miyazawa, T.; Yokoyama, S. Eur. J. Biochem. 204, 465-472, 1992 A;Title: Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproduced protein. A;Reference number: S21172; MUID:92174899 A;Accession: S21236 A;Status: preliminary A;Residues: 1-40 >S21236 MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRI PIR:S66716 >P1;S66716 glutamate--tRNA ligase (EC 6.1.1.17), mitochondrial - yeast (Saccharomyces cerevisiae) N;Alternate names: mitochondrial glutamyl-tRNA synthetase; protein O2125; protein YOL033w C;Species: Saccharomyces cerevisiae C;Date: 12-Jul-1996 #sequence_revision 12-Jul-1996 #text_change 02-Aug-1996 C;Accession: S66716; S59729 R;Habbig, B.; Hattenhorst, U.; Hollenberg, C.P.; Ramezani Rad, M. submitted to the Protein Sequence Database, July 1996 A;Reference number: S66703 A;Accession: S66716 A;Molecule type: DNA A;Residues: 1-536 A;Cross-references: EMBL:Z74775 A;Experimental source: strain S288C R;Tzagoloff, A.A.; Shtanko, A. submitted to the EMBL Data Library, January 1995 A;Reference number: S56044 A;Accession: S59729 A;Molecule type: DNA A;Residues: 1-463,'L',465-536 A;Cross-references: EMBL:L39015 A;Experimental source: strain S273-10B C;Genetics: A;Gene: MSE1 A;Map position: 15L A;Genome: nuclear C;Keywords: aminoacyl-tRNA synthetase; ATP; ligase; mitochondrion; protein biosynthesis >S66716 MIMLRIPTRSYCSPSKLIKGVGLSPLKKSLLSKKIKEDIHPSLPVRTRFAPSPTGFLHLG SLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSER KLIYDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSMASYDRCCAHLGEEEIKSK LAQGIPFTVRFKSPERYPTFTDLLHGQINLQPQVNFNDKRYDDLILVKSDKLPTYHLANV VDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIPLLTTVGDKKLSKRKGDMS ISDLKRQGVLPEALINFCALFGWSPPRDLASKKHECFSMEELETIFNLNGLTKGNAKVDD KKLWFFNKHFLQKRILNPSTLRELVDDIMPSLESIYNTSTISREKVAKILLNCGGSLSRI NDFHDEFYYFFEKPKYNDNDAVTKFLSKNESRHIAHLLKKLGQFQEGTDAQEVESMVETM YYENGFSRKVTYQAMRFALAGCHPGAKIAAMIDILGIKESNKRLSEGLQFLQREKK PIR:S51684 >P1;S51684 glutamate--tRNA ligase (EC 6.1.1.17) precursor - barley C;Species: Hordeum vulgare (barley) C;Date: 07-May-1995 #sequence_revision 01-Sep-1995 #text_change 01-Sep-1995 C;Accession: S51684 R;Andersen, R.V. submitted to the EMBL Data Library, December 1994 A;Reference number: S51684 A;Accession: S51684 A;Status: preliminary A;Molecule type: mRNA A;Residues: 1-560 A;Cross-references: EMBL:X83523 C;Keywords: ligase >S51684 MAASNFMGSSARLRVGLLPSVTPRLSRRALATRASADSGGSGPVRVRFAPSPTGNLHVGG ARTALFNYLFARSRGGKFVLRVEDTDLERSTKKSEEAVLTDLSWLGLDWDEGPDIGGDFG PYRQSERNALYKEHAQKLMESGAVYRCFCSNEELEKMKETANRMKIPPVYMGKWATASDA EVQQELEKGTPYTYRFRVPKEGSLKINDLIRGEVSWNLNTLGDFVIMRSNGQPVYNFCVT VDDATMRISHVIRAEEHLPNTLRQALIYKALGFAMPLFAHVSLILAPDKSKLSKRHGATS VGQYKEMGYLPQAMVNYLALLGWGDGTENEFFTIDDLVEKFTIDRVNKSGAVFDATKLKW MNGQHLRSLPSDLLIKDFEDQWRSTGILLESESGFAKEAAELLKEGIDLITDADAALCKL LSYPLHETLSSDEAKSVVEDKLSEVASGLISAYDSGELDQALAEGHDGWKKWVKSFGKTH KRKGKSLFMPLRVLLTGKLHGPAMDSTVILVHKAGTSGAVAPQSGFVSLDERFKILKEVN WESLQKQQESPVESAVPAAS PIR:S51685 >P1;S51685 glutamate--tRNA ligase (EC 6.1.1.17) - common tobacco C;Species: Nicotiana tabacum (common tobacco) C;Date: 07-May-1995 #sequence_revision 10-Nov-1995 #text_change 10-Nov-1995 C;Accession: S51685 R;Andersen, R.V. submitted to the EMBL Data Library, December 1994 A;Reference number: S51684 A;Accession: S51685 A;Molecule type: mRNA A;Residues: 1-569 A;Cross-references: EMBL:X83524 C;Keywords: ligase >S51685 MATLAAAPWFRVRLIPELKNSQSLLYCRGNHSYRQSLCSRRRSFSVYASAGDGGDVRVRF APSPTGNLHVGGARTALFNYLYARAKGGKFILRIEDTDLERSTKESEEAVLRDLSWLGPA WDEGPGIGGEYGPYRQSERNALYKQFAEKLLQSGHVYRCFCSNEELEKMKEIAKLKQLPP VYTGRWASATEEEVVEELAKGTPYTYRFRVPKEGSLKIDDLIRGEVSWNLDTLGDFVIMR SNGQPVYNFCVTVDDATMAISHVIRAEEHLPNTLRQALIYKALGFPMPHFAHVSLILAPD RSKLSKRHGATSVGQFRDMGYLPQAMVNYLALLGWGDGTENEFFTLEQLVEKFTIERVNK SGAIFDSTKLRWMNGQHLRSLPSEELNRIIGERWKDAGIATESQGIFIQDAVLLLKDGID LITDSEKALSSLLSYPLYETLASAEGKPILEDGVSEVAKSLLAAYDSGELSGALAEGQPG WQKWAKNFGKLLKRKGKSLFMPLRVLLTGKLHGPDIGATTVLLYKAGTSGSVVPQAGFVT FDERFKILREVQWESFSTDVPLSAGAVTR PIR:H64471 >P1;H64471 glutamate--tRNA ligase (EC 6.1.1.17) - Methanococcus jannaschii N;Alternate names: glutamyl-tRNA synthetase C;Species: Methanococcus jannaschii C;Date: 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 13-Sep-1996 C;Accession: H64471 R;Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; Hurst, M.A.; Kaine, B.P. Science 273, 1058-1073, 1996 A;Authors: Borodovsky, M.; Klenk, H.P.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. A;Title: Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. A;Reference number: A64300 A;Accession: H64471 A;Status: preliminary; nucleic acid sequence not shown; translation not shown A;Molecule type: DNA A;Residues: 1-553 A;Cross-references: GB:L77117; TIGR:MJ1377; CDS_PID:g1511393 C;Genetics: A;Map position: REV1326696-1325035 A;Start codon: GTG C;Keywords: ligase >H64471 MEEKILPIALRNAIKYNGKANPKAVLGIFLSENPEYRSKAKEVMPIVEKVVEEVNKLSLD EIKKKLEELGEDVKKKEKKEKGLELPNVKDKVVMRFAPNPSGPLHIGHARAAVLNDYFVK KYGGKLILRLEDTDPKRVLPEAYDMIKEDLDWLGVKVDEVVIQSDRIELYYEYGRKLIEM GHAYVCDCNPEEFRELRNKGVPCKCRDRAIEDNLELWEKMLNGELENVAVRLKTDIKHKN PSIRDFPIFRVEKTPHPRTGDKYCVYPLMNFSVPVDDHLLGMTHVLRGKDHIVNTEKQAY IYKYFGWEMPEFIHYGILKIEDIVLSTSSMYKGIKEGLYSGWDDVRLGTLRALRRRGIKP EAIYEIMKRIGIKQADVKFSWENLYAINKELIDKDARRFFFVWNPKKLIIEGAEKKVLKL RMHPDRPEFGERELIFDGEVYVVGDELEENKMYRLMELFNIVVEKVDDIALAKYHSDDFK IARKNKAKIIHWIPVKDSVKVKVLMPDGEIKEGFAEKDFAKVEVDDIIQFERFGFVRIDK KDNDGFVCCYAHR PIR:A64251 >P1;A64251 glutamate--tRNA ligase (EC 6.1.1.17) - Mycoplasma genitalium (SGC3) N;Alternate names: glutamyl-tRNA synthetase C;Species: Mycoplasma genitalium C;Date: 17-Nov-1995 #sequence_revision 17-Nov-1995 #text_change 19-Jul-1996 C;Accession: A64251; S18709 R;Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, C.A.; Venter, J.C. Science 270, 397-403, 1995 A;Title: The minimal gene complement of Mycoplasma genitalium. A;Reference number: A64200 A;Accession: A64251 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-484 A;Cross-references: GB:L43967; TIGR:MG462 A;Experimental source: strain G-37 A;Note: neither nucleotide sequence nor conceptual translation is shown C;Genetics: A;Genetic code: SGC3 C;Function: A;Description: aminoacylates tRNA(Glu) and tRNA(Gln) with glutamate A;Pathway: protein biosynthesis A;Note: there is no glutamine--tRNA ligase in this species; the glutamate group on the tRNA(Gln) is amidated to glutamine in a separate reaction C;Keywords: ligase; protein biosynthesis >A64251 MEKIRTRYAPSPTGYLHVGGTRTAIFNFLLAKHFNGEFIIRIEDTDTERNIKEGINSQFD NLRWLGVIADESVYNPGNYGPYLQSQKLAVYKKLAFDLIEKNLAYRCFCSKEKLESDRKQ AINNHKTPKYLGHCRNLHSKKITNHLEKNDPFTIRLKINNEAEYSWNDLVRGQITIPGSA LTDIVILKANGVATYNFAVVIDDYDMEITDVLRGAEHISNTAYQLAIYQALGFKRIPRFG HLSVIVDESGKKLSKRDEKTTQFIEQFKQQGYLPEALLNFLALLGWHPQYNQEFFNLKQL IENFSLSRVVSAPAFFDIKKLQWINANYIKQLTDNAYFNFIDNYLDVKVDYLKDKNREIS LLFKNQITHGVQINELIRESFATKIGVENLAKKSHILFKNIKLFLEQLAKSLQGLEEWKA EQIKTTINKVGAVFNLKGKQLFMPIRLIFTNKEHGPDLAHIIEIFDKESAINLIKQFINA TNLF PIR:S46900 >P1;S46900 glutamate--tRNA ligase (EC 6.1.1.17) - Mycoplasma capricolum (SGC3) N;Alternate names: glutamyl-tRNA synthetase C;Species: Mycoplasma capricolum C;Date: 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 03-Mar-1995 C;Accession: S46900 R;Bork, P.; Ouzounis, C.; Casari, G.; Sander, C.; Dolan, M.; Gillevet, P. submitted to the EMBL Data Library, July 1994 A;Description: Exploring the Mycoplasma capricolum genome: a parasite reveals it's physiology. A;Reference number: S46898 A;Accession: S46900 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-28 A;Cross-references: EMBL:Z33261 C;Genetics: A;Genetic code: SGC3 C;Keywords: ligase >S46900 MNYLFAKHYNGSFIVRIEDTDLARNVEG PIR:I40809 >P1;I40809 glutamate--tRNA ligase (EC 6.1.1.17) NAC(P)H-dependent - Clostridium josui C;Species: Clostridium josui C;Date: 16-Aug-1996 #sequence_revision 16-Aug-1996 #text_change 16-Aug-1996 C;Accession: I40809 R;Fujino, E.; Fujino, T.; Karita, S.; Sakka, K.; Ohmiya, K. J. Bacteriol. 177, 5169-5175, 1995 A;Title: Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui. A;Reference number: A57344; MUID:95394829 A;Accession: I40809 A;Status: preliminary; translated from GB/EMBL/DDBJ A;Molecule type: DNA A;Residues: 1-515 A;Cross-references: GB:D28503; NID:g536874; CDS_PID:g536875 C;Genetics: A;Gene: hemA C;Keywords: ligase >I40809 MQLGRHNSGSIKKRLEMYILSIISASLDYKSAAIDIRERFSYTSTRIREILRRIKAADGV SGAVLLCTCNRTELYISGDNIENMNPALLLCQLSGEEDHKSLMTLFSIRHDSEAIFHLME VACGLQSMVLFEDRVITQVKNAAAISREEKTIDSTLETLFRLCITAAKKAKTEIKVKAVP TSAAERAITELSKKYCFTDKRILVIGNGEIGRLCCKKLIELGAEITITLRKYKHGEIIIP VGCNTIPYDEREEVLPLSDVVISATTSPHFTITYDMIEKLERKPEIFVDLALPRDIESSI SNFTGVELYNLDRFYTDYSVLNQKEVSKIREIINHFILQFEKWKDYREEAAFTKIPDLHN DTLYGRFPLFIDLSGKKVLVVGGGEIATRRVKTLLRFGADIYLVAPHLTSELQEMLNCKL INYREGYYESQDIQNMFLVIAATNDRETNHKVYLDAKEKGIQMSIADCREECSFYFPAIF EFDGIVGGLVSQNGDNHSLVKSVAEQIRKIGQATD PIR:A53402 >F1;A53402 glutamate--tRNA ligase (EC 6.1.1.17) - Bacillus subtilis (fragment) C;Species: Bacillus subtilis C;Date: 27-Jun-1994 #sequence_revision 27-Jun-1994 #text_change 27-Jun-1994 C;Accession: A53402 R;Gagnon, Y.; Breton, R.; Putzer, H.; Pelchat, M.; Grunberg-Manago, M.; Lapointe, J. J. Biol. Chem. 269, 7473-7482, 1994 A;Title: Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis. A;Reference number: A53402 A;Accession: A53402 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-22 A;Cross-references: GB:L14580 C;Keywords: ligase >A53402 KLGFTGRAEGIAAQATVLIQKG PIR:D53402 >F1;D53402 glutamate--tRNA ligase (EC 6.1.1.17) - Bacillus stearothermophilus (fragment) C;Species: Bacillus stearothermophilus C;Date: 27-Jun-1994 #sequence_revision 27-Jun-1994 #text_change 27-Jun-1994 C;Accession: D53402 R;Gagnon, Y.; Breton, R.; Putzer, H.; Pelchat, M.; Grunberg-Manago, M.; Lapointe, J. J. Biol. Chem. 269, 7473-7482, 1994 A;Title: Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis. A;Reference number: A53402 A;Accession: D53402 A;Status: preliminary; not compared with conceptual translation A;Molecule type: DNA A;Residues: 1-24 C;Keywords: ligase >D53402 KLGFTGRGEGIAAQAVVLLKKSGE PIR:F53402 >F1;F53402 cysteine--tRNA ligase (EC 6.1.1.16) - Bacillus stearothermophilus (fragment) C;Species: Bacillus stearothermophilus C;Date: 27-Jun-1994 #sequence_revision 27-Jun-1994 #text_change 27-Jun-1994 C;Accession: F53402 R;Gagnon, Y.; Breton, R.; Putzer, H.; Pelchat, M.; Grunberg-Manago, M.; Lapointe, J. J. Biol. Chem. 269, 7473-7482, 1994 A;Title: Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis. A;Reference number: A53402 A;Accession: F53402 A;Status: preliminary; not compared with conceptual translation A;Molecule type: DNA A;Residues: 1-221 C;Keywords: ligase >F53402 MSSIRLYNTLTRKKEPFEPLEPNKVKMYVCGPTVYNYIHIGNARAAIVFDTIRRYLEFRG YDVTYVSNFTDVDDKLIKAARELGESVPAIAERFIEAYFEDIQALGCKKADIHPRVTENI GTIIEFIQALIDKGYAYEVDGDVYYRTRKFPGYGKLSHQSIDELQAGARIEVGEKKDDPL DFALWKAAKEGEICWDSPWGKGRPGWHIECSAMAGRYLGTV PIR:S45213 >P1;S45213 glutamate--tRNA ligase homolog - Escherichia coli N;Alternate names: glutamyl-tRNA synthetase homolog C;Species: Escherichia coli C;Date: 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 05-Apr-1995 C;Accession: S45213 R;Fujita, N. submitted to the EMBL Data Library, January 1994 A;Reference number: S45181 A;Accession: S45213 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-256 A;Cross-references: EMBL:D26562 >S45213 MLPPYFLFKEMTDTQYIGRFAPSPSGELHFGSLIAALGSYLQARARQGRWLVRIEDIDPP REVPGAAETILRQLEHYGLHWDGDVLWQSQRHDAYREALAWLHEQGLSYYCTCTRARIQS IGGIYDGHCRVLHHGPDNAAVRIRQQHPVTQFTDQLRGIIHADEKLAREDFIIHRRDGLF AYNLAVVVDDHFQGVTEIVRGADLIEPTVRQISLYQLFGWKVPDYIHLPLALNPQGAKLS KQNHAPALPKAIHARY PIR:S21172 >P1;S21172 glutamate--tRNA ligase - Thermus aquaticus C;Species: Thermus aquaticus C;Date: 22-Nov-1993 #sequence_revision 01-Dec-1995 #text_change 01-Dec-1995 C;Accession: S21172 R;Nureki, O.; Suzuki, K.; Hara-Yokoyama, M.; Kohno, T.; Matsuzawa, H.; Ohta, T.; Shimizu, T.; Morikawa, K.; Miyazawa, T.; Yokoyama, S. Eur. J. Biochem. 204, 465-472, 1992 A;Title: Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproduced protein. A;Reference number: S21172; MUID:92174899 A;Accession: S21172 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-468 A;Cross-references: EMBL:X64557 A;Note: the sequence from Fig. 4 is inconsistent with that from Fig. 3 in having 67-Thr A;Note: the source is designated as Thermus thermophilus >S21172 MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVPGAEERILAAL KWLGLSYDEGPDVAAPTGPYRQSERLPLYQKYAEELLKRGWAYRAFETPEELEQIRKEKG GYDGRARNIPPEEAEERARRGEPHVIRLKVPRPGTTEVKDELRGVVVYDNQEIPDVVLLK SDGYPTYHLANVVDDHLMGVTDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPD KTKISKRKSHTSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRRAVELMRPRFD TLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPRLRAQEEWTEAALEALLRGFA AEKGVKLGQVAQPLRAALTGSLETPGLFEILALLGKERALRRLERALA PIR:B64059 >P1;B64059 glutamate--tRNA ligase (EC 6.1.1.17) - Haemophilus influenzae (strain Rd KW20) N;Alternate names: glutamyl-tRNA synthetase C;Species: Haemophilus influenzae C;Date: 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 10-May-1996 C;Accession: B64059 R;Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; Phillips, C.A.; Spriggs, T.; Hedblom, E. Science 269, 496-512, 1995 A;Authors: Cotton, M.D.; Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; Fraser, C.M.; Smith, H.O.; Venter, J.C. A;Title: Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. A;Reference number: A64000 A;Accession: B64059 A;Status: nucleic acid sequence not shown; translation not shown A;Molecule type: DNA A;Residues: 1-480 A;Cross-references: GB:L42023; TIGR:HI0274 A;Note: named as homolog to a protein from Escherichia coli C;Genetics: A;Gene: gltX C;Superfamily: glutamate--tRNA ligase C;Keywords: aminoacyl-tRNA synthetase; ligase; protein biosynthesis >B64059 MKLDAPFNLDPNVKVRTRFAPSPTGYLHVGGARTALYSWLYAKHNNGEFVLRIEDTDLER STPEATAAIIEGMEWLNLPWEHGPYYQTKRFDRYNQVIDEMIEQGLAYRCYCTKEHLEEL RHTQEQNKEKPRYDRHCLHDHNHSPDEPHVVRFKNPTEGSVVFDDAVRGRIEISNSELDD LIIRRTDGSPTYNFCVVVDDWDMGITHVVRGEDHINNTPRQINILKAIGAPIPTYAHVSM INGDDGQKLSKRHGAVSVMQYRDDGYLPEALINYLVRLGWGHGDQEIFSREEMINYFELD HVSKSASAFNTEKLQWLNQHYIRELPPEYVAKHLEWHYKDQGIDTSNGPALTEIVTMLAE RCKTLKEMARSSRYFFEEFETFDEAAAKKHFKGNAAEALAKVKEKLTALSSWDLHSIHEA IEQTAAELEVGMGKVGMPLRVAVTGSGQSPSMDVTLVGIGRDRVLARIQRAIDFIHAQNA PIR:SYBSES >P1;SYBSES glutamate--tRNA ligase (EC 6.1.1.17) - Bacillus stearothermophilus N;Alternate names: glutamyl-tRNA synthetase C;Species: Bacillus stearothermophilus C;Date: 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 30-Jun-1993 C;Accession: B36090 R;Breton, R.; Watson, D.; Yaguchi, M.; Lapointe, J. J. Biol. Chem. 265, 18248-18255, 1990 A;Title: Glutamyl-tRNA synthetases of Bacillus subtilis 168T and of Bacillus stearothermophilus. Cloning and sequencing of the gltX genes and comparison with other aminoacyl-tRNA synthetases. A;Reference number: A36090; MUID:91009314 A;Accession: B36090 A;Molecule type: DNA A;Residues: 1-489 A;Cross-references: GB:M55072; GB:J05647 A;Note: the authors translated the codon AAC for residue 62 as Asp and CCG for residue 195 as Phe C;Genetics: A;Gene: gltX C;Superfamily: glutamate--tRNA ligase C;Keywords: aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis F;256/Binding site: ATP (Lys) #status predicted >SYBSES MAKDVRVGYAPSPTGHLHIGGARTALFNYLFARHHGGKMIVRIEDTDIERNVEGGEQSQL ENLQWLGIDYDESVDKDGGYGPYRQTERLDIYRKYVDELLEQGHAYKCFCTPEELERERE EQRAAGIAAPQYSGKCRRLTPEQVAELEAQGKPYTIRLKVPEGKTYEVDDLVRGKVTFES KDIGDWVIVKANGIPTYNFAVVIDDHLMEISHVFRGEEHLSNTPKQLMVYEYFGWEPPQF AHLTLIVNEQRKKLSKRDESIIQFVSQYKELGYLPEAMFNFFALLGWSPEGEEEIFSKDE LIRIFDVSRLSKSPSMFDTKKLTWMNNQYIKKLDLDRLVELALPHLVKAGRLPADMSDEQ RQWARDLIALYQEQMSYGAEIVPLSELFFKEEVEYEDEARQVLAEEQVPDVLSAFLAHVR DLDPFTADEIKAAIKAVQKATGQKGKKLFMPIRAAVTGQTHGPELPFAIQLLGKQKVIER LERALQEKF PIR:SYBSET >P1;SYBSET glutamate--tRNA ligase (EC 6.1.1.17) - Bacillus subtilis N;Alternate names: glutamyl-tRNA synthetase C;Species: Bacillus subtilis C;Date: 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 06-Dec-1996 C;Accession: A36090; S66121 R;Breton, R.; Watson, D.; Yaguchi, M.; Lapointe, J. J. Biol. Chem. 265, 18248-18255, 1990 A;Title: Glutamyl-tRNA synthetases of Bacillus subtilis 168T and of Bacillus stearothermophilus. Cloning and sequencing of the gltX genes and comparison with other aminoacyl-tRNA synthetases. A;Reference number: A36090; MUID:91009314 A;Accession: A36090 A;Molecule type: DNA A;Residues: 1-483 A;Cross-references: GB:M55073; GB:J05647 A;Experimental source: strain 168T A;Note: the authors translated the codon CCT for residue 194 as Phe R;Ogasawara, N.; Nakai, S.; Yoshikawa, H. DNA Res. 1, 1-14, 1994 A;Title: Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin. A;Reference number: S65967 A;Accession: S66121 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-483 A;Cross-references: EMBL:D26185 C;Genetics: A;Gene: gltX C;Superfamily: glutamate--tRNA ligase C;Keywords: aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis F;255/Binding site: ATP (Lys) #status predicted >SYBSET MGNEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQL NYLKWLGIDWDESVDVGGEYGPYRQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKERE EQIARGEMPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVPEGKVIAFNDIVKGEISFESD GIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFG HMTLIVNESRKKLSKRDESIIQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQF IEIFDVNRLSKSPALFDMHKLKWVNNQYVKKLDLDQVVELTLPHLQKAGKVGTELSAEEQ EWVRKLISLYHEQLSYGAEIVELTDLFFTDEIEYNQEAKAVLEEEQVPEVLSTFAAKLEE LEEFTPDNIKASIKAVQKETGHKGKKLFMPIRVAVTGQTHGPELPQSIELIGKETAIQRL KNI PIR:SYRZET >P1;SYRZET glutamate--tRNA ligase (EC 6.1.1.17) - Rhizobium meliloti N;Alternate names: glutamyl-tRNA synthetase C;Species: Rhizobium meliloti C;Date: 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 30-Jun-1993 C;Accession: A32888 R;Laberge, S.; Gagnon, Y.; Bordeleau, L.M.; Lapointe, J. J. Bacteriol. 171, 3926-3932, 1989 A;Title: Cloning and sequencing of the gltX gene, encoding the glutamyl-tRNA synthetase of Rhizobium meliloti A2. A;Reference number: A32888; MUID:89291743 A;Accession: A32888 A;Molecule type: DNA A;Residues: 1-484 A;Cross-references: GB:M27221 A;Experimental source: strain A2 C;Superfamily: glutamate--tRNA ligase C;Keywords: aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis F;256/Binding site: ATP (Lys) #status predicted >SYRZET MADSAVRVRIAPSPTGEPHVGTAYIALFNYLFAKKHGGKFILRIEDTDATRSTPEFEKKV LDALKWCGLEWSEGPDIGGPYGPYRQSDRKDIYKPYVEKIVANGHGFRCFCTPERLEQMR EAQRAAGKPPKYDGLCLSLSAEEVTSRVDAGEPHVVRMKIPTEGSCKFRDGVYGDVEIPW EAVDMQVLLKADGMPTYHMANVVDDHLMKITHVARGEEWLASVPKHILIYQYLGLEPPVF MHLSLMRNADKSKLSKRKNPTSISYYTALGYLPEALMNFLGLFFIQIAEGEELLTMEELA EKFDPENLSKAGAIFDIQKLDWLNARWIREKLSEEEFAARVLAWAMDNERLKEGLKLSQT RISKLGELPDLAAFLFKSDLGLQPAAFAGVKASPEEMLKILNTVQPDLEKILEWNKDSIE TELRASERMGKKLKAVVAPLFVACSGSQRSLPLFDSMELLGRSVVRQRLKVAAQVVASMA GSGK PIR:SYECET >P1;SYECET glutamate--tRNA ligase (EC 6.1.1.17) - Escherichia coli N;Alternate names: glutamyl-tRNA synthetase C;Species: Escherichia coli C;Date: 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 30-Jun-1993 C;Accession: A25956 R;Breton, R.; Sanfacon, H.; Papayannopoulos, I.; Biemann, K.; Lapointe, J. J. Biol. Chem. 261, 10610-10617, 1986 A;Title: Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases. A;Reference number: A25956; MUID:86278132 A;Accession: A25956 A;Molecule type: DNA A;Residues: 1-471 A;Cross-references: GB:M13687 C;Comment: The active enzyme, a monomer, is the smallest aminoacyl-tRNA synthetase of E. coli; it does not bind glutamate in the absence of cognate tRNA, which is therefore required for activation of the amino acid substrate. C;Genetics: A;Gene: gltX A;Map position: 52 min C;Superfamily: glutamate--tRNA ligase C;Keywords: aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis F;240/Binding site: ATP (Lys) #status predicted >SYECET MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDG MNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPR YDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPT YNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSK RHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNT DKLLWLNHHYINALPPEYVATHLQWHIEQENIDTRNGPQLADLVKLLGERCKTLKEMAQS CRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDKLAAITDWTAENVHHAIQATADELEVG MGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALDFIAERENQQ SWISSPROT:SYE_THETH ID SYE_THETH STANDARD; PRT; 468 AA. AC P27000; DT 01-AUG-1992 (REL. 23, CREATED) DT 01-AUG-1992 (REL. 23, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS). GN GLTX. OS THERMUS AQUATICUS (SUBSP. THERMOPHILUS). OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC UNCERTAIN. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HB8; RX MEDLINE; 92174899. RA NUREKI O., SUZUKI K., HARA-YOKOYAMA M., KOHNO T., MATSUZAWA H., RA OHTA T., SHIMIZU T., MORIKAWA K., MIYAZAWA T., YOKOYAMA S.; RL EUR. J. BIOCHEM. 204:465-472(1992). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; X64557; G48242; -. DR PIR; S21172; S21172. DR PIR; S21236; S21236. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 8 18 "HIGH" REGION. FT SIMILAR 243 247 "KMSKS" REGION. FT BINDING 246 246 ATP (BY SIMILARITY). SQ SEQUENCE 468 AA; 53901 MW; 426CEE31 CRC32; >SYE_THETH MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVPGAEERILAAL KWLGLSYDEGPDVAAPTGPYRQSERLPLYQKYAEELLKRGWAYRAFETPEELEQIRKEKG GYDGRARNIPPEEAEERARRGEPHVIRLKVPRPGTTEVKDELRGVVVYDNQEIPDVVLLK SDGYPTYHLANVVDDHLMGVTDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPD KTKISKRKSHTSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRRAVELMRPRFD TLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPRLRAQEEWTEAALEALLRGFA AEKGVKLGQVAQPLRAALTGSLETPGLFEILALLGKERALRRLERALA SWISSPROT:SYE_SYNP2 ID SYE_SYNP2 STANDARD; PRT; 159 AA. AC P31970; DT 01-JUL-1993 (REL. 26, CREATED) DT 01-FEB-1994 (REL. 28, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS) (FRAGMENT). GN GLTX. OS SYNECHOCOCCUS SP. (STRAIN PCC 7002) (AGMENELLUM QUADRUPLICATUM). OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); CHROOCOCCALES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94018606. RA ZHAO J., SNYDER W., MUHLENHOFF U., RHIEL E., BRYANT D.A.; RL MOL. MICROBIOL. 9:183-194(1993). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; M99379; E84123; -. DR HSSP; P00962; 1GTR. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 9 19 "HIGH" REGION. FT NON_TER 159 159 SQ SEQUENCE 159 AA; 18509 MW; 4F6DB637 CRC32; >SYE_SYNP2 MTVRVRIAPSPTGNLHIGTARTAVFNWLFAHHHGGTFVLRVEDTDLERSKPEYTENIKTG LQWLGLHWDEGPFFQTQRLDQYKAAIQTLLDQGLAYRCYCTPAELEAMREQQKANNQAPR YDNRHRNLTEAQRAEFEAQGRKPVIRFKIDDAQQIVWQD SWISSPROT:SYE_RHIME ID SYE_RHIME STANDARD; PRT; 485 AA. AC P15189; DT 01-APR-1990 (REL. 14, CREATED) DT 01-APR-1990 (REL. 14, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS). GN GLTX. OS RHIZOBIUM MELILOTI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC RHIZOBIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=A2; RX MEDLINE; 89291743. RA LABERGE S., GAGNON Y., BORDELEAU L.M., LAPOINTE J.; RL J. BACTERIOL. 171:3926-3932(1989). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; M27221; G717082; -. DR PIR; A32888; SYRZET. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 12 22 "HIGH" REGION. FT SIMILAR 253 257 "KMSKS" REGION. FT BINDING 256 256 ATP (BY SIMILARITY). SQ SEQUENCE 485 AA; 54356 MW; 22131735 CRC32; >SYE_RHIME MADSAVRVRIAPSPTGEPHVGTAYIALFNYLFAKKHGGKFILRIEDTDATRSTPEFEKKV LDALKWCGLEWSEGPDIGGPYGPYRQSDRKDIYKPYVEKIVANGHGFRCFCTPERLEQMR EAQRAAGKPPKYDGLCLSLSAEEVTSRVDAGEPHVVRMKIPTEGSCKFRDGVYGDVEIPW EAVDMQVLLKADGMPTYHMANVVDDHLMKITHVARGEEWLASVPKHILIYQYLGLEPPVF MHLSLMRNADKSKLSKRKNPTSISYYTALGYLPEALMNFLGLFFIQIAEGEELLTMEELA EKFDPENLSKAGAIFDIQKLDWLNARWIREKLSEEEFAARVLAWAMDNERLKEGLKLSQT RISKLGELPDLAAFLFKSDLGLQPAAFAGVKASPEEMLKILNTVQPDLEKILEWNKDSIE TELRASERMGKKLKAVVAPLFVACSGSQRSLPLFDSMELLGRSVVRQRLKVAAQVVASMA GSGKQ SWISSPROT:SYE_MYCPU ID SYE_MYCPU STANDARD; PRT; 468 AA. AC P53662; DT 01-OCT-1996 (REL. 34, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS). GN GLTX. OS MYCOPLASMA PULMONIS. OC PROKARYOTA; TENERICUTES; MOLLICUTES; MYCOPLASMA; MYCOPLASMATALES; OC MYCOPLASMATACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=KD735-16; RX MEDLINE; 95020589. RA DYBVIG K., YU H.; RL MOL. MICROBIOL. 12:547-560(1994). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; L25415; G496154; -. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 10 20 "HIGH" REGION. FT SIMILAR 252 256 "KMSKS" REGION. FT BINDING 255 255 ATP (BY SIMILARITY). SQ SEQUENCE 468 AA; 55065 MW; 80226295 CRC32; >SYE_MYCPU MKKLRTRYAPSPTGYLHIGGARTALFNYLLAKHYNGDFIIRIEDTDVKRNIADGEASQIE NLKWLNIEANESPLKPNEKYGPYRQSQKLEKYLKIAHELIEKGYAYKAYDNSEELEEQKK HSEKLGVASFRYQRDFLKISEEEKQKRDASGAYSIRVICPKNTTYQWDDLVRGNIAVNSN DIGDWIIIKSDDYPTYNFAVVIDDIDMEISHILRGEEHITNTPKQMMIYDYLNAPKPLFG HLTIITNMEGKKLSKRDLSLKQFIHEYKEEGYNSQAIFNFLTLLGWTDEKARELMDHDEI IKSFLYTRLSKSPSKFDITKMQWFSKQYWKNTPNEELIKILNLNDYDNDWINLFLDLYKE NIYSLNQLKNYLKIYKQANLNQEKDLDLNDAEKNVVKSFSSYIDYSNFSVNQIQEAINKT QEKLSIKGKNLFLPIRKATTFQEHGPELAKAIYLFGSEIIEKRMKKWK SWISSPROT:SYE_MYCGE ID SYE_MYCGE STANDARD; PRT; 484 AA. AC P47700; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS). GN GLTX OR MG462. OS MYCOPLASMA GENITALIUM. OC PROKARYOTA; TENERICUTES; MOLLICUTES; MYCOPLASMA; MYCOPLASMATALES; OC MYCOPLASMATACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 33530 / G-37; RX MEDLINE; 96026346. RA FRASER C.M., GOCAYNE J.D., WHITE O., ADAMS M.D., CLAYTON R.A., RA FLEISCHMANN R.D., BULT C.J., KERLAVAGE A.R., SUTTON G., KELLEY J.M., RA FRITCHMAN J.L., WEIDMAN J.F., SMALL K.V., SANDUSKY M., FUHRMANN J.L., RA NGUYEN D.T., UTTERBACK T.R., SAUDEK D.M., PHILLIPS C.A., MERRICK J.M., RA TOMB J.-F., DOUGHERTY B.A., BOTT K.F., HU P.-C., LUCIER T.S., RA PETERSON S.N., SMITH H.O., HUTCHISON C.A. III, VENTER J.C.; RL SCIENCE 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; U39733; G1046182; -. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 10 20 "HIGH" REGION. FT SIMILAR 252 256 "KMSKS" REGION. FT BINDING 255 255 ATP (BY SIMILARITY). SQ SEQUENCE 484 AA; 55941 MW; 238DAA61 CRC32; >SYE_MYCGE MEKIRTRYAPSPTGYLHVGGTRTAIFNFLLAKHFNGEFIIRIEDTDTERNIKEGINSQFD NLRWLGVIADESVYNPGNYGPYLQSQKLAVYKKLAFDLIEKNLAYRCFCSKEKLESDRKQ AINNHKTPKYLGHCRNLHSKKITNHLEKNDPFTIRLKINNEAEYSWNDLVRGQITIPGSA LTDIVILKANGVATYNFAVVIDDYDMEITDVLRGAEHISNTAYQLAIYQALGFKRIPRFG HLSVIVDESGKKLSKRDEKTTQFIEQFKQQGYLPEALLNFLALLGWHPQYNQEFFNLKQL IENFSLSRVVSAPAFFDIKKLQWINANYIKQLTDNAYFNFIDNYLDVKVDYLKDKNREIS LLFKNQITHGVQINELIRESFATKIGVENLAKKSHILFKNIKLFLEQLAKSLQGLEEWKA EQIKTTINKVGAVFNLKGKQLFMPIRLIFTNKEHGPDLAHIIEIFDKESAINLIKQFINA TNLF SWISSPROT:SYE_HAEIN ID SYE_HAEIN STANDARD; PRT; 480 AA. AC P43818; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS). GN GLTX OR HI0274. OS HAEMOPHILUS INFLUENZAE. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC PASTEURELLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=RD / KW20; RX MEDLINE; 95350630. RA FLEISCHMANN R.D., ADAMS M.D., WHITE O., CLAYTON R.A., KIRKNESS E.F., RA KERLAVAGE A.R., BULT C.J., TOMB J.-F., DOUGHERTY B.A., MERRICK J.M., RA MCKENNEY K., SUTTON G., FITZHUGH W., FIELDS C.A., GOCAYNE J.D., RA SCOTT J.D., SHIRLEY R., LIU L.-I., GLODEK A., KELLEY J.M., RA WEIDMAN J.F., PHILLIPS C.A., SPRIGGS T., HEDBLOM E., COTTON M.D., RA UTTERBACK T.R., HANNA M.C., NGUYEN D.T., SAUDEK D.M., BRANDON R.C., RA FINE L.D., FRITCHMAN J.L., FUHRMANN J.L., GEOGHAGEN N.S.M., RA GNEHM C.L., MCDONALD L.A., SMALL K.V., FRASER C.M., SMITH H.O., RA VENTER J.C.; RL SCIENCE 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; L44919; G1003444; -. DR EMBL; U32713; G925178; -. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 21 31 "HIGH" REGION. FT SIMILAR 248 252 "KMSKS" REGION. FT BINDING 251 251 ATP (BY SIMILARITY). SQ SEQUENCE 480 AA; 54874 MW; 2477AF72 CRC32; >SYE_HAEIN MKLDAPFNLDPNVKVRTRFAPSPTGYLHVGGARTALYSWLYAKHNNGEFVLRIEDTDLER STPEATAAIIEGMEWLNLPWEHGPYYQTKRFDRYNQVIDEMIEQGLAYRCYCTKEHLEEL RHTQEQNKEKPRYDRHCLHDHNHSPDEPHVVRFKNPTEGSVVFDDAVRGRIEISNSELDD LIIRRTDGSPTYNFCVVVDDWDMGITHVVRGEDHINNTPRQINILKAIGAPIPTYAHVSM INGDDGQKLSKRHGAVSVMQYRDDGYLPEALINYLVRLGWGHGDQEIFSREEMINYFELD HVSKSASAFNTEKLQWLNQHYIRELPPEYVAKHLEWHYKDQGIDTSNGPALTEIVTMLAE RCKTLKEMARSSRYFFEEFETFDEAAAKKHFKGNAAEALAKVKEKLTALSSWDLHSIHEA IEQTAAELEVGMGKVGMPLRVAVTGSGQSPSMDVTLVGIGRDRVLARIQRAIDFIHAQNA SWISSPROT:SYE_ECOLI ID SYE_ECOLI STANDARD; PRT; 471 AA. AC P04805; DT 13-AUG-1987 (REL. 05, CREATED) DT 13-AUG-1987 (REL. 05, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS). GN GLTX. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 86278132. RA BRETON R., SANFACON H., PAPAYANNOPOULOS I., BIEMANN K., LAPOINTE J.; RL J. BIOL. CHEM. 261:10610-10617(1986). RN [2] RP SEQUENCE OF 1-57 FROM N.A. RX MEDLINE; 90355200. RA BRUN V., SANFACON H., BRETON R., LAPOINTE J.; RL J. MOL. BIOL. 214:845-864(1990). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- THIS IS THE SMALLEST AMINOACYL-TRNA SYNTHETASE OF E.COLI; IT DOES CC NOT BIND GLUTAMATE IN THE ABSENCE OF COGNATE TRNA, WHICH IS CC THEREFORE REQUIRED FOR ACTIVATION OF THE AMINO ACID SUBSTRATE. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; X63976; G41596; -. DR EMBL; M13687; G148256; -. DR EMBL; X55737; G288086; -. DR PIR; A25956; SYECET. DR ECO2DBASE; F047.8; 6TH EDITION. DR ECOGENE; EG10407; GLTX. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 9 19 "HIGH" REGION. FT SIMILAR 237 241 "KMSKS" REGION. FT BINDING 240 240 ATP (BY SIMILARITY). SQ SEQUENCE 471 AA; 53815 MW; 4347E6FF CRC32; >SYE_ECOLI MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDG MNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPR YDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPT YNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSK RHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNT DKLLWLNHHYINALPPEYVATHLQWHIEQENIDTRNGPQLADLVKLLGERCKTLKEMAQS CRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDKLAAITDWTAENVHHAIQATADELEVG MGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALDFIAERENQQ SWISSPROT:SYE_CHLPS ID SYE_CHLPS STANDARD; PRT; 370 AA. AC Q06560; DT 01-JUN-1994 (REL. 29, CREATED) DT 01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS) (FRAGMENT). GN GLTX. OS CHLAMYDIA PSITTACI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; RICKETTSIAS; CHLAMYDIALES; OC CHLAMYDIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=6BC; RX MEDLINE; 93259937. RA WICHLAN D.W., HATCH T.P.; RL J. BACTERIOL. 175:2936-2942(1993). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; L13598; G289833; -. DR PIR; A36909; A36909. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 14 24 "HIGH" REGION. FT SIMILAR 255 259 "KMSKS" REGION. FT BINDING 258 258 ATP (BY SIMILARITY). FT NON_TER 370 370 SQ SEQUENCE 370 AA; 43093 MW; 5F53F41B CRC32; >SYE_CHLPS MRMAWENVRVRVAPSPTGDPHVGTAYMALFNEIFAKRFNGKMILRIEDTDQTRSRDDYEK NIFSALKWCGIQWDEGPDIGGPYGPYRQSERTEIYREYAELLLKTDYAYKCFATPKELEE MRAVATTLGYRGGYDRRYRYLSPEEIEARTREGQPYTIRLKVPLTGECVLDDYCKGRVVF PWADVDDQVLIKSDGFPTYHFANVVDDHLMGITHVLRGEEWLSSTPKHLLLYEAFGWEAP TFLHMPLLLNPDGTKLSKRKNPTSIFYYRDAGYVKEAFMNFLTLMGYSMEGDEEIYSLEK LIANFDPRRIGKSGAVFDTRKLDWMNKHYLTHEKSSESLLAKLKDWLINDEFFLKILPLC QSRITTLAEF SWISSPROT:SYE_BACSU ID SYE_BACSU STANDARD; PRT; 483 AA. AC P22250; DT 01-AUG-1991 (REL. 19, CREATED) DT 01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS). GN GLTX. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=168; RX MEDLINE; 91009314. RA BRETON R., WATSON D., YAGUCHI M., LAPOINTE J.; RL J. BIOL. CHEM. 265:18248-18255(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=168; RX MEDLINE; 94171772. RA GAGNON Y., BRETON R., PUTZER H., PELCHAT M., GRUNBERG-MANAGO M., RA LAPOINTE J.; RL J. BIOL. CHEM. 269:7473-7482(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=168; RX MEDLINE; 96051385. RA OGASAWARA N., NAKAI S., YOSHIKAWA H.; RL DNA RES. 1:1-14(1994). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; M55073; G143006; -. DR EMBL; L14580; G289282; -. DR EMBL; D26185; G467480; -. DR PIR; A36090; SYBSET. DR SUBTILIST; BG10154; GLTX. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 11 21 "HIGH" REGION. FT SIMILAR 252 256 "KMSKS" REGION. FT BINDING 255 255 ATP (BY SIMILARITY). SQ SEQUENCE 483 AA; 55722 MW; BBF75DA9 CRC32; >SYE_BACSU MGNEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQL NYLKWLGIDWDESVDVGGEYGPYRQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKERE EQIARGEMPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVPEGKVIAFNDIVKGEISFESD GIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFG HMTLIVNESRKKLSKRDESIIQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQF IEIFDVNRLSKSPALFDMHKLKWVNNQYVKKLDLDQVVELTLPHLQKAGKVGTELSAEEQ EWVRKLISLYHEQLSYGAEIVELTDLFFTDEIEYNQEAKAVLEEEQVPEVLSTFAAKLEE LEEFTPDNIKASIKAVQKETGHKGKKLFMPIRVAVTGQTHGPELPQSIELIGKETAIQRL KNI SWISSPROT:SYE_BACST ID SYE_BACST STANDARD; PRT; 489 AA. AC P22249; DT 01-AUG-1991 (REL. 19, CREATED) DT 01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS). GN GLTX. OS BACILLUS STEAROTHERMOPHILUS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91009314. RA BRETON R., WATSON D., YAGUCHI M., LAPOINTE J.; RL J. BIOL. CHEM. 265:18248-18255(1990). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; M55072; G143004; -. DR PIR; B36090; SYBSES. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 11 21 "HIGH" REGION. FT SIMILAR 253 257 "KMSKS" REGION. FT BINDING 256 256 ATP (BY SIMILARITY). SQ SEQUENCE 489 AA; 56183 MW; 44D27D77 CRC32; >SYE_BACST MAKDVRVGYAPSPTGHLHIGGARTALFNYLFARHHGGKMIVRIEDTDIERNVEGGEQSQL ENLQWLGIDYDESVDKDGGYGPYRQTERLDIYRKYVDELLEQGHAYKCFCTPEELERERE EQRAAGIAAPQYSGKCRRLTPEQVAELEAQGKPYTIRLKVPEGKTYEVDDLVRGKVTFES KDIGDWVIVKANGIPTYNFAVVIDDHLMEISHVFRGEEHLSNTPKQLMVYEYFGWEPPQF AHLTLIVNEQRKKLSKRDESIIQFVSQYKELGYLPEAMFNFFALLGWSPEGEEEIFSKDE LIRIFDVSRLSKSPSMFDTKKLTWMNNQYIKKLDLDRLVELALPHLVKAGRLPADMSDEQ RQWARDLIALYQEQMSYGAEIVPLSELFFKEEVEYEDEARQVLAEEQVPDVLSAFLAHVR DLDPFTADEIKAAIKAVQKATGQKGKKLFMPIRAAVTGQTHGPELPFAIQLLGKQKVIER LERALQEKF SWISSPROT:SYE_AZOBR ID SYE_AZOBR STANDARD; PRT; 451 AA. AC P45631; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE) DE (GLURS). GN GLTX. OS AZOSPIRILLUM BRASILENSE. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; OC AEROBIC, MOTILE, HELICAL AND/OR VIBRIOID. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SP245; RA COSTACURTA A., KEIJERS V., VANDERLEYDEN J.; RL SUBMITTED (NOV-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; U17699; G642524; -. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 9 19 "HIGH" REGION. FT SIMILAR 245 249 "KMSKS" REGION. FT BINDING 248 248 ATP (BY SIMILARITY). SQ SEQUENCE 451 AA; 50076 MW; F6BA9268 CRC32; >SYE_AZOBR MSVAVRFAPSPTGLLHVGNVRLALVNWLFARKAGGNFLLRLDDTDEERSKPEYAEGIERD LTWLGLTWDRFARESDRYGRYDEVAAALKASGRLYPCYETPEELNLKRASLVSQGRPPIY DRAALRLGDADRARLESEGRKRHWRFKLEHTPVEWTDLVRGPVHFEGAALSDPVLIREDG RPLYTLTSVVDDADLAITHVIRGEDHVANTAVQIQIFEALTNSEGGGVVPVFAHLPLLTD ATGQGLSKRLGSLSVASLREEEGIEPMALASLLAKLGTSDAIEPRLTLDELVAEFDIAKV SRATPKFDPEELLRLNARILHLLPFERVAGELAASVWMMPTPAFWEAVPNLSRVAEARDW WAVTHAPVARRRTIPLFLAEAAALLPEEPWDLSTWGTWTGAVKAKTGRKGKDLFLPLRRA LTGRDHGPELKNLLPLIGRTRAEKRLAGETA SWISSPROT:SYEP_HUMAN ID SYEP_HUMAN STANDARD; PRT; 1440 AA. AC P07814; DT 01-AUG-1988 (REL. 08, CREATED) DT 01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE MULTIFUNCTIONAL AMINOACYL-TRNA SYNTHETASE (CONTAINS: GLUTAMYL-TRNA DE SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE), AND PROLYL-TRNA DE SYNTHETASE (EC 6.1.1.15) (PROLINE--TRNA LIGASE)). GN EPRS OR QPRS OR GLNS. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91107633. RA FETT R., KNIPPERS R.; RL J. BIOL. CHEM. 266:1448-1455(1991). RN [2] RP PRELIMINARY SEQUENCE OF 96-887 FROM N.A. RC TISSUE=CERVIX CARCINOMA; RX MEDLINE; 88262551. RA THOEMMES P., FETT R., SCHRAY B., KUNZE N., KNIPPERS R.; RL NUCLEIC ACIDS RES. 16:5391-5406(1988). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- CATALYTIC ACTIVITY: ATP + L-PROLINE + TRNA(PRO) = AMP + CC PYROPHOSPHATE + L-PROLYL-TRNA(PRO). CC -!- SUBUNIT: COMPONENT OF THE MULTISYNTHETASE COMPLEX WHICH CONTAINS CC NINE DIFFERENT AA-TRNA SYNTHETASES. CC -!- SIMILARITY: THE N-TERMINAL DOMAIN BELONGS TO CLASS-I AMINOACYL- CC TRNA SYNTHETASES. CC -!- SIMILARITY: THE N-TERMINAL DOMAIN BELONGS TO CLASS-II AMINOACYL- CC TRNA SYNTHETASES. CC -!- SIMILARITY: CONTAINS 3 COPIES OF A DOMAIN THAT WE CALL "WHEP-TRS". CC -!- CAUTION: WAS ORIGINALLY THOUGHT TO BE A GLUTAMINYL-TRNA CC SYNTHETASE. CC -!- CAUTION: REF.2 DIFFERS FROM THAT SHOWN DUE TO A NUMBER OF SQUENCE CC ERRORS. DR EMBL; X54326; G31958; -. DR EMBL; X07466; G825664; ALT_SEQ. DR PIR; A38663; SYHUQT. DR HSSP; P00962; 1GTR. DR MIM; 138295; -. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. DR PROSITE; PS00179; AA_TRNA_LIGASE_II_1. DR PROSITE; PS00339; AA_TRNA_LIGASE_II_2. DR PROSITE; PS00762; WHEP_TRS. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING; KW MULTIFUNCTIONAL ENZYME; REPEAT. FT DOMAIN 92 687 GLUTAMYL-TRNA SYNTHETASE. FT DOMAIN 688 884 3 X 57 AA APPROXIMATE REPEATS. FT DOMAIN 935 1440 PROLYL-TRNA SYNTHETASE. FT SIMILAR 132 142 "HIGH" REGION. FT SIMILAR 360 364 "KMSKS" REGION. FT BINDING 363 363 ATP (BY SIMILARITY). FT DOMAIN 688 733 WHEP-TRS 1. FT DOMAIN 761 806 WHEP-TRS 2. FT DOMAIN 839 884 WHEP-TRS 3. FT DOMAIN 887 919 CHARGED. SQ SEQUENCE 1440 AA; 163026 MW; 1795F130 CRC32; >SYEP_HUMAN MEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNA AWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPG AEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVI LEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHR KNPIEKNLQMWEEMKKGSQFGHSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYN VYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTV LSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKI WAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFI EGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKFNLENKDYKKTTKVTWLAE TTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQL QRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPF KERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYK EKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINE AVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQG EVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKS EKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVI TKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKT HVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVR WEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTE KEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNS WGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRR RLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTV AENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEID CEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY SWISSPROT:SYEP_DROME ID SYEP_DROME STANDARD; PRT; 1714 AA. AC P28668; DT 01-DEC-1992 (REL. 24, CREATED) DT 01-DEC-1992 (REL. 24, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE MULTIFUNCTIONAL AMINOACYL-TRNA SYNTHETASE (CONTAINS: GLUTAMYL-TRNA DE SYNTHETASE (EC 6.1.1.17) (GLUTAMATE--TRNA LIGASE), AND PROLYL-TRNA DE SYNTHETASE (EC 6.1.1.15) (PROLINE--TRNA LIGASE)). GN AATS-GLUPRO. OS DROSOPHILA MELANOGASTER (FRUIT FLY). OC EUKARYOTA; METAZOA; ARTHROPODA; INSECTA; DIPTERA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92097547. RA CERINI C., KERJAN P., ASTIER M., GRATECOS D., MIRANDE M., SEMERIVA M.; RL EMBO J. 10:4267-4277(1991). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- CATALYTIC ACTIVITY: ATP + L-PROLINE + TRNA(PRO) = AMP + CC PYROPHOSPHATE + L-PROLYL-TRNA(PRO). CC -!- SUBUNIT: COMPONENT OF THE MULTISYNTHETASE COMPLEX WHICH CONTAINS CC NINE DIFFERENT AA-TRNA SYNTHETASES. CC -!- SIMILARITY: THE N-TERMINAL DOMAIN BELONGS TO CLASS-I AMINOACYL- CC TRNA SYNTHETASES. CC -!- SIMILARITY: THE N-TERMINAL DOMAIN BELONGS TO CLASS-II AMINOACYL- CC TRNA SYNTHETASES. CC -!- SIMILARITY: CONTAINS 6 COPIES OF A DOMAIN THAT WE CALL "WHEP-TRS". DR EMBL; M74104; G157564; -. DR PIR; S18644; S18644. DR HSSP; P00962; 1GTR. DR FLYBASE; FBGN0005674; AATS-GLUPRO. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. DR PROSITE; PS00179; AA_TRNA_LIGASE_II_1. DR PROSITE; PS00339; AA_TRNA_LIGASE_II_2. DR PROSITE; PS00762; WHEP_TRS. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING; KW MULTIFUNCTIONAL ENZYME; REPEAT. FT DOMAIN 170 754 GLUTAMYL-TRNA SYNTHETASE. FT DOMAIN 755 800 WHEP-TRS 1. FT DOMAIN 827 872 WHEP-TRS 2. FT DOMAIN 901 946 WHEP-TRS 3. FT DOMAIN 980 1025 WHEP-TRS 4. FT DOMAIN 1055 1100 WHEP-TRS 5. FT DOMAIN 1129 1173 WHEP-TRS 6. FT DOMAIN 1174 1180 POLY-GLY. FT DOMAIN 1207 1714 PROLYL-TRNA SYNTHETASE. FT SIMILAR 209 220 "HIGH" REGION. FT SIMILAR 438 442 "KMSKS" REGION. FT BINDING 441 441 ATP (BY SIMILARITY). SQ SEQUENCE 1714 AA; 189197 MW; 39A9D8E5 CRC32; >SYEP_DROME MSIKLKANLNNPPISGLATAHLINGTVPVEIVWSKEETSLQFPDNRLLVCHSNNDVLRAL ARAAPDYKLYGETAIERTQIDHWLSFSLTCEDDISWALSFLTSPLPPVTYLVANKLTIAD FALFNEMHSRYEFLAAKGIPQHVQRWYDLITAQPLIQKVLQSLPEDAKVKRSPQSSKEQT PAKTGERKQEGKFVDLPGAEMGKVVVRFPPEASGYLHIGHAKAALLNQYYALVCQGTLIM RFDDTNPAKETVEFENVILGDLEQLQIKPDVFTHTSNYFDLMLDYCVRLIKESKAYVDDT PPEQMKLEREQRVESANRSNSVEKNLSLWEEMVKGSEKGQNTACAAKIDMSSPNGCMRDP TIYRCKNEPHPRTGTKYKVYPTYDFACPIVDAIENVTHTLRTTEYHDRDDQFYWFIDALK LRKPYIWSYSRLNMTNTVLSKRKLTWFVDSGLVDGWDDPRFPTVRGIIRRGMTVEGLKEF IIAQGSSKSVVFMNWDKIWAFNKKVIDPIAPRYTALEKEKRVIVNVAGAKVERIQVSVHP KDESLGKKTVLLGPRIYIDYVDAEALKEGENATFINWGNILIKKVNKDASGNITSVDAAL NLENKDFKKTLKLTWLAVEDDPSAYPPTFCVYFDNIISKAVLGKDEDFKQFIGHKTRDEV PMLGDPELKKCKKGDIIQLQRRGFFKVDVAYLPPSGYTNVPSPIVLFSIPDGHTKDVPTS GLKVNAPDAKATKKASSPVSSSGQASELDSQITQQGDLVRDLKSKKAAKDQIDVAVKKLL ALKADYKSATGKDWKPGQTSATSAPVPAASSSSANDAVSVNASIVKQGDLVRDLKGKKAS KPEIDAAVKTLLELKAQYKTLTGQDWKPGTVPPTAAPSASAAPSVGGNDSVAQILSQITA QGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPGTTAPAPAAAPVKVKQEK NPDPASVLTVNTLLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWK PGTVAPAPTTVNVIDLTGGDSGSDVGSVLSKIQAQGDKIRKLKSEKAAKNVIDPEVKTLL ALKGEYKTLSGKDWTPDAKSEPAVVKKEASPVSMASPAKDELTQEINAQGEKVRAAKGNK AAKEVIDAEVAKLLALKAKYKEVTGTDFPVAGRGGGGGGGSAKKAPKEAQPKPAKPVKKE PADASGAVKKQTRLGLEATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRQWSFAIWKAI KTWFDAEITRMGVKECYFPIFVSKAVLEKEKTHIADFAPEVAWVTKSGDSDLAEPIAVRP TSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFADKE EAAKEVLDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGDYTTTVEAFISASGRAIQGAT SHHLGQNFSKMFEIVYEDPEKTQQKKYVYQNSWGITTRTIGVMIMVHADNQGLVLPPHVA CIQAIVVPCGITVNTKDDERAQLLDACKALEKRLVGGGVRCEGDYRDNYSPGWKFNHWEL KGVPLRLEVGPKDLKAQQLVAVRRDTGEKITIPLADVEKKIPALLETIHESMLNKAQEDM TSHTKKVTNWTDFCGFLEQKNILLAPFCGEISCEDKIKADSARGEEAEPGAPAMGAKSLC IPFDQPAPIAASDKCINPSCTNKPKFYTLFGRSY SWISSPROT:SYEM_YEAST ID SYEM_YEAST STANDARD; PRT; 536 AA. AC P48525; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE, MITOCHONDIRAL (EC 6.1.1.17) (GLUTAMATE--TRNA DE LIGASE) (GLURS). GN MSE1 OR YOL033W. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=D273-10B; RA TZAGOLOFF A.A., SHTANKO A.; RL SUBMITTED (JAN-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; L39015; G625182; -. DR SGD; L0002617; MSE1. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 53 61 "HIGH" REGION. SQ SEQUENCE 536 AA; 61569 MW; 7440425C CRC32; >SYEM_YEAST MIMLRIPTRSYCSPSKLIKGVGLSPLKKSLLSKKIKEDIHPSLPVRTRFAPSPTGFLHLG SLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSER KLIYDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSMASYDRCCAHLGEEEIKSK LAQGIPFTVRFKSPERYPTFTDLLHGQINLQPQVNFNDKRYDDLILVKSDKLPTYHLANV VDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIPLLTTVGDKKLSKRKGDMS ISDLKRQGVLPEALINFCALFGWSPPRDLASKKHECFSMEELETIFNLNGLTKGNAKVDD KKLWFFNKHFLQKRILNPSTLRELVDDIMPSLESIYNTSTISREKVAKILLNCGGSLSRI NDFHDEFYYFFEKPKYNDNDAVTKFLSKNESRHIAHLLKKLGQLQEGTDAQEVESMVETM YYENGFSRKVTYQAMRFALAGCHPGAKIAAMIDILGIKESNKRLSEGLQFLQREKK SWISSPROT:SYEC_YEAST ID SYEC_YEAST STANDARD; PRT; 724 AA. AC P46655; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA SYNTHETASE, CYTOPLASMIC (EC 6.1.1.17) (GLUTAMATE--TRNA DE LIGASE) (GLURS) (P85). GN YGL245W OR G0583 OR HRB724. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RA FRANTZ J.D., GILBERT W.; RL SUBMITTED (JUL-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RA VANDENBOL M., DURAND P., PORTETELLE D., HILGER F.; RL SUBMITTED (MAY-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP SEQUENCE OF 1-146 FROM N.A. RC STRAIN=S288C / FY1679; RA COISSAC E., MAILLIER E., NETTER P.; RL SUBMITTED (JAN-1996) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = AMP + CC PYROPHOSPHATE + L-GLUTAMYL-TRNA(GLU). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASES. DR EMBL; U32265; G1008483; -. DR EMBL; Z49149; G793866; -. DR EMBL; Z72767; E243901; -. DR EMBL; X94357; E215626; -. DR PROSITE; PS00178; AA_TRNA_LIGASE_I. KW AMINOACYL-TRNA SYNTHETASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT SIMILAR 226 235 "HIGH" REGION. FT SIMILAR 453 457 "KMSKS" REGION. FT BINDING 456 456 ATP (BY SIMILARITY). FT CONFLICT 225 225 E -> D (IN REF. 1). FT CONFLICT 489 489 V -> A (IN REF. 1). FT CONFLICT 526 526 P -> S (IN REF. 1). FT CONFLICT 562 562 V -> M (IN REF. 1). FT CONFLICT 714 724 GKSVNKYGAKK -> VNLSTSMVQRNKHHISNVYTYLCYFS FT TSTF (IN REF. 1). SQ SEQUENCE 724 AA; 82662 MW; 1A14885A CRC32; >SYEC_YEAST MTKLFSKVKESIEGIKMPSTLTINGKAPIVAYAELIAARIVNALAPNSIAIKLVDDKKAP AAKLDDATEDVFNKITSKFAAIFDNGDKEQVAKWVNLAQKELVIKNFAKLSQSLETLDSQ LNLRTFILGGLKYSAADVACWGALRSNGMCGSIIKNKVDVNVSRWYTLLEMDPIFGEAHD FLSKSLLELKKSANVGKKKETHKANFEIDLPDAKMGEVVTRFPPEPSGYLHIGHAKAALL NQYFAQAYKGKLIIRFDDTNPSKEKEEFQDSILEDLDLLGIKGDRITYSSDYFQEMYDYC VQMIKDGKAYCDDTPTEKMREERMDGVASARRDRSVEENLRIFTEEMKNGTEEGLKNCVR AKIDYKALNKTLRDPVIYRCNLTPHHRTGSTWKIYPTYDFCVPIVDAIEGVTHALRTIEY RDRNAQYDWMLQALRLRKVHIWDFARINFVRTLLSKRKLQWMVDKDLVGNWDDPRFPTVR GVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPIAPRHTAIVNPVKIHLE GSEAPQEPKIEMKPKHKKNPAVGEKKVIYYKDIVVDKDDADVINVDEEVTLMDWGNVIIT KKNDDGSMVAKLNLEGDFKKTKHKLTWLADTKDVVPVDLVDFDHLITKDRLEEDESFEDF LTPQTEFHTDAIADLNVKDMKIGDIIQFERKGYYRLDALPKDGKPYVFFTIPDGKSVNKY GAKK TREMBL:Q59292 ID Q59292 PRELIMINARY; PRT; 515 AA. AC Q59292; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE NAC(P)H-DEPENDENT GLUTAMYL-TRNA REDUCTASE (EC 6.1.1.17) DE (GLUTAMATE--TRNA LIGASE) (GLUTAMYL-TRNA SYNTHETASE). GN HEMA. OS CLOSTRIDIUM JOSUI. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FERM P-9684; RX MEDLINE; 95394829. RA FUJINO E., FUJINO T., KARITA S., OHMIYA K.; RL J. BACTERIOL. 177:5169-5175(1995). CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = CC AMP + DIPHOSPHATE + L-GLUTAMYL- TRNA(GLU). DR EMBL; D28503; G536875; -. KW LIGASE. SQ SEQUENCE 515 AA; 58368 MW; D42953DF CRC32; >Q59292 MQLGRHNSGSIKKRLEMYILSIISASLDYKSAAIDIRERFSYTSTRIREILRRIKAADGV SGAVLLCTCNRTELYISGDNIENMNPALLLCQLSGEEDHKSLMTLFSIRHDSEAIFHLME VACGLQSMVLFEDRVITQVKNAAAISREEKTIDSTLETLFRLCITAAKKAKTEIKVKAVP TSAAERAITELSKKYCFTDKRILVIGNGEIGRLCCKKLIELGAEITITLRKYKHGEIIIP VGCNTIPYDEREEVLPLSDVVISATTSPHFTITYDMIEKLERKPEIFVDLALPRDIESSI SNFTGVELYNLDRFYTDYSVLNQKEVSKIREIINHFILQFEKWKDYREEAAFTKIPDLHN DTLYGRFPLFIDLSGKKVLVVGGGEIATRRVKTLLRFGADIYLVAPHLTSELQEMLNCKL INYREGYYESQDIQNMFLVIAATNDRETNHKVYLDAKEKGIQMSIADCREECSFYFPAIF EFDGIVGGLVSQNGDNHSLVKSVAEQIRKIGQATD TREMBL:Q43794 ID Q43794 PRELIMINARY; PRT; 569 AA. AC Q43794; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE GLUTAMATE--TRNA LIGASE (EC 6.1.1.17) (GLUTAMYL-TRNA SYNTHETASE). OS NICOTIANA TABACUM (COMMON TOBACCO). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC SOLANALES; SOLANACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. SR1; TISSUE=LEAF; RA ANDERSEN R.V.; RL SUBMITTED (DEC-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = CC AMP + DIPHOSPHATE + L-GLUTAMYL- TRNA(GLU). DR EMBL; X83524; G603867; -. KW LIGASE; CHLOROPLAST. SQ SEQUENCE 569 AA; 63338 MW; DCDDDCDE CRC32; >Q43794 MATLAAAPWFRVRLIPELKNSQSLLYCRGNHSYRQSLCSRRRSFSVYASAGDGGDVRVRF APSPTGNLHVGGARTALFNYLYARAKGGKFILRIEDTDLERSTKESEEAVLRDLSWLGPA WDEGPGIGGEYGPYRQSERNALYKQFAEKLLQSGHVYRCFCSNEELEKMKEIAKLKQLPP VYTGRWASATEEEVVEELAKGTPYTYRFRVPKEGSLKIDDLIRGEVSWNLDTLGDFVIMR SNGQPVYNFCVTVDDATMAISHVIRAEEHLPNTLRQALIYKALGFPMPHFAHVSLILAPD RSKLSKRHGATSVGQFRDMGYLPQAMVNYLALLGWGDGTENEFFTLEQLVEKFTIERVNK SGAIFDSTKLRWMNGQHLRSLPSEELNRIIGERWKDAGIATESQGIFIQDAVLLLKDGID LITDSEKALSSLLSYPLYETLASAEGKPILEDGVSEVAKSLLAAYDSGELSGALAEGQPG WQKWAKNFGKLLKRKGKSLFMPLRVLLTGKLHGPDIGATTVLLYKAGTSGSVVPQAGFVT FDERFKILREVQWESFSTDVPLSAGAVTR TREMBL:Q43768 ID Q43768 PRELIMINARY; PRT; 560 AA. AC Q43768; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE GLUTAMATE--TRNA LIGASE PRECURSOR (EC 6.1.1.17) DE (GLUTAMYL-TRNA SYNTHETASE). OS HORDEUM VULGARE (BARLEY). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE; OC CYPERALES; GRAMINEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. SVALF'S BONUS; TISSUE=LEAF; RA ANDERSEN R.V.; RL SUBMITTED (DEC-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: ATP + L-GLUTAMATE + TRNA(GLU) = CC AMP + DIPHOSPHATE + L-GLUTAMYL- TRNA(GLU). DR EMBL; X83523; G603849; -. KW SIGNAL; LIGASE; CHLOROPLAST. FT SIGNAL 1 34 POTENTIAL. SQ SEQUENCE 560 AA; 61862 MW; 58151C7E CRC32; >Q43768 MAASNFMGSSARLRVGLLPSVTPRLSRRALATRASADSGGSGPVRVRFAPSPTGNLHVGG ARTALFNYLFARSRGGKFVLRVEDTDLERSTKKSEEAVLTDLSWLGLDWDEGPDIGGDFG PYRQSERNALYKEHAQKLMESGAVYRCFCSNEELEKMKETANRMKIPPVYMGKWATASDA EVQQELEKGTPYTYRFRVPKEGSLKINDLIRGEVSWNLNTLGDFVIMRSNGQPVYNFCVT VDDATMRISHVIRAEEHLPNTLRQALIYKALGFAMPLFAHVSLILAPDKSKLSKRHGATS VGQYKEMGYLPQAMVNYLALLGWGDGTENEFFTIDDLVEKFTIDRVNKSGAVFDATKLKW MNGQHLRSLPSDLLIKDFEDQWRSTGILLESESGFAKEAAELLKEGIDLITDADAALCKL LSYPLHETLSSDEAKSVVEDKLSEVASGLISAYDSGELDQALAEGHDGWKKWVKSFGKTH KRKGKSLFMPLRVLLTGKLHGPAMDSTVILVHKAGTSGAVAPQSGFVSLDERFKILKEVN WESLQKQQESPVESAVPAAS TREMBLNEW:ECD869_14 ID ECD869_14 standard; PRT; 471 AA. AC D90869; DR EMBL; D90869; ECD869. DE gene: "gltX"; product: "glutamate--tRNA ligase (EC 6.1.1.17)"; DE E.coli genomic DNA, Kohara clone #416(54.1-54.5 min.). OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Plasmid pColK-K235 FT CDS complement(12101..13516) FT /gene="gltX" FT /note="similar to [PIR Accession Number A25956]" FT /codon_start=1 FT /product="glutamate--tRNA ligase (EC 6.1.1.17)" FT /transl_table=11 FT /db_xref="PID:g1799814" FT /translation="MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTD FT LERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKER FT LEALREEQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFS FT NQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVP FT VYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREE FT MIKYFTLNAVSKSASAFNTDKLLWLNHHYINALPPEYVATHLQWHIEQENIDTRNGPQL FT ADLVKLLGERCKTLKEMAQSCRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDKLAAIT FT DWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERIN FT KALDFIAERENQQ" SQ Sequence 471 BP; >ECD869_14 MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDG MNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPR YDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPT YNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSK RHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNT DKLLWLNHHYINALPPEYVATHLQWHIEQENIDTRNGPQLADLVKLLGERCKTLKEMAQS CRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDKLAAITDWTAENVHHAIQATADELEVG MGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALDFIAERENQQ