|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
4-481 |
0e+00 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 731.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDEsvdvggeyGPY 83
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 84 RQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREEQIARGEMPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVPEGK 163
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 164 VIAFNDIVKGEISFESDGIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGHMT 243
Cdd:TIGR00464 153 VVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 244 LIVNESRKKLSKRDEsiIQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHKLKW 323
Cdd:TIGR00464 233 MILDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 324 VNNQYVKKLDLDQVVELTLPHLQKagKVGTELSAEEQewVRKLISLYHEQLSYGAEIVELTDLFFTDEIEYNQEAKAVLE 403
Cdd:TIGR00464 311 LNAHYIKELPDEELFELLDPHLKS--LVNTDTLNREQ--LAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490534505 404 EEQVPEVLSTFAAKLEELEEFTPDNIKASIKAVQKETGHKGKKLFMPIRVAVTGQTHGPELPQSIELIGKETAIQRLK 481
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLK 464
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-482 |
0e+00 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 670.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 1 MGNEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDEsvdvggey 80
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 81 GPYRQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREEQIARGEMPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVP 160
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 161 EGKvIAFNDIVKGEISFESDGIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFG 240
Cdd:COG0008 153 EEG-VVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 241 HMTLIVNESRKKLSKRDESIiqFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHK 320
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 321 LKWVNNQYVKKLDLDQVVELTLPHLQKAGKvgtelsaeeQEWVRKLISLYHEQLSYGAEIVELTDLFFTDEIEyNQEAKA 400
Cdd:COG0008 310 LVWLNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIERED-EKAAKK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 401 VLEEEQVPEVLSTFAAKLEELEEFTPDNIKASIKAVQKETGHKGKKLFMPIRVAVTGQTHGPELPQSIELIGKETAIQRL 480
Cdd:COG0008 380 RLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERL 459
|
..
gi 490534505 481 KN 482
Cdd:COG0008 460 GY 461
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-475 |
1.90e-174 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 500.81 E-value: 1.90e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 2 GNEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDESVDVGGEYG 81
Cdd:PLN02627 43 GGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 82 PYRQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREEQIARGEMPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVPE 161
Cdd:PLN02627 123 PYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 162 GKVIAFNDIVKGEISFESDGIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGH 241
Cdd:PLN02627 203 EGSVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 242 MTLIVNESRKKLSKRDESiiQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHKL 321
Cdd:PLN02627 283 VSLILAPDRSKLSKRHGA--TSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 322 KWVNNQYVKKLDLDQVVELTLPHLQKAGKvgteLSAEEQEWVRKLISLyheqLSYGAEIVELTDLFFTDEIEYN------ 395
Cdd:PLN02627 361 KWMNGQHLRLLPEEELVKLVGERWKSAGI----LKESDGSFVKEAVEL----LKDGIELVTDADKELLNLLSYPlaatls 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 396 -QEAKAVLE---EEQVPEVLST-----FAAKLEEleefTPDNIKASIKAVQKETGHKGKKLFMPIRVAVTGQTHGPELPQ 466
Cdd:PLN02627 433 sPEAKTVVEdnfSEVADALIAAydsgeLAAALEE----GHDGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGE 508
|
....*....
gi 490534505 467 SIELIGKET 475
Cdd:PLN02627 509 SLVLLHKAG 517
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
4-323 |
3.24e-165 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 468.72 E-value: 3.24e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDesvdvggeYGPY 83
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 84 RQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREEQIARGE--MPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVPE 161
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSpsRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 162 GKVIAFNDIVKGEISFESDGIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGH 241
Cdd:pfam00749 153 ESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 242 MTLIVNESRKKLSKRDESIIQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHKL 321
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
..
gi 490534505 322 KW 323
Cdd:pfam00749 313 DW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
4-331 |
9.06e-147 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 418.91 E-value: 9.06e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDESVDVGGEYGPY 83
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 84 RQSERNDIYKVYYEELLEKGlaykcycteeelekereeqiargemprysgkhrdltqeeqekfiaegrkpsirfrvpegk 163
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 164 viafndivkgeisfesdgigdfvivkkDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGHMT 243
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 244 LIVNESRKKLSKRDESiiQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHKLKW 323
Cdd:cd00808 154 LILNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDW 231
|
....*...
gi 490534505 324 VNNQYVKK 331
Cdd:cd00808 232 LNGQYIRE 239
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
4-481 |
0e+00 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 731.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDEsvdvggeyGPY 83
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 84 RQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREEQIARGEMPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVPEGK 163
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 164 VIAFNDIVKGEISFESDGIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGHMT 243
Cdd:TIGR00464 153 VVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 244 LIVNESRKKLSKRDEsiIQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHKLKW 323
Cdd:TIGR00464 233 MILDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 324 VNNQYVKKLDLDQVVELTLPHLQKagKVGTELSAEEQewVRKLISLYHEQLSYGAEIVELTDLFFTDEIEYNQEAKAVLE 403
Cdd:TIGR00464 311 LNAHYIKELPDEELFELLDPHLKS--LVNTDTLNREQ--LAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490534505 404 EEQVPEVLSTFAAKLEELEEFTPDNIKASIKAVQKETGHKGKKLFMPIRVAVTGQTHGPELPQSIELIGKETAIQRLK 481
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLK 464
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-482 |
0e+00 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 670.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 1 MGNEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDEsvdvggey 80
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 81 GPYRQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREEQIARGEMPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVP 160
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 161 EGKvIAFNDIVKGEISFESDGIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFG 240
Cdd:COG0008 153 EEG-VVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 241 HMTLIVNESRKKLSKRDESIiqFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHK 320
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 321 LKWVNNQYVKKLDLDQVVELTLPHLQKAGKvgtelsaeeQEWVRKLISLYHEQLSYGAEIVELTDLFFTDEIEyNQEAKA 400
Cdd:COG0008 310 LVWLNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIERED-EKAAKK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 401 VLEEEQVPEVLSTFAAKLEELEEFTPDNIKASIKAVQKETGHKGKKLFMPIRVAVTGQTHGPELPQSIELIGKETAIQRL 480
Cdd:COG0008 380 RLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERL 459
|
..
gi 490534505 481 KN 482
Cdd:COG0008 460 GY 461
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-475 |
1.90e-174 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 500.81 E-value: 1.90e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 2 GNEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDESVDVGGEYG 81
Cdd:PLN02627 43 GGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 82 PYRQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREEQIARGEMPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVPE 161
Cdd:PLN02627 123 PYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 162 GKVIAFNDIVKGEISFESDGIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGH 241
Cdd:PLN02627 203 EGSVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 242 MTLIVNESRKKLSKRDESiiQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHKL 321
Cdd:PLN02627 283 VSLILAPDRSKLSKRHGA--TSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 322 KWVNNQYVKKLDLDQVVELTLPHLQKAGKvgteLSAEEQEWVRKLISLyheqLSYGAEIVELTDLFFTDEIEYN------ 395
Cdd:PLN02627 361 KWMNGQHLRLLPEEELVKLVGERWKSAGI----LKESDGSFVKEAVEL----LKDGIELVTDADKELLNLLSYPlaatls 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 396 -QEAKAVLE---EEQVPEVLST-----FAAKLEEleefTPDNIKASIKAVQKETGHKGKKLFMPIRVAVTGQTHGPELPQ 466
Cdd:PLN02627 433 sPEAKTVVEdnfSEVADALIAAydsgeLAAALEE----GHDGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGE 508
|
....*....
gi 490534505 467 SIELIGKET 475
Cdd:PLN02627 509 SLVLLHKAG 517
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
4-323 |
3.24e-165 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 468.72 E-value: 3.24e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDesvdvggeYGPY 83
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 84 RQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREEQIARGE--MPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVPE 161
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSpsRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 162 GKVIAFNDIVKGEISFESDGIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGH 241
Cdd:pfam00749 153 ESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 242 MTLIVNESRKKLSKRDESIIQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHKL 321
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
..
gi 490534505 322 KW 323
Cdd:pfam00749 313 DW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
4-331 |
9.06e-147 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 418.91 E-value: 9.06e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDESVDVGGEYGPY 83
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 84 RQSERNDIYKVYYEELLEKGlaykcycteeelekereeqiargemprysgkhrdltqeeqekfiaegrkpsirfrvpegk 163
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 164 viafndivkgeisfesdgigdfvivkkDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGHMT 243
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 244 LIVNESRKKLSKRDESiiQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHKLKW 323
Cdd:cd00808 154 LILNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDW 231
|
....*...
gi 490534505 324 VNNQYVKK 331
Cdd:cd00808 232 LNGQYIRE 239
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
5-331 |
4.62e-83 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 256.25 E-value: 4.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 5 VRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDEsvdvggeyGPYR 84
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDE--------GPYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 85 QSERNDIYKVYYEELLEKGlaykcycteeelekereeqiargemprysgkhrdltqeeqekfiaegrkpsirfrvpegkv 164
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 165 iafndivkgeisfesdgigdfvivkkdGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGHMTL 244
Cdd:cd00418 93 ---------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPR 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 245 IVNESRKKLSKRDesIIQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHKLKWV 324
Cdd:cd00418 146 LLLEDGTKLSKRK--LNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWL 223
|
....*..
gi 490534505 325 NNQYVKK 331
Cdd:cd00418 224 NREYIRE 230
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
8-316 |
3.75e-80 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 251.31 E-value: 3.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 8 RYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDESVdvggeygpYRQSE 87
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPV--------LYQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 88 RNDIYKVYYEELLEKGLAYKCYCTeeelekerEEQIARGEM------PRYSGKHRDLTQEEQekfiaegRKPSIRFRVPE 161
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCS--------RKEIAAAAPappdggGIYPGTCRDLLHGPR-------NPPAWRLRVPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 162 GkVIAFNDIVKGEISFESDG-IGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFG 240
Cdd:PRK05710 146 A-VIAFDDRLQGRQHQDLALaVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490534505 241 HMTLIVNESRKKLSKRDESiiQFIEQYKELGYLPEALfnfiGLLGWSPVGE--EELFTKEQFIEIFDVNRLSKSPALF 316
Cdd:PRK05710 225 HLPLVLNADGQKLSKQNGA--PALDAAGPLPVLAAAL----RFLGQPPPAAdaSVEELLAQAVAHWDLTRLPRQAEIN 296
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
4-281 |
2.53e-49 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 177.35 E-value: 2.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTD--KKRNIEGGEQSQLNYLKWLGIDWDESvdvggeyg 81
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWDEV-------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 82 pYRQSERNDIYKVYYEELLEKGLAYKCYCTeeelekereeqiaRGEMPRY--SGK---HRDLTQEEQ----EKFIAEgrk 152
Cdd:PRK04156 173 -VIQSDRLEIYYEYARKLIEMGGAYVCTCD-------------PEEFKELrdAGKpcpHRDKSPEENlelwEKMLDG--- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 153 psirfRVPEGKVIAfndIVKGEISFESDGIGDFV---IVK----KDGT-----PTYNFAVAIDDYLMKMTHVLRGEDHIS 220
Cdd:PRK04156 236 -----EYKEGEAVV---RVKTDLEHPNPSVRDWVafrIVKtphpRVGDkyrvwPTYNFAVAVDDHLLGVTHVLRGKDHID 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 221 NTPKQIMIYQAFGWDIP---QFGHMTLivneSRKKLSKrdESIIQFIEQYKELGY----------------LPEALFNFI 281
Cdd:PRK04156 308 NTEKQRYIYDYFGWEYPetiHYGRLKI----EGFVLST--SKIRKGIEEGEYSGWddprlptlralrrrgiLPEAIRELI 381
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
4-289 |
1.21e-39 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 143.26 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGE--QSQLNYLKWLGIDWDESvdvggeyg 81
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEayDMIPEDLEWLGVKWDEV-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 82 pYRQSERNDIYKVYYEELLEKGLAYkcycteeelekereeqiargemprysgKHRDltqeeqekfiaegrkpsirfrvpe 161
Cdd:cd09287 73 -VIASDRIELYYEYARKLIEMGGAY---------------------------VHPR------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 162 gkviafndivkgeisfesdgIGDFVIVkkdgTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGH 241
Cdd:cd09287 101 --------------------TGSKYRV----WPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIH 156
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490534505 242 --------MTLIVNESRK-----KLSKRDESIIQFIEQYKELGYLPEALFNFIGLLGWSPV 289
Cdd:cd09287 157 wgrlkiegGKLSTSKIRKgiesgEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQT 217
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
336-483 |
5.18e-39 |
|
Anticodon binding domain; This entry represents the anticodon binding domain found at the C-terminus of the class-I glutamyl tRNA synthetase enzyme.
Pssm-ID: 466020 [Multi-domain] Cd Length: 148 Bit Score: 138.48 E-value: 5.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 336 QVVELTLPHLQKAGkvgteLSAEEQEWVRKLISLYHEQLSYGAEIVELTDLFFTDEIEYNQEA----KAVLEEEQVPEVL 411
Cdd:pfam19269 1 ELAELALPYLEEAG-----LDGLDDEYLKKVVPLLKERAETLSELAELADFFFELPLEYDEEAyakkKMKTNKEESLEVL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490534505 412 STFAAKLEELEEFTPDNIKASIKAVQKETGHKGKKLFMPIRVAVTGQTHGPELPQSIELIGKETAIQRLKNI 483
Cdd:pfam19269 76 QELLPRLEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKA 147
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
4-285 |
6.81e-39 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 148.43 E-value: 6.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDESVdvggeygpy 83
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVV--------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 84 RQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREeqiaRGEmprySGKHRDLTQEEQEKfiaegrkpsIRFRVPEGK 163
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRN----RGE----ACHCRDRSVEENLE---------RWEEMLEGK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 164 VIAFNDIV--KGEISFESDGIGDFVIVKKDGT------------PTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIY 229
Cdd:TIGR00463 227 EEGGSVVVrvKTDLKHKNPAIRDWVIFRIVKTphprtgdkyrvyPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIY 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 230 QAFGWDIPQFGHMTLI-VNESRKKLSKR-------------DESIIQFIEQYKELGYLPEALFNFIGLLG 285
Cdd:TIGR00463 307 RYFGWEPPEFIHWGRLkIDDVRALSTSSarkgilrgeysgwDDPRLPTLRAIRRRGIRPEAIRKFMLSIG 376
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
4-221 |
7.67e-19 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 89.25 E-value: 7.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDesvdvggeYGPY 83
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD--------VGPT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 84 RQSERNDIYKVYYEELLEKGLAykcYCTeeelekereeQIARGEMP--RYSG---KHRDLTQEEQEKFIAEGRKPSirfr 158
Cdd:PTZ00402 124 YSSDYMDLMYEKAEELIKKGLA---YCD----------KTPREEMQkcRFDGvptKYRDISVEETKRLWNEMKKGS---- 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490534505 159 vPEGKVIAFNdiVKGEISFESDGIGDFVIVK-------KDGT-----PTYNFAVAIDDYLMKMTHVLR-GEDHISN 221
Cdd:PTZ00402 187 -AEGQETCLR--AKISVDNENKAMRDPVIYRvnltphaRQGTkykayPTYDFCCPIIDSVEGVTHALRtNEYHDRN 259
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
4-256 |
5.42e-15 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 77.36 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDESVDVGGEYGPY 83
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 84 RQserndiykvYYEELLEKGLAYkcycteeeLEKEREEQIARGEMPRYSGKHRDLTQEEQEKFIAE---GRKpsirfrvp 160
Cdd:PLN03233 91 RC---------YAIILIEEGLAY--------MDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEmcsGKE-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 161 EGKVIAfndiVKGEISFESDG--IGDFVIVKKDGT------------PTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQI 226
Cdd:PLN03233 146 EGGAWC----LRAKIDMQSDNgtLRDPVLFRQNTTphhrsgtaykayPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFF 221
|
250 260 270
....*....|....*....|....*....|
gi 490534505 227 MIYQAFGWDIPQFgHMTLIVNESRKKLSKR 256
Cdd:PLN03233 222 WIQKALGLRRPRI-HAFARMNFMNTVLSKR 250
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
4-106 |
2.65e-14 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 72.28 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDESvdvggeygpY 83
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV---------T 71
|
90 100
....*....|....*....|...
gi 490534505 84 RQSERNDIYKVYYEELLEKGLAY 106
Cdd:cd00807 72 YASDYFDQLYEYAEQLIKKGKAY 94
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
4-72 |
1.99e-10 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 63.20 E-value: 1.99e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTD-KKRNIEGGEqsqlNYLK---WLGIDWDE 72
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNpSKESDEFVE----NILKdieTLGIKYDA 281
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
4-106 |
2.33e-10 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 62.82 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTdkkrNIEGGEQSQLNYLK----WLGIDWDESVdvgge 79
Cdd:PRK14703 31 RVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDT----NPETEDTEYVEAIKddvrWLGFDWGEHL----- 101
|
90 100
....*....|....*....|....*..
gi 490534505 80 ygpYRQSERNDIYKVYYEELLEKGLAY 106
Cdd:PRK14703 102 ---YYASDYFERMYAYAEQLIKMGLAY 125
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
2-213 |
1.29e-07 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 54.38 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 2 GNEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDT----DKKRNIEGGEQsqlnYLKWLGidWDesvdvg 77
Cdd:PLN02859 262 GGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTnpeaEKKEYIDHIEE----IVEWMG--WE------ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 78 geygPYRQSERNDIYKVYYE---ELLEKGLAYKCYCTEEelekereeqiargEMPRYSGKH-----RDLTQEEQEKFIAE 149
Cdd:PLN02859 330 ----PFKITYTSDYFQELYElavELIRRGHAYVDHQTPE-------------EIKEYREKKmnspwRDRPIEESLKLFED 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490534505 150 GRkpsiRFRVPEGKVIA----------FN--DIVKGEISFESD-GIGDfvivKKDGTPTYNFAVAIDDYLMKMTHVL 213
Cdd:PLN02859 393 MR----RGLIEEGKATLrmkqdmqndnFNmyDLIAYRIKFTPHpHAGD----KWCIYPSYDYAHCIVDSLENITHSL 461
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
3-108 |
5.00e-07 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 52.03 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490534505 3 NEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTD-KKRNIEGGEqSQLNYLKWLGIDWDESVDVGGEYg 81
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNpEKEDQEYVD-SIKEDVRWLGFDWSGELRYASDY- 105
|
90 100
....*....|....*....|....*..
gi 490534505 82 pYRQserndIYKvYYEELLEKGLAYKC 108
Cdd:PRK05347 106 -FDQ-----LYE-YAVELIKKGKAYVD 125
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
8-70 |
7.23e-06 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 48.44 E-value: 7.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490534505 8 RYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTdkkrNIEGGEQ----SQLNYLKWLGI--DW 70
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDT----NPETEEQvyidAIMEMVKWMGWkpDW 119
|
|
| |
