|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
37-521 |
3.58e-165 |
|
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: 476.21 E-value: 3.58e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE--------GPYY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQMPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQAAP 196
Cdd:COG0008 77 QSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 197 AFEDLVYGWNRHDVASVeGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFAHLPL 276
Cdd:COG0008 157 VFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 277 LLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTRVTCHSALLDLEKLPEFNR 356
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 357 LHLQRLVNNEsqrcqlveklqalVEEAFGSQLQNRDVlnPIYMERILLLRQGHICRLQDLVsPVYSYLWTRPS---VGRA 433
Cdd:COG0008 316 PYIRALDDEE-------------LAELLAPELPEAGI--REDLERLVPLVRERAKTLSELA-ELARFFFIEREdekAAKK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 434 QLDAisEEVDVIAKRVLGLLERSGmSLTQDMLSGELKKLSEGLeGTKHSNVMKLLRVALSGQQQGPPVAEMMLSLGPKEV 513
Cdd:COG0008 380 RLAP--EEVRKVLKAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERV 455
|
....*...
gi 109127906 514 RERIQKVV 521
Cdd:COG0008 456 FERLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
37-519 |
2.68e-148 |
|
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: 433.32 E-value: 2.68e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQMPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQAA 195
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 196 PAFEDLVYG---WNRHDVasveGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFA 272
Cdd:TIGR00464 154 VSFNDQVRGeitFQNSEL----DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 273 HLPLLLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTRVTCHSALLDLEKLP 352
Cdd:TIGR00464 230 HLPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 353 EFNRLHLQRLVNNEsqrcqLVEKLQALVEeafgsQLQNRDVLNPIYMERILLLRQGHICRLQDLVSPVYSYLWTRPSVgr 432
Cdd:TIGR00464 310 WLNAHYIKELPDEE-----LFELLDPHLK-----SLVNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEV-- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 433 aQLDAISEEVDVIAKRVLGLLERSGMSL---TQDMLSGELKKLSEgLEGTKHSNVMKLLRVALSGQQQGPPVAEMMLSLG 509
Cdd:TIGR00464 378 -DEDAFKKHLKKNVKEVLEALKKKLQALeewTADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKGHGPDLAQILELIG 455
|
490
....*....|
gi 109127906 510 PKEVRERIQK 519
Cdd:TIGR00464 456 KTESIKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
36-361 |
6.08e-131 |
|
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: 380.39 E-value: 6.08e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 36 AVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDESPRRGGPAGPY 115
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 116 QQSQRLELYAQATEALLKTGaaypcfcspqrlellkkealrnhqmprydnrcrnmsqeqvaqklakdpkpairfrleqaa 195
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 196 pafedlvygwnrhdvasvegdpvimksDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFAHLP 275
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 276 LLLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTRVTCHSALLDLEKLPEFN 355
Cdd:cd00808 154 LILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233
|
....*.
gi 109127906 356 RLHLQR 361
Cdd:cd00808 234 GQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
37-351 |
3.08e-104 |
|
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: 315.03 E-value: 3.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNH--QMPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQA 194
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGspSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 195 AP-AFEDLVYGwnRHDVASVEGDP-VIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFA 272
Cdd:pfam00749 154 SPyVFRDPVRG--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 273 HLPLLLNRDGSKLSKRQGDI--FLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTRVTCHSALLDLEK 350
Cdd:pfam00749 232 HEYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKK 311
|
.
gi 109127906 351 L 351
Cdd:pfam00749 312 L 312
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
16-509 |
8.89e-100 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 311.29 E-value: 8.89e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 16 AASGRRVGRREARLGTGPGVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDML 95
Cdd:PLN02627 25 RSSRRRFSVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 96 EWAGIPPDESPRRGGPAGPYQQSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQMPRYDNRCRNMSQEQV 175
Cdd:PLN02627 105 KWLGLDWDEGPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 176 AQKLAKDPKPAIRFRL-EQAAPAFEDLVYG---WNrhdvASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWL 251
Cdd:PLN02627 185 QAELAKGTPYTYRFRVpKEGSVKIDDLIRGevsWN----TDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 252 VSTAKHLLLYQALGWHPPHFAHLPLLLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELI 331
Cdd:PLN02627 261 PNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 332 TQFNLTRVTCHSALLDLEKLPEFNRLHLQRLVnnesqrcqlVEKLQALVEEafgsQLQNRDVL----NPIYMERILLLRQ 407
Cdd:PLN02627 341 EKFSIDRINKSGAVFDSTKLKWMNGQHLRLLP---------EEELVKLVGE----RWKSAGILkesdGSFVKEAVELLKD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 408 GhICRLQDLVSPVYSYL-------WTRPSVGRAQLDAISEevdvIAKRVLGLLErSGmSLTQDMLSGE------LKKLSE 474
Cdd:PLN02627 408 G-IELVTDADKELLNLLsyplaatLSSPEAKTVVEDNFSE----VADALIAAYD-SG-ELAAALEEGHdgwqkwVKAFGK 480
|
490 500 510
....*....|....*....|....*....|....*
gi 109127906 475 GLeGTKHSNVMKLLRVALSGQQQGPPVAEMMLSLG 509
Cdd:PLN02627 481 AL-KRKGKRLFMPLRVALTGKMHGPDVGESLVLLH 514
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
37-521 |
3.58e-165 |
|
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: 476.21 E-value: 3.58e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE--------GPYY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQMPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQAAP 196
Cdd:COG0008 77 QSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 197 AFEDLVYGWNRHDVASVeGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFAHLPL 276
Cdd:COG0008 157 VFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 277 LLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTRVTCHSALLDLEKLPEFNR 356
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 357 LHLQRLVNNEsqrcqlveklqalVEEAFGSQLQNRDVlnPIYMERILLLRQGHICRLQDLVsPVYSYLWTRPS---VGRA 433
Cdd:COG0008 316 PYIRALDDEE-------------LAELLAPELPEAGI--REDLERLVPLVRERAKTLSELA-ELARFFFIEREdekAAKK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 434 QLDAisEEVDVIAKRVLGLLERSGmSLTQDMLSGELKKLSEGLeGTKHSNVMKLLRVALSGQQQGPPVAEMMLSLGPKEV 513
Cdd:COG0008 380 RLAP--EEVRKVLKAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERV 455
|
....*...
gi 109127906 514 RERIQKVV 521
Cdd:COG0008 456 FERLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
37-519 |
2.68e-148 |
|
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: 433.32 E-value: 2.68e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQMPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQAA 195
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 196 PAFEDLVYG---WNRHDVasveGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFA 272
Cdd:TIGR00464 154 VSFNDQVRGeitFQNSEL----DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 273 HLPLLLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTRVTCHSALLDLEKLP 352
Cdd:TIGR00464 230 HLPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 353 EFNRLHLQRLVNNEsqrcqLVEKLQALVEeafgsQLQNRDVLNPIYMERILLLRQGHICRLQDLVSPVYSYLWTRPSVgr 432
Cdd:TIGR00464 310 WLNAHYIKELPDEE-----LFELLDPHLK-----SLVNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEV-- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 433 aQLDAISEEVDVIAKRVLGLLERSGMSL---TQDMLSGELKKLSEgLEGTKHSNVMKLLRVALSGQQQGPPVAEMMLSLG 509
Cdd:TIGR00464 378 -DEDAFKKHLKKNVKEVLEALKKKLQALeewTADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKGHGPDLAQILELIG 455
|
490
....*....|
gi 109127906 510 PKEVRERIQK 519
Cdd:TIGR00464 456 KTESIKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
36-361 |
6.08e-131 |
|
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: 380.39 E-value: 6.08e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 36 AVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDESPRRGGPAGPY 115
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 116 QQSQRLELYAQATEALLKTGaaypcfcspqrlellkkealrnhqmprydnrcrnmsqeqvaqklakdpkpairfrleqaa 195
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 196 pafedlvygwnrhdvasvegdpvimksDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFAHLP 275
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 276 LLLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTRVTCHSALLDLEKLPEFN 355
Cdd:cd00808 154 LILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233
|
....*.
gi 109127906 356 RLHLQR 361
Cdd:cd00808 234 GQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
37-351 |
3.08e-104 |
|
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: 315.03 E-value: 3.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNH--QMPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQA 194
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGspSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 195 AP-AFEDLVYGwnRHDVASVEGDP-VIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFA 272
Cdd:pfam00749 154 SPyVFRDPVRG--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 273 HLPLLLNRDGSKLSKRQGDI--FLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTRVTCHSALLDLEK 350
Cdd:pfam00749 232 HEYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKK 311
|
.
gi 109127906 351 L 351
Cdd:pfam00749 312 L 312
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
16-509 |
8.89e-100 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 311.29 E-value: 8.89e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 16 AASGRRVGRREARLGTGPGVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDML 95
Cdd:PLN02627 25 RSSRRRFSVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 96 EWAGIPPDESPRRGGPAGPYQQSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQMPRYDNRCRNMSQEQV 175
Cdd:PLN02627 105 KWLGLDWDEGPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 176 AQKLAKDPKPAIRFRL-EQAAPAFEDLVYG---WNrhdvASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWL 251
Cdd:PLN02627 185 QAELAKGTPYTYRFRVpKEGSVKIDDLIRGevsWN----TDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 252 VSTAKHLLLYQALGWHPPHFAHLPLLLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELI 331
Cdd:PLN02627 261 PNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 332 TQFNLTRVTCHSALLDLEKLPEFNRLHLQRLVnnesqrcqlVEKLQALVEEafgsQLQNRDVL----NPIYMERILLLRQ 407
Cdd:PLN02627 341 EKFSIDRINKSGAVFDSTKLKWMNGQHLRLLP---------EEELVKLVGE----RWKSAGILkesdGSFVKEAVELLKD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 408 GhICRLQDLVSPVYSYL-------WTRPSVGRAQLDAISEevdvIAKRVLGLLErSGmSLTQDMLSGE------LKKLSE 474
Cdd:PLN02627 408 G-IELVTDADKELLNLLsyplaatLSSPEAKTVVEDNFSE----VADALIAAYD-SG-ELAAALEEGHdgwqkwVKAFGK 480
|
490 500 510
....*....|....*....|....*....|....*
gi 109127906 475 GLeGTKHSNVMKLLRVALSGQQQGPPVAEMMLSLG 509
Cdd:PLN02627 481 AL-KRKGKRLFMPLRVALTGKMHGPDVGESLVLLH 514
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
40-291 |
5.31e-86 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 267.49 E-value: 5.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 40 RFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDESPRRggpagpyqQSQ 119
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLY--------QSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 120 RLELYAQATEALLKTGAAYPCFCSpqRLELLKKEALRNHQMPRYDNRCRNMSqeqvaqkLAKDPKPAIRFRLEQAAPAFE 199
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCS--RKEIAAAAPAPPDGGGIYPGTCRDLL-------HGPRNPPAWRLRVPDAVIAFD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 200 DLVYGWNRHDVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFAHLPLLLN 279
Cdd:PRK05710 152 DRLQGRQHQDLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLN 231
|
250
....*....|..
gi 109127906 280 RDGSKLSKRQGD 291
Cdd:PRK05710 232 ADGQKLSKQNGA 243
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
37-290 |
1.96e-84 |
|
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274810 Cd Length: 271 Bit Score: 262.48 E-value: 1.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDESPRRggpagpyq 116
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVY-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGAAYPCFCSpqRLELlkkeALRNHQMPRYDNRCRNMSQEQVAQKlakdpkPAIRFRLEQAAP 196
Cdd:TIGR03838 73 QSQRHALYQAALDRLLAAGLAYPCQCT--RKEI----AAARDGGGIYPGTCRNGLPGRPGRP------AAWRLRVPDGVI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 197 AFEDLVYGWNRHDVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFAHLPL 276
Cdd:TIGR03838 141 AFDDRLQGPQQQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPL 220
|
250
....*....|....
gi 109127906 277 LLNRDGSKLSKRQG 290
Cdd:TIGR03838 221 VVNADGEKLSKQNG 234
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
37-360 |
2.89e-67 |
|
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: 216.57 E-value: 2.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDE--------GPYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGaaypcfcspqrlellkkealrnhqmprydnrcrnmsqeqvaqklakdpkpairfrleqaap 196
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 197 afedlvygwnrhdvasvegdpvimksdGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPPHFAHLPL 276
Cdd:cd00418 93 ---------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPR 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 277 LLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTRVTCHSALLDLEKLPEFNR 356
Cdd:cd00418 146 LLLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNR 225
|
....
gi 109127906 357 LHLQ 360
Cdd:cd00418 226 EYIR 229
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
33-315 |
1.27e-45 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 168.11 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 33 PGVA---VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTD--QTRFVPGAAENIEDMLEWAGIPPDESpr 107
Cdd:PRK04156 95 PNAEkgkVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWDEV-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 108 rggpagpYQQSQRLELYAQATEALLKTGAAYPCFCSPqrlELLKKeaLRNHQMPrydNRCRNMSQEQVAQKLAK------ 181
Cdd:PRK04156 173 -------VIQSDRLEIYYEYARKLIEMGGAYVCTCDP---EEFKE--LRDAGKP---CPHRDKSPEENLELWEKmldgey 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 182 --------------DPKPAIR----FRLEQaapafedlvygwNRHdvaSVEGDPVIMksdgFPTYHLACVVDDHHMGISH 243
Cdd:PRK04156 238 kegeavvrvktdleHPNPSVRdwvaFRIVK------------TPH---PRVGDKYRV----WPTYNFAVAVDDHLLGVTH 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 244 VLRGSEWLVSTAKHLLLYQALGWHPP---HFAHLPLllnrDGSKLSK---RQG----------DIFLEHFAA---EGFLP 304
Cdd:PRK04156 299 VLRGKDHIDNTEKQRYIYDYFGWEYPetiHYGRLKI----EGFVLSTskiRKGieegeysgwdDPRLPTLRAlrrRGILP 374
|
330
....*....|.
gi 109127906 305 DSLLDIITNCG 315
Cdd:PRK04156 375 EAIRELIIEVG 385
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
37-290 |
4.92e-36 |
|
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: 141.11 E-value: 4.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDESprrggpagpYQ 116
Cdd:TIGR00463 94 VVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEV---------VY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQMPR--YDN-----RCRNMSQE--QVAQKLAKD---PK 184
Cdd:TIGR00463 165 QSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRsvEENlerweEMLEGKEEggSVVVRVKTDlkhKN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 185 PAIR----FRLEQAApafedlvygwnRHDVASvegdpvimKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLL 260
Cdd:TIGR00463 245 PAIRdwviFRIVKTP-----------HPRTGD--------KYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYI 305
|
250 260 270
....*....|....*....|....*....|...
gi 109127906 261 YQALGWHPPHFAHLPLLLNRDGSKLS---KRQG 290
Cdd:TIGR00463 306 YRYFGWEPPEFIHWGRLKIDDVRALStssARKG 338
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
37-315 |
1.92e-35 |
|
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: 132.47 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVP--GAAENIEDMLEWAGIPPDESprrggpagp 114
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDEV--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 115 YQQSQRLELYAQATEALLKTGAAYPcfcspqrlellkkealrnHqmPRYDNRCRnmsqeqvaqklakdpkpairfrleqa 194
Cdd:cd09287 73 VIASDRIELYYEYARKLIEMGGAYV------------------H--PRTGSKYR-------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 195 apafedlVYgwnrhdvasvegdpvimksdgfPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWHPP---HF 271
Cdd:cd09287 107 -------VW----------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPetiHW 157
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 272 AHLPLllnrDGSKLSK---RQG----------DIFLEHFAA---EGFLPDSLLDIITNCG 315
Cdd:cd09287 158 GRLKI----EGGKLSTskiRKGiesgeyegwdDPRLPTLRAlrrRGIRPEAIRDFIIEVG 213
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
37-301 |
3.45e-21 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 97.49 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTR----FVpgaaENIEDMLEWAGIPPDesprrggpA 112
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKesdeFV----ENILKDIETLGIKYD--------A 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 113 GPYQQ---SQRLELyaqaTEALLKTGAAYpcfcspqrLELLKKEALRNHQMPRYDNRCRNMSQEQvAQKLAKDPKP---- 185
Cdd:PLN02907 282 VTYTSdyfPQLMEM----AEKLIKEGKAY--------VDDTPREQMRKERMDGIESKCRNNSVEE-NLRLWKEMIAgser 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 186 ----AIRFRLEQAAP--AFEDLVYgwNR------HDVASvegdpvimKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVS 253
Cdd:PLN02907 349 glqcCVRGKLDMQDPnkSLRDPVY--YRcnptphHRIGS--------KYKVYPTYDFACPFVDALEGVTHALRSSEYHDR 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 109127906 254 TAKHLLLYQALGWHPPH---FAHlpllLNRDGSKLSKRQGDIFLEHFAAEG 301
Cdd:PLN02907 419 NAQYYRILEDMGLRKVHiweFSR----LNFVYTLLSKRKLQWFVDNGKVEG 465
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
34-295 |
1.01e-15 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 79.67 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 34 GVAVRV--RFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDESPrrggp 111
Cdd:PLN03233 7 AIAGQIvtRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVS----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 112 agpyQQSQRLELYAQATEALLKTGAAYpcfcspqrLELLKKEALRNHQMPRYDNRCRNMSqeqvaqklakdPKPAIRFRL 191
Cdd:PLN03233 82 ----FTSDYFEPIRCYAIILIEEGLAY--------MDDTPQEEMKKERADRAESKHRNQS-----------PEEALEMFK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 192 EQAAPAFEDLVYGWN-RHDVASVEG---DPVIMKSD------------GFPTYHLACVVDDHHMGISHVLRGSEWLVSTA 255
Cdd:PLN03233 139 EMCSGKEEGGAWCLRaKIDMQSDNGtlrDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHALRTTEYDDRDA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 109127906 256 KHLLLYQALGWHPPHFaHLPLLLNRDGSKLSKRQGDIFLE 295
Cdd:PLN03233 219 QFFWIQKALGLRRPRI-HAFARMNFMNTVLSKRKLTWFVD 257
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
37-302 |
1.12e-15 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 80.01 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDesprrggpAGPYQ 116
Cdd:PTZ00402 53 VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD--------VGPTY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 117 QSQRLELYAQATEALLKTGAAYpCFCSPqRLELlkkealrnhQMPRYD---NRCRNMSQEQVAqklakdpkpairfRLeq 193
Cdd:PTZ00402 125 SSDYMDLMYEKAEELIKKGLAY-CDKTP-REEM---------QKCRFDgvpTKYRDISVEETK-------------RL-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 194 aapafedlvygWNRHDVASVEG-------------------DPVI------------MKSDGFPTYHLACVVDDHHMGIS 242
Cdd:PTZ00402 179 -----------WNEMKKGSAEGqetclrakisvdnenkamrDPVIyrvnltpharqgTKYKAYPTYDFCCPIIDSVEGVT 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 243 HVLRGSEWLVSTAKHLLLYQALGWHPPHFAHLPlLLNRDGSKLSKRQGDIFLEHFAAEGF 302
Cdd:PTZ00402 248 HALRTNEYHDRNDQYYWFCDALGIRKPIVEDFS-RLNMEYSVMSKRKLTQLVDTHVVDGW 306
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
37-138 |
2.23e-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: 72.67 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDT----DQTRFVpgaaENIEDMLEWAGIPPDESprrggpa 112
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTnpekEEEEYV----DSIKEDVKWLGIKPYKV------- 70
|
90 100
....*....|....*....|....*....
gi 109127906 113 gpYQQS---QRLELYAqatEALLKTGAAY 138
Cdd:cd00807 71 --TYASdyfDQLYEYA---EQLIKKGKAY 94
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
371-521 |
8.27e-13 |
|
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: 66.06 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 371 QLVEKLQALVEEAfgsqlqNRDVLNPIYMERILLLRQGHICRLQDLVSPVYsYLWTRP------SVGRAQLDAISEEVDV 444
Cdd:pfam19269 1 ELAELALPYLEEA------GLDGLDDEYLKKVVPLLKERAETLSELAELAD-FFFELPleydeeAYAKKKMKTNKEESLE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109127906 445 IAKRVLGLLERSGmSLTQDMLSGELKKLSEGLeGTKHSNVMKLLRVALSGQQQGPPVAEMMLSLGPKEVRERIQKVV 521
Cdd:pfam19269 74 VLQELLPRLEALE-DWTAEALEAALKALAEEL-GVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
26-138 |
2.05e-08 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 57.04 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 26 EARLGTGPGVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRFVPGAAENIEDMLEWAGIPPDEs 105
Cdd:PRK14703 21 EEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGE- 99
|
90 100 110
....*....|....*....|....*....|...
gi 109127906 106 prrggpaGPYQQSQRLELYAQATEALLKTGAAY 138
Cdd:PRK14703 100 -------HLYYASDYFERMYAYAEQLIKMGLAY 125
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
40-308 |
3.18e-08 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 56.14 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 40 RFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDqtrfvPGAAEN-----IEDMLEWAGIPPDESprrggpagP 114
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTN-----PETEEQvyidaIMEMVKWMGWKPDWV--------T 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 115 YQQSQRLELYAQATEaLLKTGAAYPCFCSPqrlellkkEALRNHQMPRYDNRCRNMSQEQ-------VAQKLAKDPKPAI 187
Cdd:PTZ00437 122 FSSDYFDQLHEFAVQ-LIKDGKAYVDHSTP--------DELKQQREQREDSPWRNRSVEEnlllfehMRQGRYAEGEATL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 188 RFRLEQAA--PAFEDLVygwnRHDVASVEGDPVIMKSDGFPTYHLA-CVVDDHHmGISHVLRGSEWLVSTAKHLLLYQAL 264
Cdd:PTZ00437 193 RVKADMKSdnPNMRDFI----AYRVKYVEHPHAKDKWCIYPSYDFThCLIDSLE-DIDYSLCTLEFETRRESYFWLLEEL 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 109127906 265 GWHPPHFAHLPlLLNRDGSKLSKRQGDIFLEHFAAEGFLPDSLL 308
Cdd:PTZ00437 268 NLWRPHVWEFS-RLNVTGSLLSKRKINVLVRKGIVRGFDDPRLL 310
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
34-148 |
3.06e-07 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 53.22 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 34 GVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDqtrfvPGAA-----ENIEDMLEWAGIPPDESprr 108
Cdd:PLN02859 262 GGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEkkeyiDHIEEIVEWMGWEPFKI--- 333
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 109127906 109 ggpagPYQQSQRLELYAQATEaLLKTGAAYPCFCSPQRLE 148
Cdd:PLN02859 334 -----TYTSDYFQELYELAVE-LIRRGHAYVDHQTPEEIK 367
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
37-144 |
3.92e-06 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 49.33 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109127906 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDT-----DQtRFVpgaaENIEDMLEWAGIPPDESPRRggp 111
Cdd:PRK05347 30 VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTnpekeDQ-EYV----DSIKEDVRWLGFDWSGELRY--- 101
|
90 100 110
....*....|....*....|....*....|...
gi 109127906 112 AGPYQQsqrlELYAQAtEALLKTGAAYPCFCSP 144
Cdd:PRK05347 102 ASDYFD----QLYEYA-VELIKKGKAYVDDLSA 129
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
39-96 |
4.84e-03 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate 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: 173901 [Multi-domain] Cd Length: 143 Bit Score: 37.46 E-value: 4.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109127906 39 VRFAPSPTGFLHLGGLRTALYNYIFA-----KKYQGSFILRLEDTDQTRFVP--GAAENIEDMLE 96
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAqayrkLGYKVRCIALIDDAGGLIGDPanKKGENAKAFVE 66
|
|
| |
