NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767988280|ref|XP_011544040|]
View 

nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

glutamate--tRNA ligase( domain architecture ID 17564554)

glutamate--tRNA ligase catalyzes the attachment of glutamate to tRNA(Glu)

CATH:  3.40.50.620|3.90.800.10|1.10.1160.10|1.10.10.350|1.10.8.70
EC:  6.1.1.17
Gene Ontology:  GO:0008270|GO:0006424|GO:0004818|GO:0000049|GO:0005524
PubMed:  10704480|12458790|10447505|9746349|8078941|8274143|2053131

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 23-497 3.86e-152

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: 441.92  E-value: 3.86e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQQSQRLELYAQ 102
Cdd:COG0008   15 GYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE--------GPYYQSDRFDIYYE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQVVPAFQDLVYGWN 182
Cdd:COG0008   87 YAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVVFDDLVRGEI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 183 RHEVASVeGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLS 262
Cdd:COG0008  167 TFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKLS 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 263 KRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRLVSNE 342
Cdd:COG0008  246 KRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALDDEE 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 343 sqrrqlvgklqvlVEEAFGCQLQNRDVlnPVYVERILLLRQGHICRLQDLVsPVYSYLWTRP--AVGRAQLDAISEKVDV 420
Cdd:COG0008  326 -------------LAELLAPELPEAGI--REDLERLVPLVRERAKTLSELA-ELARFFFIERedEKAAKKRLAPEEVRKV 389

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767988280 421 IaKRVLGLLERSSmSLTQDMLNGELKKLSEGLeGTKYSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVV 497
Cdd:COG0008  390 L-KAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAI 463
 
Name Accession Description Interval E-value
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 23-497 3.86e-152

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: 441.92  E-value: 3.86e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQQSQRLELYAQ 102
Cdd:COG0008   15 GYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE--------GPYYQSDRFDIYYE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQVVPAFQDLVYGWN 182
Cdd:COG0008   87 YAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVVFDDLVRGEI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 183 RHEVASVeGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLS 262
Cdd:COG0008  167 TFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKLS 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 263 KRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRLVSNE 342
Cdd:COG0008  246 KRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALDDEE 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 343 sqrrqlvgklqvlVEEAFGCQLQNRDVlnPVYVERILLLRQGHICRLQDLVsPVYSYLWTRP--AVGRAQLDAISEKVDV 420
Cdd:COG0008  326 -------------LAELLAPELPEAGI--REDLERLVPLVRERAKTLSELA-ELARFFFIERedEKAAKKRLAPEEVRKV 389

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767988280 421 IaKRVLGLLERSSmSLTQDMLNGELKKLSEGLeGTKYSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVV 497
Cdd:COG0008  390 L-KAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAI 463
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 23-495 1.24e-138

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: 407.89  E-value: 1.24e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280   23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQQSQRLELYAQ 102
Cdd:TIGR00464  12 GYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPYYQSQRLDIYKK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQVVPAFQDLVYG- 180
Cdd:TIGR00464  84 YAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEAVVSFNDQVRGe 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  181 --WNRHEVasveGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDG 258
Cdd:TIGR00464 164 itFQNSEL----DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  259 SKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRL 338
Cdd:TIGR00464 240 KKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKEL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  339 vSNESQRRQLVGKLQvlveeafgcQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPVYSYLWTRPAVgraQLDAISEKV 418
Cdd:TIGR00464 320 -PDEELFELLDPHLK---------SLVNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEV---DEDAFKKHL 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  419 DVIAKRVLGLLERSSMSL---TQDMLNGELKKLSEgLEGTKYSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQK 495
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALeewTADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA 465
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 23-337 4.06e-120

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: 351.89  E-value: 4.06e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQ 102
Cdd:cd00808   12 GFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYRQSERLEIYRK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGaaypcfcspqrlellkkealrnhqtprydnrcrnmsqeqvaqklakdpkpairfrleqvvpafqdlvygwn 182
Cdd:cd00808   92 YAEKLLEKG----------------------------------------------------------------------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 183 rhevasvegdpvimksDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLS 262
Cdd:cd00808  101 ----------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLS 164

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767988280 263 KRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQR 337
Cdd:cd00808  165 KRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIRE 239
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 23-327 5.82e-94

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: 287.68  E-value: 5.82e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280   23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQQSQRLELYAQ 102
Cdd:pfam00749  12 GYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYYQSDRFDIYYK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNH--QTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQVVPAFQDLVY 179
Cdd:pfam00749  84 YAEELIKKGKAYVCFCTPEELEEEREEQEALGspSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIpMESPYVFRDPVR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  180 GwnRHEVASVEGDP-VIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDG 258
Cdd:pfam00749 164 G--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDG 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767988280  259 SKLSKRQGD--VFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKL 327
Cdd:pfam00749 242 TKLSKRKLSwsVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
PLN02627 PLN02627
glutamyl-tRNA synthetase
 23-485 1.21e-86

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 276.24  E-value: 1.21e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQ 102
Cdd:PLN02627  56 GNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYRQSERNAIYKQ 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRleqvVPAFQ-----DL 177
Cdd:PLN02627 136 YAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFR----VPKEGsvkidDL 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 178 VYG---WNrhevASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLL 254
Cdd:PLN02627 212 IRGevsWN----TDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLIL 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 255 NRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLH 334
Cdd:PLN02627 288 APDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQH 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 335 LqRLVSNEsqrrqlvgKLQVLVEEafgcQLQNRDVL----NPVYVERILLLRQGhICRLQDLVSPVYSYL-------WTR 403
Cdd:PLN02627 368 L-RLLPEE--------ELVKLVGE----RWKSAGILkesdGSFVKEAVELLKDG-IELVTDADKELLNLLsyplaatLSS 433

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 404 PAVGRAQLDAISEkvdvIAKRVLGLLErsSMSLTQDMLNGE------LKKLSEGLeGTKYSNVMKLLRMALSGQQQGPPV 477
Cdd:PLN02627 434 PEAKTVVEDNFSE----VADALIAAYD--SGELAAALEEGHdgwqkwVKAFGKAL-KRKGKRLFMPLRVALTGKMHGPDV 506


                 ....*...
gi 767988280 478 AEMMLALG 485
Cdd:PLN02627 507 GESLVLLH 514
 
Name Accession Description Interval E-value
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 23-497 3.86e-152

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: 441.92  E-value: 3.86e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQQSQRLELYAQ 102
Cdd:COG0008   15 GYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE--------GPYYQSDRFDIYYE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQVVPAFQDLVYGWN 182
Cdd:COG0008   87 YAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVVFDDLVRGEI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 183 RHEVASVeGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLS 262
Cdd:COG0008  167 TFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKLS 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 263 KRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRLVSNE 342
Cdd:COG0008  246 KRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALDDEE 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 343 sqrrqlvgklqvlVEEAFGCQLQNRDVlnPVYVERILLLRQGHICRLQDLVsPVYSYLWTRP--AVGRAQLDAISEKVDV 420
Cdd:COG0008  326 -------------LAELLAPELPEAGI--REDLERLVPLVRERAKTLSELA-ELARFFFIERedEKAAKKRLAPEEVRKV 389

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767988280 421 IaKRVLGLLERSSmSLTQDMLNGELKKLSEGLeGTKYSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVV 497
Cdd:COG0008  390 L-KAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAI 463
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 23-495 1.24e-138

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: 407.89  E-value: 1.24e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280   23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQQSQRLELYAQ 102
Cdd:TIGR00464  12 GYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPYYQSQRLDIYKK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQVVPAFQDLVYG- 180
Cdd:TIGR00464  84 YAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEAVVSFNDQVRGe 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  181 --WNRHEVasveGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDG 258
Cdd:TIGR00464 164 itFQNSEL----DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  259 SKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRL 338
Cdd:TIGR00464 240 KKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKEL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  339 vSNESQRRQLVGKLQvlveeafgcQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPVYSYLWTRPAVgraQLDAISEKV 418
Cdd:TIGR00464 320 -PDEELFELLDPHLK---------SLVNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEV---DEDAFKKHL 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  419 DVIAKRVLGLLERSSMSL---TQDMLNGELKKLSEgLEGTKYSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQK 495
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALeewTADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA 465
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 23-337 4.06e-120

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: 351.89  E-value: 4.06e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQ 102
Cdd:cd00808   12 GFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYRQSERLEIYRK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGaaypcfcspqrlellkkealrnhqtprydnrcrnmsqeqvaqklakdpkpairfrleqvvpafqdlvygwn 182
Cdd:cd00808   92 YAEKLLEKG----------------------------------------------------------------------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 183 rhevasvegdpvimksDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLS 262
Cdd:cd00808  101 ----------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLS 164

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767988280 263 KRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQR 337
Cdd:cd00808  165 KRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIRE 239
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 23-327 5.82e-94

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: 287.68  E-value: 5.82e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280   23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQQSQRLELYAQ 102
Cdd:pfam00749  12 GYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYYQSDRFDIYYK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNH--QTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQVVPAFQDLVY 179
Cdd:pfam00749  84 YAEELIKKGKAYVCFCTPEELEEEREEQEALGspSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIpMESPYVFRDPVR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  180 GwnRHEVASVEGDP-VIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDG 258
Cdd:pfam00749 164 G--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDG 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767988280  259 SKLSKRQGD--VFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKL 327
Cdd:pfam00749 242 TKLSKRKLSwsVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
PLN02627 PLN02627
glutamyl-tRNA synthetase
 23-485 1.21e-86

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 276.24  E-value: 1.21e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQ 102
Cdd:PLN02627  56 GNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYRQSERNAIYKQ 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRleqvVPAFQ-----DL 177
Cdd:PLN02627 136 YAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFR----VPKEGsvkidDL 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 178 VYG---WNrhevASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLL 254
Cdd:PLN02627 212 IRGevsWN----TDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLIL 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 255 NRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLH 334
Cdd:PLN02627 288 APDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQH 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 335 LqRLVSNEsqrrqlvgKLQVLVEEafgcQLQNRDVL----NPVYVERILLLRQGhICRLQDLVSPVYSYL-------WTR 403
Cdd:PLN02627 368 L-RLLPEE--------ELVKLVGE----RWKSAGILkesdGSFVKEAVELLKDG-IELVTDADKELLNLLsyplaatLSS 433

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 404 PAVGRAQLDAISEkvdvIAKRVLGLLErsSMSLTQDMLNGE------LKKLSEGLeGTKYSNVMKLLRMALSGQQQGPPV 477
Cdd:PLN02627 434 PEAKTVVEDNFSE----VADALIAAYD--SGELAAALEEGHdgwqkwVKAFGKAL-KRKGKRLFMPLRVALTGKMHGPDV 506


                 ....*...
gi 767988280 478 AEMMLALG 485
Cdd:PLN02627 507 GESLVLLH 514
PRK05710 PRK05710
tRNA glutamyl-Q(34) synthetase GluQRS;
23-268 9.17e-82

tRNA glutamyl-Q(34) synthetase GluQRS;


Pssm-ID: 235573  Cd Length: 299  Bit Score: 255.93  E-value: 9.17e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRggpagpyqQSQRLELYAQ 102
Cdd:PRK05710  16 GPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLY--------QSQRHDAYRA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGAAYPCFCSpqRLELLKKEALRNHQTPRYDNRCRNMSqeqvaqkLAKDPKPAIRFRLEQVVPAFQDLVYGWN 182
Cdd:PRK05710  88 ALDRLRAQGLVYPCFCS--RKEIAAAAPAPPDGGGIYPGTCRDLL-------HGPRNPPAWRLRVPDAVIAFDDRLQGRQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 183 RHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLS 262
Cdd:PRK05710 159 HQDLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLS 238


                 ....*.
gi 767988280 263 KRQGDV 268
Cdd:PRK05710 239 KQNGAP 244
queuosine_YadB TIGR03838
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ...
 23-266 5.94e-78

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: 245.14  E-value: 5.94e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280   23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRggpagpyqQSQRLELYAQ 102
Cdd:TIGR03838  11 GPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVY--------QSQRHALYQA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  103 ATEALLKTGAAYPCFCSpqRLELlkkeALRNHQTPRYDNRCRNMSQEQVAQKlakdpkPAIRFRLEQVVPAFQDLVYGWN 182
Cdd:TIGR03838  83 ALDRLLAAGLAYPCQCT--RKEI----AAARDGGGIYPGTCRNGLPGRPGRP------AAWRLRVPDGVIAFDDRLQGPQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  183 RHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLS 262
Cdd:TIGR03838 151 QQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLS 230


                  ....
gi 767988280  263 KRQG 266
Cdd:TIGR03838 231 KQNG 234
GlxRS_core cd00418
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ...
 23-336 5.46e-59

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: 194.23  E-value: 5.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQQSQRLELYAQ 102
Cdd:cd00418   12 GYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDE--------GPYRQSDRFDLYRA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGaaypcfcspqrlellkkealrnhqtprydnrcrnmsqeqvaqklakdpkpairfrleqvvpafqdlvygwn 182
Cdd:cd00418   84 YAEELIKKG----------------------------------------------------------------------- 92

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 183 rhevasvegdpvimksdGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLS 262
Cdd:cd00418   93 -----------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLS 155

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767988280 263 KRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQ 336
Cdd:cd00418  156 KRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNREYIR 229
gltX PRK04156
glutamyl-tRNA synthetase; Provisional
 23-291 7.01e-40

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 235229 [Multi-domain]  Cd Length: 567  Bit Score: 151.54  E-value: 7.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTD--QTRVVPGAAENIEDMLEWAGIPPDESprrggpagpYQQSQRLELY 100
Cdd:PRK04156 112 GPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWDEV---------VIQSDRLEIY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 101 AQATEALLKTGAAYPCFCSPqrlELLKKeaLRNHQTPrydNRCRNMSQEQVAQKLAK--------------------DPK 160
Cdd:PRK04156 183 YEYARKLIEMGGAYVCTCDP---EEFKE--LRDAGKP---CPHRDKSPEENLELWEKmldgeykegeavvrvktdleHPN 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 161 PAIR----FRLEQvvpafqdlvygwNRHevaSVEGDPVIMksdgFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLL 236
Cdd:PRK04156 255 PSVRdwvaFRIVK------------TPH---PRVGDKYRV----WPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYI 315

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767988280 237 YQALGWQPP---HFAHLPLllnrDGSKLSK---RQG----------DVFLEHFAA---DGFLPDSLLDIITNCG 291
Cdd:PRK04156 316 YDYFGWEYPetiHYGRLKI----EGFVLSTskiRKGieegeysgwdDPRLPTLRAlrrRGILPEAIRELIIEVG 385
gltX_arch TIGR00463
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ...
 23-266 1.79e-33

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: 133.41  E-value: 1.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280   23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESprrggpagpYQQSQRLELYAQ 102
Cdd:TIGR00463 104 GPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEV---------VYQSDRIETYYD 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  103 ATEALLKTGAAYPCFCSPQRLELLKKEALRNHqtprydnrCRNMSQEQVAQkLAKDPKPAIRFRLEQVVPAFQDLvygwn 182
Cdd:TIGR00463 175 YTRKLIEMGKAYVCDCRPEEFRELRNRGEACH--------CRDRSVEENLE-RWEEMLEGKEEGGSVVVRVKTDL----- 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  183 RHEVASVEgDPVIMKSDG------------FPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHL 250
Cdd:TIGR00463 241 KHKNPAIR-DWVIFRIVKtphprtgdkyrvYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHW 319

                         250
                  ....*....|....*....
gi 767988280  251 PLLLNRDGSKLS---KRQG 266
Cdd:TIGR00463 320 GRLKIDDVRALStssARKG 338
GluRS_non_core cd09287
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ...
 23-291 1.12e-29

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: 116.30  E-value: 1.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQT--RVVPGAAENIEDMLEWAGIPPDESprrggpagpYQQSQRLELY 100
Cdd:cd09287   12 GPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEV---------VIASDRIELY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 101 AQATEALLKTGAAYPcfcspqrlellkkealrnHqtPRYDNRCRnmsqeqvaqklakdpkpairfrleqvvpafqdlVYg 180
Cdd:cd09287   83 YEYARKLIEMGGAYV------------------H--PRTGSKYR---------------------------------VW- 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 181 wnrhevasvegdpvimksdgfPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPP---HFAHLPLllnrD 257
Cdd:cd09287  109 ---------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPetiHWGRLKI----E 163

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 767988280 258 GSKLSK---RQG----------DVFLEHFAA---DGFLPDSLLDIITNCG 291
Cdd:cd09287  164 GGKLSTskiRKGiesgeyegwdDPRLPTLRAlrrRGIRPEAIRDFIIEVG 213
PTZ00402 PTZ00402
glutamyl-tRNA synthetase; Provisional
 23-278 2.61e-14

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 240404 [Multi-domain]  Cd Length: 601  Bit Score: 75.38  E-value: 2.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDesprrggpAGPYQQSQRLELYAQ 102
Cdd:PTZ00402  63 GFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD--------VGPTYSSDYMDLMYE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGAAYpCFCSPqRLELlkkealrnhQTPRYD---NRCRNMSQEQVAqklakdpkpairfRLeqvvpafqdlvy 179
Cdd:PTZ00402 135 KAEELIKKGLAY-CDKTP-REEM---------QKCRFDgvpTKYRDISVEETK-------------RL------------ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 180 gWNRHEVASVEG-------------------DPVI------------MKSDGFPTYHLACVVDDHHMGISHVLRGSEWLV 228
Cdd:PTZ00402 179 -WNEMKKGSAEGqetclrakisvdnenkamrDPVIyrvnltpharqgTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHD 257

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 767988280 229 STAKHLLLYQALGWQPPHFAHLPlLLNRDGSKLSKRQGDVFLEHFAADGF 278
Cdd:PTZ00402 258 RNDQYYWFCDALGIRKPIVEDFS-RLNMEYSVMSKRKLTQLVDTHVVDGW 306
PLN02907 PLN02907
glutamate-tRNA ligase
 23-277 6.48e-14

glutamate-tRNA ligase


Pssm-ID: 215492 [Multi-domain]  Cd Length: 722  Bit Score: 74.38  E-value: 6.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDesprrggpAGPYQQ---SQRLEL 99
Cdd:PLN02907 224 GYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD--------AVTYTSdyfPQLMEM 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 100 yaqaTEALLKTGAAYpcfcspqrLELLKKEALRNHQTPRYDNRCRNMSQEQvAQKLAKDPKP--------AIRFRLEQVV 171
Cdd:PLN02907 296 ----AEKLIKEGKAY--------VDDTPREQMRKERMDGIESKCRNNSVEE-NLRLWKEMIAgserglqcCVRGKLDMQD 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 172 P--AFQDLVYgwNR------HEVASvegdpvimKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQ 243
Cdd:PLN02907 363 PnkSLRDPVY--YRcnptphHRIGS--------KYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR 432

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 767988280 244 PPH---FAHlpllLNRDGSKLSKRQGDVFLEHFAADG 277
Cdd:PLN02907 433 KVHiweFSR----LNFVYTLLSKRKLQWFVDNGKVEG 465
Anticodon_2 pfam19269
Anticodon binding domain; This entry represents the anticodon binding domain found at the ...
 368-497 6.50e-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: 6.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  368 DVLNPVYVERILLLRQGHICRLQDLVSPVYsYLWTRP------AVGRAQLDAISEKVDVIAKRVLGLLERSSmSLTQDML 441
Cdd:pfam19269  16 DGLDDEYLKKVVPLLKERAETLSELAELAD-FFFELPleydeeAYAKKKMKTNKEESLEVLQELLPRLEALE-DWTAEAL 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767988280  442 NGELKKLSEGLeGTKYSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVV 497
Cdd:pfam19269  94 EAALKALAEEL-GVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
PLN03233 PLN03233
putative glutamate-tRNA ligase; Provisional
 23-271 1.31e-10

putative glutamate-tRNA ligase; Provisional


Pssm-ID: 178772 [Multi-domain]  Cd Length: 523  Bit Score: 63.49  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPrrggpagpyQQSQRLELYAQ 102
Cdd:PLN03233  22 GYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVS---------FTSDYFEPIRC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 103 ATEALLKTGAAYpcfcspqrLELLKKEALRNHQTPRYDNRCRNMSqeqvaqklakdPKPAIRFrleqvvpaFQDLVYG-- 180
Cdd:PLN03233  93 YAIILIEEGLAY--------MDDTPQEEMKKERADRAESKHRNQS-----------PEEALEM--------FKEMCSGke 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 181 ----W---NRHEVASVEG---DPVIMKSD------------GFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQ 238
Cdd:PLN03233 146 eggaWclrAKIDMQSDNGtlrDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQK 225

                        250       260       270
                 ....*....|....*....|....*....|...
gi 767988280 239 ALGWQPPHFaHLPLLLNRDGSKLSKRQGDVFLE 271
Cdd:PLN03233 226 ALGLRRPRI-HAFARMNFMNTVLSKRKLTWFVD 257
GlnRS_core cd00807
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ...
 23-114 1.45e-08

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: 55.34  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESprrggpagpYQQS---QRLEL 99
Cdd:cd00807   12 GYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV---------TYASdyfDQLYE 82

                         90
                 ....*....|....*
gi 767988280 100 YAqatEALLKTGAAY 114
Cdd:cd00807   83 YA---EQLIKKGKAY 94
PRK14703 PRK14703
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
 23-114 4.40e-05

glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional


Pssm-ID: 237793 [Multi-domain]  Cd Length: 771  Bit Score: 46.25  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQQSQRLELYAQ 102
Cdd:PRK14703  42 GYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGE--------HLYYASDYFERMYA 113

                         90
                 ....*....|..
gi 767988280 103 ATEALLKTGAAY 114
Cdd:PRK14703 114 YAEQLIKMGLAY 125
PTZ00437 PTZ00437
glutaminyl-tRNA synthetase; Provisional
 23-284 7.43e-05

glutaminyl-tRNA synthetase; Provisional


Pssm-ID: 240418 [Multi-domain]  Cd Length: 574  Bit Score: 45.36  E-value: 7.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDqtrvvPGAAEN-----IEDMLEWAGIPPDESprrggpagPYQQSQRL 97
Cdd:PTZ00437  62 GFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTN-----PETEEQvyidaIMEMVKWMGWKPDWV--------TFSSDYFD 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  98 ELYAQATEaLLKTGAAYPCFCSPqrlellkkEALRNHQTPRYDNRCRNMSQEQ-------VAQKLAKDPKPAIRFRLEQV 170
Cdd:PTZ00437 129 QLHEFAVQ-LIKDGKAYVDHSTP--------DELKQQREQREDSPWRNRSVEEnlllfehMRQGRYAEGEATLRVKADMK 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280 171 V--PAFQDLVygwnRHEVASVEGDPVIMKSDGFPTYHLA-CVVDDHHmGISHVLRGSEWLVSTAKHLLLYQALGWQPPHF 247
Cdd:PTZ00437 200 SdnPNMRDFI----AYRVKYVEHPHAKDKWCIYPSYDFThCLIDSLE-DIDYSLCTLEFETRRESYFWLLEELNLWRPHV 274

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 767988280 248 AHLPlLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLL 284
Cdd:PTZ00437 275 WEFS-RLNVTGSLLSKRKINVLVRKGIVRGFDDPRLL 310
PLN02859 PLN02859
glutamine-tRNA ligase
 23-124 2.36e-03

glutamine-tRNA ligase


Pssm-ID: 178450 [Multi-domain]  Cd Length: 788  Bit Score: 40.51  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988280  23 GFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDqtrvvPGAA-----ENIEDMLEWAGIPPDESprrggpagPYQQSQRL 97
Cdd:PLN02859 275 GYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEkkeyiDHIEEIVEWMGWEPFKI--------TYTSDYFQ 341

                         90       100
                 ....*....|....*....|....*..
gi 767988280  98 ELYAQATEaLLKTGAAYPCFCSPQRLE 124
Cdd:PLN02859 342 ELYELAVE-LIRRGHAYVDHQTPEEIK 367
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH