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Conserved domains on  [gi|67461998|sp|Q7VIM2|]
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RecName: Full=Glutamate--tRNA ligase 2; AltName: Full=Glutamyl-tRNA synthetase 2; Short=GluRS 2

Protein Classification

glutamate--tRNA ligase family protein( domain architecture ID 1005264)

glutamate--tRNA ligase family protein similar to glutaminyl-tRNA synthetase (GlnRS) which catalyzes the transfer of glutamine to the A76 2' hydroxyl group of tRNA Gln isoacceptors

Gene Ontology:  GO:0000049|GO:0004818|GO:0006424

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gltX_bact super family cl36666
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 1-429 1.03e-146

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]


The actual alignment was detected with superfamily member TIGR00464:

Pssm-ID: 273092 [Multi-domain]  Cd Length: 470  Bit Score: 426.00  E-value: 1.03e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998     1 MLRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDN-LVYQSSNFERHR 79
Cdd:TIGR00464   3 RTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEgPYYQSQRLDIYK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    80 QLAQHLISKDLAFYCYCSKEFLESKRLEAKEQKKPFRYDPSWAEIEKSSNT-------KPVVRIRGASEA-ISFEDAIKG 151
Cdd:TIGR00464  83 KYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIEnklakgiPPVVRFKIPQEAvVSFNDQVRG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   152 TLRFEAHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPIILGESGSK 231
Cdd:TIGR00464 163 EITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGW-KIPVFAHLPMILDEDGKK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   232 MSKRDNASSVAWLLEEGFLPQAIMNYLISMGNHTPT--EVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNREHLKMLNE 309
Cdd:TIGR00464 242 LSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDdqEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELPD 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   310 QEFALLLDSKDSSIGA-----------LGKLHLQEASTLNEIRSKIERIFSPKCIAQNE--EGENFENECKILYDILHQM 376
Cdd:TIGR00464 322 EELFELLDPHLKSLVNtdtlnreqlaeLLLLFKERLKTLKEIAELIRLFFEDKKEVDEDafKKHLKKNVKEVLEALKKKL 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 67461998   377 IESYDESLNDYDTFKNALMAKSSLKGKKFFKPLRILLTGQTQGLELSEIYPYL 429
Cdd:TIGR00464 402 QALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELI 454
 
Name Accession Description Interval E-value
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 1-429 1.03e-146

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: 426.00  E-value: 1.03e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998     1 MLRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDN-LVYQSSNFERHR 79
Cdd:TIGR00464   3 RTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEgPYYQSQRLDIYK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    80 QLAQHLISKDLAFYCYCSKEFLESKRLEAKEQKKPFRYDPSWAEIEKSSNT-------KPVVRIRGASEA-ISFEDAIKG 151
Cdd:TIGR00464  83 KYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIEnklakgiPPVVRFKIPQEAvVSFNDQVRG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   152 TLRFEAHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPIILGESGSK 231
Cdd:TIGR00464 163 EITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGW-KIPVFAHLPMILDEDGKK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   232 MSKRDNASSVAWLLEEGFLPQAIMNYLISMGNHTPT--EVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNREHLKMLNE 309
Cdd:TIGR00464 242 LSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDdqEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELPD 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   310 QEFALLLDSKDSSIGA-----------LGKLHLQEASTLNEIRSKIERIFSPKCIAQNE--EGENFENECKILYDILHQM 376
Cdd:TIGR00464 322 EELFELLDPHLKSLVNtdtlnreqlaeLLLLFKERLKTLKEIAELIRLFFEDKKEVDEDafKKHLKKNVKEVLEALKKKL 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 67461998   377 IESYDESLNDYDTFKNALMAKSSLKGKKFFKPLRILLTGQTQGLELSEIYPYL 429
Cdd:TIGR00464 402 QALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELI 454
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-434 2.66e-145

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: 422.28  E-value: 2.66e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   1 MLRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWD-NLVYQSSNFERHR 79
Cdd:COG0008   6 RTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDeGPYYQSDRFDIYY 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  80 QLAQHLISKDLAFYCYCSKEFLESKRLEAKEQKKPFRYDPSW-----AEIEK--SSNTKPVVRIRGASEAISFEDAIKGT 152
Cdd:COG0008  86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCrdlspEELERmlAAGEPPVLRFKIPEEGVVFDDLVRGE 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 153 LRFEAHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYDKVLgYAHLPIILGESGSKM 232
Cdd:COG0008 166 ITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPE-FAHLPLILGPDGTKL 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 233 SKRDNASSVAWLLEEGFLPQAIMNYLISMGN--HTPTEVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNREHLKMLNEQ 310
Cdd:COG0008 245 SKRKGAVTVSGLRRRGYLPEAIRNYLALLGWskSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALDDE 324

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 311 EFALLLDSKDSSIGALGKL-----HLQE-ASTLNEIRSKIERIFS----PKCIAQNEEGENFENECKILYDILHQmIESY 380
Cdd:COG0008 325 ELAELLAPELPEAGIREDLerlvpLVRErAKTLSELAELARFFFIeredEKAAKKRLAPEEVRKVLKAALEVLEA-VETW 403

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 381 DEslndyDTFK---NALMAKSSLKGKKFFKPLRILLTGQTQGLELSEIYPYL---RFFLR 434
Cdd:COG0008 404 DP-----ETVKgtiHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLgkeRVFER 458
PLN02627 PLN02627
glutamyl-tRNA synthetase
 2-424 5.04e-82

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 262.37  E-value: 5.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    2 LRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDN---------LVYQS 72
Cdd:PLN02627  48 VRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgpdvggeygPYRQS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   73 SNFERHRQLAQHLISKDLAFYCYCSKEFLESKRLEAKEQKKPFRYDPSWA-------EIEKSSNTKPVVRIRGASEA-IS 144
Cdd:PLN02627 128 ERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWAtasdeevQAELAKGTPYTYRFRVPKEGsVK 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  145 FEDAIKGTLRFEAHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPII 224
Cdd:PLN02627 208 IDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGF-PMPRFAHVSLI 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  225 LGESGSKMSKRDNASSVAWLLEEGFLPQAIMNYLISMG--NHTPTEVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNRE 302
Cdd:PLN02627 287 LAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGwnDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQ 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  303 HLKMLNEQEFA-----------LLLDSKDSSIGALGKLHLQEASTLNEIRSKIERIFSPKCIAQNEEGENFENECKILYD 371
Cdd:PLN02627 367 HLRLLPEEELVklvgerwksagILKESDGSFVKEAVELLKDGIELVTDADKELLNLLSYPLAATLSSPEAKTVVEDNFSE 446

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67461998  372 ILHQMIESYD---------ESLNDYDTFKNALMAKSSLKGKKFFKPLRILLTGQTQGLELSE 424
Cdd:PLN02627 447 VADALIAAYDsgelaaaleEGHDGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGE 508
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 3-306 2.56e-77

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: 240.57  E-value: 2.56e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDNLV---------YQSS 73
Cdd:cd00808   5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPdvggpygpyRQSE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  74 NFERHRQLAQHLISKDlafycycskefleskrleakeqkkpfrydpswaeiekssntkpvvrirgaseaisfedaikgtl 153
Cdd:cd00808  85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 154 rfeaheidsfvilkeDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPIILGESGSKMS 233
Cdd:cd00808 101 ---------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGW-EPPKFAHLPLILNPDGKKLS 164

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67461998 234 KRDNASSVAWLLEEGFLPQAIMNYLISMGNHTP--TEVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNREHLKM 306
Cdd:cd00808 165 KRKGDTSISDYREEGYLPEALLNYLALLGWSPPdgEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIRE 239
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 3-298 2.31e-71

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: 227.59  E-value: 2.31e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998     3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDNLV-YQSSNFERHRQL 81
Cdd:pfam00749   5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPyYQSDRFDIYYKY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    82 AQHLISKDLAFYCYCSKEFLESKR--LEAKEQKKPFRYD----PSWAEIEKS---SNTKPVVRIRGASEA-ISFEDAIKG 151
Cdd:pfam00749  85 AEELIKKGKAYVCFCTPEELEEEReeQEALGSPSRDRYDeenlHLFEEEMKKgsaEGGPATVRAKIPMESpYVFRDPVRG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   152 TLRFEAHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYDKVLgYAHLPIILGESGSK 231
Cdd:pfam00749 165 RIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPP-FIHEYLRLNLDGTK 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67461998   232 MSKRDNASSVA--WLLEEGFLPQAIMNYLISMGnHTPT---EVFKLQDAYNWFDIKNIAKSPVKFDIKRLRF 298
Cdd:pfam00749 244 LSKRKLSWSVDisQVKGWGDPREATLNGLRRRG-WTPEgirEFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
 
Name Accession Description Interval E-value
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 1-429 1.03e-146

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: 426.00  E-value: 1.03e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998     1 MLRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDN-LVYQSSNFERHR 79
Cdd:TIGR00464   3 RTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEgPYYQSQRLDIYK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    80 QLAQHLISKDLAFYCYCSKEFLESKRLEAKEQKKPFRYDPSWAEIEKSSNT-------KPVVRIRGASEA-ISFEDAIKG 151
Cdd:TIGR00464  83 KYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIEnklakgiPPVVRFKIPQEAvVSFNDQVRG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   152 TLRFEAHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPIILGESGSK 231
Cdd:TIGR00464 163 EITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGW-KIPVFAHLPMILDEDGKK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   232 MSKRDNASSVAWLLEEGFLPQAIMNYLISMGNHTPT--EVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNREHLKMLNE 309
Cdd:TIGR00464 242 LSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDdqEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELPD 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   310 QEFALLLDSKDSSIGA-----------LGKLHLQEASTLNEIRSKIERIFSPKCIAQNE--EGENFENECKILYDILHQM 376
Cdd:TIGR00464 322 EELFELLDPHLKSLVNtdtlnreqlaeLLLLFKERLKTLKEIAELIRLFFEDKKEVDEDafKKHLKKNVKEVLEALKKKL 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 67461998   377 IESYDESLNDYDTFKNALMAKSSLKGKKFFKPLRILLTGQTQGLELSEIYPYL 429
Cdd:TIGR00464 402 QALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELI 454
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-434 2.66e-145

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: 422.28  E-value: 2.66e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   1 MLRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWD-NLVYQSSNFERHR 79
Cdd:COG0008   6 RTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDeGPYYQSDRFDIYY 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  80 QLAQHLISKDLAFYCYCSKEFLESKRLEAKEQKKPFRYDPSW-----AEIEK--SSNTKPVVRIRGASEAISFEDAIKGT 152
Cdd:COG0008  86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCrdlspEELERmlAAGEPPVLRFKIPEEGVVFDDLVRGE 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 153 LRFEAHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYDKVLgYAHLPIILGESGSKM 232
Cdd:COG0008 166 ITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPE-FAHLPLILGPDGTKL 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 233 SKRDNASSVAWLLEEGFLPQAIMNYLISMGN--HTPTEVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNREHLKMLNEQ 310
Cdd:COG0008 245 SKRKGAVTVSGLRRRGYLPEAIRNYLALLGWskSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALDDE 324

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 311 EFALLLDSKDSSIGALGKL-----HLQE-ASTLNEIRSKIERIFS----PKCIAQNEEGENFENECKILYDILHQmIESY 380
Cdd:COG0008 325 ELAELLAPELPEAGIREDLerlvpLVRErAKTLSELAELARFFFIeredEKAAKKRLAPEEVRKVLKAALEVLEA-VETW 403

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 381 DEslndyDTFK---NALMAKSSLKGKKFFKPLRILLTGQTQGLELSEIYPYL---RFFLR 434
Cdd:COG0008 404 DP-----ETVKgtiHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLgkeRVFER 458
PLN02627 PLN02627
glutamyl-tRNA synthetase
 2-424 5.04e-82

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 262.37  E-value: 5.04e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    2 LRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDN---------LVYQS 72
Cdd:PLN02627  48 VRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgpdvggeygPYRQS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   73 SNFERHRQLAQHLISKDLAFYCYCSKEFLESKRLEAKEQKKPFRYDPSWA-------EIEKSSNTKPVVRIRGASEA-IS 144
Cdd:PLN02627 128 ERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWAtasdeevQAELAKGTPYTYRFRVPKEGsVK 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  145 FEDAIKGTLRFEAHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPII 224
Cdd:PLN02627 208 IDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGF-PMPRFAHVSLI 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  225 LGESGSKMSKRDNASSVAWLLEEGFLPQAIMNYLISMG--NHTPTEVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNRE 302
Cdd:PLN02627 287 LAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGwnDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQ 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  303 HLKMLNEQEFA-----------LLLDSKDSSIGALGKLHLQEASTLNEIRSKIERIFSPKCIAQNEEGENFENECKILYD 371
Cdd:PLN02627 367 HLRLLPEEELVklvgerwksagILKESDGSFVKEAVELLKDGIELVTDADKELLNLLSYPLAATLSSPEAKTVVEDNFSE 446

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67461998  372 ILHQMIESYD---------ESLNDYDTFKNALMAKSSLKGKKFFKPLRILLTGQTQGLELSE 424
Cdd:PLN02627 447 VADALIAAYDsgelaaaleEGHDGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGE 508
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 3-306 2.56e-77

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: 240.57  E-value: 2.56e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDNLV---------YQSS 73
Cdd:cd00808   5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPdvggpygpyRQSE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  74 NFERHRQLAQHLISKDlafycycskefleskrleakeqkkpfrydpswaeiekssntkpvvrirgaseaisfedaikgtl 153
Cdd:cd00808  85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 154 rfeaheidsfvilkeDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPIILGESGSKMS 233
Cdd:cd00808 101 ---------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGW-EPPKFAHLPLILNPDGKKLS 164

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67461998 234 KRDNASSVAWLLEEGFLPQAIMNYLISMGNHTP--TEVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNREHLKM 306
Cdd:cd00808 165 KRKGDTSISDYREEGYLPEALLNYLALLGWSPPdgEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIRE 239
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 3-298 2.31e-71

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: 227.59  E-value: 2.31e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998     3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDNLV-YQSSNFERHRQL 81
Cdd:pfam00749   5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPyYQSDRFDIYYKY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    82 AQHLISKDLAFYCYCSKEFLESKR--LEAKEQKKPFRYD----PSWAEIEKS---SNTKPVVRIRGASEA-ISFEDAIKG 151
Cdd:pfam00749  85 AEELIKKGKAYVCFCTPEELEEEReeQEALGSPSRDRYDeenlHLFEEEMKKgsaEGGPATVRAKIPMESpYVFRDPVRG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   152 TLRFEAHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYDKVLgYAHLPIILGESGSK 231
Cdd:pfam00749 165 RIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPP-FIHEYLRLNLDGTK 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67461998   232 MSKRDNASSVA--WLLEEGFLPQAIMNYLISMGnHTPT---EVFKLQDAYNWFDIKNIAKSPVKFDIKRLRF 298
Cdd:pfam00749 244 LSKRKLSWSVDisQVKGWGDPREATLNGLRRRG-WTPEgirEFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
queuosine_YadB TIGR03838
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ...
 3-242 3.23e-56

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: 186.98  E-value: 3.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998     3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWD-NLVYQSSNFERHRQL 81
Cdd:TIGR03838   4 RFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDgEVVYQSQRHALYQAA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    82 AQHLISKDLAFYCYCS-KEFLESKRLEA--------KEQKKPFRyDPSWaeiekssntkpvvRIRGASEAISFEDAIKGT 152
Cdd:TIGR03838  84 LDRLLAAGLAYPCQCTrKEIAAARDGGGiypgtcrnGLPGRPGR-PAAW-------------RLRVPDGVIAFDDRLQGP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   153 LRFE-AHEIDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPIILGESGSK 231
Cdd:TIGR03838 150 QQQDlAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGL-PPPRYLHLPLVVNADGEK 228

                         250
                  ....*....|.
gi 67461998   232 MSKRDNASSVA 242
Cdd:TIGR03838 229 LSKQNGAPALD 239
PRK05710 PRK05710
tRNA glutamyl-Q(34) synthetase GluQRS;
3-278 7.85e-56

tRNA glutamyl-Q(34) synthetase GluQRS;


Pssm-ID: 235573  Cd Length: 299  Bit Score: 186.98  E-value: 7.85e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDN-LVYQSSNFERHRQL 81
Cdd:PRK05710   9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGpVLYQSQRHDAYRAA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   82 AQHLISKDLAFYCYCS-KEFLESKRLEAKEqkkPFRYDPSWAEIEKSSNTKPVVRIRGASEAISFEDAIKGTLRFE-AHE 159
Cdd:PRK05710  89 LDRLRAQGLVYPCFCSrKEIAAAAPAPPDG---GGIYPGTCRDLLHGPRNPPAWRLRVPDAVIAFDDRLQGRQHQDlALA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  160 IDSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPIILGESGSKMSKRDNAS 239
Cdd:PRK05710 166 VGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGL-PTPRYLHLPLVLNADGQKLSKQNGAP 244

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 67461998  240 SVAwllEEGFLPqAIMNYLISMGNHTPTEVFKLQDAYNW 278
Cdd:PRK05710 245 ALD---AAGPLP-VLAAALRFLGQPPPAADASVEELLAQ 279
GlxRS_core cd00418
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ...
 3-306 1.61e-48

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: 165.72  E-value: 1.61e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWD-NLVYQSSNFERHRQL 81
Cdd:cd00418   5 RFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDeGPYRQSDRFDLYRAY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  82 AQHLIskdlafycycskefleskrleakeqkkpfrydpswaeiekssntkpvvrirgaseaisfedaikgtlrfeaheid 161
Cdd:cd00418  85 AEELI--------------------------------------------------------------------------- 89

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 162 sfvilKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYdKVLGYAHLPIILGESGSKMSKRDNASSV 241
Cdd:cd00418  90 -----KKGGYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGW-EPPRFYHFPRLLLEDGTKLSKRKLNTTL 163

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67461998 242 AWLLEEGFLPQAIMNYLISMGNHTP--TEVFKLQDAYNWFDIKNIAKSPVKFDIKRLRFLNREHLKM 306
Cdd:cd00418 164 RALRRRGYLPEALRNYLALIGWSKPdgHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNREYIRE 230
gltX PRK04156
glutamyl-tRNA synthetase; Provisional
 2-262 5.21e-25

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 235229 [Multi-domain]  Cd Length: 567  Bit Score: 107.63  E-value: 5.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    2 LRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTD--IARNIVDKDKEILNLLNLFGLLWDNLVYQSSNFERHR 79
Cdd:PRK04156 104 MRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWDEVVIQSDRLEIYY 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   80 QLAQHLISKDLAFYCYCSKEflESKRLEAKEQKKPFR-YDPSWA--EIEKS-----SNTKPVVRIRgasEAISFED-AIK 150
Cdd:PRK04156 184 EYARKLIEMGGAYVCTCDPE--EFKELRDAGKPCPHRdKSPEENleLWEKMldgeyKEGEAVVRVK---TDLEHPNpSVR 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  151 --GTLRFEAH----EIDSFVILkedgiPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALG--YDKVLGYAHLP 222
Cdd:PRK04156 259 dwVAFRIVKTphprVGDKYRVW-----PTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGweYPETIHYGRLK 333

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 67461998  223 I---ILgeSGSKMSKR-DNASSVAW----------LLEEGFLPQAIMNYLISMG 262
Cdd:PRK04156 334 IegfVL--STSKIRKGiEEGEYSGWddprlptlraLRRRGILPEAIRELIIEVG 385
GluRS_non_core cd09287
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ...
 2-262 2.82e-22

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: 95.11  E-value: 2.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   2 LRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKD--KEILNLLNLFGLLWDNLVYQSSNFERHR 79
Cdd:cd09287   4 MRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEayDMIPEDLEWLGVKWDEVVIASDRIELYY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  80 QLAQHLISKDLAFycycskefleskrleakeqkkpfrydpswaeiekssntkpvVRIRGASEAISFedaikgtlrfeahe 159
Cdd:cd09287  84 EYARKLIEMGGAY-----------------------------------------VHPRTGSKYRVW-------------- 108

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 160 idsfvilkedgiPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALG--YDKVLGYAHLPIILGE-SGSKMSKRD 236
Cdd:cd09287 109 ------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGweYPETIHWGRLKIEGGKlSTSKIRKGI 176

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 67461998 237 NAS-----------SVAWLLEEGFLPQAIMNYLISMG 262
Cdd:cd09287 177 ESGeyegwddprlpTLRALRRRGIRPEAIRDFIIEVG 213
gltX_arch TIGR00463
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ...
 1-262 1.26e-20

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: 94.12  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998     1 MLRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDNLVYQSSNFERHRQ 80
Cdd:TIGR00463  95 VMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYD 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    81 LAQHLISKDLAFYCYCSKEFLESKRLEAKEQKkpfRYDPS-------WAEIE--KSSNTKPVVRIRGASEAI--SFEDAI 149
Cdd:TIGR00463 175 YTRKLIEMGKAYVCDCRPEEFRELRNRGEACH---CRDRSveenlerWEEMLegKEEGGSVVVRVKTDLKHKnpAIRDWV 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   150 KGTLRFEAHEI--DSFVILkedgiPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALG--YDKVLGYAHLPIIL 225
Cdd:TIGR00463 252 IFRIVKTPHPRtgDKYRVY-----PTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGwePPEFIHWGRLKIDD 326

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 67461998   226 GESGSKMSKRD---NASSVAW----------LLEEGFLPQAIMNYLISMG 262
Cdd:TIGR00463 327 VRALSTSSARKgilRGEYSGWddprlptlraIRRRGIRPEAIRKFMLSIG 376
PLN03233 PLN03233
putative glutamate-tRNA ligase; Provisional
 3-248 4.60e-10

putative glutamate-tRNA ligase; Provisional


Pssm-ID: 178772 [Multi-domain]  Cd Length: 523  Bit Score: 61.56  E-value: 4.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDNLVYQSSNFERHRQLA 82
Cdd:PLN03233  15 RFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPIRCYA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   83 QHLISKDLAFYCYCSKEFLESKRLEAKEQKKPFRYDPSWAEI--EKSSNTKP------VVRIRGASEAISFEDAIKGTLR 154
Cdd:PLN03233  95 IILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMfkEMCSGKEEggawclRAKIDMQSDNGTLRDPVLFRQN 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  155 FEAHEiDSFVILKedGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYDKVL--GYAHLPIIlgesGSKM 232
Cdd:PLN03233 175 TTPHH-RSGTAYK--AYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRihAFARMNFM----NTVL 247

                        250
                 ....*....|....*.
gi 67461998  233 SKRdnasSVAWLLEEG 248
Cdd:PLN03233 248 SKR----KLTWFVDNG 259
GlnRS_core cd00807
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ...
 3-92 1.61e-09

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: 58.03  E-value: 1.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTdiarNIVDKDKE----ILNLLNLFGLLWDNLVYQSSNFERH 78
Cdd:cd00807   5 RFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDT----NPEKEEEEyvdsIKEDVKWLGIKPYKVTYASDYFDQL 80

                        90
                ....*....|....
gi 67461998  79 RQLAQHLISKDLAF 92
Cdd:cd00807  81 YEYAEQLIKKGKAY 94
PTZ00402 PTZ00402
glutamyl-tRNA synthetase; Provisional
 3-235 2.82e-09

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 240404 [Multi-domain]  Cd Length: 601  Bit Score: 59.21  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWD-NLVYQSSNFERHRQL 81
Cdd:PTZ00402  56 RFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDvGPTYSSDYMDLMYEK 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   82 AQHLISKDLAfycYCSK---EFLESKRLEAkeqkKPFRY-DPS-------WAEIEKSSNTKPVVRIRGaseAISFED--- 147
Cdd:PTZ00402 136 AEELIKKGLA---YCDKtprEEMQKCRFDG----VPTKYrDISveetkrlWNEMKKGSAEGQETCLRA---KISVDNenk 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998  148 AIKGTLRFEAHEI-DSFVILKEDGIPTYNFACAIDDMLYDISFIVRGEDHVSNTPRQILIHRALGYDKvlgyahlPII-- 224
Cdd:PTZ00402 206 AMRDPVIYRVNLTpHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRK-------PIVed 278

                        250
                 ....*....|....
gi 67461998  225 ---LGESGSKMSKR 235
Cdd:PTZ00402 279 fsrLNMEYSVMSKR 292
PLN02907 PLN02907
glutamate-tRNA ligase
 2-112 3.85e-06

glutamate-tRNA ligase


Pssm-ID: 215492 [Multi-domain]  Cd Length: 722  Bit Score: 49.34  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    2 LRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDIARNIVDKDKEILNLLNLFGLLWDNLVYQSSNFERHRQL 81
Cdd:PLN02907 216 TRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEM 295

                         90       100       110
                 ....*....|....*....|....*....|.
gi 67461998   82 AQHLISKDLAFYCYCSKEFLESKRLEAKEQK 112
Cdd:PLN02907 296 AEKLIKEGKAYVDDTPREQMRKERMDGIESK 326
PLN02859 PLN02859
glutamine-tRNA ligase
 1-127 3.28e-05

glutamine-tRNA ligase


Pssm-ID: 178450 [Multi-domain]  Cd Length: 788  Bit Score: 46.29  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    1 MLRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDI---ARNIVDKDKEIlnllnLFGLLWD--NLVYQSSNF 75
Cdd:PLN02859 266 YTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPeaeKKEYIDHIEEI-----VEWMGWEpfKITYTSDYF 340

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 67461998   76 ERHRQLAQHLISKDLAFYCYCSKEflESKRLEAKEQKKPFRYDPswaeIEKS 127
Cdd:PLN02859 341 QELYELAVELIRRGHAYVDHQTPE--EIKEYREKKMNSPWRDRP----IEES 386
PRK14703 PRK14703
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
 3-92 8.59e-05

glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional


Pssm-ID: 237793 [Multi-domain]  Cd Length: 771  Bit Score: 45.10  E-value: 8.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTdiarNIVDKDKE----ILNLLNLFGLLW-DNLVYQSSNFER 77
Cdd:PRK14703  35 RFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDT----NPETEDTEyveaIKDDVRWLGFDWgEHLYYASDYFER 110

                         90
                 ....*....|....*
gi 67461998   78 HRQLAQHLISKDLAF 92
Cdd:PRK14703 111 MYAYAEQLIKMGLAY 125
Anticodon_2 pfam19269
Anticodon binding domain; This entry represents the anticodon binding domain found at the ...
 330-425 9.47e-05

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: 42.56  E-value: 9.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   330 HLQE-ASTLNEIRSKIERIFS------PKCIAQNEEGENFENECKILYDILHQM--IESYD-ESLndYDTFKnALMAKSS 399
Cdd:pfam19269  29 LLKErAETLSELAELADFFFElpleydEEAYAKKKMKTNKEESLEVLQELLPRLeaLEDWTaEAL--EAALK-ALAEELG 105

                          90       100
                  ....*....|....*....|....*.
gi 67461998   400 LKGKKFFKPLRILLTGQTQGLELSEI 425
Cdd:pfam19269 106 VKNGKVMWPLRVALTGKTVSPGLFEI 131
ArgS COG0018
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ...
 163-295 1.54e-04

Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439789 [Multi-domain]  Cd Length: 574  Bit Score: 43.98  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998 163 FVILKEDGIPTYnF----ACAID---DMLYDISFIVRGEDHVSNTPRQILIHRALGYDKVLGYAHLPI--ILGESGSKMS 233
Cdd:COG0018 303 RVLVKSDGTYTY-FttdiAYHLYkfeRYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFgmVNLRDGEKMS 381

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67461998 234 KRD-NASSVAWLLEEgflpqAIMNYLISMGNHTPTEVFKLQ-----DAYNWFDIKNIAKSPVKFDIKR 295
Cdd:COG0018 382 TRAgTVVTLDDLLDE-----AVERAREIIEEKSEEEKEEIAeqvgiDAVRYFDLSRSRDKDLDFDLDL 444
PTZ00437 PTZ00437
glutaminyl-tRNA synthetase; Provisional
 2-189 2.64e-04

glutaminyl-tRNA synthetase; Provisional


Pssm-ID: 240418 [Multi-domain]  Cd Length: 574  Bit Score: 43.43  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    2 LRFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTDiarniVDKDKEILNLLNLFGLLW-----DNLVYQSSNFE 76
Cdd:PTZ00437  54 FRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTN-----PETEEQVYIDAIMEMVKWmgwkpDWVTFSSDYFD 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998   77 RHRQLAQHLISKDLAFYCYCSKEFLESKRlEAKEQkKPFRYDP--------------SWAEIEKSSNtkpvVRIRGASEA 142
Cdd:PTZ00437 129 QLHEFAVQLIKDGKAYVDHSTPDELKQQR-EQRED-SPWRNRSveenlllfehmrqgRYAEGEATLR----VKADMKSDN 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 67461998  143 ISFEDAIKGTLRFEAHE--IDSFVILkedgiPTYNFACAIDDMLYDISF 189
Cdd:PTZ00437 203 PNMRDFIAYRVKYVEHPhaKDKWCIY-----PSYDFTHCLIDSLEDIDY 246
PRK05347 PRK05347
glutaminyl-tRNA synthetase; Provisional
 3-99 3.17e-03

glutaminyl-tRNA synthetase; Provisional


Pssm-ID: 235424 [Multi-domain]  Cd Length: 554  Bit Score: 39.70  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67461998    3 RFAPSPTGDMHIGNLRAAIFNYIIAKQQNQKFLIRIEDTdiarNIVDKDKE----ILNLLNLFGLLWDNLVYQSSN-FER 77
Cdd:PRK05347  33 RFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDT----NPEKEDQEyvdsIKEDVRWLGFDWSGELRYASDyFDQ 108

                         90       100
                 ....*....|....*....|..
gi 67461998   78 HRQLAQHLISKDLAFYCYCSKE 99
Cdd:PRK05347 109 LYEYAVELIKKGKAYVDDLSAE 130
 
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.
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