|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-423 |
1.37e-161 |
|
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: 463.50 E-value: 1.37e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIrsLQDKSG--FILRIEDTDTARNIEGKDKDIMEILSLFGIKW-QTLYYQSKNLKFHQ 79
Cdd:COG0008 8 RFAPSPTGYLHIGHARTALFNWL--FARKYGgkFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDRFDIYY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 80 EFAAKLLQEGKAFCCFCSEEELSAKKEKAKEKGVAYRYDGTCEHLSDAEV---IDNPKPFTIRLKKPTRVLKFTDAIKGE 156
Cdd:COG0008 86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELermLAAGEPPVLRFKIPEEGVVFDDLVRGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 157 ISFEPENIDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYtDEISYAHLPIILGPDGKKM 236
Cdd:COG0008 166 ITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGW-EPPEFAHLPLILGPDGTKL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 237 SKRDDASSVKWMLDTGFLPEAIANYLVLLGNK--TPREVFSIEEAVEFFDIAKISKAPAKFDIDKLAFINREHIKRASAK 314
Cdd:COG0008 245 SKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSksDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALDDE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 315 RICELF-------GVDESKVELVKFYTQESSLIPEIKAKINAIFSQKE---------IPAEFSQNAEILRNEILNLTQI- 377
Cdd:COG0008 325 ELAELLapelpeaGIREDLERLVPLVRERAKTLSELAELARFFFIEREdekaakkrlAPEEVRKVLKAALEVLEAVETWd 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2428128515 378 PAEFNELKTILMERTALKGKAFFMPLRLLLTGAPHGPELNELYPLI 423
Cdd:COG0008 405 PETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELL 450
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
1-430 |
4.92e-145 |
|
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: 421.76 E-value: 4.92e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 1 MYRFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKW-QTLYYQSKNLKFHQ 79
Cdd:TIGR00464 3 RTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWdEGPYYQSQRLDIYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 80 EFAAKLLQEGKAFCCFCSEEELSAKKEKAKEKGVAYRYDGTCEHLSDAEV---IDNPKPFTIRLKKPTR-VLKFTDAIKG 155
Cdd:TIGR00464 83 KYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIenkLAKGIPPVVRFKIPQEaVVSFNDQVRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 156 EISFEPENIDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYtDEISYAHLPIILGPDGKK 235
Cdd:TIGR00464 163 EITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGW-KIPVFAHLPMILDEDGKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 236 MSKRDDASSVKWMLDTGFLPEAIANYLVLLGNKTP--REVFSIEEAVEFFDIAKISKAPAKFDIDKLAFINREHIKRASA 313
Cdd:TIGR00464 242 LSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPddQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 314 KRICEL--------FGVDESK----VELVKFYTQESSLIPEIKAKINAIFSQKEI----------PAEFSQNAEILRNEI 371
Cdd:TIGR00464 322 EELFELldphlkslVNTDTLNreqlAELLLLFKERLKTLKEIAELIRLFFEDKKEvdedafkkhlKKNVKEVLEALKKKL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2428128515 372 LNLT-QIPAEFNELKTILMERTALKGKAFFMPLRLLLTGAPHGPELNELYPLI--KSSIKEI 430
Cdd:TIGR00464 402 QALEeWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIgkTESIKRL 463
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
3-423 |
2.35e-90 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 283.56 E-value: 2.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKWQT---------LYYQSK 73
Cdd:PLN02627 49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgpdvggeygPYRQSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 74 NLKFHQEFAAKLLQEGKAFCCFCSEEELSAKKEKAKEKGVAYRYDGTCEHLSDAEV---IDNPKPFTIRLKKP-TRVLKF 149
Cdd:PLN02627 129 RNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVqaeLAKGTPYTYRFRVPkEGSVKI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 150 TDAIKGEISFEPENIDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYTDEiSYAHLPIIL 229
Cdd:PLN02627 209 DDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMP-RFAHVSLIL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 230 GPDGKKMSKRDDASSVKWMLDTGFLPEAIANYLVLLG--NKTPREVFSIEEAVEFFDIAKISKAPAKFDIDKLAFINREH 307
Cdd:PLN02627 288 APDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGwnDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQH 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 308 IKRASAKRICELFGVDESKVELVKfyTQESSLIPE----IKAKINAIF-SQKEIPAEFSQN-AEILRNEIL------NLT 375
Cdd:PLN02627 368 LRLLPEEELVKLVGERWKSAGILK--ESDGSFVKEavelLKDGIELVTdADKELLNLLSYPlAATLSSPEAktvvedNFS 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2428128515 376 QIPA------EFNELKTILMERTA--------------LKGKAFFMPLRLLLTGAPHGPELNELYPLI 423
Cdd:PLN02627 446 EVADaliaayDSGELAAALEEGHDgwqkwvkafgkalkRKGKRLFMPLRVALTGKMHGPDVGESLVLL 513
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-300 |
2.44e-90 |
|
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: 276.51 E-value: 2.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKWQ-TLYYQSKNLKFHQEF 81
Cdd:pfam00749 5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDIYYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 82 AAKLLQEGKAFCCFCSEEELSAKKEKAKEKGVAY--RYDGTCEHLSDAEV---IDNPKPFTIRLKKPTR-VLKFTDAIKG 155
Cdd:pfam00749 85 AEELIKKGKAYVCFCTPEELEEEREEQEALGSPSrdRYDEENLHLFEEEMkkgSAEGGPATVRAKIPMEsPYVFRDPVRG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 156 EISFEPENIDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYtDEISYAHLPIILGPDGKK 235
Cdd:pfam00749 165 RIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGW-EPPPFIHEYLRLNLDGTK 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 236 MSKRDDASSV--KWMLDTGFLPEAIANYLVLLGnKTP---REVFSIEEAVEFFDIAKISKAPAKFDIDKL 300
Cdd:pfam00749 244 LSKRKLSWSVdiSQVKGWGDPREATLNGLRRRG-WTPegiREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
3-310 |
2.64e-84 |
|
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: 258.29 E-value: 2.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKW---------QTLYYQSK 73
Cdd:cd00808 5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWdegpdvggpYGPYRQSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 74 NLKFHQEFAAKLLQEGkafccfcseeelsakkekakekgvayrydgtcehlsdaevidnpkpftirlkkptrvlkftdai 153
Cdd:cd00808 85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 154 kgeisfepenidsfvimraDKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYTDEIsYAHLPIILGPDG 233
Cdd:cd00808 101 -------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPK-FAHLPLILNPDG 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2428128515 234 KKMSKRDDASSVKWMLDTGFLPEAIANYLVLLGNKTP--REVFSIEEAVEFFDIAKISKAPAKFDIDKLAFINREHIKR 310
Cdd:cd00808 161 KKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPdgEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIRE 239
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-423 |
1.37e-161 |
|
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: 463.50 E-value: 1.37e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIrsLQDKSG--FILRIEDTDTARNIEGKDKDIMEILSLFGIKW-QTLYYQSKNLKFHQ 79
Cdd:COG0008 8 RFAPSPTGYLHIGHARTALFNWL--FARKYGgkFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDRFDIYY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 80 EFAAKLLQEGKAFCCFCSEEELSAKKEKAKEKGVAYRYDGTCEHLSDAEV---IDNPKPFTIRLKKPTRVLKFTDAIKGE 156
Cdd:COG0008 86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELermLAAGEPPVLRFKIPEEGVVFDDLVRGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 157 ISFEPENIDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYtDEISYAHLPIILGPDGKKM 236
Cdd:COG0008 166 ITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGW-EPPEFAHLPLILGPDGTKL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 237 SKRDDASSVKWMLDTGFLPEAIANYLVLLGNK--TPREVFSIEEAVEFFDIAKISKAPAKFDIDKLAFINREHIKRASAK 314
Cdd:COG0008 245 SKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSksDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALDDE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 315 RICELF-------GVDESKVELVKFYTQESSLIPEIKAKINAIFSQKE---------IPAEFSQNAEILRNEILNLTQI- 377
Cdd:COG0008 325 ELAELLapelpeaGIREDLERLVPLVRERAKTLSELAELARFFFIEREdekaakkrlAPEEVRKVLKAALEVLEAVETWd 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2428128515 378 PAEFNELKTILMERTALKGKAFFMPLRLLLTGAPHGPELNELYPLI 423
Cdd:COG0008 405 PETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELL 450
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
1-430 |
4.92e-145 |
|
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: 421.76 E-value: 4.92e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 1 MYRFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKW-QTLYYQSKNLKFHQ 79
Cdd:TIGR00464 3 RTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWdEGPYYQSQRLDIYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 80 EFAAKLLQEGKAFCCFCSEEELSAKKEKAKEKGVAYRYDGTCEHLSDAEV---IDNPKPFTIRLKKPTR-VLKFTDAIKG 155
Cdd:TIGR00464 83 KYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIenkLAKGIPPVVRFKIPQEaVVSFNDQVRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 156 EISFEPENIDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYtDEISYAHLPIILGPDGKK 235
Cdd:TIGR00464 163 EITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGW-KIPVFAHLPMILDEDGKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 236 MSKRDDASSVKWMLDTGFLPEAIANYLVLLGNKTP--REVFSIEEAVEFFDIAKISKAPAKFDIDKLAFINREHIKRASA 313
Cdd:TIGR00464 242 LSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPddQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 314 KRICEL--------FGVDESK----VELVKFYTQESSLIPEIKAKINAIFSQKEI----------PAEFSQNAEILRNEI 371
Cdd:TIGR00464 322 EELFELldphlkslVNTDTLNreqlAELLLLFKERLKTLKEIAELIRLFFEDKKEvdedafkkhlKKNVKEVLEALKKKL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2428128515 372 LNLT-QIPAEFNELKTILMERTALKGKAFFMPLRLLLTGAPHGPELNELYPLI--KSSIKEI 430
Cdd:TIGR00464 402 QALEeWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIgkTESIKRL 463
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
3-423 |
2.35e-90 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 283.56 E-value: 2.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKWQT---------LYYQSK 73
Cdd:PLN02627 49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgpdvggeygPYRQSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 74 NLKFHQEFAAKLLQEGKAFCCFCSEEELSAKKEKAKEKGVAYRYDGTCEHLSDAEV---IDNPKPFTIRLKKP-TRVLKF 149
Cdd:PLN02627 129 RNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVqaeLAKGTPYTYRFRVPkEGSVKI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 150 TDAIKGEISFEPENIDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYTDEiSYAHLPIIL 229
Cdd:PLN02627 209 DDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMP-RFAHVSLIL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 230 GPDGKKMSKRDDASSVKWMLDTGFLPEAIANYLVLLG--NKTPREVFSIEEAVEFFDIAKISKAPAKFDIDKLAFINREH 307
Cdd:PLN02627 288 APDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGwnDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQH 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 308 IKRASAKRICELFGVDESKVELVKfyTQESSLIPE----IKAKINAIF-SQKEIPAEFSQN-AEILRNEIL------NLT 375
Cdd:PLN02627 368 LRLLPEEELVKLVGERWKSAGILK--ESDGSFVKEavelLKDGIELVTdADKELLNLLSYPlAATLSSPEAktvvedNFS 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2428128515 376 QIPA------EFNELKTILMERTA--------------LKGKAFFMPLRLLLTGAPHGPELNELYPLI 423
Cdd:PLN02627 446 EVADaliaayDSGELAAALEEGHDgwqkwvkafgkalkRKGKRLFMPLRVALTGKMHGPDVGESLVLL 513
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-300 |
2.44e-90 |
|
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: 276.51 E-value: 2.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKWQ-TLYYQSKNLKFHQEF 81
Cdd:pfam00749 5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDIYYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 82 AAKLLQEGKAFCCFCSEEELSAKKEKAKEKGVAY--RYDGTCEHLSDAEV---IDNPKPFTIRLKKPTR-VLKFTDAIKG 155
Cdd:pfam00749 85 AEELIKKGKAYVCFCTPEELEEEREEQEALGSPSrdRYDEENLHLFEEEMkkgSAEGGPATVRAKIPMEsPYVFRDPVRG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 156 EISFEPENIDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYtDEISYAHLPIILGPDGKK 235
Cdd:pfam00749 165 RIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGW-EPPPFIHEYLRLNLDGTK 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 236 MSKRDDASSV--KWMLDTGFLPEAIANYLVLLGnKTP---REVFSIEEAVEFFDIAKISKAPAKFDIDKL 300
Cdd:pfam00749 244 LSKRKLSWSVdiSQVKGWGDPREATLNGLRRRG-WTPegiREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
3-310 |
2.64e-84 |
|
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: 258.29 E-value: 2.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKW---------QTLYYQSK 73
Cdd:cd00808 5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWdegpdvggpYGPYRQSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 74 NLKFHQEFAAKLLQEGkafccfcseeelsakkekakekgvayrydgtcehlsdaevidnpkpftirlkkptrvlkftdai 153
Cdd:cd00808 85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 154 kgeisfepenidsfvimraDKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYTDEIsYAHLPIILGPDG 233
Cdd:cd00808 101 -------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPK-FAHLPLILNPDG 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2428128515 234 KKMSKRDDASSVKWMLDTGFLPEAIANYLVLLGNKTP--REVFSIEEAVEFFDIAKISKAPAKFDIDKLAFINREHIKR 310
Cdd:cd00808 161 KKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPdgEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIRE 239
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
3-293 |
1.17e-67 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 217.41 E-value: 1.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNY--IRSLQDKsgFILRIEDTDTARNIEGKDKDIMEILSLFGIKW-QTLYYQSKNLKFHQ 79
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWldARAHGGR--WLLRIEDIDPPREVPGAADAILADLEWLGLHWdGPVLYQSQRHDAYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 80 EFAAKLLQEGKAFCCFCSEEELSAKKEKAKEKGVAYryDGTCEHLSDAEvidnPKPFTIRLKKPTRVLKFTDAIKGEISF 159
Cdd:PRK05710 87 AALDRLRAQGLVYPCFCSRKEIAAAAPAPPDGGGIY--PGTCRDLLHGP----RNPPAWRLRVPDAVIAFDDRLQGRQHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 160 EPEN-IDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYTdEISYAHLPIILGPDGKKMSK 238
Cdd:PRK05710 161 DLALaVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLP-TPRYLHLPLVLNADGQKLSK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2428128515 239 RDDASSvkwmLDTGFLPEAIANYLVLLGNKTP----REVFSIEEAVEFFDIAKISKAPA 293
Cdd:PRK05710 240 QNGAPA----LDAAGPLPVLAAALRFLGQPPPaadaSVEELLAQAVAHWDLTRLPRQAE 294
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
3-242 |
7.36e-60 |
|
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: 196.22 E-value: 7.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYI--RSLQDKsgFILRIEDTDTARNIEGKDKDIMEILSLFGIKW-QTLYYQSKNLKFHQ 79
Cdd:TIGR03838 4 RFAPSPSGPLHFGSLVAALGSYLdaRAHGGR--WLVRIEDLDPPREVPGAADDILRTLEAYGLHWdGEVVYQSQRHALYQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 80 EFAAKLLQEGKAFCCFCSEEELSakkekaKEKGVAYRYDGTCEHLSDAEVidnPKPFTIRLKKPTRVLKFTDAIKGEISF 159
Cdd:TIGR03838 82 AALDRLLAAGLAYPCQCTRKEIA------AARDGGGIYPGTCRNGLPGRP---GRPAAWRLRVPDGVIAFDDRLQGPQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 160 EPE-NIDSFVIMRADKTPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYTdEISYAHLPIILGPDGKKMSK 238
Cdd:TIGR03838 153 DLAaAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLP-PPRYLHLPLVVNADGEKLSK 231
|
....
gi 2428128515 239 RDDA 242
Cdd:TIGR03838 232 QNGA 235
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
3-309 |
3.39e-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: 193.07 E-value: 3.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKW-QTLYYQSKNLKFHQEF 81
Cdd:cd00418 5 RFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWdEGPYRQSDRFDLYRAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 82 AAKLLQEGkafccfcseeelsakkekakekgvAYrydgtcehlsdaevidnpkpftirlkkptrvlkftdaikgeisfep 161
Cdd:cd00418 85 AEELIKKG------------------------GY---------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 162 enidsfvimradktPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGYTDEiSYAHLPIILGPDGKKMSKRDD 241
Cdd:cd00418 95 --------------PLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPP-RFYHFPRLLLEDGTKLSKRKL 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 242 ASSVKWMLDTGFLPEAIANYLVLLGNKTP--REVFSIEEAVEFFDIAKISKAPAKFDIDKLAFINREHIK 309
Cdd:cd00418 160 NTTLRALRRRGYLPEALRNYLALIGWSKPdgHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNREYIR 229
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
3-308 |
2.50e-36 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 140.37 E-value: 2.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTD--TAR-NIEGKDkDIMEILSLFGIKWQTLYYQSKNLKFHQ 79
Cdd:PRK04156 105 RFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRpDPEAYD-MILEDLKWLGVKWDEVVIQSDRLEIYY 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 80 EFAAKLLQEGKAFCCFCSEEELSakkekakekgvAYRYDGT-CEHlsdaevidnpkpftiRLKKPTRVLK-FTDAIKGEI 157
Cdd:PRK04156 184 EYARKLIEMGGAYVCTCDPEEFK-----------ELRDAGKpCPH---------------RDKSPEENLElWEKMLDGEY 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 158 SfEPE--------------NIDSFVIMRADKT------------PTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIR 211
Cdd:PRK04156 238 K-EGEavvrvktdlehpnpSVRDWVAFRIVKTphprvgdkyrvwPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 212 ECLG--YTDEISYAHLPIilgpDGKKMSKrddaSSVKWMLDT--------------------GFLPEAIANYLVLLGnkt 269
Cdd:PRK04156 317 DYFGweYPETIHYGRLKI----EGFVLST----SKIRKGIEEgeysgwddprlptlralrrrGILPEAIRELIIEVG--- 385
|
330 340 350
....*....|....*....|....*....|....*....
gi 2428128515 270 prevfsieeaveffdiakISKAPAKFDIDKLAFINREHI 308
Cdd:PRK04156 386 ------------------VKETDATISWENLYAINRKLI 406
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
3-330 |
4.67e-34 |
|
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: 133.79 E-value: 4.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKWQTLYYQSKNLKFHQEFA 82
Cdd:TIGR00463 97 RFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 83 AKLLQEGKAFCCFCSEEELSAkkekakekgvaYRYDGTCEHLSDAEVIDNPKPFTIRLKKPTRVLKFTDAIKGEISFEPE 162
Cdd:TIGR00463 177 RKLIEMGKAYVCDCRPEEFRE-----------LRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 163 NIDSFVIMRADKT------------PTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLG--YTDEISYAHLPIi 228
Cdd:TIGR00463 246 AIRDWVIFRIVKTphprtgdkyrvyPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGwePPEFIHWGRLKI- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 229 lgPDGKKMSKrddASSVKWMLD-------------------TGFLPEAIANYLVLLGnktprevfsieeaveffdiakIS 289
Cdd:TIGR00463 325 --DDVRALST---SSARKGILRgeysgwddprlptlrairrRGIRPEAIRKFMLSIG---------------------VK 378
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2428128515 290 KAPAKFDIDKLAFINREHIKRaSAKRIceLFGVDESKVELV 330
Cdd:TIGR00463 379 INDVTMSWKNIYALNRKIIDE-EARRY--FFIWNPVKIEIV 416
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
3-308 |
4.85e-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: 113.60 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKD--KDIMEILSLFGIKWQTLYYQSKNLKFHQE 80
Cdd:cd09287 5 RFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEayDMIPEDLEWLGVKWDEVVIASDRIELYYE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 81 FAAKLLQEGKAFCcfcseeelsakkekakekgvayrydgtcehlsdaevidnpkpftirlkkptrvlkftdaikgeisfE 160
Cdd:cd09287 85 YARKLIEMGGAYV------------------------------------------------------------------H 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 161 PENIDSFVIMradktPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLG--YTDEISYAHLPIilgpDGKKMSK 238
Cdd:cd09287 99 PRTGSKYRVW-----PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGweYPETIHWGRLKI----EGGKLST 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 239 rddaSSVKWMLDT--------------------GFLPEAIANYLVLLGnktprevfsieeaveffdiakISKAPAKFDID 298
Cdd:cd09287 170 ----SKIRKGIESgeyegwddprlptlralrrrGIRPEAIRDFIIEVG---------------------VKQTDATISWE 224
|
330
....*....|
gi 2428128515 299 KLAFINREHI 308
Cdd:cd09287 225 NLYAINRKLI 234
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
3-215 |
5.13e-16 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 80.01 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKWQT-LYYQSKNLKFHQEF 81
Cdd:PTZ00402 56 RFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVgPTYSSDYMDLMYEK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 82 AAKLLQEGKAFCCFCSEEELSAKkekakekgvayRYDGTCEHLSDAEVIDNPKPFTiRLKKPTRVLKFTdAIKGEISFEP 161
Cdd:PTZ00402 136 AEELIKKGLAYCDKTPREEMQKC-----------RFDGVPTKYRDISVEETKRLWN-EMKKGSAEGQET-CLRAKISVDN 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2428128515 162 EN--IDSFVIMRADKT------------PTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLG 215
Cdd:PTZ00402 203 ENkaMRDPVIYRVNLTpharqgtkykayPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALG 270
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
3-314 |
2.88e-13 |
|
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: 69.20 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKWQTLYYQSKNLKFHQEFA 82
Cdd:cd00807 5 RFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLYEYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 83 AKLLQEGKAFCCFcseeelsakkekakEKGVAYR-Ydgtcehlsdaevidnpkpftirlkkptrvlkftdaikgeisfep 161
Cdd:cd00807 85 EQLIKKGKAYVHH--------------RTGDKWCiY-------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 162 enidsfvimradktPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLGY--TDEISYAHLPIIlgpdGKKMSKR 239
Cdd:cd00807 107 --------------PTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLyrPHQWEFSRLNLT----YTVMSKR 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 240 --------------DDAS--SVKWMLDTGFLPEAIANYLVLLGnktprevfsieeaveffdiakISKAPAKFDIDKLAFI 303
Cdd:cd00807 169 kllqlvdegyvdgwDDPRlpTLRGLRRRGVTPEAIRQFILRQG---------------------VSKADSTIDWDKLEAC 227
|
330
....*....|.
gi 2428128515 304 NREHIKRASAK 314
Cdd:cd00807 228 VRKDLNPTAPR 238
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
3-215 |
7.68e-12 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 66.96 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTARNIEGKDKDIMEILSLFGIKWQTLYYQSKNLKFHQEFA 82
Cdd:PLN03233 15 RFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPIRCYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 83 AKLLQEGKAFCCFCSEEELSAKKEKAKEKgvAYRYDGTCEHLSDAEVI----DNPKPFTIRLKkptrvlkftdaikgeIS 158
Cdd:PLN03233 95 IILIEEGLAYMDDTPQEEMKKERADRAES--KHRNQSPEEALEMFKEMcsgkEEGGAWCLRAK---------------ID 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2428128515 159 FEPEN--IDSFVIMRADKT------------PTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLG 215
Cdd:PLN03233 158 MQSDNgtLRDPVLFRQNTTphhrsgtaykayPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALG 228
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
3-215 |
1.61e-08 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 56.66 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTDTArniegKDKD-----IMEILSLFGIKWQTLYYQSKNLKF 77
Cdd:PLN02907 217 RFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPS-----KESDefvenILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 78 HQEFAAKLLQEGKAFCCFCSEEELSAKkekakekgvayRYDGTCEHLSDAEVIDNpkpftIRLKK-----PTRVLKftDA 152
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKE-----------RMDGIESKCRNNSVEEN-----LRLWKemiagSERGLQ--CC 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2428128515 153 IKGEISFEPEN--IDSFVIMRADKT------------PTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNWIRECLG 215
Cdd:PLN02907 354 VRGKLDMQDPNksLRDPVYYRCNPTphhrigskykvyPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMG 430
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
3-273 |
9.74e-07 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 51.26 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTdtarNIEGKDKD----IMEILSLFGIKW-QTLYYQSKNLKF 77
Cdd:PRK14703 35 RFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDT----NPETEDTEyveaIKDDVRWLGFDWgEHLYYASDYFER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 78 HQEFAAKLLQEGKAFCCFCSEEELSakkekakekgvayRYDGTcehlsdAEVIDNPKPFTIR-------LKKPTRVLKFT 150
Cdd:PRK14703 111 MYAYAEQLIKMGLAYVDSVSEEEIR-------------ELRGT------VTEPGTPSPYRDRsveenldLFRRMRAGEFP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 151 D---AIKGEISFEPENidsfVIMR---------------ADK---TPTYNFACATDDMLEGVTFVIRGEDHVSNTPKQNW 209
Cdd:PRK14703 172 DgahVLRAKIDMSSPN----MKLRdpllyrirhahhyrtGDEwciYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDW 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 210 IRECLGYTDEISYAHLPIILGPDGKKMSKR--------------DDAS--SVKWMLDTGFLPEAIANYLVLLG-NKTPRE 272
Cdd:PRK14703 248 VLDHLGPWPPRPRQYEFARLALGYTVMSKRklrelveegyvsgwDDPRmpTIAGQRRRGVTPEAIRDFADQIGvAKTNST 327
|
.
gi 2428128515 273 V 273
Cdd:PRK14703 328 V 328
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
2-101 |
5.11e-06 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 48.83 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 2 YRFAPSPTGDMHIGNLRAAIFNYIRSLQDKSGFILRIEDTdtarNIEGKDK----DIMEILSLFGIKWQTLYYQSKNLKF 77
Cdd:PTZ00437 54 FRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDT----NPETEEQvyidAIMEMVKWMGWKPDWVTFSSDYFDQ 129
|
90 100
....*....|....*....|....
gi 2428128515 78 HQEFAAKLLQEGKAFCCFCSEEEL 101
Cdd:PTZ00437 130 LHEFAVQLIKDGKAYVDHSTPDEL 153
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
212-302 |
5.51e-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: 42.06 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 212 ECLGYTDEISYAHLPI--ILGPDGKKMSKRD-DASSVKWMLDtgflpEAIANYLVLLGNKTPREVFSIEE-----AVEFF 283
Cdd:COG0018 354 KALGYDPAKDLEHLLFgmVNLRDGEKMSTRAgTVVTLDDLLD-----EAVERAREIIEEKSEEEKEEIAEqvgidAVRYF 428
|
90 100
....*....|....*....|
gi 2428128515 284 DIAKISKAPAKFDIDK-LAF 302
Cdd:COG0018 429 DLSRSRDKDLDFDLDLaLSF 448
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
6-239 |
1.02e-03 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 40.24 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 6 PSPTGDMHIGNLRAAIF------------------NYIrslqDKSG-----FILRIEDTDTARNIEGK-DKDIMEILslf 61
Cdd:cd00671 9 ANPTGPLHVGHLRNAIIgdslarileflgydvtreYYI----NDWGrqiglLILSLEKWRKLVEESIKaDLETYGRL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 62 GIKWQTLYYQSKNLKFHQEfAAKLLQEGkafccfcseeelsakkekakekGVAYRYDGTcehlsdaevidnpkpftirlk 141
Cdd:cd00671 82 DVRFDVWFGESSYLGLMGK-VVELLEEL----------------------GLLYEEDGA--------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 142 kptRVLKFTdaikgEISFEPEnidsFVIMRADKTPTY---NFACATDDMLEGVTFVIR--GEDHVSNTPKQNWIRECLGY 216
Cdd:cd00671 118 ---LWLDLT-----EFGDDKD----RVLVRSDGTYTYftrDIAYHLDKFERGADKIIYvvGADHHGHFKRLFAALELLGY 185
|
250 260
....*....|....*....|....*
gi 2428128515 217 TDEISYAHLP--IILGPDGKKMSKR 239
Cdd:cd00671 186 DEAKKLEHLLygMVNLPKEGKMSTR 210
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
327-419 |
1.12e-03 |
|
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: 39.09 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 327 VELVKFYTQESsliPEIKAKINAIFSQKEIPAEFSQNAEILRNEILNLTQIPAE--FNELKTiLMERTALKGKAFFMPLR 404
Cdd:pfam19269 41 AELADFFFELP---LEYDEEAYAKKKMKTNKEESLEVLQELLPRLEALEDWTAEalEAALKA-LAEELGVKNGKVMWPLR 116
|
90
....*....|....*
gi 2428128515 405 LLLTGAPHGPELNEL 419
Cdd:pfam19269 117 VALTGKTVSPGLFEI 131
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
161-240 |
3.13e-03 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 37.84 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 161 PENIDSFVIMRADKTPTYNFACATDDMLEGVT---FVIRGEDHVSNTPKQNWIRECLGYTDEISYAHLPIILGPDGKKMS 237
Cdd:cd00802 61 AKAFVERWIERIKEDVEYMFLQAADFLLLYETecdIHLGGSDQLGHIELGLELLKKAGGPARPFGLTFGRVMGADGTKMS 140
|
...
gi 2428128515 238 KRD 240
Cdd:cd00802 141 KSK 143
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
3-100 |
6.16e-03 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 38.93 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428128515 3 RFAPSPTGDMHIGNLRAAIFNYirSLQDKSG--FILRIEDTdtarNIEGKDKD----IMEILSLFGIKWQT-LYYQSKnl 75
Cdd:PRK05347 33 RFPPEPNGYLHIGHAKSICLNF--GLAQDYGgkCNLRFDDT----NPEKEDQEyvdsIKEDVRWLGFDWSGeLRYASD-- 104
|
90 100
....*....|....*....|....*..
gi 2428128515 76 KFHQ--EFAAKLLQEGKAFCCFCSEEE 100
Cdd:PRK05347 105 YFDQlyEYAVELIKKGKAYVDDLSAEE 131
|
|
| |
