|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
3-488 |
0e+00 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 645.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 3 IRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPtcggpyepYV 82
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGP--------YY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 83 QSKRTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKIQTVNKMAPGYDRHCRNLSESEIKDVLSLGITPVIRFKIPLDGE 162
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 163 TCFNDILLDKVTWANKDISpDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCHLP 242
Cdd:TIGR00464 154 VSFNDQVRGEITFQNSELD-DFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 243 MVMGSDGQKLSKRHGATALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKLDFFN 322
Cdd:TIGR00464 233 MILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 323 SHYIREKGDDELAKLLIPFLQKAGyikeDINSCDEQKLMLLIPLIKPRIRKLSEAVTMLKFFYEDIKTWNLDEFlgKKKT 402
Cdd:TIGR00464 313 AHYIKELPDEELFELLDPHLKSLV----NTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAF--KKHL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 403 ASDIYLLLEKIKPVLEDFETRMLPDNEKIFYNFAKENNLKIGEVLLPIRIAVLGSKVSPPLFDSLQLLGKVKVFDRISqa 482
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLK-- 464
|
....*.
gi 501390573 483 QQFLKR 488
Cdd:TIGR00464 465 AQFIAA 470
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-487 |
0e+00 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 605.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 1 MNIRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPtcggpyep 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 81 YVQSKRTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKIQTVNKMAPGYDRHCRNLSESEIKDVLSLGITPVIRFKIPLD 160
Cdd:COG0008 75 YYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 161 GeTCFNDILLDKVTWANKDISpDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCH 240
Cdd:COG0008 155 G-VVFDDLVRGEITFPNPNLR-DPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 241 LPMVMGSDGQKLSKRHGATALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKLDF 320
Cdd:COG0008 233 LPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVW 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 321 FNSHYIREKGDDELAKLLIPFLQKAGYikedinscdEQKLMLLIPLIKPRIRKLSEAVTMLKFFYEDIKtwnlDEFLGKK 400
Cdd:COG0008 313 LNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIERE----DEKAAKK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 401 K-TASDIYLLLEKIKPVLEDFETRMLPDNEKIFYNFAKENNLKIGEVLLPIRIAVLGSKVSPPLFDSLQLLGKVKVFDRI 479
Cdd:COG0008 380 RlAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERL 459
|
....*...
gi 501390573 480 SQAQQFLK 487
Cdd:COG0008 460 GYAIDKLA 467
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-328 |
3.83e-140 |
|
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: 402.35 E-value: 3.83e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 2 NIRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPTCGGPYEPY 81
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 82 VQSKRTAIYQKYAKQLIELGnayycyckpdrlerirkiqtvnkmapgydrhcrnlseseikdvlslgitpvirfkipldg 161
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 162 etcfndilldkvtwankdispdpvilksDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCHL 241
Cdd:cd00808 101 ----------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHL 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 242 PMVMGSDGQKLSKRHGATALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKLDFF 321
Cdd:cd00808 153 PLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWL 232
|
....*..
gi 501390573 322 NSHYIRE 328
Cdd:cd00808 233 NGQYIRE 239
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
3-485 |
3.93e-136 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 403.35 E-value: 3.93e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 3 IRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPTCGGPYEPYV 82
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 83 QSKRTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKIQTVNKMAPGYDRHCRNLSESEIKDVLSLGITPVIRFKIPLDGE 162
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEGS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 163 TCFNDILLDKVTWaNKDISPDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCHLP 242
Cdd:PLN02627 206 VKIDDLIRGEVSW-NTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 243 MVMGSDGQKLSKRHGATALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKLDFFN 322
Cdd:PLN02627 285 LILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMN 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 323 SHYIREKGDDELAKLLIPFLQKAGYIKEDINSCDEQKlmllIPLIKPRIRKLSEAVTMLKffyeDIKTWNLDEFL----G 398
Cdd:PLN02627 365 GQHLRLLPEEELVKLVGERWKSAGILKESDGSFVKEA----VELLKDGIELVTDADKELL----NLLSYPLAATLsspeA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 399 KKKTASDIYLLLEKIkpvLEDFETRMLP--------DNEKIFYNFAKENNLKIGEVLLPIRIAVLGSKVSPPLFDSLQLL 470
Cdd:PLN02627 437 KTVVEDNFSEVADAL---IAAYDSGELAaaleeghdGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGESLVLL 513
|
490
....*....|....*
gi 501390573 471 GKVKVFDRISQAQQF 485
Cdd:PLN02627 514 HKAGTPDSVTEQAGF 528
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-320 |
8.94e-116 |
|
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: 343.53 E-value: 8.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 3 IRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDegptcggpYEPYV 82
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 83 QSKRTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKIQTVNKMA--PGYDRHCRNLSESEIKDVLSLGITPVIRFKIPLD 160
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 161 GETCFNDILLDKVTWANKDIsPDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCH 240
Cdd:pfam00749 154 SPYVFRDPVRGRIKFTPQEI-HDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 241 LPMVMGSDGQKLSKRHGAT--ALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKL 318
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
..
gi 501390573 319 DF 320
Cdd:pfam00749 313 DW 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
3-488 |
0e+00 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 645.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 3 IRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPtcggpyepYV 82
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGP--------YY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 83 QSKRTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKIQTVNKMAPGYDRHCRNLSESEIKDVLSLGITPVIRFKIPLDGE 162
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 163 TCFNDILLDKVTWANKDISpDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCHLP 242
Cdd:TIGR00464 154 VSFNDQVRGEITFQNSELD-DFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 243 MVMGSDGQKLSKRHGATALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKLDFFN 322
Cdd:TIGR00464 233 MILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 323 SHYIREKGDDELAKLLIPFLQKAGyikeDINSCDEQKLMLLIPLIKPRIRKLSEAVTMLKFFYEDIKTWNLDEFlgKKKT 402
Cdd:TIGR00464 313 AHYIKELPDEELFELLDPHLKSLV----NTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAF--KKHL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 403 ASDIYLLLEKIKPVLEDFETRMLPDNEKIFYNFAKENNLKIGEVLLPIRIAVLGSKVSPPLFDSLQLLGKVKVFDRISqa 482
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLK-- 464
|
....*.
gi 501390573 483 QQFLKR 488
Cdd:TIGR00464 465 AQFIAA 470
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-487 |
0e+00 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 605.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 1 MNIRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPtcggpyep 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 81 YVQSKRTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKIQTVNKMAPGYDRHCRNLSESEIKDVLSLGITPVIRFKIPLD 160
Cdd:COG0008 75 YYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 161 GeTCFNDILLDKVTWANKDISpDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCH 240
Cdd:COG0008 155 G-VVFDDLVRGEITFPNPNLR-DPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 241 LPMVMGSDGQKLSKRHGATALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKLDF 320
Cdd:COG0008 233 LPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVW 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 321 FNSHYIREKGDDELAKLLIPFLQKAGYikedinscdEQKLMLLIPLIKPRIRKLSEAVTMLKFFYEDIKtwnlDEFLGKK 400
Cdd:COG0008 313 LNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIERE----DEKAAKK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 401 K-TASDIYLLLEKIKPVLEDFETRMLPDNEKIFYNFAKENNLKIGEVLLPIRIAVLGSKVSPPLFDSLQLLGKVKVFDRI 479
Cdd:COG0008 380 RlAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERL 459
|
....*...
gi 501390573 480 SQAQQFLK 487
Cdd:COG0008 460 GYAIDKLA 467
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-328 |
3.83e-140 |
|
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: 402.35 E-value: 3.83e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 2 NIRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPTCGGPYEPY 81
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 82 VQSKRTAIYQKYAKQLIELGnayycyckpdrlerirkiqtvnkmapgydrhcrnlseseikdvlslgitpvirfkipldg 161
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 162 etcfndilldkvtwankdispdpvilksDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCHL 241
Cdd:cd00808 101 ----------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHL 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 242 PMVMGSDGQKLSKRHGATALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKLDFF 321
Cdd:cd00808 153 PLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWL 232
|
....*..
gi 501390573 322 NSHYIRE 328
Cdd:cd00808 233 NGQYIRE 239
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
3-485 |
3.93e-136 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 403.35 E-value: 3.93e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 3 IRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPTCGGPYEPYV 82
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 83 QSKRTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKIQTVNKMAPGYDRHCRNLSESEIKDVLSLGITPVIRFKIPLDGE 162
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEGS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 163 TCFNDILLDKVTWaNKDISPDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCHLP 242
Cdd:PLN02627 206 VKIDDLIRGEVSW-NTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 243 MVMGSDGQKLSKRHGATALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKLDFFN 322
Cdd:PLN02627 285 LILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMN 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 323 SHYIREKGDDELAKLLIPFLQKAGYIKEDINSCDEQKlmllIPLIKPRIRKLSEAVTMLKffyeDIKTWNLDEFL----G 398
Cdd:PLN02627 365 GQHLRLLPEEELVKLVGERWKSAGILKESDGSFVKEA----VELLKDGIELVTDADKELL----NLLSYPLAATLsspeA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 399 KKKTASDIYLLLEKIkpvLEDFETRMLP--------DNEKIFYNFAKENNLKIGEVLLPIRIAVLGSKVSPPLFDSLQLL 470
Cdd:PLN02627 437 KTVVEDNFSEVADAL---IAAYDSGELAaaleeghdGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGESLVLL 513
|
490
....*....|....*
gi 501390573 471 GKVKVFDRISQAQQF 485
Cdd:PLN02627 514 HKAGTPDSVTEQAGF 528
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-320 |
8.94e-116 |
|
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: 343.53 E-value: 8.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 3 IRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDegptcggpYEPYV 82
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 83 QSKRTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKIQTVNKMA--PGYDRHCRNLSESEIKDVLSLGITPVIRFKIPLD 160
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 161 GETCFNDILLDKVTWANKDIsPDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCH 240
Cdd:pfam00749 154 SPYVFRDPVRGRIKFTPQEI-HDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 241 LPMVMGSDGQKLSKRHGAT--ALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKL 318
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
..
gi 501390573 319 DF 320
Cdd:pfam00749 313 DW 314
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
3-328 |
4.72e-78 |
|
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: 243.53 E-value: 4.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 3 IRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPtcggpyepYV 82
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGP--------YR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 83 QSKRTAIYQKYAKQLIELGnayycyckpdrlerirkiqtvnkmapgydrhcrnlseseikdvlslgitpvirfkipldge 162
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 163 tcfndilldkvtwankdispdpvilksdGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCHLP 242
Cdd:cd00418 93 ----------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFP 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 243 MVMGSDGQKLSKRHGATALKQFIADGYLPEAIINYITLLGWSYDDKSEFFTKNELQRLFSIERVNKSPAVFDYNKLDFFN 322
Cdd:cd00418 145 RLLLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWLN 224
|
....*.
gi 501390573 323 SHYIRE 328
Cdd:cd00418 225 REYIRE 230
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
6-284 |
3.01e-77 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 243.99 E-value: 3.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 6 RYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEgptcggpyEPYVQSK 85
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDG--------PVLYQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 86 RTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKIQTvnKMAPGYDRHCRNLSESEIKDvlslgitPVIRFKIPlDGETCF 165
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCSRKEIAAAAPAPP--DGGGIYPGTCRDLLHGPRNP-------PAWRLRVP-DAVIAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 166 NDILLDKVtWANKDISPDPVILK-SDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCHLPMV 244
Cdd:PRK05710 151 DDRLQGRQ-HQDLALAVGDFVLRrADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 501390573 245 MGSDGQKLSKRHGATALkqfiADGYLPEAIINYITLLGWS 284
Cdd:PRK05710 230 LNADGQKLSKQNGAPAL----DAAGPLPVLAAALRFLGQP 265
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-284 |
1.12e-69 |
|
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: 223.19 E-value: 1.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 6 RYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEgptcggpyEPYVQSK 85
Cdd:TIGR03838 4 RFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDG--------EVVYQSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 86 RTAIYQKYAKQLIELGNAYYCYCKpdrleriRK-IQTVNKMAPGYDRHCRNLSESeikdvlSLGITPVIRFKIPlDGETC 164
Cdd:TIGR03838 76 RHALYQAALDRLLAAGLAYPCQCT-------RKeIAAARDGGGIYPGTCRNGLPG------RPGRPAAWRLRVP-DGVIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 165 FNDILLDKVTWANKDISPDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYCHLPMV 244
Cdd:TIGR03838 142 FDDRLQGPQQQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLV 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 501390573 245 MGSDGQKLSKRHGATALkqfiADGYLPEAIINYITLLGWS 284
Cdd:TIGR03838 222 VNADGEKLSKQNGAPAL----DDSRPLPALLAALRFLGLP 257
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
2-282 |
5.81e-39 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 148.85 E-value: 5.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 2 NIRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTD--QSRYFQEAEEDLYQSLKWLGIDFDegptcggpyE 79
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWD---------E 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 80 PYVQSKRTAIYQKYAKQLIELGNAYYCYCKPDRLERIRKiqtvNKMAPgydrHCRNLSeseIKDVLSLgitpvirFKIPL 159
Cdd:PRK04156 172 VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRD----AGKPC----PHRDKS---PEENLEL-------WEKML 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 160 DGETCFNDILLDKVTwankDIS-PDP-----VILKSDG------------LPTYHLANVVDDHLMEISHVLRAQEWVSSG 221
Cdd:PRK04156 234 DGEYKEGEAVVRVKT----DLEhPNPsvrdwVAFRIVKtphprvgdkyrvWPTYNFAVAVDDHLLGVTHVLRGKDHIDNT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 222 PLHVLLYNAFGWKPPIYCHLPMvMGSDGQKLSKrhgaTALKQFIAD--------------------GYLPEAIINYITLL 281
Cdd:PRK04156 310 EKQRYIYDYFGWEYPETIHYGR-LKIEGFVLST----SKIRKGIEEgeysgwddprlptlralrrrGILPEAIRELIIEV 384
|
.
gi 501390573 282 G 282
Cdd:PRK04156 385 G 385
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
6-268 |
5.35e-31 |
|
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: 126.09 E-value: 5.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 6 RYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDegptcggpyEPYVQSK 85
Cdd:TIGR00463 97 RFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD---------EVVYQSD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 86 RTAIYQKYAKQLIELGNAYYCYCKPDRLERIRkiqtvNKmapGYDRHCRNLSESE-------IKDVLSLGITPVIRFKIP 158
Cdd:TIGR00463 168 RIETYYDYTRKLIEMGKAYVCDCRPEEFRELR-----NR---GEACHCRDRSVEEnlerweeMLEGKEEGGSVVVRVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 159 LDGEtcfNDILLDKVTWANKDISPDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIY 238
Cdd:TIGR00463 240 LKHK---NPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEF 316
|
250 260 270
....*....|....*....|....*....|
gi 501390573 239 CHLPMVMGSDGQKLSkrhgATALKQFIADG 268
Cdd:TIGR00463 317 IHWGRLKIDDVRALS----TSSARKGILRG 342
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
2-305 |
1.11e-28 |
|
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: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 2 NIRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTD--QSRYFQEAEEDLYQSLKWLGIDFDegptcggpyE 79
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDprTKRPDPEAYDMIPEDLEWLGVKWD---------E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 80 PYVQSKRTAIYQKYAKQLIELGNAYYcyckpdrlerirkiqtvnkmapgydrHcrnlseseikdvlslgitpvirfkiPL 159
Cdd:cd09287 72 VVIASDRIELYYEYARKLIEMGGAYV--------------------------H-------------------------PR 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 160 DGETcfndilldKVTWankdispdpvilksdglPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPIYC 239
Cdd:cd09287 101 TGSK--------YRVW-----------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETI 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 240 HLPMVMgSDGQKLSK---RHGATA-------------LKQFIADGYLPEAIINYITLLGWSYDDkSEFFTKNelqrLFSI 303
Cdd:cd09287 156 HWGRLK-IEGGKLSTskiRKGIESgeyegwddprlptLRALRRRGIRPEAIRDFIIEVGVKQTD-ATISWEN----LYAI 229
|
..
gi 501390573 304 ER 305
Cdd:cd09287 230 NR 231
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
333-482 |
2.22e-26 |
|
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: 104.19 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 333 ELAKLLIPFLQKAGYIKEDinscdEQKLMLLIPLIKPRIRKLSEAVTMLKFFYEDIKTWNLDEFLGKK-KTASDIYL-LL 410
Cdd:pfam19269 1 ELAELALPYLEEAGLDGLD-----DEYLKKVVPLLKERAETLSELAELADFFFELPLEYDEEAYAKKKmKTNKEESLeVL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501390573 411 EKIKPVLE---DFETRMLpdnEKIFYNFAKENNLKIGEVLLPIRIAVLGSKVSPPLFDSLQLLGKVKVFDRISQA 482
Cdd:pfam19269 76 QELLPRLEaleDWTAEAL---EAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKA 147
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
6-411 |
3.16e-13 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 71.92 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 6 RYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPTCGGPYepyvqsk 85
Cdd:PTZ00402 56 RFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDY------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 86 RTAIYQKyAKQLIELGNAyycYCKPDRLERIRKIQtVNKMAPGYdrhcRNLSE-------SEIKDVLSLGITPVIRFKIP 158
Cdd:PTZ00402 129 MDLMYEK-AEELIKKGLA---YCDKTPREEMQKCR-FDGVPTKY----RDISVeetkrlwNEMKKGSAEGQETCLRAKIS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 159 LDGEtcfNDILLDKVTWANKDISPDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGPLHVLLYNAFGWKPPI- 237
Cdd:PTZ00402 200 VDNE---NKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIv 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 238 --YCHLPM---VMgsdgqklSKRHgataLKQFIADGYLPeaiinyitllGWsydDKSEFFT----------KNELQRLFS 302
Cdd:PTZ00402 277 edFSRLNMeysVM-------SKRK----LTQLVDTHVVD----------GW---DDPRFPTvralvrrglkMEALRQFVQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 303 IERVNKSPAVFDYNKLDFFNSHYIR---------------------EKGDDELAKLL---IPFLQKAGYIKEDINSCDEQ 358
Cdd:PTZ00402 333 EQGMSKTVNFMEWSKLWYFNTQILDpsvprytvvsntlkvrctvegQIHLEACEKLLhkkVPDMGEKTYYKSDVIFLDAE 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 501390573 359 KLMLLiplikprirKLSEAVTMLKF---FYEDIKTWNLDEFLgkkkTASDIYLLLE 411
Cdd:PTZ00402 413 DVALL---------KEGDEVTLMDWgnaYIKNIRRSGEDALI----TDADIVLHLE 455
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
2-104 |
2.36e-12 |
|
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: 66.51 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 2 NIRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDfdegptcggPYEPY 81
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIK---------PYKVT 71
|
90 100
....*....|....*....|...
gi 501390573 82 VQSKRTAIYQKYAKQLIELGNAY 104
Cdd:cd00807 72 YASDYFDQLYEYAEQLIKKGKAY 94
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
2-217 |
5.54e-12 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 68.21 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 2 NIRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEgPTCGGPYEPY 81
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDA-VTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 82 VqskrtaiyQKYAKQLIELGNAYYCYCKPD--RLERIRKIQTVnkmapgydrhCRNLSeseIKDVLSL----------GI 149
Cdd:PLN02907 292 L--------MEMAEKLIKEGKAYVDDTPREqmRKERMDGIESK----------CRNNS---VEENLRLwkemiagserGL 350
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501390573 150 TPVIRFKIPLDGEtcfNDILLDKVTWAnkdISPDP---VILKSDGLPTYHLANVVDDHLMEISHVLRAQEW 217
Cdd:PLN02907 351 QCCVRGKLDMQDP---NKSLRDPVYYR---CNPTPhhrIGSKYKVYPTYDFACPFVDALEGVTHALRSSEY 415
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
3-217 |
8.03e-12 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 67.34 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 3 IRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFDEGPTCGGPYEPyv 82
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 83 qskrtaiYQKYAKQLIELGNAYYCYCKPDRLERIRkiqtvnkMAPGYDRHcRNLSESEIKDVLSL-------GITPVIRF 155
Cdd:PLN03233 90 -------IRCYAIILIEEGLAYMDDTPQEEMKKER-------ADRAESKH-RNQSPEEALEMFKEmcsgkeeGGAWCLRA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501390573 156 KIPLDGEtcfNDILLDKVTWANKDISPDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEW 217
Cdd:PLN03233 155 KIDMQSD---NGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEY 213
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
2-117 |
8.62e-11 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 64.36 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 2 NIRVRYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDQSRYFQEAEEDLYQSLKWLGIDFdegptcgGPYEPY 81
Cdd:PRK14703 31 RVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDW-------GEHLYY 103
|
90 100 110
....*....|....*....|....*....|....*.
gi 501390573 82 VQSKRTAIYQkYAKQLIELGNAYYCYCKPDRLERIR 117
Cdd:PRK14703 104 ASDYFERMYA-YAEQLIKMGLAYVDSVSEEEIRELR 138
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
6-118 |
1.34e-08 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 57.30 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 6 RYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDqsryfQEAEEDLY-----QSLKWLGidfdegptcggpYEP 80
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTN-----PETEEQVYidaimEMVKWMG------------WKP 117
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 501390573 81 YVQSKRTAIYQK---YAKQLIELGNAYYCYCKPDRLERIRK 118
Cdd:PTZ00437 118 DWVTFSSDYFDQlheFAVQLIKDGKAYVDHSTPDELKQQRE 158
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
6-233 |
3.03e-05 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 46.68 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 6 RYAPSPTGLQHIGGIRTALFNYFFARSCGGKFLLRIEDTDqsryfQEAEEDLY-----QSLKWLGidfdegptcggpYEP 80
Cdd:PLN02859 268 RFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEKKEYidhieEIVEWMG------------WEP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 81 YVQSKRTAIYQK---YAKQLIELGNAYYCYCKPDRLERIRKiqtvNKM-APGYDrhcRNLSES-EIKDVLSLGITP---- 151
Cdd:PLN02859 331 FKITYTSDYFQElyeLAVELIRRGHAYVDHQTPEEIKEYRE----KKMnSPWRD---RPIEESlKLFEDMRRGLIEegka 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 152 VIRFKIPLDGETcFNdiLLDKVTWANKDISPDPVILKSDGLPTYHLANVVDDHLMEISHVLRAQEWVSSGP-----LHVL 226
Cdd:PLN02859 404 TLRMKQDMQNDN-FN--MYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRAsyywlLDSL 480
|
....*...
gi 501390573 227 -LYNAFGW 233
Cdd:PLN02859 481 gLYQPYVW 488
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
182-257 |
2.81e-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: 43.60 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 182 PDPVILKSDGLPTYH---LA---------------NVVD----DHLMEISHVLRAQEWVSSGPLHVLLYNafgwkppiyc 239
Cdd:COG0018 301 KDRVLVKSDGTYTYFttdIAyhlykferygfdrviYVVGadqhGHFKRLFAALKALGYDPAKDLEHLLFG---------- 370
|
90
....*....|....*...
gi 501390573 240 hlpMVMGSDGQKLSKRHG 257
Cdd:COG0018 371 ---MVNLRDGEKMSTRAG 385
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
181-257 |
2.23e-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: 39.47 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390573 181 SPDPVILKSDGLPTY-----------------HLANVVD----DHLMEISHVLRAQEWVSSGPLHVLLYNafgwkppiyc 239
Cdd:cd00671 128 DKDRVLVRSDGTYTYftrdiayhldkfergadKIIYVVGadhhGHFKRLFAALELLGYDEAKKLEHLLYG---------- 197
|
90
....*....|....*...
gi 501390573 240 hlpMVMGSDGQKLSKRHG 257
Cdd:cd00671 198 ---MVNLPKEGKMSTRAG 212
|
|
| |
