|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-482 |
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: 592.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPdkdggygpY 82
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGP--------Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERckSGLYMEYAKQLIEKGEAYYCFCDKERLDSLK--QNINGKEIsVYDKHCLHLSKEEIEANLAAGKPYVIRANVP 160
Cdd:COG0008 76 YQSDR--FDIYYEYAEKLIEKGKAYVCFCTPEELEALRetQTAPGKPP-RYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 161 NEGeTTFHDEIYGDITQPNSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYI 240
Cdd:COG0008 153 EEG-VVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 241 HCPLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMVKLK 320
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 321 WMNGEYIKAMDFDAFYELAEPYIKEVIHRDcDYKKIAQMVKTRIEIFPDIKEHIDFFEAVPEYDIAmythKKMKTTAETS 400
Cdd:COG0008 312 WLNGPYIRALDDEELAELLAPELPEAGIRE-DLERLVPLVRERAKTLSELAELARFFFIEREDEKA----AKKRLAPEEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 401 LAVLKDVLPLMEAQEDYSNDALYAMLSSYVKENGYKNGYVMWPIRTALSGKQMTPgGATELMEVLGKEESIARIKAAIEK 480
Cdd:COG0008 387 RKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEP-SLFDVLELLGKERVFERLGYAIDK 465
|
..
gi 545615998 481 LA 482
Cdd:COG0008 466 LA 467
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
3-476 |
3.10e-175 |
|
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: 500.34 E-value: 3.10e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPdkdggygpY 82
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGP--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERckSGLYMEYAKQLIEKGEAYYCFCDKERLDSLKQ-NINGKEISVYDKHCLHLSKEEIEANLAAGKPYVIRANVPN 161
Cdd:TIGR00464 73 YQSQR--LDIYKKYAKELLEEGLAYRCYCSKERLERLREeQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 162 EGETTFHDEIYGDITQPNSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYIH 241
Cdd:TIGR00464 151 EAVVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 242 CPLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMVKLKW 321
Cdd:TIGR00464 231 LPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 322 MNGEYIKAMDFDAFYELAEPYIKEVIHRDC----DYKKIAQMVKTRIEIFPDIKEHID-FFEAVPEYDIAMYTHKKMKTT 396
Cdd:TIGR00464 311 LNAHYIKELPDEELFELLDPHLKSLVNTDTlnreQLAELLLLFKERLKTLKEIAELIRlFFEDKKEVDEDAFKKHLKKNV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 397 AEtslaVLKDVLPLMEAQEDYSNDALYAMLSSYVKENGYKNGYVMWPIRTALSGKQMTPGGAtELMEVLGKEESIARIKA 476
Cdd:TIGR00464 391 KE----VLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLA-QILELIGKTESIKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
3-328 |
1.26e-128 |
|
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: 373.07 E-value: 1.26e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPDKDGGYGPY 82
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERckSGLYMEYAKQLIEKGeayycfcdkerldslkqningkeisvydkhclhlskeeieanlaagkpyviranvpne 162
Cdd:cd00808 81 RQSER--LEIYRKYAEKLLEKG---------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 163 gettfhdeiygditqpnselddmiliksDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYIHC 242
Cdd:cd00808 101 ----------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHL 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 243 PLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMVKLKWM 322
Cdd:cd00808 153 PLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWL 232
|
....*.
gi 545615998 323 NGEYIK 328
Cdd:cd00808 233 NGQYIR 238
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
4-470 |
8.19e-125 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 374.08 E-value: 8.19e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 4 VRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPDKDGGYGPYI 83
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 84 QSERckSGLYMEYAKQLIEKGEAYYCFCDKERLDSLKQNINGKEIS-VYDKHCLHLSKEEIEANLAAGKPYVIRANVPNE 162
Cdd:PLN02627 126 QSER--NAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPpRYTGKWATASDEEVQAELAKGTPYTYRFRVPKE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 163 GETTFHDEIYGDITQPNSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYIHC 242
Cdd:PLN02627 204 GSVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 243 PLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMVKLKWM 322
Cdd:PLN02627 284 SLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWM 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 323 NGEYIKAMDFDAFYELAEPYIKE---VIHRDCDY-KKIAQMVKTRIEIFPDIKEHIdffEAVPEYDI-AMYTHKKMKTTA 397
Cdd:PLN02627 364 NGQHLRLLPEEELVKLVGERWKSagiLKESDGSFvKEAVELLKDGIELVTDADKEL---LNLLSYPLaATLSSPEAKTVV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 398 ETSLAVLKDVL-------PLMEAQEDYSNDALyAMLSSYVKENGYKNGYVMWPIRTALSGKQMTPgGATELMEVLGKEES 470
Cdd:PLN02627 441 EDNFSEVADALiaaydsgELAAALEEGHDGWQ-KWVKAFGKALKRKGKRLFMPLRVALTGKMHGP-DVGESLVLLHKAGT 518
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-321 |
7.52e-117 |
|
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: 345.84 E-value: 7.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLihdegpdkDGGYGPY 82
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGI--------KWDYGPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERCKsgLYMEYAKQLIEKGEAYYCFCDKERLDSLKQNINGKEISV---YDKHCLHLSKEEIEANLAAGKPYVIRANV 159
Cdd:pfam00749 73 YQSDRFD--IYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPSrdrYDEENLHLFEEEMKKGSAEGGPATVRAKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 160 PNEGETTFHDEIYGDITQPNSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKY 239
Cdd:pfam00749 151 PMESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 240 IHCPLITNEEHQKLSKRSGHSSY--EDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMV 317
Cdd:pfam00749 231 IHEYLRLNLDGTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRK 310
|
....
gi 545615998 318 KLKW 321
Cdd:pfam00749 311 KLDW 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-482 |
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: 592.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPdkdggygpY 82
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGP--------Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERckSGLYMEYAKQLIEKGEAYYCFCDKERLDSLK--QNINGKEIsVYDKHCLHLSKEEIEANLAAGKPYVIRANVP 160
Cdd:COG0008 76 YQSDR--FDIYYEYAEKLIEKGKAYVCFCTPEELEALRetQTAPGKPP-RYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 161 NEGeTTFHDEIYGDITQPNSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYI 240
Cdd:COG0008 153 EEG-VVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 241 HCPLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMVKLK 320
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 321 WMNGEYIKAMDFDAFYELAEPYIKEVIHRDcDYKKIAQMVKTRIEIFPDIKEHIDFFEAVPEYDIAmythKKMKTTAETS 400
Cdd:COG0008 312 WLNGPYIRALDDEELAELLAPELPEAGIRE-DLERLVPLVRERAKTLSELAELARFFFIEREDEKA----AKKRLAPEEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 401 LAVLKDVLPLMEAQEDYSNDALYAMLSSYVKENGYKNGYVMWPIRTALSGKQMTPgGATELMEVLGKEESIARIKAAIEK 480
Cdd:COG0008 387 RKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEP-SLFDVLELLGKERVFERLGYAIDK 465
|
..
gi 545615998 481 LA 482
Cdd:COG0008 466 LA 467
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
3-476 |
3.10e-175 |
|
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: 500.34 E-value: 3.10e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPdkdggygpY 82
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGP--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERckSGLYMEYAKQLIEKGEAYYCFCDKERLDSLKQ-NINGKEISVYDKHCLHLSKEEIEANLAAGKPYVIRANVPN 161
Cdd:TIGR00464 73 YQSQR--LDIYKKYAKELLEEGLAYRCYCSKERLERLREeQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 162 EGETTFHDEIYGDITQPNSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYIH 241
Cdd:TIGR00464 151 EAVVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 242 CPLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMVKLKW 321
Cdd:TIGR00464 231 LPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 322 MNGEYIKAMDFDAFYELAEPYIKEVIHRDC----DYKKIAQMVKTRIEIFPDIKEHID-FFEAVPEYDIAMYTHKKMKTT 396
Cdd:TIGR00464 311 LNAHYIKELPDEELFELLDPHLKSLVNTDTlnreQLAELLLLFKERLKTLKEIAELIRlFFEDKKEVDEDAFKKHLKKNV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 397 AEtslaVLKDVLPLMEAQEDYSNDALYAMLSSYVKENGYKNGYVMWPIRTALSGKQMTPGGAtELMEVLGKEESIARIKA 476
Cdd:TIGR00464 391 KE----VLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLA-QILELIGKTESIKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
3-328 |
1.26e-128 |
|
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: 373.07 E-value: 1.26e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPDKDGGYGPY 82
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERckSGLYMEYAKQLIEKGeayycfcdkerldslkqningkeisvydkhclhlskeeieanlaagkpyviranvpne 162
Cdd:cd00808 81 RQSER--LEIYRKYAEKLLEKG---------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 163 gettfhdeiygditqpnselddmiliksDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYIHC 242
Cdd:cd00808 101 ----------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHL 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 243 PLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMVKLKWM 322
Cdd:cd00808 153 PLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWL 232
|
....*.
gi 545615998 323 NGEYIK 328
Cdd:cd00808 233 NGQYIR 238
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
4-470 |
8.19e-125 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 374.08 E-value: 8.19e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 4 VRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPDKDGGYGPYI 83
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 84 QSERckSGLYMEYAKQLIEKGEAYYCFCDKERLDSLKQNINGKEIS-VYDKHCLHLSKEEIEANLAAGKPYVIRANVPNE 162
Cdd:PLN02627 126 QSER--NAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPpRYTGKWATASDEEVQAELAKGTPYTYRFRVPKE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 163 GETTFHDEIYGDITQPNSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYIHC 242
Cdd:PLN02627 204 GSVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 243 PLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMVKLKWM 322
Cdd:PLN02627 284 SLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWM 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 323 NGEYIKAMDFDAFYELAEPYIKE---VIHRDCDY-KKIAQMVKTRIEIFPDIKEHIdffEAVPEYDI-AMYTHKKMKTTA 397
Cdd:PLN02627 364 NGQHLRLLPEEELVKLVGERWKSagiLKESDGSFvKEAVELLKDGIELVTDADKEL---LNLLSYPLaATLSSPEAKTVV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 398 ETSLAVLKDVL-------PLMEAQEDYSNDALyAMLSSYVKENGYKNGYVMWPIRTALSGKQMTPgGATELMEVLGKEES 470
Cdd:PLN02627 441 EDNFSEVADALiaaydsgELAAALEEGHDGWQ-KWVKAFGKALKRKGKRLFMPLRVALTGKMHGP-DVGESLVLLHKAGT 518
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-321 |
7.52e-117 |
|
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: 345.84 E-value: 7.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLihdegpdkDGGYGPY 82
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGI--------KWDYGPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERCKsgLYMEYAKQLIEKGEAYYCFCDKERLDSLKQNINGKEISV---YDKHCLHLSKEEIEANLAAGKPYVIRANV 159
Cdd:pfam00749 73 YQSDRFD--IYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPSrdrYDEENLHLFEEEMKKGSAEGGPATVRAKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 160 PNEGETTFHDEIYGDITQPNSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKY 239
Cdd:pfam00749 151 PMESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 240 IHCPLITNEEHQKLSKRSGHSSY--EDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMV 317
Cdd:pfam00749 231 IHEYLRLNLDGTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRK 310
|
....
gi 545615998 318 KLKW 321
Cdd:pfam00749 311 KLDW 314
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
3-328 |
4.26e-76 |
|
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: 238.53 E-value: 4.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPdkdggygpY 82
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGP--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERCKsgLYMEYAKQLIEKGeayycfcdkerldslkqningkeisvydkhclhlskeeieanlaagkpyviranvpne 162
Cdd:cd00418 73 RQSDRFD--LYRAYAEELIKKG---------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 163 gettfhdeiygditqpnselddmiliksdGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYIHC 242
Cdd:cd00418 93 -----------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHF 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 243 PLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAVVNFVALLGWSPVDNREIFSLEELVENFDYHHISKSPAVFDMVKLKWM 322
Cdd:cd00418 144 PRLLLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWL 223
|
....*.
gi 545615998 323 NGEYIK 328
Cdd:cd00418 224 NREYIR 229
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-314 |
4.04e-74 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 235.52 E-value: 4.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 1 MAKVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDeGPdkdggyg 80
Cdd:PRK05710 3 MTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWD-GP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 81 PYIQSERCksGLYMEYAKQLIEKGEAYYCFCDKERLDSLKQNINGKEIsVYDKHCLHLSkeeieanLAAGKPYVIRANVP 160
Cdd:PRK05710 75 VLYQSQRH--DAYRAALDRLRAQGLVYPCFCSRKEIAAAAPAPPDGGG-IYPGTCRDLL-------HGPRNPPAWRLRVP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 161 nEGETTFHDEIYGDITQ-PNSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKY 239
Cdd:PRK05710 145 -DAVIAFDDRLQGRQHQdLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRY 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545615998 240 IHCPLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAvvnfVALLGWSPVDNREIFSLEE--LVENFDYHHISKSPAVF 314
Cdd:PRK05710 224 LHLPLVLNADGQKLSKQNGAPALDAAGPLPVLAAA----LRFLGQPPPAADASVEELLaqAVAHWDLTRLPRQAEIN 296
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
4-299 |
4.10e-65 |
|
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: 211.25 E-value: 4.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 4 VRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPDkdggygpyI 83
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVV--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 84 QSERckSGLYMEYAKQLIEKGEAYYCFCD-KERLDSLKQNIngkeisVYDKHCLHLSKEeieanlAAGKPYVIRANVPNe 162
Cdd:TIGR03838 73 QSQR--HALYQAALDRLLAAGLAYPCQCTrKEIAAARDGGG------IYPGTCRNGLPG------RPGRPAAWRLRVPD- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 163 GETTFHDEIYGDITQP-NSELDDMILIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYIH 241
Cdd:TIGR03838 138 GVIAFDDRLQGPQQQDlAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLH 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 545615998 242 CPLITNEEHQKLSKRSGHSSYEDLIEQGFLSEAvvnfVALLGWSPVDNREIFSLEELV 299
Cdd:TIGR03838 218 LPLVVNADGEKLSKQNGAPALDDSRPLPALLAA----LRFLGLPPPPELAAASPAELL 271
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
335-478 |
1.88e-58 |
|
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: 189.71 E-value: 1.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 335 FYELAEPYIKEVIHRDCD---YKKIAQMVKTRIEIFPDIKEHIDFFEAVP-EYDIAMYTHKKMKTTAETSLAVLKDVLPL 410
Cdd:pfam19269 2 LAELALPYLEEAGLDGLDdeyLKKVVPLLKERAETLSELAELADFFFELPlEYDEEAYAKKKMKTNKEESLEVLQELLPR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545615998 411 MEAQEDYSNDALYAMLSSYVKENGYKNGYVMWPIRTALSGKQMTPgGATELMEVLGKEESIARIKAAI 478
Cdd:pfam19269 82 LEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSP-GLFEIMEILGKEETLARLRKAI 148
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
3-241 |
7.99e-39 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 148.46 E-value: 7.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQE--RFVEEALGIIYRTLEKTGLihdeGPDKDggyg 80
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGV----KWDEV---- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 81 pYIQSERCKsgLYMEYAKQLIEKGEAYYCFCDKERLDSLKqnINGKEisvydkhCLHLSKeEIEANLA------AGKpYv 154
Cdd:PRK04156 173 -VIQSDRLE--IYYEYARKLIEMGGAYVCTCDPEEFKELR--DAGKP-------CPHRDK-SPEENLElwekmlDGE-Y- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 155 iranvpNEGETTFhdEIYGDITQPNSELDDMIL--IKS-------DGY---PTYNFANVVDDHLMHITHVVRGNEYLSSA 222
Cdd:PRK04156 238 ------KEGEAVV--RVKTDLEHPNPSVRDWVAfrIVKtphprvgDKYrvwPTYNFAVAVDDHLLGVTHVLRGKDHIDNT 309
|
250
....*....|....*....
gi 545615998 223 PKYTRLYHAFGWEEPKYIH 241
Cdd:PRK04156 310 EKQRYIYDYFGWEYPETIH 328
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
1-283 |
1.07e-32 |
|
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: 130.71 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 1 MAKVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEgpdkdggyg 80
Cdd:TIGR00463 91 MGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDE--------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 81 PYIQSERCKsgLYMEYAKQLIEKGEAYYCFCDKERLDSLKQN---INGKEISVYDKhcLHLSKEEIEANLAAGKpYVIRA 157
Cdd:TIGR00463 162 VVYQSDRIE--TYYDYTRKLIEMGKAYVCDCRPEEFRELRNRgeaCHCRDRSVEEN--LERWEEMLEGKEEGGS-VVVRV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 158 NVpnegettfhdeiygDITQPNSELDDMILIKSDG------------YPTYNFANVVDDHLMHITHVVRGNEYLSSAPKY 225
Cdd:TIGR00463 237 KT--------------DLKHKNPAIRDWVIFRIVKtphprtgdkyrvYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQ 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545615998 226 TRLYHAFGWEEPKYIHCPLITNEEHQKLS--------KRSGHSSYED--------LIEQGFLSEAVVNFVALLG 283
Cdd:TIGR00463 303 EYIYRYFGWEPPEFIHWGRLKIDDVRALStssarkgiLRGEYSGWDDprlptlraIRRRGIRPEAIRKFMLSIG 376
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
3-298 |
6.43e-32 |
|
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: 122.46 E-value: 6.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVE--EALGIIYRTLEKTGLIHDEgpdkdggyg 80
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 81 PYIQSERCKsgLYMEYAKQLIEKGEAYYcfcdkerldslkqningkeisvydkHCLhlskeeieanlaAGKPYVIranvp 160
Cdd:cd09287 72 VVIASDRIE--LYYEYARKLIEMGGAYV-------------------------HPR------------TGSKYRV----- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 161 negettfhdeiygditqpnselddmiliksdgYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGWEEPKYI 240
Cdd:cd09287 108 --------------------------------WPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETI 155
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545615998 241 HCPLITNEEhQKLSK--------RSGHSSYED--------LIEQGFLSEAVVNFVALLGWSPVDnrEIFSLEEL 298
Cdd:cd09287 156 HWGRLKIEG-GKLSTskirkgieSGEYEGWDDprlptlraLRRRGIRPEAIRDFIIEVGVKQTD--ATISWENL 226
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
3-256 |
2.84e-15 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 78.47 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIHDEGPDKDGGYgpy 82
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDY--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 iqserckSGLYMEYAKQLIEKGEAYycfCDKE-RLDSLKQNING-----KEISVYDKHCLHlskEEIEANLAAGKPYVIR 156
Cdd:PTZ00402 129 -------MDLMYEKAEELIKKGLAY---CDKTpREEMQKCRFDGvptkyRDISVEETKRLW---NEMKKGSAEGQETCLR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 157 A--NVPNEGETTFHDEIYGDITQPNSELDdmilIKSDGYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGw 234
Cdd:PTZ00402 196 AkiSVDNENKAMRDPVIYRVNLTPHARQG----TKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALG- 270
|
250 260
....*....|....*....|....*..
gi 545615998 235 eepkyIHCPLIT-----NEEHQKLSKR 256
Cdd:PTZ00402 271 -----IRKPIVEdfsrlNMEYSVMSKR 292
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
3-256 |
5.58e-15 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 77.36 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLIhdegPDKDGGYGPY 82
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK----PDSVSFTSDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSERCksglymeYAKQLIEKGEAYYC-----FCDKERLD---SLKQNINGKEISVYDKHCLHLSKEeieanlaaGKPYV 154
Cdd:PLN03233 87 FEPIRC-------YAIILIEEGLAYMDdtpqeEMKKERADraeSKHRNQSPEEALEMFKEMCSGKEE--------GGAWC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 155 IRANVpnegettfhdeiygDITQPNSELDDMILIKSD------------GYPTYNFANVVDDHLMHITHVVRGNEYLSSA 222
Cdd:PLN03233 152 LRAKI--------------DMQSDNGTLRDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHALRTTEYDDRD 217
|
250 260 270
....*....|....*....|....*....|....
gi 545615998 223 PKYTRLYHAFGWEEPKyIHCPLITNEEHQKLSKR 256
Cdd:PLN03233 218 AQFFWIQKALGLRRPR-IHAFARMNFMNTVLSKR 250
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
1-233 |
2.47e-12 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 69.37 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 1 MAKVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDT--DQER--FVE------EALGIIYRTLEKTglihd 70
Cdd:PLN02907 211 EGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTnpSKESdeFVEnilkdiETLGIKYDAVTYT----- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 71 egpdkdGGYGPYIqsercksglyMEYAKQLIEKGEAYYCFCDKERLDslKQNINGKEI-----SVYDKhcLHLSKEEIeA 145
Cdd:PLN02907 286 ------SDYFPQL----------MEMAEKLIKEGKAYVDDTPREQMR--KERMDGIESkcrnnSVEEN--LRLWKEMI-A 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 146 NLAAGKPYVIRANVpnegettfhdeiygDITQPNSELDD------------MILIKSDGYPTYNFANVVDDHLMHITHVV 213
Cdd:PLN02907 345 GSERGLQCCVRGKL--------------DMQDPNKSLRDpvyyrcnptphhRIGSKYKVYPTYDFACPFVDALEGVTHAL 410
|
250 260
....*....|....*....|
gi 545615998 214 RGNEYLSSAPKYTRLYHAFG 233
Cdd:PLN02907 411 RSSEYHDRNAQYYRILEDMG 430
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
3-289 |
4.59e-10 |
|
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: 59.96 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLihdeGPDKDGGYGPY 82
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGI----KPYKVTYASDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQsercksgLYMEYAKQLIEKGEAYycfcdkerldslkqningkeisVYDKHclhlskeeieanlaaGKPYVIranvpne 162
Cdd:cd00807 77 FD-------QLYEYAEQLIKKGKAY----------------------VHHRT---------------GDKWCI------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 163 gettfhdeiygditqpnselddmiliksdgYPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYHAFGweepkyIHC 242
Cdd:cd00807 106 ------------------------------YPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALR------LYR 149
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545615998 243 PLI-----TNEEHQKLSKR-------SGH-SSYED--------LIEQGFLSEAVVNFVALLGWSPVDN 289
Cdd:cd00807 150 PHQwefsrLNLTYTVMSKRkllqlvdEGYvDGWDDprlptlrgLRRRGVTPEAIRQFILRQGVSKADS 217
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
3-211 |
3.46e-07 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 52.80 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLihdegpdkDGGYGPY 82
Cdd:PRK14703 31 RVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGF--------DWGEHLY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQS---ERcksglYMEYAKQLIEKGEAYYCFCDKERLDSLKQNIN--GKEiSVYdkhclhlSKEEIEANLA------AGK 151
Cdd:PRK14703 103 YASdyfER-----MYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTepGTP-SPY-------RDRSVEENLDlfrrmrAGE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545615998 152 ----PYVIRANVpnegettfhdeiygDITQPNSELDDMILIK---------SDG---YPTYNFANVVDDHLMHITH 211
Cdd:PRK14703 170 fpdgAHVLRAKI--------------DMSSPNMKLRDPLLYRirhahhyrtGDEwciYPMYDFAHPLEDAIEGVTH 231
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
7-235 |
5.33e-07 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 52.29 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 7 RFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQErfVEEALGI--IYRTLEKTGLihdeGPDKDGGYGPYIQ 84
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPE--TEEQVYIdaIMEMVKWMGW----KPDWVTFSSDYFD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 85 SercksgLYmEYAKQLIEKGEAYycfCDKERLDSLKQNINGKEISVYdkhclhlSKEEIEANLAAGKPyvIRANVPNEGE 164
Cdd:PTZ00437 129 Q------LH-EFAVQLIKDGKAY---VDHSTPDELKQQREQREDSPW-------RNRSVEENLLLFEH--MRQGRYAEGE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 165 TTFHDEIygDITQPNSELDDMILIK---------SDG---YPTYNFANVVDDHLMHITHVVRGNEYLSSAPKY------T 226
Cdd:PTZ00437 190 ATLRVKA--DMKSDNPNMRDFIAYRvkyvehphaKDKwciYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYfwlleeL 267
|
....*....
gi 545615998 227 RLYHAFGWE 235
Cdd:PTZ00437 268 NLWRPHVWE 276
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
3-237 |
4.74e-06 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 49.37 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 3 KVRTRFAPSPTGRMHVGNLRTALYTYLIAKHEGGEFILRIEDTDQERFVEEALGIIYRTLEKTGLihdeGPDKDGGYGPY 82
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGW----EPFKITYTSDY 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 83 IQSercksgLYmEYAKQLIEKGEAYycfCDKERLDSLKQNINGKEISVYDKHCLHLSKEEIEAnlaagkpyvIRANVPNE 162
Cdd:PLN02859 340 FQE------LY-ELAVELIRRGHAY---VDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFED---------MRRGLIEE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545615998 163 GETTFhdEIYGDITQPNSELDDMIL--IKSDG----------YPTYNFANVVDDHLMHITHVVRGNEYLSSAPKYTRLYH 230
Cdd:PLN02859 401 GKATL--RMKQDMQNDNFNMYDLIAyrIKFTPhphagdkwciYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLD 478
|
....*..
gi 545615998 231 AFGWEEP 237
Cdd:PLN02859 479 SLGLYQP 485
|
|
| |
