|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
37-497 |
1.92e-152 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 444.24 E-value: 1.92e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE--------GPYY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQVVP 196
Cdd:COG0008 77 QSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 197 AFQDLVYGWNRHEVASVeGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPL 276
Cdd:COG0008 157 VFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 277 LLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNR 356
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 357 LHLQRLVSNEsqrrqlvgklqvlVEEAFGCQLQNRDVlnPVYVERILLLRQGHICRLQDLVsPVYSYLWTRP--AVGRAQ 434
Cdd:COG0008 316 PYIRALDDEE-------------LAELLAPELPEAGI--REDLERLVPLVRERAKTLSELA-ELARFFFIERedEKAAKK 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815891074 435 LDAISEKVDVIaKRVLGLLERSSmSLTQDMLNGELKKLSEGLeGTKYSNVMKLLRMALSGQQV 497
Cdd:COG0008 380 RLAPEEVRKVL-KAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTV 439
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
37-508 |
2.37e-140 |
|
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: 413.67 E-value: 2.37e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQVV 195
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 196 PAFQDLVYG---WNRHEVasveGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFA 272
Cdd:TIGR00464 154 VSFNDQVRGeitFQNSEL----DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 273 HLPLLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLP 352
Cdd:TIGR00464 230 HLPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 353 EFNRLHLQRLvSNESQRRQLVGKLQvlveeafgcQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPVYSYLWTRPAVgr 432
Cdd:TIGR00464 310 WLNAHYIKEL-PDEELFELLDPHLK---------SLVNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEV-- 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815891074 433 aQLDAISEKVDVIAKRVLGLLERSSMSL---TQDMLNGELKKLSEgLEGTKYSNVMKLLRMALSGQQvrQGHGLDCSLE 508
Cdd:TIGR00464 378 -DEDAFKKHLKKNVKEVLEALKKKLQALeewTADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKG--HGPDLAQILE 452
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
36-361 |
1.32e-130 |
|
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: 379.62 E-value: 1.32e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 36 AVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPY 115
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 116 QQSQRLELYAQATEALLKTGaaypcfcspqrlellkkealrnhqtprydnrcrnmsqeqvaqklakdpkpairfrleqvv 195
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 196 pafqdlvygwnrhevasvegdpvimksDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLP 275
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 276 LLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFN 355
Cdd:cd00808 154 LILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233
|
....*.
gi 815891074 356 RLHLQR 361
Cdd:cd00808 234 GQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
37-351 |
4.25e-103 |
|
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: 312.33 E-value: 4.25e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNH--QTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQ 193
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGspSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIpME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 194 VVPAFQDLVYGwnRHEVASVEGDP-VIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFA 272
Cdd:pfam00749 154 SPYVFRDPVRG--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 273 HLPLLLNRDGSKLSKRQGD--VFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEK 350
Cdd:pfam00749 232 HEYLRLNLDGTKLSKRKLSwsVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKK 311
|
.
gi 815891074 351 L 351
Cdd:pfam00749 312 L 312
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
14-366 |
1.65e-96 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 302.82 E-value: 1.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 14 PSAASGRPVGRREANLGTDAGVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIED 93
Cdd:PLN02627 23 RSRSSRRRFSVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 94 MLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQE 173
Cdd:PLN02627 103 DLKWLGLDWDEGPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 174 QVAQKLAKDPKPAIRFRleqvVPAFQ-----DLVYG---WNrhevASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVL 245
Cdd:PLN02627 183 EVQAELAKGTPYTYRFR----VPKEGsvkidDLIRGevsWN----TDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 246 RGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGR 325
Cdd:PLN02627 255 RAEEHLPNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIF 334
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 815891074 326 TLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRLVSNE 366
Cdd:PLN02627 335 TLEELVEKFSIDRINKSGAVFDSTKLKWMNGQHLRLLPEEE 375
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
37-497 |
1.92e-152 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 444.24 E-value: 1.92e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE--------GPYY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQVVP 196
Cdd:COG0008 77 QSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 197 AFQDLVYGWNRHEVASVeGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPL 276
Cdd:COG0008 157 VFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 277 LLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNR 356
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 357 LHLQRLVSNEsqrrqlvgklqvlVEEAFGCQLQNRDVlnPVYVERILLLRQGHICRLQDLVsPVYSYLWTRP--AVGRAQ 434
Cdd:COG0008 316 PYIRALDDEE-------------LAELLAPELPEAGI--REDLERLVPLVRERAKTLSELA-ELARFFFIERedEKAAKK 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815891074 435 LDAISEKVDVIaKRVLGLLERSSmSLTQDMLNGELKKLSEGLeGTKYSNVMKLLRMALSGQQV 497
Cdd:COG0008 380 RLAPEEVRKVL-KAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTV 439
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
37-508 |
2.37e-140 |
|
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: 413.67 E-value: 2.37e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQVV 195
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 196 PAFQDLVYG---WNRHEVasveGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFA 272
Cdd:TIGR00464 154 VSFNDQVRGeitFQNSEL----DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 273 HLPLLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLP 352
Cdd:TIGR00464 230 HLPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 353 EFNRLHLQRLvSNESQRRQLVGKLQvlveeafgcQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPVYSYLWTRPAVgr 432
Cdd:TIGR00464 310 WLNAHYIKEL-PDEELFELLDPHLK---------SLVNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEV-- 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815891074 433 aQLDAISEKVDVIAKRVLGLLERSSMSL---TQDMLNGELKKLSEgLEGTKYSNVMKLLRMALSGQQvrQGHGLDCSLE 508
Cdd:TIGR00464 378 -DEDAFKKHLKKNVKEVLEALKKKLQALeewTADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKG--HGPDLAQILE 452
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
36-361 |
1.32e-130 |
|
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: 379.62 E-value: 1.32e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 36 AVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPY 115
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 116 QQSQRLELYAQATEALLKTGaaypcfcspqrlellkkealrnhqtprydnrcrnmsqeqvaqklakdpkpairfrleqvv 195
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 196 pafqdlvygwnrhevasvegdpvimksDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLP 275
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 276 LLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFN 355
Cdd:cd00808 154 LILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233
|
....*.
gi 815891074 356 RLHLQR 361
Cdd:cd00808 234 GQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
37-351 |
4.25e-103 |
|
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: 312.33 E-value: 4.25e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNH--QTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRL-EQ 193
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGspSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIpME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 194 VVPAFQDLVYGwnRHEVASVEGDP-VIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFA 272
Cdd:pfam00749 154 SPYVFRDPVRG--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 273 HLPLLLNRDGSKLSKRQGD--VFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEK 350
Cdd:pfam00749 232 HEYLRLNLDGTKLSKRKLSwsVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKK 311
|
.
gi 815891074 351 L 351
Cdd:pfam00749 312 L 312
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
14-366 |
1.65e-96 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 302.82 E-value: 1.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 14 PSAASGRPVGRREANLGTDAGVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIED 93
Cdd:PLN02627 23 RSRSSRRRFSVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 94 MLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQE 173
Cdd:PLN02627 103 DLKWLGLDWDEGPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 174 QVAQKLAKDPKPAIRFRleqvVPAFQ-----DLVYG---WNrhevASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVL 245
Cdd:PLN02627 183 EVQAELAKGTPYTYRFR----VPKEGsvkidDLIRGevsWN----TDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 246 RGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGR 325
Cdd:PLN02627 255 RAEEHLPNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIF 334
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 815891074 326 TLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRLVSNE 366
Cdd:PLN02627 335 TLEELVEKFSIDRINKSGAVFDSTKLKWMNGQHLRLLPEEE 375
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
40-292 |
1.81e-88 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 274.04 E-value: 1.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 40 RFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRggpagpyqQSQ 119
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLY--------QSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 120 RLELYAQATEALLKTGAAYPCFCSpqRLELLKKEALRNHQTPRYDNRCRNMSqeqvaqkLAKDPKPAIRFRLEQVVPAFQ 199
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCS--RKEIAAAAPAPPDGGGIYPGTCRDLL-------HGPRNPPAWRLRVPDAVIAFD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 200 DLVYGWNRHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLN 279
Cdd:PRK05710 152 DRLQGRQHQDLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLN 231
|
250
....*....|...
gi 815891074 280 RDGSKLSKRQGDV 292
Cdd:PRK05710 232 ADGQKLSKQNGAP 244
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
37-290 |
1.09e-84 |
|
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: 263.63 E-value: 1.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRggpagpyq 116
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVY-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGAAYPCFCSpqRLELlkkeALRNHQTPRYDNRCRNMSQEQVAQKlakdpkPAIRFRLEQVVP 196
Cdd:TIGR03838 73 QSQRHALYQAALDRLLAAGLAYPCQCT--RKEI----AAARDGGGIYPGTCRNGLPGRPGRP------AAWRLRVPDGVI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 197 AFQDLVYGWNRHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPL 276
Cdd:TIGR03838 141 AFDDRLQGPQQQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPL 220
|
250
....*....|....
gi 815891074 277 LLNRDGSKLSKRQG 290
Cdd:TIGR03838 221 VVNADGEKLSKQNG 234
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
37-360 |
6.59e-67 |
|
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: 215.80 E-value: 6.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDE--------GPYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGaaypcfcspqrlellkkealrnhqtprydnrcrnmsqeqvaqklakdpkpairfrleqvvp 196
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 197 afqdlvygwnrhevasvegdpvimksdGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPL 276
Cdd:cd00418 93 ---------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPR 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 277 LLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNR 356
Cdd:cd00418 146 LLLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNR 225
|
....
gi 815891074 357 LHLQ 360
Cdd:cd00418 226 EYIR 229
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
37-315 |
1.87e-46 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 170.80 E-value: 1.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTD--QTRVVPGAAENIEDMLEWAGIPPDESprrggpagp 114
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWDEV--------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 115 YQQSQRLELYAQATEALLKTGAAYPCFCSPqrlELLKKeaLRNHQTPrydNRCRNMSQEQVAQKLAK------------- 181
Cdd:PRK04156 173 VIQSDRLEIYYEYARKLIEMGGAYVCTCDP---EEFKE--LRDAGKP---CPHRDKSPEENLELWEKmldgeykegeavv 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 182 -------DPKPAIR----FRLEQvvpafqdlvygwNRHevaSVEGDPVIMksdgFPTYHLACVVDDHHMGISHVLRGSEW 250
Cdd:PRK04156 245 rvktdleHPNPSVRdwvaFRIVK------------TPH---PRVGDKYRV----WPTYNFAVAVDDHLLGVTHVLRGKDH 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 251 LVSTAKHLLLYQALGWQPP---HFAHLPLllnrDGSKLSK---RQG----------DVFLEHFAA---DGFLPDSLLDII 311
Cdd:PRK04156 306 IDNTEKQRYIYDYFGWEYPetiHYGRLKI----EGFVLSTskiRKGieegeysgwdDPRLPTLRAlrrRGILPEAIRELI 381
|
....
gi 815891074 312 TNCG 315
Cdd:PRK04156 382 IEVG 385
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
37-290 |
1.20e-38 |
|
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: 148.82 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESprrggpagpYQ 116
Cdd:TIGR00463 94 VVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEV---------VY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHqtprydnrCRNMSQEQVAQkLAKDPKPAIRFRLEQVVP 196
Cdd:TIGR00463 165 QSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACH--------CRDRSVEENLE-RWEEMLEGKEEGGSVVVR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 197 AFQDLvygwnRHEVASVEgDPVIMKSDG------------FPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQAL 264
Cdd:TIGR00463 236 VKTDL-----KHKNPAIR-DWVIFRIVKtphprtgdkyrvYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYF 309
|
250 260
....*....|....*....|....*....
gi 815891074 265 GWQPPHFAHLPLLLNRDGSKLS---KRQG 290
Cdd:TIGR00463 310 GWEPPEFIHWGRLKIDDVRALStssARKG 338
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
37-315 |
2.35e-36 |
|
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: 135.17 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQT--RVVPGAAENIEDMLEWAGIPPDESprrggpagp 114
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEV--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 115 YQQSQRLELYAQATEALLKTGAAYPcfcspqrlellkkealrnHqtPRYDNRCRnmsqeqvaqklakdpkpairfrleqv 194
Cdd:cd09287 73 VIASDRIELYYEYARKLIEMGGAYV------------------H--PRTGSKYR-------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 195 vpafqdlVYgwnrhevasvegdpvimksdgfPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPP---HF 271
Cdd:cd09287 107 -------VW----------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPetiHW 157
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 272 AHLPLllnrDGSKLSK---RQG----------DVFLEHFAA---DGFLPDSLLDIITNCG 315
Cdd:cd09287 158 GRLKI----EGGKLSTskiRKGiesgeyegwdDPRLPTLRAlrrRGIRPEAIRDFIIEVG 213
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
37-301 |
2.83e-19 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 91.32 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDesprrggpAGPYQ 116
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD--------AVTYT 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 Q---SQRLELyaqaTEALLKTGAAYpcfcspqrLELLKKEALRNHQTPRYDNRCRNMSQEQvAQKLAKDPKP-------- 185
Cdd:PLN02907 286 SdyfPQLMEM----AEKLIKEGKAY--------VDDTPREQMRKERMDGIESKCRNNSVEE-NLRLWKEMIAgserglqc 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 186 AIRFRLEQVVP--AFQDLVYgwNR------HEVASvegdpvimKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKH 257
Cdd:PLN02907 353 CVRGKLDMQDPnkSLRDPVY--YRcnptphHRIGS--------KYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQY 422
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 815891074 258 LLLYQALGWQPPH---FAHlpllLNRDGSKLSKRQGDVFLEHFAADG 301
Cdd:PLN02907 423 YRILEDMGLRKVHiweFSR----LNFVYTLLSKRKLQWFVDNGKVEG 465
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
37-302 |
5.64e-17 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 83.86 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDesprrggpAGPYQ 116
Cdd:PTZ00402 53 VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD--------VGPTY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 117 QSQRLELYAQATEALLKTGAAYpCFCSPqRLELlkkealrnhQTPRYD---NRCRNMSQEQVAqklakdpkpairfRLeq 193
Cdd:PTZ00402 125 SSDYMDLMYEKAEELIKKGLAY-CDKTP-REEM---------QKCRFDgvpTKYRDISVEETK-------------RL-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 194 vvpafqdlvygWNRHEVASVEG-------------------DPVI------------MKSDGFPTYHLACVVDDHHMGIS 242
Cdd:PTZ00402 179 -----------WNEMKKGSAEGqetclrakisvdnenkamrDPVIyrvnltpharqgTKYKAYPTYDFCCPIIDSVEGVT 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 243 HVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPlLLNRDGSKLSKRQGDVFLEHFAADGF 302
Cdd:PTZ00402 248 HALRTNEYHDRNDQYYWFCDALGIRKPIVEDFS-RLNMEYSVMSKRKLTQLVDTHVVDGW 306
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
32-295 |
6.78e-15 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 77.36 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 32 DAGVAVRV--RFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPrrg 109
Cdd:PLN03233 5 EGAIAGQIvtRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVS--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 110 gpagpyQQSQRLELYAQATEALLKTGAAYpcfcspqrLELLKKEALRNHQTPRYDNRCRNMSqeqvaqklakdPKPAIRF 189
Cdd:PLN03233 82 ------FTSDYFEPIRCYAIILIEEGLAY--------MDDTPQEEMKKERADRAESKHRNQS-----------PEEALEM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 190 rleqvvpaFQDLVYG------W---NRHEVASVEG---DPVIMKSD------------GFPTYHLACVVDDHHMGISHVL 245
Cdd:PLN03233 137 --------FKEMCSGkeeggaWclrAKIDMQSDNGtlrDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHAL 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 815891074 246 RGSEWLVSTAKHLLLYQALGWQPPHFaHLPLLLNRDGSKLSKRQGDVFLE 295
Cdd:PLN03233 209 RTTEYDDRDAQFFWIQKALGLRRPRI-HAFARMNFMNTVLSKRKLTWFVD 257
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
37-138 |
1.34e-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: 70.36 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESprrggpagpYQ 116
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV---------TY 72
|
90 100
....*....|....*....|....*
gi 815891074 117 QS---QRLELYAqatEALLKTGAAY 138
Cdd:cd00807 73 ASdyfDQLYEYA---EQLIKKGKAY 94
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
18-308 |
2.21e-08 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 56.91 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 18 SGRPV----GRREANLGTDA--GVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDqtrvvPGAAEN- 90
Cdd:PTZ00437 27 TGRPVpgcrNTPELLEKHEAvtGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTN-----PETEEQv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 91 ----IEDMLEWAGIPPDESprrggpagPYQQSQRLELYAQATEaLLKTGAAYPCFCSPqrlellkkEALRNHQTPRYDNR 166
Cdd:PTZ00437 102 yidaIMEMVKWMGWKPDWV--------TFSSDYFDQLHEFAVQ-LIKDGKAYVDHSTP--------DELKQQREQREDSP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 167 CRNMSQEQ-------VAQKLAKDPKPAIRFRLEQVV--PAFQDLVygwnRHEVASVEGDPVIMKSDGFPTYHLA-CVVDD 236
Cdd:PTZ00437 165 WRNRSVEEnlllfehMRQGRYAEGEATLRVKADMKSdnPNMRDFI----AYRVKYVEHPHAKDKWCIYPSYDFThCLIDS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815891074 237 HHmGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPlLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLL 308
Cdd:PTZ00437 241 LE-DIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFS-RLNVTGSLLSKRKINVLVRKGIVRGFDDPRLL 310
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
37-138 |
2.22e-08 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 57.04 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDEsprrggpaGPYQ 116
Cdd:PRK14703 32 VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGE--------HLYY 103
|
90 100
....*....|....*....|..
gi 815891074 117 QSQRLELYAQATEALLKTGAAY 138
Cdd:PRK14703 104 ASDYFERMYAYAEQLIKMGLAY 125
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
34-148 |
3.16e-07 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 53.22 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 34 GVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDqtrvvPGAA-----ENIEDMLEWAGIPPDESprr 108
Cdd:PLN02859 262 GGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEkkeyiDHIEEIVEWMGWEPFKI--- 333
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 815891074 109 ggpagPYQQSQRLELYAQATEaLLKTGAAYPCFCSPQRLE 148
Cdd:PLN02859 334 -----TYTSDYFQELYELAVE-LIRRGHAYVDHQTPEEIK 367
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
37-144 |
6.87e-06 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 48.56 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891074 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDT-----DQTRVvpgaaENIEDMLEWAGIPPDESPRRggp 111
Cdd:PRK05347 30 VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTnpekeDQEYV-----DSIKEDVRWLGFDWSGELRY--- 101
|
90 100 110
....*....|....*....|....*....|...
gi 815891074 112 AGPYQQsqrlELYAQAtEALLKTGAAYPCFCSP 144
Cdd:PRK05347 102 ASDYFD----QLYEYA-VELIKKGKAYVDDLSA 129
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
39-96 |
1.69e-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: 39.00 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815891074 39 VRFAPSPTGFLHLGGLRTALYNYIFA-----KKYQGSFILRLEDTDQTRVVP--GAAENIEDMLE 96
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAqayrkLGYKVRCIALIDDAGGLIGDPanKKGENAKAFVE 66
|
|
| |
