|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
33-521 |
8.40e-157 |
|
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: 455.02 E-value: 8.40e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 33 PGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpa 112
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 113 GPYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLAVDPKPAIRFRLE 192
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 193 EAVPAFQDLVYGWTQHEVASVeGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFA 272
Cdd:COG0008 153 EEGVVFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 273 HLPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLP 352
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 353 EFNRLHLRRLVSSEtqrpqlveklqglVKEAFGSELQNKDVLDpaYMERILLLRQGHISRLQDLVSPVYSYLWTRPAVHR 432
Cdd:COG0008 312 WLNGPYIRALDDEE-------------LAELLAPELPEAGIRE--DLERLVPLVRERAKTLSELAELARFFFIEREDEKA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 433 SELGASSENVDVIAKRLLGLLERPGlSLTQDVLNRELKKLSEGLeGAKHSSVMKLLRMALSGQLQGPPVAEMMVSLGPKE 512
Cdd:COG0008 377 AKKRLAPEEVRKVLKAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKER 454
|
....*....
gi 21312986 513 VRERIQKVL 521
Cdd:COG0008 455 VFERLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
36-519 |
1.01e-149 |
|
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: 437.17 E-value: 1.01e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPY 115
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 116 CQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLAVDPKPAIRFRL-EEA 194
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 195 VPAFQDLVYGwtQHEVASVE-GDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFAH 273
Cdd:TIGR00464 153 VVSFNDQVRG--EITFQNSElDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 274 LPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPE 353
Cdd:TIGR00464 231 LPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 354 FNRLHLRRLvSSETQRPQLVEKLQGLVkeafgselqNKDVLDPAYMERILLLRQGHISRLQDLVSPVYSYL-----WTRP 428
Cdd:TIGR00464 311 LNAHYIKEL-PDEELFELLDPHLKSLV---------NTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFedkkeVDED 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 429 AVHRSELGASSENVDVIAKRLLGLLERpglslTQDVLNRELKKLSEgLEGAKHSSVMKLLRMALSGQLQGPPVAEMMVSL 508
Cdd:TIGR00464 381 AFKKHLKKNVKEVLEALKKKLQALEEW-----TADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKGHGPDLAQILELI 454
|
490
....*....|.
gi 21312986 509 GPKEVRERIQK 519
Cdd:TIGR00464 455 GKTESIKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
37-361 |
8.44e-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: 372.30 E-value: 8.44e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRRGGPAGPYC 116
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 117 QSQRLALYAQATEALLRSGaaypcfclpqrlellkkealrsrqtprydnrcrnlsqaqvaqklavdpkpairfrleeavp 196
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 197 afqdlvygwtqhevasvegdpvilksDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFAHLPL 276
Cdd:cd00808 101 --------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 277 LLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFNR 356
Cdd:cd00808 155 ILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNG 234
|
....*
gi 21312986 357 LHLRR 361
Cdd:cd00808 235 QYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
36-351 |
1.70e-102 |
|
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: 310.41 E-value: 1.70e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPY 115
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 116 CQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKK--EALRSRQTPRYDNRCRNLSQAQVAQKLAVDPKPAIRFRL-E 192
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREeqEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIpM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 193 EAVPAFQDLVYGwtQHEVASVEGDP-VILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRF 271
Cdd:pfam00749 153 ESPYVFRDPVRG--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 272 AHLPLLLNRDGSKLSKRQGDI--FLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLE 349
Cdd:pfam00749 231 IHEYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRK 310
|
..
gi 21312986 350 KL 351
Cdd:pfam00749 311 KL 312
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
25-509 |
7.48e-99 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 308.59 E-value: 7.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 25 REASLGPDPGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDE 104
Cdd:PLN02627 34 RAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 105 SPRRGGPAGPYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLAVDPK 184
Cdd:PLN02627 114 GPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 185 PAIRFRL-EEAVPAFQDLVYGwtqhEV---ASVEGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLL 260
Cdd:PLN02627 194 YTYRFRVpKEGSVKIDDLIRG----EVswnTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 261 YQALGWQPPRFAHLPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRIT 340
Cdd:PLN02627 270 YKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRIN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 341 CHSALLDLEKLPEFNRLHLRRLvSSETQRPQLVEKL--QGLVKEAFGSELQnkdvldpaymERILLLRQGhISRLQDLVS 418
Cdd:PLN02627 350 KSGAVFDSTKLKWMNGQHLRLL-PEEELVKLVGERWksAGILKESDGSFVK----------EAVELLKDG-IELVTDADK 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 419 PVYSYLwtrpAVHRSELGASSENVDVIAKRLLGLLErpglSLTQDVLNRELKK-LSEGLEGAKH-----SSVMKL----- 487
Cdd:PLN02627 418 ELLNLL----SYPLAATLSSPEAKTVVEDNFSEVAD----ALIAAYDSGELAAaLEEGHDGWQKwvkafGKALKRkgkrl 489
|
490 500
....*....|....*....|....*
gi 21312986 488 ---LRMALSGQLQGPPVAEMMVSLG 509
Cdd:PLN02627 490 fmpLRVALTGKMHGPDVGESLVLLH 514
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
33-521 |
8.40e-157 |
|
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: 455.02 E-value: 8.40e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 33 PGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpa 112
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 113 GPYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLAVDPKPAIRFRLE 192
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 193 EAVPAFQDLVYGWTQHEVASVeGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFA 272
Cdd:COG0008 153 EEGVVFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 273 HLPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLP 352
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 353 EFNRLHLRRLVSSEtqrpqlveklqglVKEAFGSELQNKDVLDpaYMERILLLRQGHISRLQDLVSPVYSYLWTRPAVHR 432
Cdd:COG0008 312 WLNGPYIRALDDEE-------------LAELLAPELPEAGIRE--DLERLVPLVRERAKTLSELAELARFFFIEREDEKA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 433 SELGASSENVDVIAKRLLGLLERPGlSLTQDVLNRELKKLSEGLeGAKHSSVMKLLRMALSGQLQGPPVAEMMVSLGPKE 512
Cdd:COG0008 377 AKKRLAPEEVRKVLKAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKER 454
|
....*....
gi 21312986 513 VRERIQKVL 521
Cdd:COG0008 455 VFERLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
36-519 |
1.01e-149 |
|
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: 437.17 E-value: 1.01e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPY 115
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 116 CQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLAVDPKPAIRFRL-EEA 194
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 195 VPAFQDLVYGwtQHEVASVE-GDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFAH 273
Cdd:TIGR00464 153 VVSFNDQVRG--EITFQNSElDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 274 LPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPE 353
Cdd:TIGR00464 231 LPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 354 FNRLHLRRLvSSETQRPQLVEKLQGLVkeafgselqNKDVLDPAYMERILLLRQGHISRLQDLVSPVYSYL-----WTRP 428
Cdd:TIGR00464 311 LNAHYIKEL-PDEELFELLDPHLKSLV---------NTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFedkkeVDED 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 429 AVHRSELGASSENVDVIAKRLLGLLERpglslTQDVLNRELKKLSEgLEGAKHSSVMKLLRMALSGQLQGPPVAEMMVSL 508
Cdd:TIGR00464 381 AFKKHLKKNVKEVLEALKKKLQALEEW-----TADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKGHGPDLAQILELI 454
|
490
....*....|.
gi 21312986 509 GPKEVRERIQK 519
Cdd:TIGR00464 455 GKTESIKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
37-361 |
8.44e-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: 372.30 E-value: 8.44e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRRGGPAGPYC 116
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 117 QSQRLALYAQATEALLRSGaaypcfclpqrlellkkealrsrqtprydnrcrnlsqaqvaqklavdpkpairfrleeavp 196
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 197 afqdlvygwtqhevasvegdpvilksDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFAHLPL 276
Cdd:cd00808 101 --------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 277 LLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFNR 356
Cdd:cd00808 155 ILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNG 234
|
....*
gi 21312986 357 LHLRR 361
Cdd:cd00808 235 QYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
36-351 |
1.70e-102 |
|
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: 310.41 E-value: 1.70e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPY 115
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 116 CQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKK--EALRSRQTPRYDNRCRNLSQAQVAQKLAVDPKPAIRFRL-E 192
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREeqEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIpM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 193 EAVPAFQDLVYGwtQHEVASVEGDP-VILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRF 271
Cdd:pfam00749 153 ESPYVFRDPVRG--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 272 AHLPLLLNRDGSKLSKRQGDI--FLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLE 349
Cdd:pfam00749 231 IHEYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRK 310
|
..
gi 21312986 350 KL 351
Cdd:pfam00749 311 KL 312
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
25-509 |
7.48e-99 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 308.59 E-value: 7.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 25 REASLGPDPGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDE 104
Cdd:PLN02627 34 RAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 105 SPRRGGPAGPYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLAVDPK 184
Cdd:PLN02627 114 GPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 185 PAIRFRL-EEAVPAFQDLVYGwtqhEV---ASVEGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLL 260
Cdd:PLN02627 194 YTYRFRVpKEGSVKIDDLIRG----EVswnTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 261 YQALGWQPPRFAHLPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRIT 340
Cdd:PLN02627 270 YKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRIN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 341 CHSALLDLEKLPEFNRLHLRRLvSSETQRPQLVEKL--QGLVKEAFGSELQnkdvldpaymERILLLRQGhISRLQDLVS 418
Cdd:PLN02627 350 KSGAVFDSTKLKWMNGQHLRLL-PEEELVKLVGERWksAGILKESDGSFVK----------EAVELLKDG-IELVTDADK 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 419 PVYSYLwtrpAVHRSELGASSENVDVIAKRLLGLLErpglSLTQDVLNRELKK-LSEGLEGAKH-----SSVMKL----- 487
Cdd:PLN02627 418 ELLNLL----SYPLAATLSSPEAKTVVEDNFSEVAD----ALIAAYDSGELAAaLEEGHDGWQKwvkafGKALKRkgkrl 489
|
490 500
....*....|....*....|....*
gi 21312986 488 ---LRMALSGQLQGPPVAEMMVSLG 509
Cdd:PLN02627 490 fmpLRVALTGKMHGPDVGESLVLLH 514
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
36-291 |
1.99e-85 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 265.95 E-value: 1.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRRggpagpy 115
Cdd:PRK05710 5 PYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLY------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 116 cQSQRLALYAQATEALLRSGAAYPCFClpQRLELLKKEALRSRQTPRYDNRCRNLSQAQvaqklavDPKPAIRFRLEEAV 195
Cdd:PRK05710 78 -QSQRHDAYRAALDRLRAQGLVYPCFC--SRKEIAAAAPAPPDGGGIYPGTCRDLLHGP-------RNPPAWRLRVPDAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 196 PAFQDLVYGWTQHEVASVEGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFAHLP 275
Cdd:PRK05710 148 IAFDDRLQGRQHQDLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLP 227
|
250
....*....|....*.
gi 21312986 276 LLLNRDGSKLSKRQGD 291
Cdd:PRK05710 228 LVLNADGQKLSKQNGA 243
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
37-290 |
1.27e-81 |
|
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: 255.16 E-value: 1.27e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRrggpagpyC 116
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVV--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 117 QSQRLALYAQATEALLRSGAAYPCFClpQRLELlkkeALRSRQTPRYDNRCRNLSQAQVAQKlavdpkPAIRFRLEEAVP 196
Cdd:TIGR03838 73 QSQRHALYQAALDRLLAAGLAYPCQC--TRKEI----AAARDGGGIYPGTCRNGLPGRPGRP------AAWRLRVPDGVI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 197 AFQDLVYGWTQHEVASVEGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFAHLPL 276
Cdd:TIGR03838 141 AFDDRLQGPQQQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPL 220
|
250
....*....|....
gi 21312986 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 |
1.76e-64 |
|
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: 209.25 E-value: 1.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPYC 116
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDE--------GPYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 117 QSQRLALYAQATEALLRSGaaypcfclpqrlellkkealrsrqtprydnrcrnlsqaqvaqklavdpkpairfrleeavp 196
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 197 afqdlvygwtqhevasvegdpvilksdGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFAHLPL 276
Cdd:cd00418 93 ---------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPR 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 277 LLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFNR 356
Cdd:cd00418 146 LLLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNR 225
|
....
gi 21312986 357 LHLR 360
Cdd:cd00418 226 EYIR 229
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
25-315 |
1.87e-41 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 156.55 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 25 REASLGPDPGA---PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTD--QSRLVPGAAESIEDMLEWAG 99
Cdd:PRK04156 87 EKKGLPPLPNAekgKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 100 IPPDESprrggpagpYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLK--KEALRSRQTPRYDNRCR-------NL 170
Cdd:PRK04156 167 VKWDEV---------VIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRdaGKPCPHRDKSPEENLELwekmldgEY 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 171 SQAQVAQKLAVD---PKPAIR----FRLEEavpafqdlvygwTQHevaSVEGDPVILksdgFPTYHLACVVDDHHMSISH 243
Cdd:PRK04156 238 KEGEAVVRVKTDlehPNPSVRdwvaFRIVK------------TPH---PRVGDKYRV----WPTYNFAVAVDDHLLGVTH 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 244 VLRGSEWLVSTSKHLLLYQALGWQPPRFAH---LPLllnrDGSKLSK---RQG----------DIFLEHFAAT---GFLP 304
Cdd:PRK04156 299 VLRGKDHIDNTEKQRYIYDYFGWEYPETIHygrLKI----EGFVLSTskiRKGieegeysgwdDPRLPTLRALrrrGILP 374
|
330
....*....|.
gi 21312986 305 EALLDIITNCG 315
Cdd:PRK04156 375 EAIRELIIEVG 385
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
37-323 |
8.76e-35 |
|
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: 137.65 E-value: 8.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESprrggpagpYC 116
Cdd:TIGR00463 94 VVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEV---------VY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 117 QSQRLALYAQATEALLRSGAAYPCFCLPqrlELLKKEALRSRQTPRYDNRCRN------------LSQAQVAQKLAVD-- 182
Cdd:TIGR00463 165 QSDRIETYYDYTRKLIEMGKAYVCDCRP---EEFRELRNRGEACHCRDRSVEEnlerweemlegkEEGGSVVVRVKTDlk 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 183 -PKPAIR----FRLEEavpafqdlvygwTQHEVAsveGDPVILksdgFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKH 257
Cdd:TIGR00463 242 hKNPAIRdwviFRIVK------------TPHPRT---GDKYRV----YPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 258 LLLYQALGWQPPRFAHLPLLLNRDGSKLS---KRQGDI-------------FLEHFAATGFLPEALLDIITNCGSGFAEN 321
Cdd:TIGR00463 303 EYIYRYFGWEPPEFIHWGRLKIDDVRALStssARKGILrgeysgwddprlpTLRAIRRRGIRPEAIRKFMLSIGVKINDV 382
|
..
gi 21312986 322 QM 323
Cdd:TIGR00463 383 TM 384
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
36-315 |
4.61e-34 |
|
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: 128.62 E-value: 4.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTD--QSRLVPGAAESIEDMLEWAGIPPDESprrggpag 113
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDprTKRPDPEAYDMIPEDLEWLGVKWDEV-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 114 pYCQSQRLALYAQATEALLRSGAAYpcfclpqrlellkkealrsrqtprydnrcrnlsqaqvaqklaVDPKPAIRFRlee 193
Cdd:cd09287 73 -VIASDRIELYYEYARKLIEMGGAY------------------------------------------VHPRTGSKYR--- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 194 avpafqdlVYgwtqhevasvegdpvilksdgfPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFAH 273
Cdd:cd09287 107 --------VW----------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIH 156
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 21312986 274 LPlLLNRDGSKLSK---RQG----------DIFLEHFAA---TGFLPEALLDIITNCG 315
Cdd:cd09287 157 WG-RLKIEGGKLSTskiRKGiesgeyegwdDPRLPTLRAlrrRGIRPEAIRDFIIEVG 213
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
34-302 |
2.62e-15 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 78.51 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 34 GAPVRV--RFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRRGGP 111
Cdd:PLN03233 7 AIAGQIvtRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 112 AGPycqsqrLALYAQateALLRSGAAYpcfclpqrLELLKKEALRSRQTPRYDNRCRNLSQaqvaqklavdpkpairfrl 191
Cdd:PLN03233 87 FEP------IRCYAI---ILIEEGLAY--------MDDTPQEEMKKERADRAESKHRNQSP------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 192 EEAVPAFQDLVYG------W---TQHEVASVEG---DPVILKSD------------GFPTYHLACVVDDHHMSISHVLRG 247
Cdd:PLN03233 131 EEALEMFKEMCSGkeeggaWclrAKIDMQSDNGtlrDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHALRT 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 21312986 248 SEWLVSTSKHLLLYQALGWQPPRFaHLPLLLNRDGSKLSKRQGDIFLEHFAATGF 302
Cdd:PLN03233 211 TEYDDRDAQFFWIQKALGLRRPRI-HAFARMNFMNTVLSKRKLTWFVDNGHVTGW 264
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
33-301 |
1.52e-14 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 76.30 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 33 PGAP---VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDesprrg 109
Cdd:PLN02907 207 PGAEegkVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD------ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 110 gpAGPYCQSQRLALYAQAtEALLRSGAAYpcfclpqrLELLKKEALRSRQTPRYDNRCRNLSqaqVAQKLA--------- 180
Cdd:PLN02907 281 --AVTYTSDYFPQLMEMA-EKLIKEGKAY--------VDDTPREQMRKERMDGIESKCRNNS---VEENLRlwkemiags 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 181 -VDPKPAIRFRLEEAVP--AFQDLVY----GWTQHEVASvegdpvilKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVS 253
Cdd:PLN02907 347 eRGLQCCVRGKLDMQDPnkSLRDPVYyrcnPTPHHRIGS--------KYKVYPTYDFACPFVDALEGVTHALRSSEYHDR 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 21312986 254 TSKHLLLYQALG------WQPPRfahlpllLNRDGSKLSKRQGDIFLEHFAATG 301
Cdd:PLN02907 419 NAQYYRILEDMGlrkvhiWEFSR-------LNFVYTLLSKRKLQWFVDNGKVEG 465
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
10-289 |
7.27e-14 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 74.23 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 10 LAEPHVVALGHRVGRREASLGPDPGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAE 89
Cdd:PTZ00402 26 LSNTYFTAANANEENDKLQLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 90 SIEDMLEWAGIPPDesprrggpAGPYCQSQRLALYAQATEALLRSGAAYpCfclpqrlellkkealrsRQTPRYDnrcrn 169
Cdd:PTZ00402 106 AILDDLATLGVSWD--------VGPTYSSDYMDLMYEKAEELIKKGLAY-C-----------------DKTPREE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 170 lsqaqvAQKLAVDPKPAiRFR---LEEAVPAFQDLVYGWTQHEVASVEG------------DPVIL------------KS 222
Cdd:PTZ00402 155 ------MQKCRFDGVPT-KYRdisVEETKRLWNEMKKGSAEGQETCLRAkisvdnenkamrDPVIYrvnltpharqgtKY 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312986 223 DGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPRFAHLPlLLNRDGSKLSKRQ 289
Cdd:PTZ00402 228 KAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFS-RLNMEYSVMSKRK 293
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
389-521 |
9.80e-14 |
|
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: 68.76 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 389 QNKDVLDPAYMERILLLRQGHISRLQDLVSPVYSYLW------TRPAVHRSELGASSENVDVIaKRLLGLLErpGLS-LT 461
Cdd:pfam19269 13 AGLDGLDDEYLKKVVPLLKERAETLSELAELADFFFElpleydEEAYAKKKMKTNKEESLEVL-QELLPRLE--ALEdWT 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 462 QDVLNRELKKLSEGLeGAKHSSVMKLLRMALSGQLQGPPVAEMMVSLGPKEVRERIQKVL 521
Cdd:pfam19269 90 AEALEAALKALAEEL-GVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
37-138 |
1.00e-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: 70.74 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESprrggpagpYC 116
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV---------TY 72
|
90 100
....*....|....*....|....*
gi 21312986 117 QS---QRLALYAqatEALLRSGAAY 138
Cdd:cd00807 73 ASdyfDQLYEYA---EQLIKKGKAY 94
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
34-340 |
8.41e-09 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 58.07 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 34 GAPVrVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRrggpAG 113
Cdd:PTZ00437 50 GKPY-FRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTF----SS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 114 PYCQSqrlaLYAQATEaLLRSGAAYPCFCLPQRLellkKEALRSRQTPRYDNRC--------RNLSQAQVAQKLAVdpkP 185
Cdd:PTZ00437 125 DYFDQ----LHEFAVQ-LIKDGKAYVDHSTPDEL----KQQREQREDSPWRNRSveenlllfEHMRQGRYAEGEAT---L 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 186 AIRFRLEEAVPAFQDLVygwtQHEVASVEGDPVILKSDGFPTYHLA-CVVDDHHmSISHVLRGSEWLVSTSKHLLLYQAL 264
Cdd:PTZ00437 193 RVKADMKSDNPNMRDFI----AYRVKYVEHPHAKDKWCIYPSYDFThCLIDSLE-DIDYSLCTLEFETRRESYFWLLEEL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 265 G-WQPP--RFAHlpllLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAenqmgrtlPELITQF-DLTRIT 340
Cdd:PTZ00437 268 NlWRPHvwEFSR----LNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYT--------PAAINRFcELVGIT 335
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
34-157 |
4.54e-07 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 52.84 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 34 GAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDqsrlvPGAAES-----IEDMLEWAGIPPDESprr 108
Cdd:PLN02859 262 GGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEKKeyidhIEEIVEWMGWEPFKI--- 333
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 21312986 109 ggpagPYCQSQRLALYAQATEaLLRSGAAYPCFCLPQRLELLKKEALRS 157
Cdd:PLN02859 334 -----TYTSDYFQELYELAVE-LIRRGHAYVDHQTPEEIKEYREKKMNS 376
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
37-138 |
2.76e-06 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 50.11 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPYC 116
Cdd:PRK14703 32 VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGE--------HLYY 103
|
90 100
....*....|....*....|..
gi 21312986 117 QSQRLALYAQATEALLRSGAAY 138
Cdd:PRK14703 104 ASDYFERMYAYAEQLIKMGLAY 125
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
37-141 |
3.10e-03 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 40.09 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312986 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDT-----DQsRLVpgaaESIEDMLEWAGIPPDESPRRggp 111
Cdd:PRK05347 30 VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTnpekeDQ-EYV----DSIKEDVRWLGFDWSGELRY--- 101
|
90 100 110
....*....|....*....|....*....|
gi 21312986 112 AGPYCQSqrlaLYAQAtEALLRSGAAYPCF 141
Cdd:PRK05347 102 ASDYFDQ----LYEYA-VELIKKGKAYVDD 126
|
|
| |
