|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
2-466 |
0e+00 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 789.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDR 81
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 82 YNNVIDEMLEAGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHH-----ADDEPCVVRFANPQEGSVIFDDQI 156
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEienklAKGIPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 157 RGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDDGK 236
Cdd:TIGR00464 161 RGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 237 KLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHG-DQEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNHHYINTLP 315
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPdDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 316 AEYVATHLQWHIEQE-NIDTRNGPQLAELVKLLGERCKTLKEMAQSCRYFYEEFAEFDADAAKKHLRPVARQPLEVVRDK 394
Cdd:TIGR00464 321 DEELFELLDPHLKSLvNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLKKNVKEVLEALKKK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490247453 395 LAAISDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKSRSVDRINKalAFIAE 466
Cdd:TIGR00464 401 LQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA--QFIAA 470
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-465 |
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: 704.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 1 MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFD 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 81 RYNNVIDEMLEAGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRH-SHEHH----ADDEPCVVRFANPQEGsVIFDDQ 155
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDlSPEELermlAAGEPPVLRFKIPEEG-VVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 156 IRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDDG 235
Cdd:COG0008 162 VRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 236 KKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSH-GDQEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNHHYINTL 314
Cdd:COG0008 242 TKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKsDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 315 PAEYVATHLQWHIEQENIDTRngpqLAELVKLLGERCKTLKEMAQSCRYFYEEFAefDADAAKKHLRP-VARQPLEVVRD 393
Cdd:COG0008 322 DDEELAELLAPELPEAGIRED----LERLVPLVRERAKTLSELAELARFFFIERE--DEKAAKKRLAPeEVRKVLKAALE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490247453 394 KLAAISDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKSRSVDRINKALAFIA 465
Cdd:COG0008 396 VLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAIDKLA 467
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
2-305 |
1.27e-163 |
|
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: 464.48 E-value: 1.27e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDR 81
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 82 YNNVIDEMLEAGTAYKCYCSKERLEALREEQMAKGEK--PRYDGRCRHSHEH-----HADDEPCVVRFANPQEGSVIFDD 154
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEemkkgSAEGGPATVRAKIPMESPYVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 155 QIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDD 234
Cdd:pfam00749 161 PVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490247453 235 GKKLSKRHGAVSV--MQYRDDGYLPEALLNYLVRLGWS-HGDQEIFTREEMIEFFSLGAVSKSASAFNTDKLLW 305
Cdd:pfam00749 241 GTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTpEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
3-454 |
2.18e-149 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 436.48 E-value: 2.18e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 3 IKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGP--------YF 74
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygpYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 75 QTKRFDRYNNVIDEMLEAGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDE-----PCVVRFANPQEGS 149
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAElakgtPYTYRFRVPKEGS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 150 VIFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSM 229
Cdd:PLN02627 206 VKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 230 INGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHG-DQEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNH 308
Cdd:PLN02627 286 ILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGtENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 309 HYINTLPAEyvathlqwhieqenidtrngpqlaELVKLLGERCKTLKEMAQSCRYFYEEFAEFDADA------AKKHLRP 382
Cdd:PLN02627 366 QHLRLLPEE------------------------ELVKLVGERWKSAGILKESDGSFVKEAVELLKDGielvtdADKELLN 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 383 VARQPL----------EVVRDKLAAISD----------WTA--ENVHHAIQATADELEVGMGKVG----MPLRVAVTGAG 436
Cdd:PLN02627 422 LLSYPLaatlsspeakTVVEDNFSEVADaliaaydsgeLAAalEEGHDGWQKWVKAFGKALKRKGkrlfMPLRVALTGKM 501
|
490 500
....*....|....*....|...
gi 490247453 437 QSPalDVT-----VHAIGKSRSV 454
Cdd:PLN02627 502 HGP--DVGeslvlLHKAGTPDSV 522
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-313 |
9.12e-135 |
|
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: 388.10 E-value: 9.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDE--------GPY 73
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 74 FQTKRFDRYNNVIDEMLEAGtaykcycskerlealreeqmakgekprydgrcrhshehhaddepcvvrfanpqegsvifd 153
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 154 dqirgpiefsnqelddliirrtDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGD 233
Cdd:cd00808 101 ----------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNP 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 234 DGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGD-QEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNHHYIN 312
Cdd:cd00808 159 DGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDgEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIR 238
|
.
gi 490247453 313 T 313
Cdd:cd00808 239 E 239
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
2-466 |
0e+00 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 789.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDR 81
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 82 YNNVIDEMLEAGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHH-----ADDEPCVVRFANPQEGSVIFDDQI 156
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEienklAKGIPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 157 RGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDDGK 236
Cdd:TIGR00464 161 RGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 237 KLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHG-DQEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNHHYINTLP 315
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPdDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 316 AEYVATHLQWHIEQE-NIDTRNGPQLAELVKLLGERCKTLKEMAQSCRYFYEEFAEFDADAAKKHLRPVARQPLEVVRDK 394
Cdd:TIGR00464 321 DEELFELLDPHLKSLvNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLKKNVKEVLEALKKK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490247453 395 LAAISDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKSRSVDRINKalAFIAE 466
Cdd:TIGR00464 401 LQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA--QFIAA 470
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-465 |
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: 704.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 1 MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFD 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 81 RYNNVIDEMLEAGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRH-SHEHH----ADDEPCVVRFANPQEGsVIFDDQ 155
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDlSPEELermlAAGEPPVLRFKIPEEG-VVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 156 IRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDDG 235
Cdd:COG0008 162 VRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 236 KKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSH-GDQEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNHHYINTL 314
Cdd:COG0008 242 TKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKsDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 315 PAEYVATHLQWHIEQENIDTRngpqLAELVKLLGERCKTLKEMAQSCRYFYEEFAefDADAAKKHLRP-VARQPLEVVRD 393
Cdd:COG0008 322 DDEELAELLAPELPEAGIRED----LERLVPLVRERAKTLSELAELARFFFIERE--DEKAAKKRLAPeEVRKVLKAALE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490247453 394 KLAAISDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKSRSVDRINKALAFIA 465
Cdd:COG0008 396 VLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAIDKLA 467
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
2-305 |
1.27e-163 |
|
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: 464.48 E-value: 1.27e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDR 81
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 82 YNNVIDEMLEAGTAYKCYCSKERLEALREEQMAKGEK--PRYDGRCRHSHEH-----HADDEPCVVRFANPQEGSVIFDD 154
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEemkkgSAEGGPATVRAKIPMESPYVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 155 QIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDD 234
Cdd:pfam00749 161 PVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490247453 235 GKKLSKRHGAVSV--MQYRDDGYLPEALLNYLVRLGWS-HGDQEIFTREEMIEFFSLGAVSKSASAFNTDKLLW 305
Cdd:pfam00749 241 GTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTpEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
3-454 |
2.18e-149 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 436.48 E-value: 2.18e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 3 IKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGP--------YF 74
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygpYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 75 QTKRFDRYNNVIDEMLEAGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDE-----PCVVRFANPQEGS 149
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAElakgtPYTYRFRVPKEGS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 150 VIFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSM 229
Cdd:PLN02627 206 VKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 230 INGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHG-DQEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNH 308
Cdd:PLN02627 286 ILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGtENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 309 HYINTLPAEyvathlqwhieqenidtrngpqlaELVKLLGERCKTLKEMAQSCRYFYEEFAEFDADA------AKKHLRP 382
Cdd:PLN02627 366 QHLRLLPEE------------------------ELVKLVGERWKSAGILKESDGSFVKEAVELLKDGielvtdADKELLN 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 383 VARQPL----------EVVRDKLAAISD----------WTA--ENVHHAIQATADELEVGMGKVG----MPLRVAVTGAG 436
Cdd:PLN02627 422 LLSYPLaatlsspeakTVVEDNFSEVADaliaaydsgeLAAalEEGHDGWQKWVKAFGKALKRKGkrlfMPLRVALTGKM 501
|
490 500
....*....|....*....|...
gi 490247453 437 QSPalDVT-----VHAIGKSRSV 454
Cdd:PLN02627 502 HGP--DVGeslvlLHKAGTPDSV 522
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-313 |
9.12e-135 |
|
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: 388.10 E-value: 9.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDE--------GPY 73
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 74 FQTKRFDRYNNVIDEMLEAGtaykcycskerlealreeqmakgekprydgrcrhshehhaddepcvvrfanpqegsvifd 153
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 154 dqirgpiefsnqelddliirrtDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGD 233
Cdd:cd00808 101 ----------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNP 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 234 DGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGD-QEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNHHYIN 312
Cdd:cd00808 159 DGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDgEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIR 238
|
.
gi 490247453 313 T 313
Cdd:cd00808 239 E 239
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
5-270 |
5.57e-89 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 273.65 E-value: 5.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 5 TRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDRYNN 84
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHDAYRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 85 VIDEMLEAGTAYKCYCSKERLEALREEQMAKGekPRYDGRCRhsHEHHADDEPCVVRFANPqEGSVIFDDQIRGPIEF-S 163
Cdd:PRK05710 88 ALDRLRAQGLVYPCFCSRKEIAAAAPAPPDGG--GIYPGTCR--DLLHGPRNPPAWRLRVP-DAVIAFDDRLQGRQHQdL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 164 NQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDDGKKLSKRHG 243
Cdd:PRK05710 163 ALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQNG 242
|
250 260
....*....|....*....|....*...
gi 490247453 244 AVSVmqyRDDGylPEALLNYLVR-LGWS 270
Cdd:PRK05710 243 APAL---DAAG--PLPVLAAALRfLGQP 265
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-270 |
9.39e-88 |
|
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: 269.41 E-value: 9.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 6 RFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDRYNNV 85
Cdd:TIGR03838 4 RFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALYQAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 86 IDEMLEAGTAYKCYCSKERLEALREEQmakgekPRYDGRCRHSHeHHADDEPCVVRFANPqEGSVIFDDQIRGPIEF-SN 164
Cdd:TIGR03838 84 LDRLLAAGLAYPCQCTRKEIAAARDGG------GIYPGTCRNGL-PGRPGRPAAWRLRVP-DGVIAFDDRLQGPQQQdLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 165 QELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDDGKKLSKRHGA 244
Cdd:TIGR03838 156 AAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGA 235
|
250 260
....*....|....*....|....*..
gi 490247453 245 VSVmqyrDDGYlPEALLNYLVR-LGWS 270
Cdd:TIGR03838 236 PAL----DDSR-PLPALLAALRfLGLP 257
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
2-312 |
1.26e-83 |
|
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: 257.40 E-value: 1.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDR 81
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 82 YNNVIDEMLEAGtaykcycskerlealreeqmakgekprydgrcrhshehhaddepcvvrfanpqegsvifddqirgpie 161
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 162 fsnqelddliirrtdGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDDGKKLSKR 241
Cdd:cd00418 93 ---------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLSKR 157
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490247453 242 HGAVSVMQYRDDGYLPEALLNYLVRLGWSHGD-QEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNHHYIN 312
Cdd:cd00418 158 KLNTTLRALRRRGYLPEALRNYLALIGWSKPDgHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNREYIR 229
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
319-461 |
3.92e-43 |
|
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: 149.26 E-value: 3.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 319 VATHLQWHIEQENIDTRNGPQLAELVKLLGERCKTLKEMAQSCRYFYEEFAEFDADAAKKH----LRPVARQPLEVVRDK 394
Cdd:pfam19269 2 LAELALPYLEEAGLDGLDDEYLKKVVPLLKERAETLSELAELADFFFELPLEYDEEAYAKKkmktNKEESLEVLQELLPR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490247453 395 LAAISDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKSRSVDRINKAL 461
Cdd:pfam19269 82 LEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
2-268 |
1.11e-41 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 156.16 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLE--RSTPEAIEAIMDGMNWLNLQWDEgPYFQTKRF 79
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDE-VVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 80 DRYNNVIDEMLEAGTAYKCYCSKERLEALREEQmakgekprydgrcrhshehhaddEPCVVRFANPQEGSVIFDDQIRGp 159
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKELRDAG-----------------------KPCPHRDKSPEENLELWEKMLDG- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 160 iEFSNQE---------------LDDLIIRRTD-------GS-----PTYNFCVVVDDWDMAITHVIRGEDHINNTPRQIN 212
Cdd:PRK04156 236 -EYKEGEavvrvktdlehpnpsVRDWVAFRIVktphprvGDkyrvwPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRY 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490247453 213 ILKALNAPVPVYAH---VSMingdDGKKLSKR--HGAVSVMQY--RDD------------GYLPEALLNYLVRLG 268
Cdd:PRK04156 315 IYDYFGWEYPETIHygrLKI----EGFVLSTSkiRKGIEEGEYsgWDDprlptlralrrrGILPEAIRELIIEVG 385
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
2-273 |
1.23e-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: 139.19 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYfQTKRFDR 81
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVY-QSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 82 YNNVIDEMLEAGTAYKCYCSKERleaLREEQMaKGEKprydgrCRHSHEHHADDEPCVVRFANPQE--GSVIFddQIRGP 159
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEE---FRELRN-RGEA------CHCRDRSVEENLERWEEMLEGKEegGSVVV--RVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 160 IEFSNQELDDLIIRRTD-------GS-----PTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHV 227
Cdd:TIGR00463 240 LKHKNPAIRDWVIFRIVktphprtGDkyrvyPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHW 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490247453 228 SMINGDDGKKLS---KRHGAV-------------SVMQYRDDGYLPEALLNYLVRLGWSHGD 273
Cdd:TIGR00463 320 GRLKIDDVRALStssARKGILrgeysgwddprlpTLRAIRRRGIRPEAIRKFMLSIGVKIND 381
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
2-276 |
2.26e-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: 123.23 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTP--EAIEAIMDGMNWLNLQWDEgPYFQTKRF 79
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDE-VVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 80 DRYNNVIDEMLEAGTAYKcycskerlealreeqmakgeKPRydgrcrhshehhADDEPCVVrfanpqegsvifddqirgp 159
Cdd:cd09287 80 ELYYEYARKLIEMGGAYV--------------------HPR------------TGSKYRVW------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 160 iefsnqelddliirrtdgsPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDDGK-KL 238
Cdd:cd09287 109 -------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGKlST 169
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490247453 239 SKRHGAVSVMQY--RDD------------GYLPEALLNYLVRLGWSHGDQEI 276
Cdd:cd09287 170 SKIRKGIESGEYegWDDprlptlralrrrGIRPEAIRDFIIEVGVKQTDATI 221
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
2-307 |
1.40e-18 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 88.48 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDR 81
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 82 YNNVIDEMLEAGTAykcYCSKerleALREEQmakgEKPRYDGRcrhshehhaddePCVVRFANPQEGSVIFDDQIRG--- 158
Cdd:PTZ00402 132 MYEKAEELIKKGLA---YCDK----TPREEM----QKCRFDGV------------PTKYRDISVEETKRLWNEMKKGsae 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 159 ----------PIEFSNQELDDLIIRRTD------------GSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKA 216
Cdd:PTZ00402 189 gqetclrakiSVDNENKAMRDPVIYRVNltpharqgtkykAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 217 LNAPVPVYAHVSMINGD----DGKKLSKRHGAvSVMQYRDDGYLPEalLNYLVRLGwshgdqeiFTREEMIEFFSLGAVS 292
Cdd:PTZ00402 269 LGIRKPIVEDFSRLNMEysvmSKRKLTQLVDT-HVVDGWDDPRFPT--VRALVRRG--------LKMEALRQFVQEQGMS 337
|
330
....*....|....*
gi 490247453 293 KSASAFNTDKLLWLN 307
Cdd:PTZ00402 338 KTVNFMEWSKLWYFN 352
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
2-169 |
2.45e-18 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 87.86 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDR 81
Cdd:PRK14703 31 RVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASDYFER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 82 YNNVIDEMLEAGTAYKCYCSKERLEALR-----------------EE------QMAKGEKPryDG--------------- 123
Cdd:PRK14703 111 MYAYAEQLIKMGLAYVDSVSEEEIRELRgtvtepgtpspyrdrsvEEnldlfrRMRAGEFP--DGahvlrakidmsspnm 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490247453 124 --------RCRHSHEHHADDEPCV---VRFANPQEgsvifdDQIRG------PIEF-SNQELDD 169
Cdd:PRK14703 189 klrdpllyRIRHAHHYRTGDEWCIypmYDFAHPLE------DAIEGvthsicTLEFeNNRAIYD 246
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
2-96 |
1.13e-15 |
|
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: 76.14 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEgPYFQTKRFDR 81
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYK-VTYASDYFDQ 79
|
90
....*....|....*
gi 490247453 82 YNNVIDEMLEAGTAY 96
Cdd:cd00807 80 LYEYAEQLIKKGKAY 94
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
2-126 |
4.11e-13 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 71.68 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYfQTKRFDR 81
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTY-TSDYFPQ 291
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 490247453 82 YNNVIDEMLEAGtayKCYCSKERLEALREEQMAKGEKprydgRCR 126
Cdd:PLN02907 292 LMEMAEKLIKEG---KAYVDDTPREQMRKERMDGIES-----KCR 328
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
2-113 |
8.56e-12 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 67.48 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNlqWDegPYFQTKRFDR 81
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WE--PFKITYTSDY 339
|
90 100 110
....*....|....*....|....*....|....*
gi 490247453 82 YNNVID---EMLEAGTAYKCYCSKERLEALREEQM 113
Cdd:PLN02859 340 FQELYElavELIRRGHAYVDHQTPEEIKEYREKKM 374
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
2-241 |
1.86e-11 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 66.19 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWD----EGPYFQTK 77
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDsvsfTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 78 RfdRYNNVideMLEAGTAYkcycskerLEALREEQMAKgekprydGRCRHSHEHHaddepcvvRFANPQEGSVIFDDQ-- 155
Cdd:PLN03233 91 R--CYAII---LIEEGLAY--------MDDTPQEEMKK-------ERADRAESKH--------RNQSPEEALEMFKEMcs 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 156 ---------IRGPIEFS--NQELDDLIIRRTDGS------------PTYNF-CVVVDDWDmAITHVIRGEDHINNTPRQI 211
Cdd:PLN03233 143 gkeeggawcLRAKIDMQsdNGTLRDPVLFRQNTTphhrsgtaykayPTYDLaCPIVDSIE-GVTHALRTTEYDDRDAQFF 221
|
250 260 270
....*....|....*....|....*....|...
gi 490247453 212 NILKALNAPVP---VYAHVSMINgddgKKLSKR 241
Cdd:PLN03233 222 WIQKALGLRRPrihAFARMNFMN----TVLSKR 250
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
2-147 |
2.55e-11 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 65.51 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 2 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDR 81
Cdd:PRK05347 29 RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSGELRYASDYFDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 82 YNNVIDEMLEAGTAYKCYCSKERLEALR-----------------EE------QMAKGEKPryDG--------------- 123
Cdd:PRK05347 109 LYEYAVELIKKGKAYVDDLSAEEIREYRgtltepgknspyrdrsvEEnldlfeRMRAGEFP--EGsavlrakidmaspni 186
|
170 180 190
....*....|....*....|....*....|....*
gi 490247453 124 --------RCRHSHEHHADDEPCVV---RFANPQE 147
Cdd:PRK05347 187 nmrdpvlyRIRHAHHHRTGDKWCIYpmyDFAHCIS 221
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
6-112 |
8.26e-11 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 64.23 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 6 RFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDeGPYFQTKRFDRYNNV 85
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPD-WVTFSSDYFDQLHEF 133
|
90 100
....*....|....*....|....*..
gi 490247453 86 IDEMLEAGTAYKCYCSKERLEALREEQ 112
Cdd:PTZ00437 134 AVQLIKDGKAYVDHSTPDELKQQREQR 160
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
166-243 |
1.01e-03 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 41.67 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 166 ELDDLIIRRTDGSPTYnFCVvvddwDMAiTHVIR-------------GEDHINNTPRQINILKALN-APVPVYAHVS--M 229
Cdd:COG0018 299 DDKDRVLVKSDGTYTY-FTT-----DIA-YHLYKferygfdrviyvvGADQHGHFKRLFAALKALGyDPAKDLEHLLfgM 371
|
90
....*....|....
gi 490247453 230 INGDDGKKLSKRHG 243
Cdd:COG0018 372 VNLRDGEKMSTRAG 385
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
169-243 |
6.95e-03 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 38.98 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247453 169 DLIIRRTDGSPTYnFCVvvddwDMAiTHVIR-----------GEDHINNTPRQINILKALN---APVPVYAH--VSMING 232
Cdd:PRK01611 245 DRVLIKSDGTYTY-FTR-----DIA-YHLYKferfdrviyvvGADHHGHFKRLKAALKALGydpDALEVLLHqmVGLVRG 317
|
90
....*....|.
gi 490247453 233 DDGKKLSKRHG 243
Cdd:PRK01611 318 GEGVKMSTRAG 328
|
|
| |
