|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
10-482 |
0e+00 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 645.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEI 89
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 90 YQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLPPRYDGRCRNITQNEVASRLKSNKSYVLRLKTPKNQTVeFDDVV 169
Cdd:COG0008 84 YYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVV-FDDLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 170 YGKIKVNSNDIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLPNILGANKK 249
Cdd:COG0008 163 RGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 250 KLSKRTGDVSVEDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLNDINGQYIRKLS 329
Cdd:COG0008 243 KLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 330 KQKITEMCLPYLVEtygdalqNYSDEYIASVVALEQERLKKLSDITSSTKLFFTNELDYDA--KLLpwkkTPTNAKETLL 407
Cdd:COG0008 323 DEELAELLAPELPE-------AGIREDLERLVPLVRERAKTLSELAELARFFFIEREDEKAakKRL----APEEVRKVLK 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277777456 408 SAQTVLMSVKKWTKEGLEETLTDFIFHNKLTHGEALWPLRVALSGQENSPGPFEIAAVLGKEESLKRVRAAIDKL 482
Cdd:COG0008 392 AALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAIDKL 466
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
10-477 |
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: 555.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEI 89
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 90 YQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLPPRYDGRCRNITQNEVASRLKSNKSYVLRLKTPKNQTVEFDDVV 169
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 170 YGKIKVNSNDIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLPNILGANKK 249
Cdd:TIGR00464 161 RGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 250 KLSKRTGDVSVEDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLNDINGQYIRKLS 329
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 330 KQKITEMCLPYLVETYGDALQNysDEYIASVVALEQERLKKLSDITSSTKLFFTNELDYDAKLLPWKKTPtNAKETLLSA 409
Cdd:TIGR00464 321 DEELFELLDPHLKSLVNTDTLN--REQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLKK-NVKEVLEAL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277777456 410 QTVLMSVKKWTKEGLEETLTDFIFHNKLTHGEALWPLRVALSGQENSPGPFEIAAVLGKEESLKRVRA 477
Cdd:TIGR00464 398 KKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA 465
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
10-319 |
5.72e-142 |
|
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: 409.79 E-value: 5.72e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEI 89
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 90 YQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLP--PRYDGRCRNITQNEVASRLKSNKSYVLRLKTPKNQTVEFDD 167
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMESPYVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 168 VVYGKIKVNSNDIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLPNILGAN 247
Cdd:pfam00749 161 PVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277777456 248 KKKLSKRTGDVSV--EDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLND 319
Cdd:pfam00749 241 GTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
10-389 |
3.41e-137 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 405.66 E-value: 3.41e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIV------- 82
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVggeygpy 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 83 -QSKRLEIYQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLPPRYDGRCRNITQNEVASRLKSNKSYVLRLKTPKNQ 161
Cdd:PLN02627 125 rQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 162 TVEFDDVVYGKIKVNSNDIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLP 241
Cdd:PLN02627 205 SVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 242 NILGANKKKLSKRTGDVSVEDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLNDIN 321
Cdd:PLN02627 285 LILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMN 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277777456 322 GQYIRKLSKQKITEMCLPYLVETygDALQNYSDEYIASVVALeqerLKKLSDITSSTKLFFTNELDYD 389
Cdd:PLN02627 365 GQHLRLLPEEELVKLVGERWKSA--GILKESDGSFVKEAVEL----LKDGIELVTDADKELLNLLSYP 426
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
10-327 |
1.18e-131 |
|
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: 380.39 E-value: 1.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDD--------EPI 81
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 82 VQSKRLEIYQKYAQQLIDGGhayycfctpeeltkmreeqekkklpprydgrcrnitqnevasrlksnksyvlrlktpknq 161
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 162 tvefddvvygkikvnsndiddqvllksDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLP 241
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 242 NILGANKKKLSKRTGDVSVEDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLNDIN 321
Cdd:cd00808 154 LILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233
|
....*.
gi 1277777456 322 GQYIRK 327
Cdd:cd00808 234 GQYIRE 239
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
10-482 |
0e+00 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 645.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEI 89
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 90 YQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLPPRYDGRCRNITQNEVASRLKSNKSYVLRLKTPKNQTVeFDDVV 169
Cdd:COG0008 84 YYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVV-FDDLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 170 YGKIKVNSNDIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLPNILGANKK 249
Cdd:COG0008 163 RGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 250 KLSKRTGDVSVEDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLNDINGQYIRKLS 329
Cdd:COG0008 243 KLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPYIRALD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 330 KQKITEMCLPYLVEtygdalqNYSDEYIASVVALEQERLKKLSDITSSTKLFFTNELDYDA--KLLpwkkTPTNAKETLL 407
Cdd:COG0008 323 DEELAELLAPELPE-------AGIREDLERLVPLVRERAKTLSELAELARFFFIEREDEKAakKRL----APEEVRKVLK 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277777456 408 SAQTVLMSVKKWTKEGLEETLTDFIFHNKLTHGEALWPLRVALSGQENSPGPFEIAAVLGKEESLKRVRAAIDKL 482
Cdd:COG0008 392 AALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAIDKL 466
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
10-477 |
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: 555.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEI 89
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 90 YQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLPPRYDGRCRNITQNEVASRLKSNKSYVLRLKTPKNQTVEFDDVV 169
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 170 YGKIKVNSNDIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLPNILGANKK 249
Cdd:TIGR00464 161 RGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 250 KLSKRTGDVSVEDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLNDINGQYIRKLS 329
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAHYIKELP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 330 KQKITEMCLPYLVETYGDALQNysDEYIASVVALEQERLKKLSDITSSTKLFFTNELDYDAKLLPWKKTPtNAKETLLSA 409
Cdd:TIGR00464 321 DEELFELLDPHLKSLVNTDTLN--REQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLKK-NVKEVLEAL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277777456 410 QTVLMSVKKWTKEGLEETLTDFIFHNKLTHGEALWPLRVALSGQENSPGPFEIAAVLGKEESLKRVRA 477
Cdd:TIGR00464 398 KKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA 465
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
10-319 |
5.72e-142 |
|
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: 409.79 E-value: 5.72e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEI 89
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 90 YQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLP--PRYDGRCRNITQNEVASRLKSNKSYVLRLKTPKNQTVEFDD 167
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMESPYVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 168 VVYGKIKVNSNDIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLPNILGAN 247
Cdd:pfam00749 161 PVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277777456 248 KKKLSKRTGDVSV--EDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLND 319
Cdd:pfam00749 241 GTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
10-389 |
3.41e-137 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 405.66 E-value: 3.41e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIV------- 82
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVggeygpy 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 83 -QSKRLEIYQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLPPRYDGRCRNITQNEVASRLKSNKSYVLRLKTPKNQ 161
Cdd:PLN02627 125 rQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 162 TVEFDDVVYGKIKVNSNDIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLP 241
Cdd:PLN02627 205 SVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 242 NILGANKKKLSKRTGDVSVEDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLNDIN 321
Cdd:PLN02627 285 LILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMN 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277777456 322 GQYIRKLSKQKITEMCLPYLVETygDALQNYSDEYIASVVALeqerLKKLSDITSSTKLFFTNELDYD 389
Cdd:PLN02627 365 GQHLRLLPEEELVKLVGERWKSA--GILKESDGSFVKEAVEL----LKDGIELVTDADKELLNLLSYP 426
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
10-327 |
1.18e-131 |
|
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: 380.39 E-value: 1.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDD--------EPI 81
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 82 VQSKRLEIYQKYAQQLIDGGhayycfctpeeltkmreeqekkklpprydgrcrnitqnevasrlksnksyvlrlktpknq 161
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 162 tvefddvvygkikvnsndiddqvllksDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLP 241
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 242 NILGANKKKLSKRTGDVSVEDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLNDIN 321
Cdd:cd00808 154 LILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233
|
....*.
gi 1277777456 322 GQYIRK 327
Cdd:cd00808 234 GQYIRE 239
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
12-312 |
6.90e-94 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 286.36 E-value: 6.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 12 RTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEIYQ 91
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHDAYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 92 KYAQQLIDGGHAYYCFCTPEELtkMREEQEKKKLPPRYDGRCRNITQNEVASRlksnksyVLRLKTPkNQTVEFDDVVYG 171
Cdd:PRK05710 87 AALDRLRAQGLVYPCFCSRKEI--AAAAPAPPDGGGIYPGTCRDLLHGPRNPP-------AWRLRVP-DAVIAFDDRLQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 172 KIKVN-SNDIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLPNILGANKKK 250
Cdd:PRK05710 157 RQHQDlALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQK 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277777456 251 LSKRTGDVSVEDFKnkgylPEALINYIA-LLGWNPGTE--QEIFSLDQLIKQFDINKLHKSGAIF 312
Cdd:PRK05710 237 LSKQNGAPALDAAG-----PLPVLAAALrFLGQPPPAAdaSVEELLAQAVAHWDLTRLPRQAEIN 296
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
11-297 |
4.64e-86 |
|
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: 265.17 E-value: 4.64e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 11 VRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEIY 90
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 91 QKYAQQLIDGGHAYYCFCTPEELTKMREEQekkklpPRYDGRCRNITQNEVAsrlksnKSYVLRLKTPkNQTVEFDDVVY 170
Cdd:TIGR03838 81 QAALDRLLAAGLAYPCQCTRKEIAAARDGG------GIYPGTCRNGLPGRPG------RPAAWRLRVP-DGVIAFDDRLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 171 GKIKVNSN-DIDDQVLLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLPNILGANKK 249
Cdd:TIGR03838 148 GPQQQDLAaAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1277777456 250 KLSKRTGDVSVEDFKNKGYLPEALinyiALLGWNPGTEQEIFSLDQLI 297
Cdd:TIGR03838 228 KLSKQNGAPALDDSRPLPALLAAL----RFLGLPPPPELAAASPAELL 271
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
11-327 |
1.05e-81 |
|
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: 252.78 E-value: 1.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 11 VRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEIY 90
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 91 QKYAQQLIDGGhayycfctpeeltkmreeqekkklpprydgrcrnitqnevasrlksnksyvlrlktpknqtvefddvvy 170
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 171 gkikvnsndiddqvllksdGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLPNILGANKKK 250
Cdd:cd00418 93 -------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTK 153
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277777456 251 LSKRTGDVSVEDFKNKGYLPEALINYIALLGWNPGTEQEIFSLDQLIKQFDINKLHKSGAIFDIKKLNDINGQYIRK 327
Cdd:cd00418 154 LSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNREYIRE 230
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
10-281 |
3.08e-45 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 166.18 E-value: 3.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTD-RT-RFVPGATEKIYEMLAWVKLKFDDEpIVQSKRL 87
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDpRTkRPDPEAYDMILEDLKWLGVKWDEV-VIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 88 EIYQKYAQQLIDGGHAYYCFCTPEELTKMREeqEKKKLPprydgrCRNITQNEVASRLK-------SNKSYVLRLKTP-- 158
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKELRD--AGKPCP------HRDKSPEENLELWEkmldgeyKEGEAVVRVKTDle 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 159 -KNQTVEfdDVVYGKIKVNSNDI--DDQVLlksdgFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSP 235
Cdd:PRK04156 252 hPNPSVR--DWVAFRIVKTPHPRvgDKYRV-----WPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEYP 324
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277777456 236 VYCHLpNILGANKKKLSKRTGDVSVED----------------FKNKGYLPEALINYIALLG 281
Cdd:PRK04156 325 ETIHY-GRLKIEGFVLSTSKIRKGIEEgeysgwddprlptlraLRRRGILPEAIRELIIEVG 385
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
10-281 |
1.69e-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: 147.28 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFdDEPIVQSKRLEI 89
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKW-DEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 90 YQKYAQQLIDGGHAYYCFCTPEEltkMREEQEKKKLPPRydgRCRNITQN-EVASRLKSNK----SYVLRLKTP---KNQ 161
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEE---FRELRNRGEACHC---RDRSVEENlERWEEMLEGKeeggSVVVRVKTDlkhKNP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 162 TVEfDDVVYGKIKVNSNDIDDQVLLksdgFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCH-- 239
Cdd:TIGR00463 246 AIR-DWVIFRIVKTPHPRTGDKYRV----YPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHwg 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1277777456 240 ------LPNILGANKKKLSKRtGDVS---------VEDFKNKGYLPEALINYIALLG 281
Cdd:TIGR00463 321 rlkiddVRALSTSSARKGILR-GEYSgwddprlptLRAIRRRGIRPEAIRKFMLSIG 376
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
10-281 |
1.18e-35 |
|
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: 132.47 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTD--RTRFVPGATEKIYEMLAWVKLKFDDEpIVQSKRL 87
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDprTKRPDPEAYDMIPEDLEWLGVKWDEV-VIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 88 EIYQKYAQQLIDGGHAYycfctpeeltkmreeqekkkLPPRYDGRCRnitqnevasrlksnksyvlrlktpknqtvefdd 167
Cdd:cd09287 80 ELYYEYARKLIEMGGAY--------------------VHPRTGSKYR--------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 168 vVYgkikvnsndiddqvllksdgfPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPVYCHLpNILGAN 247
Cdd:cd09287 107 -VW---------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHW-GRLKIE 163
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1277777456 248 KKKLSK-----------RTG--DV---SVEDFKNKGYLPEALINYIALLG 281
Cdd:cd09287 164 GGKLSTskirkgiesgeYEGwdDPrlpTLRALRRRGIRPEAIRDFIIEVG 213
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
332-479 |
1.39e-32 |
|
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: 121.14 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 332 KITEMCLPYLVEtygDALQNYSDEYIASVVALEQERLKKLSDITSSTKLFFTNELDYDAKLL---PWKKTPTNAKETLLS 408
Cdd:pfam19269 1 ELAELALPYLEE---AGLDGLDDEYLKKVVPLLKERAETLSELAELADFFFELPLEYDEEAYakkKMKTNKEESLEVLQE 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277777456 409 AQTVLMSVKKWTKEGLEETLTDFIFHNKLTHGEALWPLRVALSGQENSPGPFEIAAVLGKEESLKRVRAAI 479
Cdd:pfam19269 78 LLPRLEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
10-235 |
6.20e-13 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 70.81 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKfDDEPIVQSKRLEI 89
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 90 YQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLpprydgrcRNITQNE-------VASRLKSNKSYVLRlktpknqt 162
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKH--------RNQSPEEalemfkeMCSGKEEGGAWCLR-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 163 vefddvvyGKIKVNSND--IDDQVLLKSD------------GFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYE 228
Cdd:PLN03233 154 --------AKIDMQSDNgtLRDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQK 225
|
....*..
gi 1277777456 229 ALGWQSP 235
Cdd:PLN03233 226 ALGLRRP 232
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
10-104 |
7.72e-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: 68.05 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDT----DRTRFVpgatEKIYEMLAWvkLKFDDEPIV-QS 84
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTnpekEEEEYV----DSIKEDVKW--LGIKPYKVTyAS 74
|
90 100
....*....|....*....|
gi 1277777456 85 KRLEIYQKYAQQLIDGGHAY 104
Cdd:cd00807 75 DYFDQLYEYAEQLIKKGKAY 94
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
10-236 |
1.10e-12 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 69.99 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDRTRFVPGATEKIYEMLAWVKLKFDDEPIVQSKRLEI 89
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 90 YQKYAQQLIDGGHAyYCFCTPeeltkmREEQEKkklpPRYDG---RCRNIT-------QNEVASRLKSNKSYVLRLKTP- 158
Cdd:PTZ00402 132 MYEKAEELIKKGLA-YCDKTP------REEMQK----CRFDGvptKYRDISveetkrlWNEMKKGSAEGQETCLRAKISv 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 159 --KNQTVEfDDVVYgkiKVNSNDIDDQVlLKSDGFPTYHLAVIIDDHEMKITHIMRGEEWLPSTPKHILLYEALGWQSPV 236
Cdd:PTZ00402 201 dnENKAMR-DPVIY---RVNLTPHARQG-TKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPI 275
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
10-156 |
4.35e-11 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 65.13 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTD----RTRFVpgatEKIYEMLAWVKLKFDDEPIVQSK 85
Cdd:PRK14703 31 RVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNpeteDTEYV----EAIKDDVRWLGFDWGEHLYYASD 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277777456 86 RLEIYQKYAQQLIDGGHAYYCFCTPEELTKMREEQEKKKLPPRYdgRCRNITQN-EVASRLKS----NKSYVLRLK 156
Cdd:PRK14703 107 YFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPY--RDRSVEENlDLFRRMRAgefpDGAHVLRAK 180
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
14-121 |
5.52e-11 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 64.62 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 14 RMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDrtrfvPGATEKIY-----EMLAWVKLKfDDEPIVQSKRLE 88
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTN-----PETEEQVYidaimEMVKWMGWK-PDWVTFSSDYFD 128
|
90 100 110
....*....|....*....|....*....|...
gi 1277777456 89 IYQKYAQQLIDGGHAYYCFCTPEELTKMREEQE 121
Cdd:PTZ00437 129 QLHEFAVQLIKDGKAYVDHSTPDELKQQREQRE 161
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
2-121 |
2.64e-09 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 59.77 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 2 KRITHTTIEVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTDrtrfvPGATEK-----IYEMLAWVKLKF 76
Cdd:PLN02859 256 KHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEKKeyidhIEEIVEWMGWEP 330
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1277777456 77 DDEPIVQSKRLEIYQKyAQQLIDGGHAYYCFCTPEELTKMREEQE 121
Cdd:PLN02859 331 FKITYTSDYFQELYEL-AVELIRRGHAYVDHQTPEEIKEYREKKM 374
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
10-140 |
2.27e-08 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 56.66 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDT----DRTRFVpgatEKIYEMLAWVKLKFdDEPIVQSK 85
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTnpskESDEFV----ENILKDIETLGIKY-DAVTYTSD 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1277777456 86 RLEIYQKYAQQLIDGGHAyYCFCTPEELtkMREEqekkklppRYDG---RCRNITQNE 140
Cdd:PLN02907 288 YFPQLMEMAEKLIKEGKA-YVDDTPREQ--MRKE--------RMDGiesKCRNNSVEE 334
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
10-117 |
1.46e-07 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 53.95 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277777456 10 EVRTRMAPSPTGMLHIGGLRTALYNYLFAKQNGGDFLLRIEDTD----RTRFVpgatEKIYEMLAWVKLKFDDEPIVQSK 85
Cdd:PRK05347 29 RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNpekeDQEYV----DSIKEDVRWLGFDWSGELRYASD 104
|
90 100 110
....*....|....*....|....*....|..
gi 1277777456 86 RLEIYQKYAQQLIDGGHAYYCFCTPEELTKMR 117
Cdd:PRK05347 105 YFDQLYEYAVELIKKGKAYVDDLSAEEIREYR 136
|
|
| |
