|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
19-500 |
1.94e-177 |
|
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: 507.02 E-value: 1.94e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 19 SQVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPgfggqlgp 98
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 99 YVQSQRTEIYSKAIEELLHNGTAYRCFCTERRLDLLRKEALRTRQVPRYDNKCRHLTTSEVDSLLAKGTPYCIRFKLTDH 178
Cdd:COG0008 75 YYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 179 EEPLDDLIYGKVHHNvSDNEGDPVVMKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGHL 258
Cdd:COG0008 155 GVVFDDLVRGEITFP-NPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 259 PLLVNADGTKLSKRQGDIGIQHFRERGYFPQALVNYVVSAGGGfeHRTNakQQLLSMQALHEQFHIERVNSHPSRLNPEL 338
Cdd:COG0008 234 PLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWS--KSDD--QEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 339 LDDLNRLEIVQRlsgnesrtklvnEVQQLVKEAYPQHSNLDLaEEHILDVLNWSSKRLTLLQDLTsSKLSFLWVKPSD-- 416
Cdd:COG0008 310 LVWLNGPYIRAL------------DDEELAELLAPELPEAGI-REDLERLVPLVRERAKTLSELA-ELARFFFIEREDek 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 417 FQIKDLTAEQ----LAHLLQLINAIQDFHKDELNVKLKSFAQKENIKFPLMMKTLRAALSGLKEGPGVAEMMEILGKSVT 492
Cdd:COG0008 376 AAKKRLAPEEvrkvLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERV 455
|
....*...
gi 24665321 493 LERLKEAL 500
Cdd:COG0008 456 FERLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
21-498 |
2.31e-152 |
|
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: 443.33 E-value: 2.31e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 21 VRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPgfggqlgpYV 100
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGP--------YY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 101 QSQRTEIYSKAIEELLHNGTAYRCFCTERRLDLLRKEALRTRQVPRYDNKCRHLTTSEVDSLLAKGTPYCIRFKLTDHEE 180
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 181 P-LDDLIYGKVHHNVSDNeGDPVVMKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGHLP 259
Cdd:TIGR00464 154 VsFNDQVRGEITFQNSEL-DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 260 LLVNADGTKLSKRQGDIGIQHFRERGYFPQALVNYVVSAGGGFEHrtnaKQQLLSMQALHEQFHIERVNSHPSRLNPELL 339
Cdd:TIGR00464 233 MILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPD----DQEFFSLEELIEIFSLNRVSKSPAKFDWKKL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 340 DDLNRlEIVQRLSGNESRTKLVNEVQQLVKEAYPQHSNLDLaeehILDVLNWSSKRLTLLQDLTssklSFLWVKPSDFQ- 418
Cdd:TIGR00464 309 QWLNA-HYIKELPDEELFELLDPHLKSLVNTDTLNREQLAE----LLLLFKERLKTLKEIAELI----RLFFEDKKEVDe 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 419 ------IKDLTAEQLAHLLQLINAIQDFHKDELNVKLKSFAQKENIKFPLMMKTLRAALSGLKEGPGVAEMMEILGKSVT 492
Cdd:TIGR00464 380 dafkkhLKKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTES 459
|
....*.
gi 24665321 493 LERLKE 498
Cdd:TIGR00464 460 IKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
21-349 |
7.86e-129 |
|
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: 374.62 E-value: 7.86e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 21 VRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPGFGGQLGPYV 100
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 101 QSQRTEIYSKAIEELLHNGtayrcfcterrldllrkealrtrqvprydnkcrhlttsevdsllakgtpycirfkltdhee 180
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 181 plddliygkvhhnvsdnegdpvvmksDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGHLPL 260
Cdd:cd00808 101 --------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 261 LVNADGTKLSKRQGDIGIQHFRERGYFPQALVNYVVSAGGGFEHrtnaKQQLLSMQALHEQFHIERVNSHPSRLNPELLD 340
Cdd:cd00808 155 ILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPD----GEEFFTLEELIELFDLERVSKSPAIFDPEKLD 230
|
....*....
gi 24665321 341 DLNRLEIVQ 349
Cdd:cd00808 231 WLNGQYIRE 239
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
19-489 |
3.85e-114 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 347.88 E-value: 3.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 19 SQVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPGFGGQLGP 98
Cdd:PLN02627 44 GPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 99 YVQSQRTEIYSKAIEELLHNGTAYRCFCTERRLDLLRKEALRTRQVPRYDNKCRHLTTSEVDSLLAKGTPYCIRFKLTDH 178
Cdd:PLN02627 124 YRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 179 EE-PLDDLIYGKVHHNvSDNEGDPVVMKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGH 257
Cdd:PLN02627 204 GSvKIDDLIRGEVSWN-TDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 258 LPLLVNADGTKLSKRQGDIGIQHFRERGYFPQALVNYVVSAGGGfehrTNAKQQLLSMQALHEQFHIERVNSHPSRLNPE 337
Cdd:PLN02627 283 VSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN----DGTENEIFTLEELVEKFSIDRINKSGAVFDST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 338 LLDDLNRLEIvqRLSGNESRTKLVNEvqQLVKEAYPQHSNLDLAEEHILDVlnwsSKRLTLLQDL---TSSKLSF-LWVK 413
Cdd:PLN02627 359 KLKWMNGQHL--RLLPEEELVKLVGE--RWKSAGILKESDGSFVKEAVELL----KDGIELVTDAdkeLLNLLSYpLAAT 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 414 PSDFQIKDLTAEQLAHLLQ----------LINAIQDFHkDELNVKLKSFAQKENIKFPLMMKTLRAALSGLKEGPGVAEM 483
Cdd:PLN02627 431 LSSPEAKTVVEDNFSEVADaliaaydsgeLAAALEEGH-DGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGES 509
|
....*.
gi 24665321 484 MEILGK 489
Cdd:PLN02627 510 LVLLHK 515
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
20-341 |
9.79e-111 |
|
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: 331.21 E-value: 9.79e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 20 QVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPgfggqlgpY 99
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGP--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 100 VQSQRTEIYSKAIEELLHNGTAYRCFCTERRLDLLRK--EALRTRQVPRYDNKCRHLTTSEVDSLLAKGTPYCIRFKLtD 177
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREeqEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKI-P 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 178 HEEP--LDDLIYGKVhhNVSDNEGDPVVM-KSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPK 254
Cdd:pfam00749 152 MESPyvFRDPVRGRI--KFTPQEIHDRTGvKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 255 FGHLPLLVNADGTKLSKRQGDI--GIQHFRERGYFPQALVNYVVSAGGGFEhrtnAKQQLLSMQALHEQFHIERVNSHPS 332
Cdd:pfam00749 230 FIHEYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPE----GIREFFTREGVIKSFDVNRLSKSLE 305
|
....*....
gi 24665321 333 RLNPELLDD 341
Cdd:pfam00749 306 AFDRKKLDW 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
19-500 |
1.94e-177 |
|
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: 507.02 E-value: 1.94e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 19 SQVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPgfggqlgp 98
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 99 YVQSQRTEIYSKAIEELLHNGTAYRCFCTERRLDLLRKEALRTRQVPRYDNKCRHLTTSEVDSLLAKGTPYCIRFKLTDH 178
Cdd:COG0008 75 YYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 179 EEPLDDLIYGKVHHNvSDNEGDPVVMKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGHL 258
Cdd:COG0008 155 GVVFDDLVRGEITFP-NPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 259 PLLVNADGTKLSKRQGDIGIQHFRERGYFPQALVNYVVSAGGGfeHRTNakQQLLSMQALHEQFHIERVNSHPSRLNPEL 338
Cdd:COG0008 234 PLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWS--KSDD--QEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 339 LDDLNRLEIVQRlsgnesrtklvnEVQQLVKEAYPQHSNLDLaEEHILDVLNWSSKRLTLLQDLTsSKLSFLWVKPSD-- 416
Cdd:COG0008 310 LVWLNGPYIRAL------------DDEELAELLAPELPEAGI-REDLERLVPLVRERAKTLSELA-ELARFFFIEREDek 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 417 FQIKDLTAEQ----LAHLLQLINAIQDFHKDELNVKLKSFAQKENIKFPLMMKTLRAALSGLKEGPGVAEMMEILGKSVT 492
Cdd:COG0008 376 AAKKRLAPEEvrkvLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERV 455
|
....*...
gi 24665321 493 LERLKEAL 500
Cdd:COG0008 456 FERLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
21-498 |
2.31e-152 |
|
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: 443.33 E-value: 2.31e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 21 VRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPgfggqlgpYV 100
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGP--------YY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 101 QSQRTEIYSKAIEELLHNGTAYRCFCTERRLDLLRKEALRTRQVPRYDNKCRHLTTSEVDSLLAKGTPYCIRFKLTDHEE 180
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 181 P-LDDLIYGKVHHNVSDNeGDPVVMKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGHLP 259
Cdd:TIGR00464 154 VsFNDQVRGEITFQNSEL-DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 260 LLVNADGTKLSKRQGDIGIQHFRERGYFPQALVNYVVSAGGGFEHrtnaKQQLLSMQALHEQFHIERVNSHPSRLNPELL 339
Cdd:TIGR00464 233 MILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPD----DQEFFSLEELIEIFSLNRVSKSPAKFDWKKL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 340 DDLNRlEIVQRLSGNESRTKLVNEVQQLVKEAYPQHSNLDLaeehILDVLNWSSKRLTLLQDLTssklSFLWVKPSDFQ- 418
Cdd:TIGR00464 309 QWLNA-HYIKELPDEELFELLDPHLKSLVNTDTLNREQLAE----LLLLFKERLKTLKEIAELI----RLFFEDKKEVDe 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 419 ------IKDLTAEQLAHLLQLINAIQDFHKDELNVKLKSFAQKENIKFPLMMKTLRAALSGLKEGPGVAEMMEILGKSVT 492
Cdd:TIGR00464 380 dafkkhLKKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTES 459
|
....*.
gi 24665321 493 LERLKE 498
Cdd:TIGR00464 460 IKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
21-349 |
7.86e-129 |
|
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: 374.62 E-value: 7.86e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 21 VRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPGFGGQLGPYV 100
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 101 QSQRTEIYSKAIEELLHNGtayrcfcterrldllrkealrtrqvprydnkcrhlttsevdsllakgtpycirfkltdhee 180
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 181 plddliygkvhhnvsdnegdpvvmksDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGHLPL 260
Cdd:cd00808 101 --------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 261 LVNADGTKLSKRQGDIGIQHFRERGYFPQALVNYVVSAGGGFEHrtnaKQQLLSMQALHEQFHIERVNSHPSRLNPELLD 340
Cdd:cd00808 155 ILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPD----GEEFFTLEELIELFDLERVSKSPAIFDPEKLD 230
|
....*....
gi 24665321 341 DLNRLEIVQ 349
Cdd:cd00808 231 WLNGQYIRE 239
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
19-489 |
3.85e-114 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 347.88 E-value: 3.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 19 SQVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPGFGGQLGP 98
Cdd:PLN02627 44 GPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 99 YVQSQRTEIYSKAIEELLHNGTAYRCFCTERRLDLLRKEALRTRQVPRYDNKCRHLTTSEVDSLLAKGTPYCIRFKLTDH 178
Cdd:PLN02627 124 YRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 179 EE-PLDDLIYGKVHHNvSDNEGDPVVMKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGH 257
Cdd:PLN02627 204 GSvKIDDLIRGEVSWN-TDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 258 LPLLVNADGTKLSKRQGDIGIQHFRERGYFPQALVNYVVSAGGGfehrTNAKQQLLSMQALHEQFHIERVNSHPSRLNPE 337
Cdd:PLN02627 283 VSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN----DGTENEIFTLEELVEKFSIDRINKSGAVFDST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 338 LLDDLNRLEIvqRLSGNESRTKLVNEvqQLVKEAYPQHSNLDLAEEHILDVlnwsSKRLTLLQDL---TSSKLSF-LWVK 413
Cdd:PLN02627 359 KLKWMNGQHL--RLLPEEELVKLVGE--RWKSAGILKESDGSFVKEAVELL----KDGIELVTDAdkeLLNLLSYpLAAT 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 414 PSDFQIKDLTAEQLAHLLQ----------LINAIQDFHkDELNVKLKSFAQKENIKFPLMMKTLRAALSGLKEGPGVAEM 483
Cdd:PLN02627 431 LSSPEAKTVVEDNFSEVADaliaaydsgeLAAALEEGH-DGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGES 509
|
....*.
gi 24665321 484 MEILGK 489
Cdd:PLN02627 510 LVLLHK 515
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
20-341 |
9.79e-111 |
|
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: 331.21 E-value: 9.79e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 20 QVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPgfggqlgpY 99
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGP--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 100 VQSQRTEIYSKAIEELLHNGTAYRCFCTERRLDLLRK--EALRTRQVPRYDNKCRHLTTSEVDSLLAKGTPYCIRFKLtD 177
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREeqEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKI-P 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 178 HEEP--LDDLIYGKVhhNVSDNEGDPVVM-KSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPK 254
Cdd:pfam00749 152 MESPyvFRDPVRGRI--KFTPQEIHDRTGvKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 255 FGHLPLLVNADGTKLSKRQGDI--GIQHFRERGYFPQALVNYVVSAGGGFEhrtnAKQQLLSMQALHEQFHIERVNSHPS 332
Cdd:pfam00749 230 FIHEYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPE----GIREFFTREGVIKSFDVNRLSKSLE 305
|
....*....
gi 24665321 333 RLNPELLDD 341
Cdd:pfam00749 306 AFDRKKLDW 314
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
17-336 |
2.50e-82 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 257.47 E-value: 2.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 17 AHSQVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDeGPgfggql 96
Cdd:PRK05710 2 TMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWD-GP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 97 gPYVQSQRTEIYSKAIEELLHNGTAYRCFCTerRLDLLRKEALRTRQVPRYDNKCRHLttsevdsLLAKGTPYCIRFKLT 176
Cdd:PRK05710 75 -VLYQSQRHDAYRAALDRLRAQGLVYPCFCS--RKEIAAAAPAPPDGGGIYPGTCRDL-------LHGPRNPPAWRLRVP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 177 DHEEPLDDLIYGKVHHNVSDNEGDPVVMKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFG 256
Cdd:PRK05710 145 DAVIAFDDRLQGRQHQDLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 257 HLPLLVNADGTKLSKRQGDIGIqhfRERGyfPQALVNYVVSAGGGFEHRTNAKQQLLSMQALhEQFHIERVNSHPSRLNP 336
Cdd:PRK05710 225 HLPLVLNADGQKLSKQNGAPAL---DAAG--PLPVLAAALRFLGQPPPAADASVEELLAQAV-AHWDLTRLPRQAEINPA 298
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
21-274 |
3.99e-74 |
|
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: 235.51 E-value: 3.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 21 VRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEgpgfggqlGPYV 100
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDG--------EVVY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 101 QSQRTEIYSKAIEELLHNGTAYRCFCTerrldllRKE-ALRTRQVPRYDNKCRHlttsevdSLLAK-GTPYCIRFKLTDH 178
Cdd:TIGR03838 73 QSQRHALYQAALDRLLAAGLAYPCQCT-------RKEiAAARDGGGIYPGTCRN-------GLPGRpGRPAAWRLRVPDG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 179 EEPLDDLIYGKVHHNVSDNEGDPVVMKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGHL 258
Cdd:TIGR03838 139 VIAFDDRLQGPQQQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHL 218
|
250
....*....|....*.
gi 24665321 259 PLLVNADGTKLSKRQG 274
Cdd:TIGR03838 219 PLVVNADGEKLSKQNG 234
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
21-347 |
1.25e-68 |
|
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: 219.65 E-value: 1.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 21 VRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPgfggqlgpYV 100
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGP--------YR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 101 QSQRTEIYSKAIEELLHNGtayrcfcterrldllrkealrtrqvprydnkcrhlttsevdsllakgtpycirfkltdhee 180
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 181 plddlIYgkvhhnvsdnegdpvvmksdqfPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPKFGHLPL 260
Cdd:cd00418 93 -----GY----------------------PLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPR 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 261 LVNADGTKLSKRQGDIGIQHFRERGYFPQALVNYVvsAGGGFEHRTNakQQLLSMQALHEQFHIERVNSHPSRLNPELLD 340
Cdd:cd00418 146 LLLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYL--ALIGWSKPDG--HELFTLEEMIAAFSVERVNSADATFDWAKLE 221
|
....*..
gi 24665321 341 DLNRLEI 347
Cdd:cd00418 222 WLNREYI 228
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
20-299 |
1.06e-47 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 173.88 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 20 QVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTD--QTRLVPGASERLVEDLLWAGIEIDEgpgfggqlg 97
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWDE--------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 98 PYVQSQRTEIYSKAIEELLHNGTAYRCFCTERRLDLLR--KEALrtrqvprydnKCRHLTTSEVDSLLAK---GTpY--- 169
Cdd:PRK04156 172 VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRdaGKPC----------PHRDKSPEENLELWEKmldGE-Ykeg 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 170 --CIRFKlTD--HEEP-LDDLIYGKVHHNVSDNEGDpvvmKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLL 244
Cdd:PRK04156 241 eaVVRVK-TDleHPNPsVRDWVAFRIVKTPHPRVGD----KYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYI 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24665321 245 YKAFGWQPPK---FGHLPLlvnaDGTKLSK---RQG----------DI---GIQHFRERGYFPQALVNYVVSAG 299
Cdd:PRK04156 316 YDYFGWEYPEtihYGRLKI----EGFVLSTskiRKGieegeysgwdDPrlpTLRALRRRGILPEAIRELIIEVG 385
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
20-299 |
2.56e-41 |
|
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: 148.27 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 20 QVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQT--RLVPGASERLVEDLLWAGIEIDEgpgfggqlg 97
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 98 PYVQSQRTEIYSKAIEELLHNGTAYrcfcterrldllrkealrTRqvPRYDNKcrhlttsevdsllakgtpYCIrfkltd 177
Cdd:cd09287 72 VVIASDRIELYYEYARKLIEMGGAY------------------VH--PRTGSK------------------YRV------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 178 heeplddliygkvhhnvsdnegdpvvmksdqFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPK--- 254
Cdd:cd09287 108 -------------------------------WPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPEtih 156
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24665321 255 FGHLPLlvnaDGTKLSK---RQG----------DI---GIQHFRERGYFPQALVNYVVSAG 299
Cdd:cd09287 157 WGRLKI----EGGKLSTskiRKGiesgeyegwdDPrlpTLRALRRRGIRPEAIRDFIIEVG 213
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
20-299 |
3.06e-39 |
|
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: 149.97 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 20 QVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEgpgfggqlgPY 99
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDE---------VV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 100 VQSQRTEIYSKAIEELLHNGTAYRCFCTERRldlLRKeaLRTRQVPrydNKCRHLTTSEVDSLLAK-------GTPYCIR 172
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEE---FRE--LRNRGEA---CHCRDRSVEENLERWEEmlegkeeGGSVVVR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 173 FKlTD--HEEPL--DDLIYGKV---HHNVSDnegdpvvmKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLY 245
Cdd:TIGR00463 236 VK-TDlkHKNPAirDWVIFRIVktpHPRTGD--------KYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIY 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 246 KAFGWQPPKFGHLPLLVNADGTKLSKRQGDIGIQH----------------FRERGYFPQALVNYVVSAG 299
Cdd:TIGR00463 307 RYFGWEPPEFIHWGRLKIDDVRALSTSSARKGILRgeysgwddprlptlraIRRRGIRPEAIRKFMLSIG 376
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
366-500 |
3.26e-21 |
|
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: 89.94 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 366 QLVKEAYPQHSNLDLA---EEHILDVLNWSSKRLTLLQDLTSsKLSFLWVKPSDFQIKDLT-----------AEQLAHLL 431
Cdd:pfam19269 1 ELAELALPYLEEAGLDgldDEYLKKVVPLLKERAETLSELAE-LADFFFELPLEYDEEAYAkkkmktnkeesLEVLQELL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24665321 432 QLINAIQDFHKDELNVKLKSFAQKENIKFPLMMKTLRAALSGLKEGPGVAEMMEILGKSVTLERLKEAL 500
Cdd:pfam19269 80 PRLEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
20-273 |
1.60e-20 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 94.69 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 20 QVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDegpgfggqlgpy 99
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPD------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 100 vQSQRTEIYSKAIEE----LLHNGTAYrcfcterrLDLLRKEALRTRQVPRYDNKCRHLTTSE-------VDSLLAKGTP 168
Cdd:PLN03233 79 -SVSFTSDYFEPIRCyaiiLIEEGLAY--------MDDTPQEEMKKERADRAESKHRNQSPEEalemfkeMCSGKEEGGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 169 YCIRFKL---TDHEEPLDDLIYgkvHHNVSDNEGDPVVMKSdqFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLY 245
Cdd:PLN03233 150 WCLRAKIdmqSDNGTLRDPVLF---RQNTTPHHRSGTAYKA--YPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQ 224
|
250 260
....*....|....*....|....*...
gi 24665321 246 KAFGWQPPKFgHLPLLVNADGTKLSKRQ 273
Cdd:PLN03233 225 KALGLRRPRI-HAFARMNFMNTVLSKRK 251
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
20-234 |
2.69e-16 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 82.08 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 20 QVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPgfggqlgpY 99
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVT--------Y 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 100 VQSQRTEIYSKAiEELLHNGTAYrcfcterrLDLLRKEALRTRQVPRYDNKCRHLTTSEVDSLLA-------KGTPYCIR 172
Cdd:PLN02907 285 TSDYFPQLMEMA-EKLIKEGKAY--------VDDTPREQMRKERMDGIESKCRNNSVEENLRLWKemiagseRGLQCCVR 355
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24665321 173 FKLtDHEEP---LDDLIYGKV----HHNVSDnegdpvvmKSDQFPTYHFANVVDDHLMGITHVLRGVEW 234
Cdd:PLN02907 356 GKL-DMQDPnksLRDPVYYRCnptpHHRIGS--------KYKVYPTYDFACPFVDALEGVTHALRSSEY 415
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
20-273 |
4.28e-15 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 78.08 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 20 QVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPGFGGQlgpY 99
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSD---Y 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 100 VQSqrteIYSKAiEELLHNGTAYrCFCTERRldllRKEALRTRQVPrydNKCRHLTTSEVDSLL-------AKGTPYCIR 172
Cdd:PTZ00402 129 MDL----MYEKA-EELIKKGLAY-CDKTPRE----EMQKCRFDGVP---TKYRDISVEETKRLWnemkkgsAEGQETCLR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 173 FKLT--DHEEPLDDLIYGKVHHNVSDNEGdpvvMKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGW 250
Cdd:PTZ00402 196 AKISvdNENKAMRDPVIYRVNLTPHARQG----TKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGI 271
|
250 260
....*....|....*....|...
gi 24665321 251 QPPKFGHLPLLvNADGTKLSKRQ 273
Cdd:PTZ00402 272 RKPIVEDFSRL-NMEYSVMSKRK 293
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
20-299 |
3.75e-12 |
|
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: 66.12 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 20 QVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEidegpgfggqlgPY 99
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIK------------PY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 100 VQSQRT----EIYSKAiEELLHNGTAYrcfcterrldllrkealrtrqvprydnkcrhlttsevdsllakgtpycirfkl 175
Cdd:cd00807 69 KVTYASdyfdQLYEYA-EQLIKKGKAY----------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 176 tdheeplddliygkVHHNVSDnegdpvvmKSDQFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFGWQPPK- 254
Cdd:cd00807 95 --------------VHHRTGD--------KWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHq 152
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24665321 255 --FGHLpllvNADGTKLSKRQGDIGIQH----------------FRERGYFPQALVNYVVSAG 299
Cdd:cd00807 153 weFSRL----NLTYTVMSKRKLLQLVDEgyvdgwddprlptlrgLRRRGVTPEAIRQFILRQG 211
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
18-294 |
9.29e-11 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 64.36 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 18 HSQVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDQTRLVPGASERLVEDLLWAGIEIDEGPGFGG--- 94
Cdd:PRK14703 29 YPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASdyf 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 95 -----------QLG-PYVQSQRTEiyskAIEELlhNGTA--------YRCFCTERRLDLLRKeaLRTRQVPryDNKcrHL 154
Cdd:PRK14703 109 ermyayaeqliKMGlAYVDSVSEE----EIREL--RGTVtepgtpspYRDRSVEENLDLFRR--MRAGEFP--DGA--HV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 155 TTSEVDsllaKGTPyciRFKLTDheePLDDLIYGKVHHNVSDnegdpvvmKSDQFPTYHFANVVDDHLMGITHVLRGVEW 234
Cdd:PRK14703 177 LRAKID----MSSP---NMKLRD---PLLYRIRHAHHYRTGD--------EWCIYPMYDFAHPLEDAIEGVTHSICTLEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 235 QISTTKHLLLYKAFGWQPPK-----FGHLPLlvnaDGTKLSKRQ-------GDIG---------IQHFRERGYFPQALVN 293
Cdd:PRK14703 239 ENNRAIYDWVLDHLGPWPPRprqyeFARLAL----GYTVMSKRKlrelveeGYVSgwddprmptIAGQRRRGVTPEAIRD 314
|
.
gi 24665321 294 Y 294
Cdd:PRK14703 315 F 315
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
24-291 |
9.97e-08 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 54.60 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 24 RFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDqtrlvPGASERLVEDllwAGIEIDEGPGFGGQLGPYVQSQ 103
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTN-----PETEEQVYID---AIMEMVKWMGWKPDWVTFSSDY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 104 RTEIYSKAIeELLHNGTAYrcfcterrLDLLRKEALRTRQVPRYDNKCRHLTTSEvdSLL----------AKGTPyCIRF 173
Cdd:PTZ00437 127 FDQLHEFAV-QLIKDGKAY--------VDHSTPDELKQQREQREDSPWRNRSVEE--NLLlfehmrqgryAEGEA-TLRV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 174 KL-TDHEEP-LDDLIYGKVHHNVSDNEGDPVVMksdqFPTYHFANVVDDHLMGITHVLRGVEWQISTTKHLLLYKAFG-W 250
Cdd:PTZ00437 195 KAdMKSDNPnMRDFIAYRVKYVEHPHAKDKWCI----YPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNlW 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 24665321 251 QPP--KFGHLpllvNADGTKLSKRQGDIGIQH----------------FRERGYFPQAL 291
Cdd:PTZ00437 271 RPHvwEFSRL----NVTGSLLSKRKINVLVRKgivrgfddprlltlagMRRRGYTPAAI 325
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
5-273 |
1.90e-06 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 50.53 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 5 NPRMLMQQCLRHAHSQVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDTDqtrlvPGAS--------ERLV 76
Cdd:PLN02859 249 NTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEkkeyidhiEEIV 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 77 EDLLWAGIEIdegpgfggqlgPYVQSQRTEIYSKAIeELLHNGTAYRCFCTERRLDLLRKEAL----RTRQVP---RYDN 149
Cdd:PLN02859 324 EWMGWEPFKI-----------TYTSDYFQELYELAV-ELIRRGHAYVDHQTPEEIKEYREKKMnspwRDRPIEeslKLFE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665321 150 KCRHLTTSEvdsllAKGTpycIRFKLTDHEEPLD--DLIYGKVHHNVSDNEGDpvvmKSDQFPTYHFANVVDDHLMGITH 227
Cdd:PLN02859 392 DMRRGLIEE-----GKAT---LRMKQDMQNDNFNmyDLIAYRIKFTPHPHAGD----KWCIYPSYDYAHCIVDSLENITH 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24665321 228 VLRGVEWQISTTKH------LLLYKAFGWQppkFGHLpllvNADGTKLSKRQ 273
Cdd:PLN02859 460 SLCTLEFETRRASYywlldsLGLYQPYVWE---YSRL----NVTNTVMSKRK 504
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
18-62 |
2.05e-05 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 47.02 E-value: 2.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 24665321 18 HSQVRVRFAPSPTGYLHLGGLRTALYNFLYARHLGGKFLLRIEDT 62
Cdd:PRK05347 27 HTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDT 71
|
|
| |
