|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-485 |
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: 664.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 1 MAKEIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGtdiggpy 80
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEG------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 81 gPYRQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGETPRILEKHRHVTPEQREQYEREGRTPSIHFMVP 160
Cdd:COG0008 74 -PYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 161 DDkQYVVNDLIRGQVTFDSKEMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFG 240
Cdd:COG0008 153 EE-GVVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 241 HLALILNQEGKKMSKRDESIiqFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTK 320
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 321 MNWMNNFYIKRQSVDLITEMCIPHLQKAGFideelseekKAWVRSIVALYQEQMSYCAQIVPLAALFFLEEvvYDEEA-R 399
Cdd:COG0008 310 LVWLNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIER--EDEKAaK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 400 AVLKEPQLPEVLTSFAKHLEAAAEYNADTIKAILKDVQKETGHKGKALFMPVRVAATGQAHGRDLAETLYLLGQQTVLER 479
Cdd:COG0008 379 KRLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFER 458
|
....*.
gi 489487066 480 VKRVLA 485
Cdd:COG0008 459 LGYAID 464
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
4-482 |
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: 621.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGtdiggpygPY 83
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEG--------PY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 84 RQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGETPRILEKHRHVTPEQREQYEREGRTPSIHFMVPDDK 163
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 164 QYVVNDLIRGQVTFDSKEMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGHLA 243
Cdd:TIGR00464 153 VVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 244 LILNQEGKKMSKRDEsiIQFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTKMNW 323
Cdd:TIGR00464 233 MILDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 324 MNNFYIKRQSVDLITEMCIPHLQKAGFIDeELSEEKkawVRSIVALYQEQMSYCAQIVPLAALFFLEEVVYDEEARAVLK 403
Cdd:TIGR00464 311 LNAHYIKELPDEELFELLDPHLKSLVNTD-TLNREQ---LAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489487066 404 EPQLPEVLTSFAKHLEAAAEYNADTIKAILKDVQKETGHKGKALFMPVRVAATGQAHGRDLAETLYLLGQQTVLERVKR 482
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA 465
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
4-473 |
7.31e-170 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 489.25 E-value: 7.31e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGTDIGGPYGPY 83
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 84 RQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGETPRILEKHRHVTPEQREQYEREGRTPSIHFMVPDDK 163
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 164 QYVVNDLIRGQVTFDSKEMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGHLA 243
Cdd:PLN02627 205 SVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 244 LILNQEGKKMSKRDESiiQFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTKMNW 323
Cdd:PLN02627 285 LILAPDRSKLSKRHGA--TSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKW 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 324 MNNFYIKRQSVDLITEMCIPHLQKAGFideeLSEEKKAWVRSIVALYQEQMSYCAQIVP-LAAL--FFLEEVVYDEEARA 400
Cdd:PLN02627 363 MNGQHLRLLPEEELVKLVGERWKSAGI----LKESDGSFVKEAVELLKDGIELVTDADKeLLNLlsYPLAATLSSPEAKT 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489487066 401 VLkEPQLPEVLTSF-AKH----LEAAAEYNADTIKAILKDVQKETGHKGKALFMPVRVAATGQAHGRDLAETLYLLGQ 473
Cdd:PLN02627 439 VV-EDNFSEVADALiAAYdsgeLAAALEEGHDGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGESLVLLHK 515
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
4-323 |
6.39e-147 |
|
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: 422.50 E-value: 6.39e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEegtdiggpYGPY 83
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 84 RQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGE--TPRILEKHRHVTPEQREQYEREGRTPSIHFMVPD 161
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSpsRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 162 DKQYVVNDLIRGQVTFDSKEMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGH 241
Cdd:pfam00749 153 ESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 242 LALILNQEGKKMSKRDESIIQFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTKM 321
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
..
gi 489487066 322 NW 323
Cdd:pfam00749 313 DW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
4-331 |
1.20e-143 |
|
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: 411.21 E-value: 1.20e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGTDIGGPYGPY 83
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 84 RQMDRLDIYRKYIDQLLAEGkayycyatkeeldaereeqiargetprilekhrhvtpeqreqyeregrtpsihfmvpddk 163
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 164 qyvvndlirgqvtfdskemgdfvicrpDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGHLA 243
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 244 LILNQEGKKMSKRDESiiQFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTKMNW 323
Cdd:cd00808 154 LILNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDW 231
|
....*...
gi 489487066 324 MNNFYIKR 331
Cdd:cd00808 232 LNGQYIRE 239
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-485 |
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: 664.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 1 MAKEIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGtdiggpy 80
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEG------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 81 gPYRQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGETPRILEKHRHVTPEQREQYEREGRTPSIHFMVP 160
Cdd:COG0008 74 -PYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 161 DDkQYVVNDLIRGQVTFDSKEMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFG 240
Cdd:COG0008 153 EE-GVVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 241 HLALILNQEGKKMSKRDESIiqFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTK 320
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 321 MNWMNNFYIKRQSVDLITEMCIPHLQKAGFideelseekKAWVRSIVALYQEQMSYCAQIVPLAALFFLEEvvYDEEA-R 399
Cdd:COG0008 310 LVWLNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIER--EDEKAaK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 400 AVLKEPQLPEVLTSFAKHLEAAAEYNADTIKAILKDVQKETGHKGKALFMPVRVAATGQAHGRDLAETLYLLGQQTVLER 479
Cdd:COG0008 379 KRLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFER 458
|
....*.
gi 489487066 480 VKRVLA 485
Cdd:COG0008 459 LGYAID 464
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
4-482 |
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: 621.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGtdiggpygPY 83
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEG--------PY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 84 RQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGETPRILEKHRHVTPEQREQYEREGRTPSIHFMVPDDK 163
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 164 QYVVNDLIRGQVTFDSKEMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGHLA 243
Cdd:TIGR00464 153 VVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 244 LILNQEGKKMSKRDEsiIQFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTKMNW 323
Cdd:TIGR00464 233 MILDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 324 MNNFYIKRQSVDLITEMCIPHLQKAGFIDeELSEEKkawVRSIVALYQEQMSYCAQIVPLAALFFLEEVVYDEEARAVLK 403
Cdd:TIGR00464 311 LNAHYIKELPDEELFELLDPHLKSLVNTD-TLNREQ---LAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489487066 404 EPQLPEVLTSFAKHLEAAAEYNADTIKAILKDVQKETGHKGKALFMPVRVAATGQAHGRDLAETLYLLGQQTVLERVKR 482
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA 465
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
4-473 |
7.31e-170 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 489.25 E-value: 7.31e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGTDIGGPYGPY 83
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 84 RQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGETPRILEKHRHVTPEQREQYEREGRTPSIHFMVPDDK 163
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 164 QYVVNDLIRGQVTFDSKEMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGHLA 243
Cdd:PLN02627 205 SVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 244 LILNQEGKKMSKRDESiiQFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTKMNW 323
Cdd:PLN02627 285 LILAPDRSKLSKRHGA--TSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKW 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 324 MNNFYIKRQSVDLITEMCIPHLQKAGFideeLSEEKKAWVRSIVALYQEQMSYCAQIVP-LAAL--FFLEEVVYDEEARA 400
Cdd:PLN02627 363 MNGQHLRLLPEEELVKLVGERWKSAGI----LKESDGSFVKEAVELLKDGIELVTDADKeLLNLlsYPLAATLSSPEAKT 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489487066 401 VLkEPQLPEVLTSF-AKH----LEAAAEYNADTIKAILKDVQKETGHKGKALFMPVRVAATGQAHGRDLAETLYLLGQ 473
Cdd:PLN02627 439 VV-EDNFSEVADALiAAYdsgeLAAALEEGHDGWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGESLVLLHK 515
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
4-323 |
6.39e-147 |
|
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: 422.50 E-value: 6.39e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEegtdiggpYGPY 83
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 84 RQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGE--TPRILEKHRHVTPEQREQYEREGRTPSIHFMVPD 161
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSpsRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 162 DKQYVVNDLIRGQVTFDSKEMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGH 241
Cdd:pfam00749 153 ESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 242 LALILNQEGKKMSKRDESIIQFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTKM 321
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
..
gi 489487066 322 NW 323
Cdd:pfam00749 313 DW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
4-331 |
1.20e-143 |
|
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: 411.21 E-value: 1.20e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGTDIGGPYGPY 83
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 84 RQMDRLDIYRKYIDQLLAEGkayycyatkeeldaereeqiargetprilekhrhvtpeqreqyeregrtpsihfmvpddk 163
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 164 qyvvndlirgqvtfdskemgdfvicrpDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGHLA 243
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 244 LILNQEGKKMSKRDESiiQFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTKMNW 323
Cdd:cd00808 154 LILNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDW 231
|
....*...
gi 489487066 324 MNNFYIKR 331
Cdd:cd00808 232 LNGQYIRE 239
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
5-330 |
4.36e-82 |
|
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: 253.93 E-value: 4.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 5 IRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGtdiggpygPYR 84
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEG--------PYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 85 QMDRLDIYRKYIDQLLAEGkayycyatkeeldaereeqiargetprilekhrhvtpeqreqyeregrtpsihfmvpddkq 164
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 165 yvvndlirgqvtfdskemgdfvicrpdGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGHLAL 244
Cdd:cd00418 93 ---------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPR 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 245 ILNQEGKKMSKRDesIIQFIEQYRELGFLPDAIVNFLVLLGWSPGGEEEIFSLDELIKLFSEERVSKSPAVFDSTKMNWM 324
Cdd:cd00418 146 LLLEDGTKLSKRK--LNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWL 223
|
....*.
gi 489487066 325 NNFYIK 330
Cdd:cd00418 224 NREYIR 229
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
6-319 |
4.10e-78 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 245.92 E-value: 4.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 6 RTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEegtdigGPygPYRQ 85
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWD------GP--VLYQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 86 MDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGET-PRIlekHRHVTPEQREQyeregrtPSIHFMVPDDkQ 164
Cdd:PRK05710 79 SQRHDAYRAALDRLRAQGLVYPCFCSRKEIAAAAPAPPDGGGIyPGT---CRDLLHGPRNP-------PAWRLRVPDA-V 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 165 YVVNDLIRGQVTFD-SKEMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGHLA 243
Cdd:PRK05710 148 IAFDDRLQGRQHQDlALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLP 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489487066 244 LILNQEGKKMSKRDESiiQFIeqyRELGFLPdAIVNFLVLLGWSPGGEEEIFSLDE--LIKLFSEERVSKSPAVFDST 319
Cdd:PRK05710 228 LVLNADGQKLSKQNGA--PAL---DAAGPLP-VLAAALRFLGQPPPAADASVEELLaqAVAHWDLTRLPRQAEINPAF 299
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-257 |
1.11e-72 |
|
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: 230.89 E-value: 1.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 6 RTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEgtdiggpyGPYRQ 85
Cdd:TIGR03838 2 RGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDG--------EVVYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 86 MDRLDIYRKYIDQLLAEGKAYYCYATKEELDAereeqiARGETPRILEKHRHVTPeqreqyEREGRTPSIHFMVPDDkQY 165
Cdd:TIGR03838 74 SQRHALYQAALDRLLAAGLAYPCQCTRKEIAA------ARDGGGIYPGTCRNGLP------GRPGRPAAWRLRVPDG-VI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 166 VVNDLIRGQVTFDSK-EMGDFVICRPDGIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGHLAL 244
Cdd:TIGR03838 141 AFDDRLQGPQQQDLAaAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPL 220
|
250
....*....|...
gi 489487066 245 ILNQEGKKMSKRD 257
Cdd:TIGR03838 221 VVNADGEKLSKQN 233
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
4-285 |
3.76e-48 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 174.27 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTD-QTRNVE-NADEEQMKNLKWLGITWEEgtdiggpyg 81
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDpRTKRPDpEAYDMILEDLKWLGVKWDE--------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 82 PYRQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIArgetprilEKHRHVTPE-QREQYER--EGrtpsiHFm 158
Cdd:PRK04156 172 VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKP--------CPHRDKSPEeNLELWEKmlDG-----EY- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 159 vpDDKQYVV---NDL------IRgqvtfdskemgDFVICRpdgI---------------PTYNFAVVIDDYLMKISHVFR 214
Cdd:PRK04156 238 --KEGEAVVrvkTDLehpnpsVR-----------DWVAFR---IvktphprvgdkyrvwPTYNFAVAVDDHLLGVTHVLR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 215 GEEHLSNTPRQLMIYEAFGWEPP---QFGHLALilnqEGKKMSKrdESIIQFIEQY----------------RELGFLPD 275
Cdd:PRK04156 302 GKDHIDNTEKQRYIYDYFGWEYPetiHYGRLKI----EGFVLST--SKIRKGIEEGeysgwddprlptlralRRRGILPE 375
|
330
....*....|
gi 489487066 276 AIVNFLVLLG 285
Cdd:PRK04156 376 AIRELIIEVG 385
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
4-288 |
2.65e-42 |
|
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: 150.58 E-value: 2.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQM--KNLKWLGITWEEgtdiggpyg 81
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEAYDMipEDLEWLGVKWDE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 82 PYRQMDRLDIYRKYIDQLLAEGKAYycyatkeeldaereeqiargetprilekhrhvtpeqreqyeregrtpsIHFMVPD 161
Cdd:cd09287 72 VVIASDRIELYYEYARKLIEMGGAY------------------------------------------------VHPRTGS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 162 dkQYVVndlirgqvtfdskemgdfvicrpdgIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPPQFGH 241
Cdd:cd09287 104 --KYRV-------------------------WPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIH 156
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489487066 242 LAlILNQEGKKMSK--------------RDESIIQFIEQYRELGFLPDAIVNFLVLLGWSP 288
Cdd:cd09287 157 WG-RLKIEGGKLSTskirkgiesgeyegWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQ 216
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
4-285 |
6.25e-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: 145.74 E-value: 6.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEEGTdiggpygpy 83
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVV--------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 84 RQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIARGETPRILEKHRHVTPEQREQYEREGrtpSIHFMVPDDK 163
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGG---SVVVRVKTDL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 164 QYvVNDLIRGQVTFDSKE-----MGD-FVIcrpdgIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAFGWEPP 237
Cdd:TIGR00463 241 KH-KNPAIRDWVIFRIVKtphprTGDkYRV-----YPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPP 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489487066 238 QFGHLALILNQEGKKMSKRdeSIIQFIEQ----------------YRELGFLPDAIVNFLVLLG 285
Cdd:TIGR00463 315 EFIHWGRLKIDDVRALSTS--SARKGILRgeysgwddprlptlraIRRRGIRPEAIRKFMLSIG 376
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
337-484 |
2.59e-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: 120.37 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 337 ITEMCIPHLQKAGFideelSEEKKAWVRSIVALYQEQMSYCAQIVPLAALFFLEEVVYDEEARA----VLKEPQLPEVLT 412
Cdd:pfam19269 2 LAELALPYLEEAGL-----DGLDDEYLKKVVPLLKERAETLSELAELADFFFELPLEYDEEAYAkkkmKTNKEESLEVLQ 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489487066 413 SFAKHLEAAAEYNADTIKAILKDVQKETGHKGKALFMPVRVAATGQAHGRDLAETLYLLGQQTVLERVKRVL 484
Cdd:pfam19269 77 ELLPRLEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
1-272 |
8.59e-17 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 82.75 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 1 MAKEIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITweegtdiggPY 80
Cdd:PLN03233 8 IAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK---------PD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 81 GPYRQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEqiargetpRILEKHRHVTPEQREQYEREGRTPSihfmvP 160
Cdd:PLN03233 79 SVSFTSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERAD--------RAESKHRNQSPEEALEMFKEMCSGK-----E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 161 DDKQYVVNDLIrgQVTFDSKEMGDFVICRPD------------GIPTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMI 228
Cdd:PLN03233 146 EGGAWCLRAKI--DMQSDNGTLRDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWI 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489487066 229 YEAFGWEPPQFGHLALIlNQEGKKMSKRdeSIIQFIEQYRELGF 272
Cdd:PLN03233 224 QKALGLRRPRIHAFARM-NFMNTVLSKR--KLTWFVDNGHVTGW 264
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
7-335 |
1.02e-16 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 82.70 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 7 TRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRNVENADEEQMKNLKWLGITWEegtdiggpYGPYRQM 86
Cdd:PTZ00402 55 TRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD--------VGPTYSS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 87 DRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEQIArgetprilEKHRHVTPEQREQYEREGRTPSihfmvpDDKQYV 166
Cdd:PTZ00402 127 DYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVP--------TKYRDISVEETKRLWNEMKKGS------AEGQET 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 167 VndlIRGQVTFD--SKEMGDFVICRPDGI------------PTYNFAVVIDDYLMKISHVFRGEEHLSNTPRQLMIYEAF 232
Cdd:PTZ00402 193 C---LRAKISVDneNKAMRDPVIYRVNLTpharqgtkykayPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 233 GWEPPQFGHLALiLNQEGKKMSKRdeSIIQFIEQYRELGF----LPdaIVNFLVLLGwspggeeeiFSLDELIKLFSEER 308
Cdd:PTZ00402 270 GIRKPIVEDFSR-LNMEYSVMSKR--KLTQLVDTHVVDGWddprFP--TVRALVRRG---------LKMEALRQFVQEQG 335
|
330 340
....*....|....*....|....*..
gi 489487066 309 VSKSPAVfdstkMNWMNNFYIKRQSVD 335
Cdd:PTZ00402 336 MSKTVNF-----MEWSKLWYFNTQILD 357
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
4-106 |
1.59e-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: 75.75 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTdqtrNVENADEEQ----MKNLKWLGITWeegtdiggp 79
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDT----NPEKEEEEYvdsiKEDVKWLGIKP--------- 67
|
90 100
....*....|....*....|....*..
gi 489487066 80 YGPYRQMDRLDIYRKYIDQLLAEGKAY 106
Cdd:cd00807 68 YKVTYASDYFDQLYEYAEQLIKKGKAY 94
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
3-285 |
3.24e-12 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 68.98 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 3 KEIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTdqtrNVENADEEQMKNLK----WLGITWEEGTdigg 78
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDT----NPETEDTEYVEAIKddvrWLGFDWGEHL---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 79 pygpYRQMDRLDIYRKYIDQLLAEGKAYycyatkeeLDAEREEQIA--RG--ETPRILEKHRHVTPEQR-EQYER--EGR 151
Cdd:PRK14703 102 ----YYASDYFERMYAYAEQLIKMGLAY--------VDSVSEEEIRelRGtvTEPGTPSPYRDRSVEENlDLFRRmrAGE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 152 TPsihfmvpdDKQYVvndlIRGQVTFDSKEMG--DFVICRpdgI---------------PTYNFAVVIDDYLMKISHVFR 214
Cdd:PRK14703 170 FP--------DGAHV----LRAKIDMSSPNMKlrDPLLYR---IrhahhyrtgdewciyPMYDFAHPLEDAIEGVTHSIC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 215 GEEHLSNTPRQLMIYEAFGWEPP-----QFGHLALilnqEGKKMSKR--------------DESIIQFIEQYRELGFLPD 275
Cdd:PRK14703 235 TLEFENNRAIYDWVLDHLGPWPPrprqyEFARLAL----GYTVMSKRklrelveegyvsgwDDPRMPTIAGQRRRGVTPE 310
|
330
....*....|
gi 489487066 276 AIVNFLVLLG 285
Cdd:PRK14703 311 AIRDFADQIG 320
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
4-129 |
3.41e-12 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 68.98 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 4 EIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTDQTRN----VENAdeeqMKNLKWLGITWEEGTdiggp 79
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKEsdefVENI----LKDIETLGIKYDAVT----- 283
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489487066 80 ygpYRQmDRLDIYRKYIDQLLAEGKAYYCYATKEELDAER---EEQIARGETP 129
Cdd:PLN02907 284 ---YTS-DYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERmdgIESKCRNNSV 332
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
8-285 |
1.00e-10 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 63.85 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 8 RYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTdqtrNVENadEEQ------MKNLKWLGitWEegtdiggPYG 81
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDT----NPET--EEQvyidaiMEMVKWMG--WK-------PDW 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 82 PYRQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAEREEqiaRGETPRileKHRHVTPEQRE-QYEREGRtpsihfmvp 160
Cdd:PTZ00437 120 VTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQ---REDSPW---RNRSVEENLLLfEHMRQGR--------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 161 ddkqYVVNDL---IRGQVTFDSKEMGDFVICRPDGI------------PTYNFAVVIDDYLMKISHVF-------RGEEH 218
Cdd:PTZ00437 185 ----YAEGEAtlrVKADMKSDNPNMRDFIAYRVKYVehphakdkwciyPSYDFTHCLIDSLEDIDYSLctlefetRRESY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 219 LSnTPRQLMIYEAFGWEPPQfghlaliLNQEGKKMSKR--------------DESIIQFIEQYRELGFLPDAIVNFLVLL 284
Cdd:PTZ00437 261 FW-LLEELNLWRPHVWEFSR-------LNVTGSLLSKRkinvlvrkgivrgfDDPRLLTLAGMRRRGYTPAAINRFCELV 332
|
.
gi 489487066 285 G 285
Cdd:PTZ00437 333 G 333
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
7-211 |
2.09e-08 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 56.69 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 7 TRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTdqtrNVENADEEQMKNLK----WLGitWEegtdiggpygP 82
Cdd:PLN02859 267 TRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDT----NPEAEKKEYIDHIEeiveWMG--WE----------P 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 83 YRQMDRLDIYRKYID---QLLAEGKAYYCYATKEELDAEREEQIargETP---RILEKHRHVTPEQREQYEREGRTPSIH 156
Cdd:PLN02859 331 FKITYTSDYFQELYElavELIRRGHAYVDHQTPEEIKEYREKKM---NSPwrdRPIEESLKLFEDMRRGLIEEGKATLRM 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489487066 157 FMVPDDKQYVVNDLIRGQVTFDSKEMGDFVICRpdgIPTYNFAVVIDDYLMKISH 211
Cdd:PLN02859 408 KQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCI---YPSYDYAHCIVDSLENITH 459
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
3-119 |
2.54e-07 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 53.18 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489487066 3 KEIRTRYAPSPTGHLHIGGARTALFNYLFAKHHGGSFIVRIEDTdqtrNVENADEE----QMKNLKWLGITWEEgtdigg 78
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDT----NPEKEDQEyvdsIKEDVRWLGFDWSG------ 97
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489487066 79 pyGPYRQMDRLDIYRKYIDQLLAEGKAYYCYATKEELDAER 119
Cdd:PRK05347 98 --ELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYR 136
|
|
| |
