|
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: 615.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 1 MSTEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDEsidvggef 80
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 81 GPYRQTERLDIYKTYWQDLLDRGLAYRCYCTEEELEREREEQMERGETPRYSGKHRDLTEEQCQAFEAEGRVPSIRFRVP 160
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 161 EDrEYTFDDIVKGQITFNSKESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFG 240
Cdd:COG0008 153 EE-GVVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 241 HMTLIVGEDHKKLSKRNE--SIIQFMEQydklGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDT 318
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGavTVSGLRRR----GYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 319 NKLAYLNNHYIKKADPERIASMAIPHLQAAGLlpndlsaeqQDWAKALVRLYQEQMTSASDIVALSELFFRSHlELDADA 398
Cdd:COG0008 308 VKLVWLNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIER-EDEKAA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 399 AAVLAEEQVPDVLRAFAAKVETSEEFTAPQMAKLIKEVQKETGFKGKQLFMPIRVALTGQTHGRDLNETIYLLGRDKVLD 478
Cdd:COG0008 378 KKRLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFE 457
|
....*..
gi 515997315 479 RLKAQIK 485
Cdd:COG0008 458 RLGYAID 464
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
4-484 |
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: 613.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDEsidvggefGPY 83
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGLAYRCYCTEEELEREREEQMERGETPRYSGKHRDLTEEQCQAFEAEGRVPSIRFRVPEDR 163
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 164 EYTFDDIVKGQITFNSKESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGHMT 243
Cdd:TIGR00464 153 VVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 244 LIVGEDHKKLSKRNEsiIQFMEQYDKLGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDTNKLAY 323
Cdd:TIGR00464 233 MILDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 324 LNNHYIKKADPERIASMAIPHLQAAGLLpnDLSAEQQdwAKALVRLYQEQMTSASDIVALSELFFRSHLELDADAAAVLA 403
Cdd:TIGR00464 311 LNAHYIKELPDEELFELLDPHLKSLVNT--DTLNREQ--LAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 404 EEQVPDVLRAFAAKVETSEEFTAPQMAKLIKEVQKETGFKGKQLFMPIRVALTGQTHGRDLNETIYLLGRDKVLDRLKAQ 483
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKAQ 466
|
.
gi 515997315 484 I 484
Cdd:TIGR00464 467 F 467
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
4-473 |
4.22e-162 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 469.61 E-value: 4.22e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDESIDVGGEFGPY 83
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGLAYRCYCTEEELEREREEQMERGETPRYSGKHRDLTEEQCQAFEAEGRVPSIRFRVPEDR 163
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 164 EYTFDDIVKGQITFNSKESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGHMT 243
Cdd:PLN02627 205 SVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 244 LIVGEDHKKLSKRN--ESIIQFMEQydklGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDTNKL 321
Cdd:PLN02627 285 LILAPDRSKLSKRHgaTSVGQFREM----GYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 322 AYLNNHYIKKADPERIASMAIPHLQAAGLlpndLSAEQQDWAKALVRLYQEQMtsasDIVALSELFFRSHLELDADAAAV 401
Cdd:PLN02627 361 KWMNGQHLRLLPEEELVKLVGERWKSAGI----LKESDGSFVKEAVELLKDGI----ELVTDADKELLNLLSYPLAATLS 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 402 LAEEQ--VPDVLRAFAAKVET---SEEFTAPQMA------KLIKEVQKETGFKGKQLFMPIRVALTGQTHGRDLNETIYL 470
Cdd:PLN02627 433 SPEAKtvVEDNFSEVADALIAaydSGELAAALEEghdgwqKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGESLVL 512
|
...
gi 515997315 471 LGR 473
Cdd:PLN02627 513 LHK 515
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
4-321 |
7.44e-144 |
|
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: 414.79 E-value: 7.44e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDesidvggeFGPY 83
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGLAYRCYCTEEE--LEREREEQMERGETPRYSGKHRDLTEEQCQAFEAEGRVPSIRFRVPE 161
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEEleEEREEQEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 162 DREYTFDDIVKGQITFNSKESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGH 241
Cdd:pfam00749 153 ESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 242 MTLIVGEDHKKLSKRNESIIQFMEQYDKLGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDTNKL 321
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
4-331 |
2.14e-137 |
|
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: 395.42 E-value: 2.14e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDESIDVGGEFGPY 83
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGlayrcycteeelerereeqmergetprysgkhrdlteeqcqafeaegrvpsirfrvpedr 163
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 164 eytfddivkgqitfnskesgdfvivkkDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGHMT 243
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 244 LIVGEDHKKLSKRNESiiQFMEQYDKLGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDTNKLAY 323
Cdd:cd00808 154 LILNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDW 231
|
....*...
gi 515997315 324 LNNHYIKK 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: 615.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 1 MSTEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDEsidvggef 80
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 81 GPYRQTERLDIYKTYWQDLLDRGLAYRCYCTEEELEREREEQMERGETPRYSGKHRDLTEEQCQAFEAEGRVPSIRFRVP 160
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 161 EDrEYTFDDIVKGQITFNSKESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFG 240
Cdd:COG0008 153 EE-GVVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 241 HMTLIVGEDHKKLSKRNE--SIIQFMEQydklGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDT 318
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGavTVSGLRRR----GYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 319 NKLAYLNNHYIKKADPERIASMAIPHLQAAGLlpndlsaeqQDWAKALVRLYQEQMTSASDIVALSELFFRSHlELDADA 398
Cdd:COG0008 308 VKLVWLNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIER-EDEKAA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 399 AAVLAEEQVPDVLRAFAAKVETSEEFTAPQMAKLIKEVQKETGFKGKQLFMPIRVALTGQTHGRDLNETIYLLGRDKVLD 478
Cdd:COG0008 378 KKRLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFE 457
|
....*..
gi 515997315 479 RLKAQIK 485
Cdd:COG0008 458 RLGYAID 464
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
4-484 |
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: 613.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDEsidvggefGPY 83
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGLAYRCYCTEEELEREREEQMERGETPRYSGKHRDLTEEQCQAFEAEGRVPSIRFRVPEDR 163
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 164 EYTFDDIVKGQITFNSKESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGHMT 243
Cdd:TIGR00464 153 VVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 244 LIVGEDHKKLSKRNEsiIQFMEQYDKLGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDTNKLAY 323
Cdd:TIGR00464 233 MILDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 324 LNNHYIKKADPERIASMAIPHLQAAGLLpnDLSAEQQdwAKALVRLYQEQMTSASDIVALSELFFRSHLELDADAAAVLA 403
Cdd:TIGR00464 311 LNAHYIKELPDEELFELLDPHLKSLVNT--DTLNREQ--LAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 404 EEQVPDVLRAFAAKVETSEEFTAPQMAKLIKEVQKETGFKGKQLFMPIRVALTGQTHGRDLNETIYLLGRDKVLDRLKAQ 483
Cdd:TIGR00464 387 KKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKAQ 466
|
.
gi 515997315 484 I 484
Cdd:TIGR00464 467 F 467
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
4-473 |
4.22e-162 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 469.61 E-value: 4.22e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDESIDVGGEFGPY 83
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGLAYRCYCTEEELEREREEQMERGETPRYSGKHRDLTEEQCQAFEAEGRVPSIRFRVPEDR 163
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 164 EYTFDDIVKGQITFNSKESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGHMT 243
Cdd:PLN02627 205 SVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 244 LIVGEDHKKLSKRN--ESIIQFMEQydklGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDTNKL 321
Cdd:PLN02627 285 LILAPDRSKLSKRHgaTSVGQFREM----GYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 322 AYLNNHYIKKADPERIASMAIPHLQAAGLlpndLSAEQQDWAKALVRLYQEQMtsasDIVALSELFFRSHLELDADAAAV 401
Cdd:PLN02627 361 KWMNGQHLRLLPEEELVKLVGERWKSAGI----LKESDGSFVKEAVELLKDGI----ELVTDADKELLNLLSYPLAATLS 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 402 LAEEQ--VPDVLRAFAAKVET---SEEFTAPQMA------KLIKEVQKETGFKGKQLFMPIRVALTGQTHGRDLNETIYL 470
Cdd:PLN02627 433 SPEAKtvVEDNFSEVADALIAaydSGELAAALEEghdgwqKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGESLVL 512
|
...
gi 515997315 471 LGR 473
Cdd:PLN02627 513 LHK 515
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
4-321 |
7.44e-144 |
|
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: 414.79 E-value: 7.44e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDesidvggeFGPY 83
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGLAYRCYCTEEE--LEREREEQMERGETPRYSGKHRDLTEEQCQAFEAEGRVPSIRFRVPE 161
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEEleEEREEQEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 162 DREYTFDDIVKGQITFNSKESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGH 241
Cdd:pfam00749 153 ESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 242 MTLIVGEDHKKLSKRNESIIQFMEQYDKLGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDTNKL 321
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKL 312
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
4-331 |
2.14e-137 |
|
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: 395.42 E-value: 2.14e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDESIDVGGEFGPY 83
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGlayrcycteeelerereeqmergetprysgkhrdlteeqcqafeaegrvpsirfrvpedr 163
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 164 eytfddivkgqitfnskesgdfvivkkDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGHMT 243
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 244 LIVGEDHKKLSKRNESiiQFMEQYDKLGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDTNKLAY 323
Cdd:cd00808 154 LILNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDW 231
|
....*...
gi 515997315 324 LNNHYIKK 331
Cdd:cd00808 232 LNGQYIRE 239
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-316 |
1.73e-83 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 259.78 E-value: 1.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 1 MSTEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDESidvggef 80
Cdd:PRK05710 2 TMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 81 gPYRQTERLDIYKTYWQDLLDRGLAYRCYCTeeELEREREEQMERGETPRYSGKHRDLTeeqcqafEAEGRVPSIRFRVP 160
Cdd:PRK05710 75 -VLYQSQRHDAYRAALDRLRAQGLVYPCFCS--RKEIAAAAPAPPDGGGIYPGTCRDLL-------HGPRNPPAWRLRVP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 161 eDREYTFDDIVKGQITFN-SKESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRF 239
Cdd:PRK05710 145 -DAVIAFDDRLQGRQHQDlALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRY 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515997315 240 GHMTLIVGEDHKKLSKRNESiiQFMEQYDKLGYLPEAifnfIALLGWSPEGE--EEIYDREQLISIFDPNRLSKSPAVF 316
Cdd:PRK05710 224 LHLPLVLNADGQKLSKQNGA--PALDAAGPLPVLAAA----LRFLGQPPPAAdaSVEELLAQAVAHWDLTRLPRQAEIN 296
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
5-331 |
5.56e-78 |
|
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: 243.15 E-value: 5.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 5 VRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDEsidvggefGPYR 84
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDE--------GPYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 85 QTERLDIYKTYWQDLLDRGlayrcycteeelerereeqmergetprysgkhrdlteeqcqafeaegrvpsirfrvpedre 164
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 165 ytfddivkgqitfnskesgdfvivkkdGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGHMTL 244
Cdd:cd00418 93 ---------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPR 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 245 IVGEDHKKLSKRneSIIQFMEQYDKLGYLPEAIFNFIALLGWSPEGEEEIYDREQLISIFDPNRLSKSPAVFDTNKLAYL 324
Cdd:cd00418 146 LLLEDGTKLSKR--KLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWL 223
|
....*..
gi 515997315 325 NNHYIKK 331
Cdd:cd00418 224 NREYIRE 230
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
5-257 |
3.29e-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: 234.74 E-value: 3.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 5 VRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDESidvggefgPYR 84
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGE--------VVY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 85 QTERLDIYktywQDLLDR----GLAYRCYCTEEELEREREEqmergeTPRYSGKHRDLTEEqcqafeAEGRVPSIRFRVP 160
Cdd:TIGR03838 73 QSQRHALY----QAALDRllaaGLAYPCQCTRKEIAAARDG------GGIYPGTCRNGLPG------RPGRPAAWRLRVP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 161 eDREYTFDDIVKGQITFNSK-ESGDFVIVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRF 239
Cdd:TIGR03838 137 -DGVIAFDDRLQGPQQQDLAaAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRY 215
|
250
....*....|....*...
gi 515997315 240 GHMTLIVGEDHKKLSKRN 257
Cdd:TIGR03838 216 LHLPLVVNADGEKLSKQN 233
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
4-285 |
5.68e-47 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 171.19 E-value: 5.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTD--VKRNIEGGEESQLKYLKWLGMDWDESidvggefg 81
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWDEV-------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 82 pYRQTERLDIYKTYWQDLLDRGLAYRCYCTEEELEREreeqmergetpRYSGK---HRDLT-EEQCQAFEA-------EG 150
Cdd:PRK04156 173 -VIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKEL-----------RDAGKpcpHRDKSpEENLELWEKmldgeykEG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 151 ----RV--------PSIR----FRV---PEDREytfddivkgqitfnskesGDFVIVkkdgIPTYNFAVAVDDYLMKISH 211
Cdd:PRK04156 241 eavvRVktdlehpnPSVRdwvaFRIvktPHPRV------------------GDKYRV----WPTYNFAVAVDDHLLGVTH 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 212 VLRGEDHVSNTPRQLMIFEALGWEPPR---FGHMTLivgeDHKKLSKrnESIIQFMEQ-----YD-----------KLGY 272
Cdd:PRK04156 299 VLRGKDHIDNTEKQRYIYDYFGWEYPEtihYGRLKI----EGFVLST--SKIRKGIEEgeysgWDdprlptlralrRRGI 372
|
330
....*....|...
gi 515997315 273 LPEAIFNFIALLG 285
Cdd:PRK04156 373 LPEAIRELIIEVG 385
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
4-285 |
6.89e-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: 148.43 E-value: 6.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDESIdvggefgpy 83
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVV--------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGLAYRCYCTEEELEREreeqmergetpRYSG---KHRDLT-EEQCQAFEaegrvpsirfRV 159
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFREL-----------RNRGeacHCRDRSvEENLERWE----------EM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 160 PEDREYTFDDIVKGQITFNSKESG--DFVIVK-------KDG-----IPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQ 225
Cdd:TIGR00463 223 LEGKEEGGSVVVRVKTDLKHKNPAirDWVIFRivktphpRTGdkyrvYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQ 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515997315 226 LMIFEALGWEPPRFGHMTLIVGEDHKKLSkrNESIIQFMEQYD----------------KLGYLPEAIFNFIALLG 285
Cdd:TIGR00463 303 EYIYRYFGWEPPEFIHWGRLKIDDVRALS--TSSARKGILRGEysgwddprlptlrairRRGIRPEAIRKFMLSIG 376
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
4-288 |
8.54e-39 |
|
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: 140.95 E-value: 8.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTD--VKRNIEGGEESQLKYLKWLGMDWDESidvggefg 81
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDprTKRPDPEAYDMIPEDLEWLGVKWDEV-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 82 pYRQTERLDIYKTYWQDLLDRGLAYrcycteeelerereeqmergeTPRYSGKhrdlteeqcqafeaegrvpsiRFRVpe 161
Cdd:cd09287 73 -VIASDRIELYYEYARKLIEMGGAY---------------------VHPRTGS---------------------KYRV-- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 162 dreytfddivkgqitfnskesgdfvivkkdgIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPRFGH 241
Cdd:cd09287 108 -------------------------------WPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIH 156
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 242 MTLIVGEDHK-KLSKRNESIIQ-FMEQYD-----------KLGYLPEAIFNFIALLGWSP 288
Cdd:cd09287 157 WGRLKIEGGKlSTSKIRKGIESgEYEGWDdprlptlralrRRGIRPEAIRDFIIEVGVKQ 216
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
336-484 |
6.28e-29 |
|
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: 111.13 E-value: 6.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 336 RIASMAIPHLQAAGLLPNDlsaeqQDWAKALVRLYQEQMTSASDIVALSELFFRSHLE----LDADAAAVLAEEQVPDVL 411
Cdd:pfam19269 1 ELAELALPYLEEAGLDGLD-----DEYLKKVVPLLKERAETLSELAELADFFFELPLEydeeAYAKKKMKTNKEESLEVL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515997315 412 RAFAAKVETSEEFTAPQMAKLIKEVQKETGFKGKQLFMPIRVALTGQTHGRDLNETIYLLGRDKVLDRLKAQI 484
Cdd:pfam19269 76 QELLPRLEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
4-237 |
2.83e-14 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 75.38 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDesidvggeFGPY 83
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD--------VGPT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQTERLDIYKTYWQDLLDRGLAYrCYCTEEELEREReeqmergetpRYSG---KHRDLTEEQCQAF-------EAEGRVP 153
Cdd:PTZ00402 124 YSSDYMDLMYEKAEELIKKGLAY-CDKTPREEMQKC----------RFDGvptKYRDISVEETKRLwnemkkgSAEGQET 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 154 SIRFRVPEDRE-YTFDD--IVKGQITFNSKESgdfviVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFE 230
Cdd:PTZ00402 193 CLRAKISVDNEnKAMRDpvIYRVNLTPHARQG-----TKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCD 267
|
....*..
gi 515997315 231 ALGWEPP 237
Cdd:PTZ00402 268 ALGIRKP 274
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
4-256 |
2.93e-13 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 71.96 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDESIDVGGEFGPY 83
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 84 RQterldiyktYWQDLLDRGLAYrcycteeeLEREREEQMERGETPRYSGKHRDLT-EEQCQAFE------AEGRVPSIR 156
Cdd:PLN03233 91 RC---------YAIILIEEGLAY--------MDDTPQEEMKKERADRAESKHRNQSpEEALEMFKemcsgkEEGGAWCLR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 157 FRV--PEDREYTFDDIVKGQITFNSKESGdfviVKKDGIPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGW 234
Cdd:PLN03233 154 AKIdmQSDNGTLRDPVLFRQNTTPHHRSG----TAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGL 229
|
250 260
....*....|....*....|....*
gi 515997315 235 EPPR---FGHMTLIvgedHKKLSKR 256
Cdd:PLN03233 230 RRPRihaFARMNFM----NTVLSKR 250
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
4-287 |
1.14e-11 |
|
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: 64.58 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTD-VKRNIEGgEESQLKYLKWLGMDWDESidvggefgp 82
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNpEKEEEEY-VDSIKEDVKWLGIKPYKV--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 83 YRQTERLDIYKTYWQDLLDRGLAYrcycteeelerereeqmergETPRYSGKHRdlteeqcqafeaegrvpsirfrvped 162
Cdd:cd00807 71 TYASDYFDQLYEYAEQLIKKGKAY--------------------VHHRTGDKWC-------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 163 rEYtfddivkgqitfnskesgdfvivkkdgiPTYNFAVAVDDYLMKISHVLRGEDHVSNTPRQLMIFEALGWEPPR---F 239
Cdd:cd00807 105 -IY----------------------------PTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHqweF 155
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515997315 240 G--HMTLIVgedhkkLSKRneSIIQFMEQ----------------YDKLGYLPEAIFNFIALLGWS 287
Cdd:cd00807 156 SrlNLTYTV------MSKR--KLLQLVDEgyvdgwddprlptlrgLRRRGVTPEAIRQFILRQGVS 213
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
4-72 |
4.51e-11 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 65.13 E-value: 4.51e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRniEGGE--ESQLKYLKWLGMDWDE 72
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSK--ESDEfvENILKDIETLGIKYDA 281
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
4-106 |
2.45e-08 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 56.65 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 4 EVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGMDWDESIdvggefgpY 83
Cdd:PRK14703 31 RVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHL--------Y 102
|
90 100
....*....|....*....|...
gi 515997315 84 RQTERLDIYKTYWQDLLDRGLAY 106
Cdd:PRK14703 103 YASDYFERMYAYAEQLIKMGLAY 125
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
3-74 |
4.68e-06 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 48.95 E-value: 4.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515997315 3 TEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTD-VKRNIEGgEESQLKYLKWLGMDWDESI 74
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNpEKEDQEY-VDSIKEDVRWLGFDWSGEL 99
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
5-111 |
1.09e-05 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 48.22 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997315 5 VRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTdvkrNIEGGEESQLKYLK----WLGmdWDesidvggef 80
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDT----NPEAEKKEYIDHIEeiveWMG--WE--------- 329
|
90 100 110
....*....|....*....|....*....|....*...
gi 515997315 81 gPYRQTERLDiyktYWQDLLD-------RGLAYRCYCT 111
Cdd:PLN02859 330 -PFKITYTSD----YFQELYElavelirRGHAYVDHQT 362
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
8-70 |
1.15e-05 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 47.67 E-value: 1.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515997315 8 RYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRIEDTDVKRNIEGGEESQLKYLKWLGM--DW 70
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDW 119
|
|
| |
