|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
108-663 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 612.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 108 HPKIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPV-RVTNASDNF 186
Cdd:PRK05347 27 HTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSgELRYASDYF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 187 DRLYELAKELIRRDGAYVCHCNKAEIKAQRGEAdGERGKARyacPHRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLE 266
Cdd:PRK05347 107 DQLYEYAVELIKKGKAYVDDLSAEEIREYRGTL-TEPGKNS---PYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 267 DPNPQMWDIFAWRILDVDtkgHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDV-YRPMQR 345
Cdd:PRK05347 183 SPNINMRDPVLYRIRHAH---HHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIpPHPRQY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 346 EYGRLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLE 425
Cdd:PRK05347 260 EFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLN 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 426 TTVPRLMVVLEPLKVVISNLPDGYEEMVEVPF-SKDPAFGSHLVPFTKVVYIERSDFREEDSPDYFRLAPGKTVGLMKAP 504
Cdd:PRK05347 340 ENAPRAMAVLDPLKLVITNYPEGQVEELEAPNhPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 505 FpITATTFDKDpETGAVTCVYAHYEkPE--DGSATPTKKAKTYIHWVgeSATHksPVKAEVRAFNSLFKSNDPNAHPDgF 582
Cdd:PRK05347 420 V-IKCEEVVKD-ADGNITEIHCTYD-PDtlSGNPADGRKVKGTIHWV--SAAH--AVPAEVRLYDRLFTVPNPAAGKD-F 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 583 LADINPDSEEIYEnalvdiGFhdVSKSApwpkesgevgGEASPYsTRFQGMRTAYFAVDKDSTADKVVLNRIVTLKDTQG 662
Cdd:PRK05347 492 LDFLNPDSLVIKQ------GF--VEPSL----------ADAKPE-DRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWA 552
|
.
gi 121710810 663 K 663
Cdd:PRK05347 553 K 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
111-660 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 576.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 111 IRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPV-RVTNASDNFDRL 189
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 190 YELAKELIRRDGAYVCHCNKAEIKAQRGEADgERGkarYACPHRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLEDPN 269
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLT-DPG---KNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 270 PQMWDIFAWRILDVDtkgHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVY-RPMQREYG 348
Cdd:TIGR00440 157 PVMRDPVAYRIKFAP---HHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 349 RLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLETTV 428
Cdd:TIGR00440 234 RLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 429 PRLMVVLEPLKVVISNLPDGYeEMVEVPFSKD-PAFGSHLVPFTKVVYIERSDFREEDSPDYFRLAPGKTVgLMKAPFPI 507
Cdd:TIGR00440 314 PRAMAVIDPVEVVIENLSDEY-ELATIPNHPNtPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEV-RLRNAYVI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 508 TATTFDKDpETGAVTCVYAHYE-KPEDGSATPTKKAKTYIHWVgeSATHKSPVkaEVRAFNSLFKSNDPnAHPDGFLADI 586
Cdd:TIGR00440 392 KAERVEKD-AAGKITTIFCTYDnKTLGKEPADGRKVKGVIHWV--SASSKYPT--ETRLYDRLFKVPNP-GAPDDFLSVI 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121710810 587 NPDSeEIYENALVDIGFHDVSKsapwpkesgevggeaspySTRFQGMRTAYFAVD-KDSTADKVVLNRIVTLKDT 660
Cdd:TIGR00440 466 NPES-LVIKQGFMEHSLGDAVA------------------NKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDA 521
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
110-430 |
3.00e-124 |
|
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: 368.12 E-value: 3.00e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPVRVTNASDNFDRL 189
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 190 YELAKELIRRDGAYVchcnkaeikaqrgeadgergkaryacphrsrpieeslqefeamregkykageaalrmkmdledpn 269
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 270 pqmwdifawrildvdtkgHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRPMQREYGR 349
Cdd:cd00807 96 ------------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSR 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 350 LNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLETTVP 429
Cdd:cd00807 158 LNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAP 237
|
.
gi 121710810 430 R 430
Cdd:cd00807 238 R 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
110-425 |
2.29e-116 |
|
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: 350.85 E-value: 2.29e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPV-RVTNASDNFDR 188
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 189 LYELAKELIRRDGAYVCHCNKAEIKAQRGEadgergKARYACPHRSRPIEESLQEF-EAMREGKYKAGEAALRMKMDLED 267
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREE------QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 268 PnPQMWDIFAWRILDVDTKGHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRP-MQRE 346
Cdd:pfam00749 155 P-YVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPpFIHE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 347 YGRLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAI-VQTVKLDQVVRQYLE 425
Cdd:pfam00749 234 YLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
110-503 |
9.38e-88 |
|
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: 282.07 E-value: 9.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYK----PVRvtnASDN 185
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPYY---QSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 186 FDRLYELAKELIRRDGAYVCHCNKAEIKAQRGEAdGERGKA-RYACPHRSRPIEEsLQEFEAmrEGKykagEAALRMKMD 264
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQ-TAPGKPpRYDGRCRDLSPEE-LERMLA--AGE----PPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 265 LED-------------PNPQMWDIfawrILdvdtkghFRTGGqwkmYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYE 331
Cdd:COG0008 153 EEGvvfddlvrgeitfPNPNLRDP----VL-------YRADG----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 332 WLNDKLDVYRPmqrEYGRLNLT----GTVLSKRKiielvkksyvrgwddpRLYTLLAIRRRGIPPGAILSFVNNLGVTKA 407
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLIlgpdGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 408 TAivQTVK-LDQVVRQYLETTVPRLMVVLEPLKVVISNLP--------------------DGYEEMVE--VPFSKDPA-F 463
Cdd:COG0008 279 DD--QEIFsLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPyiralddeelaellapelpeAGIREDLErlVPLVRERAkT 356
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 121710810 464 GSHLVPFTKVVYIERSDfreEDSPDyFRLAPGKTVGLMKA 503
Cdd:COG0008 357 LSELAELARFFFIERED---EKAAK-KRLAPEEVRKVLKA 392
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
108-663 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 612.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 108 HPKIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPV-RVTNASDNF 186
Cdd:PRK05347 27 HTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSgELRYASDYF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 187 DRLYELAKELIRRDGAYVCHCNKAEIKAQRGEAdGERGKARyacPHRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLE 266
Cdd:PRK05347 107 DQLYEYAVELIKKGKAYVDDLSAEEIREYRGTL-TEPGKNS---PYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 267 DPNPQMWDIFAWRILDVDtkgHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDV-YRPMQR 345
Cdd:PRK05347 183 SPNINMRDPVLYRIRHAH---HHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIpPHPRQY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 346 EYGRLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLE 425
Cdd:PRK05347 260 EFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLN 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 426 TTVPRLMVVLEPLKVVISNLPDGYEEMVEVPF-SKDPAFGSHLVPFTKVVYIERSDFREEDSPDYFRLAPGKTVGLMKAP 504
Cdd:PRK05347 340 ENAPRAMAVLDPLKLVITNYPEGQVEELEAPNhPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 505 FpITATTFDKDpETGAVTCVYAHYEkPE--DGSATPTKKAKTYIHWVgeSATHksPVKAEVRAFNSLFKSNDPNAHPDgF 582
Cdd:PRK05347 420 V-IKCEEVVKD-ADGNITEIHCTYD-PDtlSGNPADGRKVKGTIHWV--SAAH--AVPAEVRLYDRLFTVPNPAAGKD-F 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 583 LADINPDSEEIYEnalvdiGFhdVSKSApwpkesgevgGEASPYsTRFQGMRTAYFAVDKDSTADKVVLNRIVTLKDTQG 662
Cdd:PRK05347 492 LDFLNPDSLVIKQ------GF--VEPSL----------ADAKPE-DRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWA 552
|
.
gi 121710810 663 K 663
Cdd:PRK05347 553 K 553
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
101-663 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 580.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 101 ERPLSEQHPKIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPVRVT 180
Cdd:PLN02859 255 EKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKIT 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 181 NASDNFDRLYELAKELIRRDGAYVCHCNKAEIKAQRGEadgergkaRYACPHRSRPIEESLQEFEAMREGKYKAGEAALR 260
Cdd:PLN02859 335 YTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREK--------KMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 261 MKMDLEDPNPQMWDIFAWRILDVDtkgHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVY 340
Cdd:PLN02859 407 MKQDMQNDNFNMYDLIAYRIKFTP---HPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 341 RPMQREYGRLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKA-TAIVQTVKLDQV 419
Cdd:PLN02859 484 QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdNSLIRMDRLEHH 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 420 VRQYLETTVPRLMVVLEPLKVVISNLPDGYEEMVEVP----FSKDPAFGSHLVPFTKVVYIERSDFREEDSPDYFRLAPG 495
Cdd:PLN02859 564 IREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKrwpdAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPG 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 496 KTVgLMKAPFPITATTFDKDPETGAVTCVYAHYEkpedgsatPTK--KAKTYIHWVGESATHKSPVKAEVRAFNSLFKSN 573
Cdd:PLN02859 644 KSV-LLRYAFPIKCTDVVLADDNETVVEIRAEYD--------PEKktKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 574 DPNAHPDgFLADINPDSEEIyenalvdigfhdVSKSAPWPKESGEVGGEaspystRFQGMRTAYFAVDKDSTADKVVLNR 653
Cdd:PLN02859 715 NPAELED-WLEDLNPQSKEV------------ISGAYAVPSLKDAKVGD------RFQFERLGYFAVDKDSTPEKLVFNR 775
|
570
....*....|
gi 121710810 654 IVTLKDTQGK 663
Cdd:PLN02859 776 TVTLKDSYGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
111-660 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 576.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 111 IRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPV-RVTNASDNFDRL 189
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 190 YELAKELIRRDGAYVCHCNKAEIKAQRGEADgERGkarYACPHRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLEDPN 269
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLT-DPG---KNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 270 PQMWDIFAWRILDVDtkgHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVY-RPMQREYG 348
Cdd:TIGR00440 157 PVMRDPVAYRIKFAP---HHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 349 RLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLETTV 428
Cdd:TIGR00440 234 RLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 429 PRLMVVLEPLKVVISNLPDGYeEMVEVPFSKD-PAFGSHLVPFTKVVYIERSDFREEDSPDYFRLAPGKTVgLMKAPFPI 507
Cdd:TIGR00440 314 PRAMAVIDPVEVVIENLSDEY-ELATIPNHPNtPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEV-RLRNAYVI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 508 TATTFDKDpETGAVTCVYAHYE-KPEDGSATPTKKAKTYIHWVgeSATHKSPVkaEVRAFNSLFKSNDPnAHPDGFLADI 586
Cdd:TIGR00440 392 KAERVEKD-AAGKITTIFCTYDnKTLGKEPADGRKVKGVIHWV--SASSKYPT--ETRLYDRLFKVPNP-GAPDDFLSVI 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121710810 587 NPDSeEIYENALVDIGFHDVSKsapwpkesgevggeaspySTRFQGMRTAYFAVD-KDSTADKVVLNRIVTLKDT 660
Cdd:TIGR00440 466 NPES-LVIKQGFMEHSLGDAVA------------------NKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDA 521
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
85-664 |
7.53e-180 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 530.06 E-value: 7.53e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 85 DPEAMFKVGFLADVYQERPLSEQHPKIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRG 164
Cdd:PRK14703 6 RPRMLVSPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 165 IEDIVSWLGYK-PVRVTNASDNFDRLYELAKELIRRDGAYVCHCNKAEIKAQRGEADgERGKARyacPHRSRPIEESLQE 243
Cdd:PRK14703 86 IKDDVRWLGFDwGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVT-EPGTPS---PYRDRSVEENLDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 244 FEAMREGKYKAGEAALRMKMDLEDPNPQMWDIFAWRILDvdtKGHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEF 323
Cdd:PRK14703 162 FRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRH---AHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 324 EMSRQSYEWLNDKLDVY--RPMQREYGRLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNN 401
Cdd:PRK14703 239 ENNRAIYDWVLDHLGPWppRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 402 LGVTKATAIVQTVKLDQVVRQYLETTVPRLMVVLEPLKVVISNLPDGYEEMVEVPF--SKDPAFGSHLVPFTKVVYIERS 479
Cdd:PRK14703 319 IGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYwpHDVPKEGSRKVPFTRELYIERD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 480 DFREEDSPDYFRLAPGKTVGLMKAPFpITATTFDKDpETGAVTCVYAHYEKPEDGSATPTKKAKTYIHWVgeSATHKSPv 559
Cdd:PRK14703 399 DFSEDPPKGFKRLTPGREVRLRGAYI-IRCDEVVRD-ADGAVTELRCTYDPESAKGEDTGRKAAGVIHWV--SAKHALP- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 560 kAEVRAFNSLFKSNDPNAHPDGFLADINPDSEEIYENALvdigfhdvsksapwpkesgEVGGEASPYSTRFQGMRTAYFA 639
Cdd:PRK14703 474 -AEVRLYDRLFKVPQPEAADEDFLEFLNPDSLRVAQGRV-------------------EPAVRDDPADTRYQFERQGYFW 533
|
570 580
....*....|....*....|....*.
gi 121710810 640 VDK-DSTADKVVLNRIVTLKDTQGKT 664
Cdd:PRK14703 534 ADPvDSRPDALVFNRIITLKDTWGAR 559
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
71-664 |
1.43e-150 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 448.28 E-value: 1.43e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 71 AKPAKEAVTDLRSLDPEAMFKVGFLADVYQERP-LSEQHPKIRT-----RFPPEPNGFLHIGHSKAIAVNFGFAKYHGGE 144
Cdd:PTZ00437 6 AGPAAAEVPELETKRDLSLLQTGRPVPGCRNTPeLLEKHEAVTGgkpyfRFPPEPNGFLHIGHAKSMNLNFGSARAHGGK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 145 CILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPVRVTNASDNFDRLYELAKELIRRDGAYVCHCNKAEIKAQRgeadgerg 224
Cdd:PTZ00437 86 CYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQR-------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 225 KARYACPHRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLEDPNPQMWDIFAWRILDVDtkgHFRTGGQWKMYPTYDFA 304
Cdd:PTZ00437 158 EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFIAYRVKYVE---HPHAKDKWCIYPSYDFT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 305 HPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRPMQREYGRLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLA 384
Cdd:PTZ00437 235 HCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 385 IRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLETTVPRLMVVLEPLKVVISNLpDGyEEMVEVP-FSKDPAF 463
Cdd:PTZ00437 315 MRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPIKVVVDNW-KG-EREFECPnHPRKPEL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 464 GSHLVPFTKVVYIERSDFREEDSPD-YFRLAPGKTVGLMKAPFPITATTFDKDpETGAVTCVYAH--YEKpedgsatpTK 540
Cdd:PTZ00437 393 GSRKVMFTDTFYVDRSDFRTEDNNSkFYGLAPGPRVVGLKYSGNVVCKGFEVD-AAGQPSVIHVDidFER--------KD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 541 KAKTYIHWVgeSATHKSPVkaEVRAFNSLFKSNDPNAHPDgFLADINPDSEEIYEnalvdiGFhdvsksapwpkesGEVG 620
Cdd:PTZ00437 464 KPKTNISWV--SATACTPV--EVRLYNALLKDDRAAIDPE-FLKFIDEDSEVVSH------GY-------------AEKG 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 121710810 621 GEASPYSTRFQGMRTAYFAVDKDSTADKVVLNRIVTLKDTQGKT 664
Cdd:PTZ00437 520 IENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEKA 563
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
110-430 |
3.00e-124 |
|
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: 368.12 E-value: 3.00e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPVRVTNASDNFDRL 189
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 190 YELAKELIRRDGAYVchcnkaeikaqrgeadgergkaryacphrsrpieeslqefeamregkykageaalrmkmdledpn 269
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 270 pqmwdifawrildvdtkgHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRPMQREYGR 349
Cdd:cd00807 96 ------------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSR 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 350 LNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLETTVP 429
Cdd:cd00807 158 LNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAP 237
|
.
gi 121710810 430 R 430
Cdd:cd00807 238 R 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
110-425 |
2.29e-116 |
|
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: 350.85 E-value: 2.29e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPV-RVTNASDNFDR 188
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 189 LYELAKELIRRDGAYVCHCNKAEIKAQRGEadgergKARYACPHRSRPIEESLQEF-EAMREGKYKAGEAALRMKMDLED 267
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREE------QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 268 PnPQMWDIFAWRILDVDTKGHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRP-MQRE 346
Cdd:pfam00749 155 P-YVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPpFIHE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 347 YGRLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAI-VQTVKLDQVVRQYLE 425
Cdd:pfam00749 234 YLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
110-492 |
1.36e-90 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 292.53 E-value: 1.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEG---EEEMYYRGIEDIvSWLGYKPVRVTNASDNF 186
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTkrpDPEAYDMILEDL-KWLGVKWDEVVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 187 DRLYELAKELIRRDGAYVCHCNKAEIKAQRGEadgerGKAryaCPHRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLE 266
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKELRDA-----GKP---CPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 267 DPNPQMWDIFAWRIldVDTKgHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMS--RQSYewlndkldVYR--- 341
Cdd:PRK04156 252 HPNPSVRDWVAFRI--VKTP-HPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNteKQRY--------IYDyfg 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 342 ---PMQREYGRLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQ 418
Cdd:PRK04156 321 weyPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYA 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121710810 419 VVRQYLETTVPRLMVVLEPLKVVISNLPdgyEEMVEVPFSKD-PAFGSHLVPFTKVVYIERSDFREEDSPdyFRL 492
Cdd:PRK04156 401 INRKLIDPIANRYFFVRDPVELEIEGAE---PLEAKIPLHPDrPERGEREIPVGGKVYVSSDDLEAEGKM--VRL 470
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
110-503 |
9.38e-88 |
|
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: 282.07 E-value: 9.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYK----PVRvtnASDN 185
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPYY---QSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 186 FDRLYELAKELIRRDGAYVCHCNKAEIKAQRGEAdGERGKA-RYACPHRSRPIEEsLQEFEAmrEGKykagEAALRMKMD 264
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQ-TAPGKPpRYDGRCRDLSPEE-LERMLA--AGE----PPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 265 LED-------------PNPQMWDIfawrILdvdtkghFRTGGqwkmYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYE 331
Cdd:COG0008 153 EEGvvfddlvrgeitfPNPNLRDP----VL-------YRADG----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 332 WLNDKLDVYRPmqrEYGRLNLT----GTVLSKRKiielvkksyvrgwddpRLYTLLAIRRRGIPPGAILSFVNNLGVTKA 407
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLIlgpdGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 408 TAivQTVK-LDQVVRQYLETTVPRLMVVLEPLKVVISNLP--------------------DGYEEMVE--VPFSKDPA-F 463
Cdd:COG0008 279 DD--QEIFsLEELIEAFDLDRVSRSPAVFDPVKLVWLNGPyiralddeelaellapelpeAGIREDLErlVPLVRERAkT 356
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 121710810 464 GSHLVPFTKVVYIERSDfreEDSPDyFRLAPGKTVGLMKA 503
Cdd:COG0008 357 LSELAELARFFFIERED---EKAAK-KRLAPEEVRKVLKA 392
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
110-487 |
1.94e-84 |
|
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: 275.93 E-value: 1.94e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPVRVTNASDNFDRL 189
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 190 YELAKELIRRDGAYVCHCNKAEIKAQRGeaDGErgkaryACPHRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLEDPN 269
Cdd:TIGR00463 173 YDYTRKLIEMGKAYVCDCRPEEFRELRN--RGE------ACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 270 PQMWDifaWRILDVDTKGHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRPMQREYGR 349
Cdd:TIGR00463 245 PAIRD---WVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHWGR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 350 L--NLTGTVLSKRKIIELVKKSYVrGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLETT 427
Cdd:TIGR00463 322 LkiDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEE 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121710810 428 VPRLMVVLEPLKVVISNLPDgyEEMVEVPFSKD-PAFGSHLVPFTKVVYIERSDFREEDSP 487
Cdd:TIGR00463 401 ARRYFFIWNPVKIEIVGLPE--PKRVERPLHPDhPEIGERVLILRGEIYVPKDDLEEGVEP 459
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
110-651 |
5.23e-78 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 260.28 E-value: 5.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYK-PVRVTNASDNFDR 188
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSwDVGPTYSSDYMDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 189 LYELAKELIRRDGAYVCHCNKAEIkaQRGEADGERGKaryacpHRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLEDP 268
Cdd:PTZ00402 132 MYEKAEELIKKGLAYCDKTPREEM--QKCRFDGVPTK------YRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 269 NPQMWDIFAWRildVDTKGHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRPMQREYG 348
Cdd:PTZ00402 204 NKAMRDPVIYR---VNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 349 RLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLETTV 428
Cdd:PTZ00402 281 RLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 429 PRLMVVLEPLKVVISNLPDGYEEMVEVPF-SKDPAFGshlvpfTKVVYieRSDFREEDSPDYFRLAPGKTVGLMKapfpi 507
Cdd:PTZ00402 361 PRYTVVSNTLKVRCTVEGQIHLEACEKLLhKKVPDMG------EKTYY--KSDVIFLDAEDVALLKEGDEVTLMD----- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 508 TATTFDKDPETGAvtcvyahyekpedGSATPT------------KKAKTYIHWVGESAthkspvKAEVRAFNSLfksndp 575
Cdd:PTZ00402 428 WGNAYIKNIRRSG-------------EDALITdadivlhlegdvKKTKFKLTWVPESP------KAEVMELNEY------ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 576 nahpDGFLADINPDSEEIYENALvdigfhdvsksAPWPKESGEVGGEASPYSTR----FQGMRTAYFAVDKDsTADKVVL 651
Cdd:PTZ00402 483 ----DHLLTKKKPDPEESIDDII-----------APVTKYTQEVYGEEALSVLKkgdiIQLERRGYYIVDDV-TPKKVLI 546
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
66-480 |
2.04e-74 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 253.49 E-value: 2.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 66 GKKGGAKPA----KEAVTDLRSLDPE---AMFKVGFladvyqerPLSEQHpKIRTRFPPEPNGFLHIGHSKAIAVNFGFA 138
Cdd:PLN02907 171 GKRGAGKPAaaksKEKVADAGKADGAkdkGSFEVDL--------PGAEEG-KVCTRFPPEPSGYLHIGHAKAALLNQYFA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 139 KYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPVRVTNASDNFDRLYELAKELIRRDGAYVCHCNKAEIKAQRGe 218
Cdd:PLN02907 242 RRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERM- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 219 aDGERGKAryacphRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLEDPNPQMWDIFAWRildVDTKGHFRTGGQWKMY 298
Cdd:PLN02907 321 -DGIESKC------RNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYR---CNPTPHHRIGSKYKVY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 299 PTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRPMQREYGRLNLTGTVLSKRKIIELVKKSYVRGWDDPR 378
Cdd:PLN02907 391 PTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPR 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 379 LYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLETTVPRLMVVLEPLKVVISnLPDGYEEmvevPFS 458
Cdd:PLN02907 471 FPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLT-LTDGPET----PFV 545
|
410 420
....*....|....*....|....*....
gi 121710810 459 -------KDPAFGSHLVPFTKVVYIERSD 480
Cdd:PLN02907 546 riiprhkKYEGAGKKATTFTNRIWLDYAD 574
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
110-606 |
4.49e-73 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 244.92 E-value: 4.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYKPVRVTNASDNFDRL 189
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 190 YELAKELIRRDGAYVCHCNKAEIKAQRGEadgergkaRYACPHRSRPIEESLQEFEAMREGKYKAGEAALRMKMDLEDPN 269
Cdd:PLN03233 91 RCYAIILIEEGLAYMDDTPQEEMKKERAD--------RAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 270 PQMWDIFAWRildVDTKGHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRPMQREYGR 349
Cdd:PLN03233 163 GTLRDPVLFR---QNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 350 LNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQVVRQYLETTVP 429
Cdd:PLN03233 240 MNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 430 RLMVV--LEPLKVVISNLPDG----YEEMVEVPfsKDPAFGSHLVPFTKVVYIERSDFREedspdyfrLAPGKTVGLMKA 503
Cdd:PLN03233 320 RFMAIdkADHTALTVTNADEEadfaFSETDCHP--KDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLLRW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 504 PFpITATTFDKDPEtgavtcvyAHYEKPEDgsatpTKKAKTYIHWVGESATHKSPVKAEvraFNSLFkSNDPNAHPDGFL 583
Cdd:PLN03233 390 GV-IEISKIDGDLE--------GHFIPDGD-----FKAAKKKISWIADVSDNIPVVLSE---FDNLI-IKEKLEEDDKFE 451
|
490 500
....*....|....*....|....*..
gi 121710810 584 ADINPD----SEEIYENALVDIGFHDV 606
Cdd:PLN03233 452 DFINPDtlaeTDVIGDAGLKTLKEHDI 478
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
110-430 |
1.94e-43 |
|
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: 156.36 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEM--YYRGIEDIVSWLGYKPVRVTNASDNFD 187
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDpeAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 188 RLYELAKELIRRDGAYVchcnkaeikaqrgeadgergkaryacphrsrpieeslqefeamregkykageaalrmkmdled 267
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 268 pnpqmwdifawrildvdtkgHFRTGGQWKMYPTYDFAHPLCDSIEEITHSLCTVEFEMS--RQSYewlndkldVYR---- 341
Cdd:cd09287 98 --------------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNteKQRY--------IYEyfgw 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 342 --PMQREYGRLNLTGTVLSKRKIIELVKKSYVRGWDDPRLYTLLAIRRRGIPPGAILSFVNNLGVTKATAIVQTVKLDQV 419
Cdd:cd09287 150 eyPETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAI 229
|
330
....*....|.
gi 121710810 420 VRQYLETTVPR 430
Cdd:cd09287 230 NRKLIDPRANR 240
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
429-641 |
2.98e-40 |
|
tRNA synthetases class I (E and Q), anti-codon binding 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: 427609 [Multi-domain] Cd Length: 175 Bit Score: 145.11 E-value: 2.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 429 PRLMVVLEPLKVVISNLPDGYEEMVEVP-FSKDPAFGSHLVPFTKVVYIERSDFreedspdyFRLAPGKTVGLMKApFPI 507
Cdd:pfam03950 2 PRYMAVLDPVKVVIENYPEGQEETAEVPnHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDA-YNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 508 TATTFDKDpETGAVTCVYAHYEkPEDGSATPTKKAKTyIHWVgeSATHksPVKAEVRAFNSLFKSNDpnahPDGFLadIN 587
Cdd:pfam03950 73 KVTEVVKD-EDGNVTELHCTYD-GDDLGGARKVKGKI-IHWV--SASD--AVPAEVRLYDRLFKDED----DADFL--LN 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 121710810 588 PDSEEIYENALVDIGFHDVsksapwpkesgEVGgeaspysTRFQGMRTAYFAVD 641
Cdd:pfam03950 140 PDSLKVLTEGLAEPALANL-----------KPG-------DIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
110-407 |
6.41e-40 |
|
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: 146.08 E-value: 6.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGYK----PVRvtnASDN 185
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPYR---QSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 186 FDRLYELAKELIRRDGayvchcnkaeikaqrgeadgergkaryacphrsrpieeslqefeamregkykageaalrmkmdl 265
Cdd:cd00418 78 FDLYRAYAEELIKKGG---------------------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 266 edpnpqmwdifawrildvdtkghfrtggqwkmYPTYDFAHPLCDSIEEITHSLCTVEFEMSRQSYEWLNDKLDVYRPMQR 345
Cdd:cd00418 94 --------------------------------YPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFY 141
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121710810 346 EYGRLNL-TGTVLSKRKIIElvkksyvrgwddprlyTLLAIRRRGIPPGAILSFVNNLGVTKA 407
Cdd:cd00418 142 HFPRLLLeDGTKLSKRKLNT----------------TLRALRRRGYLPEALRNYLALIGWSKP 188
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
110-201 |
2.73e-14 |
|
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: 73.00 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 110 KIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLG------------YKPV 177
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldwdegpdvggpYGPY 80
|
90 100
....*....|....*....|....*
gi 121710810 178 RvtnASDNFDRLYELAKELIRR-DG 201
Cdd:cd00808 81 R---QSERLEIYRKYAEKLLEKgDG 102
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
111-318 |
6.54e-11 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 65.15 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 111 IRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTN-----PEGEEEMyyrgIEDIvSWLG------------ 173
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDlarstKESEEAV----LRDL-KWLGldwdegpdvgge 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 174 YKPVRvtnASDNFDRLYELAKELIRRDGAYVCHCNKAEIKAQRGEADGERGKARYACPHRSRPIEESLQE---------- 243
Cdd:PLN02627 121 YGPYR---QSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAElakgtpytyr 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121710810 244 FEAMREGKYKAGEaALRMKMdledpnpqmwdifAWrilDVDTKGHF---RTGGQwkmyPTYDFAHPLCDSIEEITHSL 318
Cdd:PLN02627 198 FRVPKEGSVKIDD-LIRGEV-------------SW---NTDTLGDFvllRSNGQ----PVYNFCVAVDDATMGITHVI 254
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
109-236 |
2.64e-10 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 61.79 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121710810 109 PKIRTRFPPEPNGFLHIGHSKAIAVNFGFAKYHGGECILRFDDTNPEGEEEMYYRGIEDIVSWLGY---KPVRVTnaSDN 185
Cdd:PRK05710 4 TPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLhwdGPVLYQ--SQR 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 121710810 186 FDRlYELAKE-LIRRDGAYVCHCNKAEIKAQRG-EADGER---GKARYACPHRSRP 236
Cdd:PRK05710 82 HDA-YRAALDrLRAQGLVYPCFCSRKEIAAAAPaPPDGGGiypGTCRDLLHGPRNP 136
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
113-154 |
2.40e-06 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate 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: 173901 [Multi-domain] Cd Length: 143 Bit Score: 47.47 E-value: 2.40e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 121710810 113 TRFPPEPNGFLHIGHSKAIAVNFGFAKYH-----GGECILRFDDTNP 154
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYrklgyKVRCIALIDDAGG 48
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
113-168 |
8.22e-04 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 39.44 E-value: 8.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 121710810 113 TRFPPEPnGFLHIGHSKAIAVNFGFAkyhgGECILRFDDTNPEGEEEMYYRGIEDI 168
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPHELEERK 52
|
|
| |
