|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
5-771 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 843.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 5 SLSLFTAIGLSEQKARETLKNEALSLVLRDAIVQAQKTLGpsVDKVTGTLLYNVATRLKdTKRL---GFLVEYIASKKIT 81
Cdd:PLN02859 8 PLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNG--CDKTVGNLLYTVATKYP-ANALvhrPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 82 TDLQLNAALDYVKAHPLDPINTSHFEKECGVGVTVTPEQIEEAVEAVIQKFKAPLQAERYRFNMGLLMGEARNQLKWADG 161
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 162 KIIKNEVDMQVLHLLGPKTEADLEKKPKVTKPKAAEPEKKgnatvngEVKIELASLMEQLRGEALKFHKPGENYK----- 236
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEK-------KVAVAAAPPSEEELNPYSIFPQPEENFKvhtev 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 237 --TEGYVVTP-KTMELLKKHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFT 313
Cdd:PLN02859 238 ffSDGSVLRPsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 314 AIKDMVEWLGYKPYAVTHASDNFDQLYEWAVELIRRGHAYVCHQKVEEIKGH--NPPPSPWRDRPIEESLLLFEGMKKGK 391
Cdd:PLN02859 318 HIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDMRRGL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 392 FAEGEVTLRMKLVM--EDGKM-DPVAYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLC 468
Cdd:PLN02859 398 IEEGKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 469 NALDVYCPVQWEYGRLNLHYTVVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTM-EP 547
Cdd:PLN02859 478 DSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLiRM 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 548 HSLEACVRDVLNETAPRIMAILEPLKVTITNFPTEKAIDVSV---PNFPADESKGFHVVPFSSTVYIEKSDFREVMEKGY 624
Cdd:PLN02859 558 DRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDY 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 625 KRLTPEQPVGLRHAGYVISVQNIVKDQSGNVIELEVTcMKTDVAEKPKAFIHWVS------DPLPCEVRLYDRLFLhksP 698
Cdd:PLN02859 638 YGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAE-YDPEKKTKPKGVLHWVAepspgvEPLKVEVRLFDKLFL---S 713
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512838623 699 EDPSEVPgGFLSDLNPNSLTTIPNALVDQSVKNAKALDKFQFERLGYFSLDPDTTPEKIIFNRTVTLKEDPGK 771
Cdd:PLN02859 714 ENPAELE-DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
261-767 |
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: 598.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 261 VRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YAVTHASDNFDQL 339
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 340 YEWAVELIRRGHAYVCHQKVEEIK---GHNPPP---SPWRDRPIEESLLLFEGMKKGKFAEGEVTLRMKLVMEDGKM--- 410
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 411 DPVAYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYC-PVQWEYGRLNLHYT 489
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 490 VVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPRIMAIL 569
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 570 EPLKVTITNFPTEKAIdVSVPNFPADESKGFHVVPFSSTVYIEKSDFREVMEKGYKRLTPEQPVGLRHAgYVISVQNIVK 649
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 650 DQSGNVIELEVT----CMKTDVAE--KPKAFIHWVS--DPLPCEVRLYDRLFlhkSPEDPSEvPGGFLSDLNPNSLtTIP 721
Cdd:TIGR00440 399 DAAGKITTIFCTydnkTLGKEPADgrKVKGVIHWVSasSKYPTETRLYDRLF---KVPNPGA-PDDFLSVINPESL-VIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 512838623 722 NALVDQSVKNAKALDKFQFERLGYFSLDP-DTTPEKIIFNRTVTLKE 767
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
260-564 |
1.06e-164 |
|
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: 475.20 E-value: 1.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 260 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYAVTHASDNFDQL 339
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 340 YEWAVELIRRGHAYVchqkveeikghnpppspwrdrpieeslllfegmkkgkfaegevtlrmklvmedgkmdpvayriky 419
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 420 tpHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYTVVSKRKIIKL 499
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512838623 500 VETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPR 564
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
260-560 |
1.90e-150 |
|
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: 441.76 E-value: 1.90e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 260 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YAVTHASDNFDQ 338
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 339 LYEWAVELIRRGHAYVCHQKVEEIKGHNPP----PSPWRDRPIEESLLLF-EGMKKGKFAEGEVTLRMKLVME-DGKM-D 411
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqealGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 412 PVAYRIKYTP---HHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV-QWEYGRLNLH 487
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512838623 488 YTVVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQ-TTMEPHSLEACVRDVLNE 560
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
257-695 |
1.54e-86 |
|
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: 281.68 E-value: 1.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 257 TGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK----PYavtHA 332
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 333 SDNFDQLYEWAVELIRRGHAYVCHQKVEEI---------KGHNPP-PSPWRDRPIEEslllfegmKKGKFAEGE-VTLRM 401
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEE--------LERMLAAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 402 KL-----VMED---GKM--------DPVAYRikytphhrtGDKwciYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYF 465
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 466 WLCNALDVYCPvqwEYGRLNLHY----TVVSKRKiiklvetGAVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVA 541
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 542 --QTTMEPHSLEACVRdvLNETaPRIMAILEPLKVTITNFPTEKAIDVS------VPNFPAD--ESKGFHVVPFS----- 606
Cdd:COG0008 279 ddQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNGPYIRALDDEelaellAPELPEAgiREDLERLVPLVrerak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 607 ---------STVYIEKSDFREVMekgyKRLTPEQpvglrhagyVISVQNIVKDQSGNVIELEvtcmktdvAEKPKAFIHW 677
Cdd:COG0008 356 tlselaelaRFFFIEREDEKAAK----KRLAPEE---------VRKVLKAALEVLEAVETWD--------PETVKGTIHW 414
|
490
....*....|....*...
gi 512838623 678 VSDPLpcEVRlyDRLFLH 695
Cdd:COG0008 415 VSAEA--GVK--DGLLFM 428
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
5-771 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 843.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 5 SLSLFTAIGLSEQKARETLKNEALSLVLRDAIVQAQKTLGpsVDKVTGTLLYNVATRLKdTKRL---GFLVEYIASKKIT 81
Cdd:PLN02859 8 PLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNG--CDKTVGNLLYTVATKYP-ANALvhrPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 82 TDLQLNAALDYVKAHPLDPINTSHFEKECGVGVTVTPEQIEEAVEAVIQKFKAPLQAERYRFNMGLLMGEARNQLKWADG 161
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 162 KIIKNEVDMQVLHLLGPKTEADLEKKPKVTKPKAAEPEKKgnatvngEVKIELASLMEQLRGEALKFHKPGENYK----- 236
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEK-------KVAVAAAPPSEEELNPYSIFPQPEENFKvhtev 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 237 --TEGYVVTP-KTMELLKKHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFT 313
Cdd:PLN02859 238 ffSDGSVLRPsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 314 AIKDMVEWLGYKPYAVTHASDNFDQLYEWAVELIRRGHAYVCHQKVEEIKGH--NPPPSPWRDRPIEESLLLFEGMKKGK 391
Cdd:PLN02859 318 HIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDMRRGL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 392 FAEGEVTLRMKLVM--EDGKM-DPVAYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLC 468
Cdd:PLN02859 398 IEEGKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 469 NALDVYCPVQWEYGRLNLHYTVVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTM-EP 547
Cdd:PLN02859 478 DSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLiRM 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 548 HSLEACVRDVLNETAPRIMAILEPLKVTITNFPTEKAIDVSV---PNFPADESKGFHVVPFSSTVYIEKSDFREVMEKGY 624
Cdd:PLN02859 558 DRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDY 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 625 KRLTPEQPVGLRHAGYVISVQNIVKDQSGNVIELEVTcMKTDVAEKPKAFIHWVS------DPLPCEVRLYDRLFLhksP 698
Cdd:PLN02859 638 YGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAE-YDPEKKTKPKGVLHWVAepspgvEPLKVEVRLFDKLFL---S 713
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512838623 699 EDPSEVPgGFLSDLNPNSLTTIPNALVDQSVKNAKALDKFQFERLGYFSLDPDTTPEKIIFNRTVTLKEDPGK 771
Cdd:PLN02859 714 ENPAELE-DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
259-771 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 745.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 259 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYA-VTHASDNFD 337
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSGeLRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 338 QLYEWAVELIRRGHAYVCHQKVEEIK---------GHNpppSPWRDRPIEESLLLFEGMKKGKFAEGEVTLRMKLVMEDG 408
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIReyrgtltepGKN---SPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 409 KM---DPVAYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYC-PVQWEYGRL 484
Cdd:PRK05347 185 NInmrDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSRL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 485 NLHYTVVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPR 564
Cdd:PRK05347 265 NLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 565 IMAILEPLKVTITNFPTEKAIDVSVPNFPADESKGFHVVPFSSTVYIEKSDFREVMEKGYKRLTPEQPVGLRHAgYVISV 644
Cdd:PRK05347 345 AMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNA-YVIKC 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 645 QNIVKDQSGNVIELEVTCM------KTDVAEKPKAFIHWVS--DPLPCEVRLYDRLFLHKSPEDPSEvpggFLSDLNPNS 716
Cdd:PRK05347 424 EEVVKDADGNITEIHCTYDpdtlsgNPADGRKVKGTIHWVSaaHAVPAEVRLYDRLFTVPNPAAGKD----FLDFLNPDS 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 512838623 717 LtTIPNALVDQSVKNAKALDKFQFERLGYFSLDPDTTPEKIIFNRTVTLKEDPGK 771
Cdd:PRK05347 500 L-VIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
259-771 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 608.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 259 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK-PYAVTHASDNFD 337
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 338 QLYEWAVELIRRGHAYVCHQKVEEIKGH----NPP--PSPWRDRPIEESLLLFEGMKKGKFAEGEVTLRMKLVMEDGKM- 410
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEIRELrgtvTEPgtPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMk 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 411 --DPVAYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYC--PVQWEYGRLNL 486
Cdd:PRK14703 190 lrDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPprPRQYEFARLAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 487 HYTVVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPRIM 566
Cdd:PRK14703 270 GYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVM 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 567 AILEPLKVTITNFPTEKAIDVSVPNFPADESK-GFHVVPFSSTVYIEKSDFREVMEKGYKRLTPEQPVGLRHAgYVISVQ 645
Cdd:PRK14703 350 AVLDPLKVVIENLPAGKVEELDLPYWPHDVPKeGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRGA-YIIRCD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 646 NIVKDQSGNVIELEVTCM-----KTDVAEKPKAFIHWVS--DPLPCEVRLYDRLFlhkSPEDPSEVPGGFLSDLNPNSLT 718
Cdd:PRK14703 429 EVVRDADGAVTELRCTYDpesakGEDTGRKAAGVIHWVSakHALPAEVRLYDRLF---KVPQPEAADEDFLEFLNPDSLR 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 512838623 719 TIPNaLVDQSVKNAKALDKFQFERLGYFSLDP-DTTPEKIIFNRTVTLKEDPGK 771
Cdd:PRK14703 506 VAQG-RVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGA 558
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
261-767 |
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: 598.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 261 VRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YAVTHASDNFDQL 339
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 340 YEWAVELIRRGHAYVCHQKVEEIK---GHNPPP---SPWRDRPIEESLLLFEGMKKGKFAEGEVTLRMKLVMEDGKM--- 410
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 411 DPVAYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYC-PVQWEYGRLNLHYT 489
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 490 VVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPRIMAIL 569
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 570 EPLKVTITNFPTEKAIdVSVPNFPADESKGFHVVPFSSTVYIEKSDFREVMEKGYKRLTPEQPVGLRHAgYVISVQNIVK 649
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 650 DQSGNVIELEVT----CMKTDVAE--KPKAFIHWVS--DPLPCEVRLYDRLFlhkSPEDPSEvPGGFLSDLNPNSLtTIP 721
Cdd:TIGR00440 399 DAAGKITTIFCTydnkTLGKEPADgrKVKGVIHWVSasSKYPTETRLYDRLF---KVPNPGA-PDDFLSVINPESL-VIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 512838623 722 NALVDQSVKNAKALDKFQFERLGYFSLDP-DTTPEKIIFNRTVTLKE 767
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
239-771 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 538.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 239 GYVVTPktmELLKKHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDM 318
Cdd:PTZ00437 33 GCRNTP---ELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 319 VEWLGYKPYAVTHASDNFDQLYEWAVELIRRGHAYVCHQKVEEIKGH--NPPPSPWRDRPIEESLLLFEGMKKGKFAEGE 396
Cdd:PTZ00437 110 VKWMGWKPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEGE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 397 VTLRMKLVMEDGK---MDPVAYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDV 473
Cdd:PTZ00437 190 ATLRVKADMKSDNpnmRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 474 YCPVQWEYGRLNLHYTVVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEAC 553
Cdd:PTZ00437 270 WRPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 554 VRDVLNETAPRIMAILEPLKVTITNFPTEKaiDVSVPNFPADESKGFHVVPFSSTVYIEKSDFR-EVMEKGYKRLTP-EQ 631
Cdd:PTZ00437 350 LREDLDERCERRLMVIDPIKVVVDNWKGER--EFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPgPR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 632 PVGLRHAGYVIsVQNIVKDQSG--NVIELEVTCMKTDvaeKPKAFIHWVSDP--LPCEVRLYDRLFlhksPEDPSEVPGG 707
Cdd:PTZ00437 428 VVGLKYSGNVV-CKGFEVDAAGqpSVIHVDIDFERKD---KPKTNISWVSATacTPVEVRLYNALL----KDDRAAIDPE 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512838623 708 FLSDLNPNSlTTIPNALVDQSVKNAKALDKFQFERLGYFSLDPDTTPEKIIFNRTVTLKEDPGK 771
Cdd:PTZ00437 500 FLKFIDEDS-EVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
260-564 |
1.06e-164 |
|
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: 475.20 E-value: 1.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 260 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYAVTHASDNFDQL 339
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 340 YEWAVELIRRGHAYVchqkveeikghnpppspwrdrpieeslllfegmkkgkfaegevtlrmklvmedgkmdpvayriky 419
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 420 tpHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYTVVSKRKIIKL 499
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512838623 500 VETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPR 564
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
260-560 |
1.90e-150 |
|
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: 441.76 E-value: 1.90e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 260 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YAVTHASDNFDQ 338
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 339 LYEWAVELIRRGHAYVCHQKVEEIKGHNPP----PSPWRDRPIEESLLLF-EGMKKGKFAEGEVTLRMKLVME-DGKM-D 411
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqealGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 412 PVAYRIKYTP---HHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV-QWEYGRLNLH 487
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512838623 488 YTVVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQ-TTMEPHSLEACVRDVLNE 560
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
259-749 |
9.12e-93 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 305.50 E-value: 9.12e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 259 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYAVTHASDNFDQ 338
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 339 LYEWAVELIRRGHAYVCHQKVEEIKGH--NPPPSPWRDRPIEESLLLFEGMKKGKFAEGEVTLRMKLVMED--GKM-DPV 413
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKErmDGIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDpnKSLrDPV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 414 AYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYcPVQ-WEYGRLNLHYTVVS 492
Cdd:PLN02907 372 YYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFSRLNFVYTLLS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 493 KRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPRIMAILEPL 572
Cdd:PLN02907 451 KRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEG 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 573 KV--TITNFPtEKAIDVSVPNFPADESKGFHVVPFSSTVYIEKSDfREVMEKGykrltpeQPVGLRHAGYVIsVQNIVKD 650
Cdd:PLN02907 531 RVllTLTDGP-ETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD-AEAISEG-------EEVTLMDWGNAI-IKEITKD 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 651 QSGNVIELE-VTCMKTDVaEKPKAFIHW---VSDPLPCEVRLYDRLFLHKSPEDPSEvpggFLSDLNPNSLTTIPnALVD 726
Cdd:PLN02907 601 EGGAVTALSgELHLEGSV-KTTKLKLTWlpdTNELVPLSLVEFDYLITKKKLEEDDN----FLDVLNPCTKKETA-ALGD 674
|
490 500
....*....|....*....|...
gi 512838623 727 QSVKNAKALDKFQFERLGYFSLD 749
Cdd:PLN02907 675 SNMRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
213-749 |
1.03e-89 |
|
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: 292.88 E-value: 1.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 213 ELASLMEQLRGEALKFHKPGENYKTEGYVVTPKTMELLKKHL-EITG---GQVRTRFPPEPNGILHIGHAKAINFNFGYA 288
Cdd:TIGR00463 42 EVLEAVEAAVEEVNSLSPEEQKELMKRLGLDIKKKEKKRKGLrELPGakmGEVVMRFAPNPSGPLHIGHARAAILNHEYA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 289 KANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYAVTHASDNFDQLYEWAVELIRRGHAYVCHQKVEEIKG--HN 366
Cdd:TIGR00463 122 KKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRElrNR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 367 PPPSPWRDRPIEESLLLFEGMKKGKFAEGEVTLRMKLVMEDGK---MDPVAYRIKYTPHHRTGDKWCIYPTYDYTHCLCD 443
Cdd:TIGR00463 202 GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNpaiRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 444 SIEHITHSLCTKEFQA--RRSSYFWLCNALDVYCPVQWEYGRLNLHYTVVSKRKiIKLVETGAVRDWDDPRLFTLTALRR 521
Cdd:TIGR00463 282 HLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALSTSSA-RKGILRGEYSGWDDPRLPTLRAIRR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 522 RGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPRIMAILEPLKVTITNFPTEKaiDVSVPNFPADESKGFH 601
Cdd:TIGR00463 361 RGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPK--RVERPLHPDHPEIGER 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 602 VVPFSSTVYIEKSDFREVMekgykrltpeQPVGLRHAGYVISVQnivKDQSGNVIELEVtcmktdVAEKPKAFIHWVSDP 681
Cdd:TIGR00463 439 VLILRGEIYVPKDDLEEGV----------EPVRLMDAVNVIYSK---KELRYHSEGLEG------ARKLGKSIIHWLPAK 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512838623 682 LPCEVRLYDrlflhkspEDPSEVPGgflsdlnpnslttipnaLVDQSVKNAKALDKFQFERLGYFSLD 749
Cdd:TIGR00463 500 DAVKVKVIM--------PDASIVEG-----------------VIEADASELEVGDVVQFERFGFARLD 542
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
257-695 |
1.54e-86 |
|
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: 281.68 E-value: 1.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 257 TGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK----PYavtHA 332
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 333 SDNFDQLYEWAVELIRRGHAYVCHQKVEEI---------KGHNPP-PSPWRDRPIEEslllfegmKKGKFAEGE-VTLRM 401
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEE--------LERMLAAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 402 KL-----VMED---GKM--------DPVAYRikytphhrtGDKwciYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYF 465
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 466 WLCNALDVYCPvqwEYGRLNLHY----TVVSKRKiiklvetGAVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVA 541
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 542 --QTTMEPHSLEACVRdvLNETaPRIMAILEPLKVTITNFPTEKAIDVS------VPNFPAD--ESKGFHVVPFS----- 606
Cdd:COG0008 279 ddQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNGPYIRALDDEelaellAPELPEAgiREDLERLVPLVrerak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 607 ---------STVYIEKSDFREVMekgyKRLTPEQpvglrhagyVISVQNIVKDQSGNVIELEvtcmktdvAEKPKAFIHW 677
Cdd:COG0008 356 tlselaelaRFFFIEREDEKAAK----KRLAPEE---------VRKVLKAALEVLEAVETWD--------PETVKGTIHW 414
|
490
....*....|....*...
gi 512838623 678 VSDPLpcEVRlyDRLFLH 695
Cdd:COG0008 415 VSAEA--GVK--DGLLFM 428
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
259-759 |
3.12e-86 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 283.67 E-value: 3.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 259 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEK---EEEKYfTAIKDMVEWLGYKPYAVTHASDN 335
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTkrpDPEAY-DMILEDLKWLGVKWDEVVIQSDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 336 FDQLYEWAVELIRRGHAYVCHQKVEEIKG--HNPPPSPWRDRPIEESLLLFEGMKKGKFAEGEVTLRMKLVMEDGkmDP- 412
Cdd:PRK04156 179 LEIYYEYARKLIEMGGAYVCTCDPEEFKElrDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHP--NPs 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 413 ----VAYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQ--ARRSSYFWLCNALDVycPVQWEYGRLNL 486
Cdd:PRK04156 257 vrdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRYIYDYFGWEY--PETIHYGRLKI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 487 HYTVVSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPRIM 566
Cdd:PRK04156 335 EGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYF 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 567 AILEPLKVTITNFPTEKAidvSVPNFPADESKGFHVVPFSSTVYIEKSDFREV------MEKGYKRLTPEQPVGLRHAGY 640
Cdd:PRK04156 415 FVRDPVELEIEGAEPLEA---KIPLHPDRPERGEREIPVGGKVYVSSDDLEAEgkmvrlMDLFNVEITGVSVDKARYHSD 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 641 VIsvqnivkdqsgnvielevtcmktDVAEKPKA-FIHWV--SDPLPCEVRLydrlflhkspEDPSEVPGgflsdlnpnsl 717
Cdd:PRK04156 492 DL-----------------------EEARKNKApIIQWVpeDESVPVRVLK----------PDGGDIEG----------- 527
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 512838623 718 ttipnaLVDQSVKNAKALDKFQFERLGYFSLDpDTTPEKIIF 759
Cdd:PRK04156 528 ------LAEPDVADLEVDDIVQFERFGFVRID-SVEDDEVVA 562
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
259-758 |
1.86e-83 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 277.61 E-value: 1.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 259 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYkPYAV--THASDNF 336
Cdd:PTZ00402 51 GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGV-SWDVgpTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 337 DQLYEWAVELIRRGHAYVCHQKVEEIKG--HNPPPSPWRDRPIEESLLLFEGMKKGKfAEGEVT-LRMKLVMED---GKM 410
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNenkAMR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 411 DPVAYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYTV 490
Cdd:PTZ00402 209 DPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 491 VSKRKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPRIMAILE 570
Cdd:PTZ00402 289 MSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 571 PLKVTITnfpTEKAIDVsvpnfpADESKGFH-VVPFSSTVYIEKSDFREVMEKGYKRLTPEQPVGLRHAG--YVISVQNI 647
Cdd:PTZ00402 369 TLKVRCT---VEGQIHL------EACEKLLHkKVPDMGEKTYYKSDVIFLDAEDVALLKEGDEVTLMDWGnaYIKNIRRS 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 648 VKD----QSGNVIELEVTCMKTD-----VAEKPKAFIhwvsdplpCEVRLYDRLFLHKSPeDPSEVPGGFLSDLNPNSLT 718
Cdd:PTZ00402 440 GEDalitDADIVLHLEGDVKKTKfkltwVPESPKAEV--------MELNEYDHLLTKKKP-DPEESIDDIIAPVTKYTQE 510
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 512838623 719 TIPnalvDQSVKNAKALDKFQFERLGYFSLDpDTTPEKII 758
Cdd:PTZ00402 511 VYG----EEALSVLKKGDIIQLERRGYYIVD-DVTPKKVL 545
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
259-756 |
1.03e-81 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 270.73 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 259 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYAVTHASDNFDQ 338
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 339 LYEWAVELIRRGHAYVCHQKVEEIKGH--NPPPSPWRDRPIEESLLLFEGMKKGKFAEGEVTLRMKLVM--EDGKM-DPV 413
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKEraDRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMqsDNGTLrDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 414 AYRIKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYTVVSK 493
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 494 RKIIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPRIMAI--LEP 571
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkADH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 572 LKVTITNFPTEKAIDVSVPNF-PADESKGFHVVPFSSTVYIEKSDFREVMekgykrlTPEQPVGLRHAgyVISVQNIVKD 650
Cdd:PLN03233 330 TALTVTNADEEADFAFSETDChPKDPGFGKRAMRICDEVLLEKADTEDIQ-------LGEDIVLLRWG--VIEISKIDGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 651 QSGNVIElevtcmKTDV--AEKPKAFIHWVSDPLPCEVRLYDRLFLHKSPEDPSEvpggFLSDLNPNSLtTIPNALVDQS 728
Cdd:PLN03233 401 LEGHFIP------DGDFkaAKKKISWIADVSDNIPVVLSEFDNLIIKEKLEEDDK----FEDFINPDTL-AETDVIGDAG 469
|
490 500
....*....|....*....|....*....
gi 512838623 729 VKNAKALDKFQFERLGYFSLD-PDTTPEK 756
Cdd:PLN03233 470 LKTLKEHDIIQLERRGFYRVDrPYMGEEK 498
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
3-161 |
9.51e-67 |
|
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N terminal to the catalytic domain of glutaminyl-tRNA synthetase (EC 6.1.1.18) in eukaryotes but not in Escherichia coli. This region is thought to bind RNA in a non-specific manner, enhancing interactions between the tRNA and enzyme, but is not essential for enzyme function.
Pssm-ID: 461353 Cd Length: 161 Bit Score: 217.81 E-value: 9.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 3 AESLSLFTAIGLSEQKARETLKNEALSLVLRDAIVQAQKTLGPsvDKVTGTLLYNVATRLKDT--KRLGFLVEYIASKKI 80
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGC--DKKQGNLLYTLATKLKGNalPHRPYLVKYIVDGKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 81 TTDLQLNAALDYVKAHPLDPINTSHFEKECGVGVTVTPEQIEEAVEAVIQKFKAPLQAERYRFNMGLLMGEARN--QLKW 158
Cdd:pfam04558 79 KTTLQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKlpELKW 158
|
...
gi 512838623 159 ADG 161
Cdd:pfam04558 159 ADP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
562-749 |
2.64e-62 |
|
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: 206.74 E-value: 2.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 562 APRIMAILEPLKVTITNFPTEKAIDVSVPNFPADESKGFHVVPFSSTVYIEKSDFrevmekgyKRLTPEQPVGLRHAgYV 641
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDA-YN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 642 ISVQNIVKDQSGNVIELEVTCMKTDVAE--KPKA-FIHWVS--DPLPCEVRLYDRLFLHKSPEDpsevpggFLsdLNPNS 716
Cdd:pfam03950 72 IKVTEVVKDEDGNVTELHCTYDGDDLGGarKVKGkIIHWVSasDAVPAEVRLYDRLFKDEDDAD-------FL--LNPDS 142
|
170 180 190
....*....|....*....|....*....|...
gi 512838623 717 LTTIPNALVDQSVKNAKALDKFQFERLGYFSLD 749
Cdd:pfam03950 143 LKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
260-564 |
4.84e-49 |
|
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: 172.92 E-value: 4.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 260 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPE--KEEEKYFTAIKDMVEWLGYKPYAVTHASDNFD 337
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 338 QLYEWAVELIRRGHAYVchqkveeikghnpppspwrdrpieeslllfegmkkgkfaegevtlrmklvmedgkmdpvayri 417
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 418 kytpHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQ--ARRSSYFWLCNALDVycPVQWEYGRLNLHYTVVSKRK 495
Cdd:cd09287 98 ----HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRYIYEYFGWEY--PETIHWGRLKIEGGKLSTSK 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512838623 496 IIKLVETGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHSLEACVRDVLNETAPR 564
Cdd:cd09287 172 IRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
261-560 |
5.08e-49 |
|
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: 172.27 E-value: 5.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 261 VRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK----PYavtHASDNF 336
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPY---RQSDRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 337 DQLYEWAVELIRRGhayvchqkveeikghnpppspwrdrpieeslllfegmkkgkfaegevtlrmklvmedgkmdpvayr 416
Cdd:cd00418 79 DLYRAYAEELIKKG------------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 417 ikytphhrtgdkwcIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHY-TVVSKRK 495
Cdd:cd00418 93 --------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDgTKLSKRK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 496 IIKlvetgavrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVAQT-----------------------TMEPHSLEA 552
Cdd:cd00418 159 LNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGhelftleemiaafsvervnsadaTFDWAKLEW 222
|
....*...
gi 512838623 553 CVRDVLNE 560
Cdd:cd00418 223 LNREYIRE 230
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
164-251 |
6.52e-34 |
|
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N terminal to the catalytic domain of glutaminyl-tRNA synthetase (EC 6.1.1.18) in eukaryotes but not in Escherichia coli. This region is thought to bind RNA in a non-specific manner, enhancing interactions between the tRNA and enzyme, but is not essential for enzyme function.
Pssm-ID: 461352 [Multi-domain] Cd Length: 87 Bit Score: 124.73 E-value: 6.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 164 IKNEVDMQVLHLLGPKTEADLEKKPK-VTKPKAAEPEKKGNATVNGEVKIELASLMEQlrGEALKFHKPGENYKTEGYVV 242
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPPKkKKKAKKKKAAKKKKKKAPIEEEENKRSMFSE--GFLGKFHKPGENPKTDGYVV 78
|
....*....
gi 512838623 243 TPKTMELLK 251
Cdd:pfam04557 79 TEHTMRLLK 87
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
261-350 |
1.30e-13 |
|
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: 71.08 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 261 VRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLG------------YKPYa 328
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldwdegpdvggpYGPY- 80
|
90 100
....*....|....*....|..
gi 512838623 329 vtHASDNFDQLYEWAVELIRRG 350
Cdd:cd00808 81 --RQSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
255-362 |
2.21e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 70.16 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 255 EITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPE---KEEEKyfTAIKDMvEWLG-------- 323
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLArstKESEE--AVLRDL-KWLGldwdegpd 116
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 512838623 324 ----YKPYavtHASDNFDQLYEWAVELIRRGHAYVCHQKVEEI 362
Cdd:PLN02627 117 vggeYGPY---RQSERNAIYKQYAEKLLESGHVYPCFCTDEEL 156
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
260-356 |
4.05e-08 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 55.63 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 260 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANGGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYA-VTHASDNFDq 338
Cdd:PRK05710 5 PYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGpVLYQSQRHD- 83
|
90
....*....|....*....
gi 512838623 339 LYEWAVE-LIRRGHAYVCH 356
Cdd:PRK05710 84 AYRAALDrLRAQGLVYPCF 102
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
263-365 |
8.20e-05 |
|
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: 43.24 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512838623 263 TRFPPEPNGILHIGHAKAINFNFGYAKA-----NGGICFLRYDDTNPekeeekyFTAIKDMVEWLGYKPYaVTHASDNFD 337
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGG-------LIGDPANKKGENAKAF-VERWIERIK 73
|
90 100 110
....*....|....*....|....*....|...
gi 512838623 338 QLYEWAVE-LIRRGHAYVCHQKV----EEIKGH 365
Cdd:cd00802 74 EDVEYMFLqAADFLLLYETECDIhlggSDQLGH 106
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
263-313 |
1.36e-03 |
|
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: 39.06 E-value: 1.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 512838623 263 TRFPPEPnGILHIGHAKAINFNFGYAkangGICFLRYDDTNPEKEEEKYFT 313
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPHE 47
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|
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