|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
4-755 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 846.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 4 AVSIFMSIGLSEQKAKETLKNEALSSTLKKAIEQAQglLGSACiDKTAGTLLYNMVTRL--KDLNRLSFLTEYIITRKIT 81
Cdd:PLN02859 8 PLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAG--VTNGC-DKTVGNLLYTVATKYpaNALVHRPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 82 SELQLSAALDFLKSDPQENLDRLEFEATCGVGVVVTPEQIEDAVELIIRKHKDQLLAERYHFNMGILMGEARTALKWADG 161
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 162 KIVKNEVDMQVLHFLGPKTEADLEKKPKAAKPKAAekdmKIEQVSVENGK-------------FHKPGENYK-------T 221
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPA----KVEEKKVAVAAappseeelnpysiFPQPEENFKvhtevffS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 222 EGYVVTP-NTMTLLKKHLEETGGQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIR 300
Cdd:PLN02859 241 DGSVLRPsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 301 EMVEWLGYRPYAVTHASDNFQLLYDLAVDLIRRGHAYVCHQRGEELKGH--NVPPSPWRERPVEESLLLFDRMRKGMFAE 378
Cdd:PLN02859 321 EIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDMRRGLIEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 379 GEVTLRMKMVM--EDGKM-DPVAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNAL 455
Cdd:PLN02859 401 GKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 456 DVYCPVQWEYGRLNLTYTVVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTM-EPHLL 534
Cdd:PLN02859 481 GLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLiRMDRL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 535 EACVREVLNDTAPRAMAVLEPLKVTITNLPTNAQKEV---RVPDFPANEAKGSHVVPFSNTIFIEQSDFREVMEKGYKRL 611
Cdd:PLN02859 561 EHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 612 TPDQPVGLRHAGYVISVQRVIKDGCGNVCELEVSCASSDSVeKPKAFIQWVS------DPLQCEVRLYERLFlhkNPEDP 685
Cdd:PLN02859 641 APGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKT-KPKGVLHWVAepspgvEPLKVEVRLFDKLF---LSENP 716
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 686 AEVPAgFLSDINPYSITMIESALVDRSVGKAKVFDKFQFERVGYFSVDPDSTSEKLVFNRTVTLKEDPGK 755
Cdd:PLN02859 717 AELED-WLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
245-751 |
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: 579.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 245 VRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRP-YAVTHASDNFQLL 323
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 324 YDLAVDLIRRGHAYVCHQRGEELK---GHNVPP---SPWRERPVEESLLLFDRMRKGMFAEGEVTLRMKMVMEDGKM--- 394
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 395 DPVAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYC-PVQWEYGRLNLTYT 473
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 474 VVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPRAMAVL 553
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 554 EPLKVTITNLPTNAQKeVRVPDFPANEAKGSHVVPFSNTIFIEQSDFREVMEKGYKRLTPDQPVGLRHAgYVISVQRVIK 633
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 634 DGCGNV----CELEVSCASSDSVE--KPKAFIQWVS--DPLQCEVRLYERLFLHKNPedpaEVPAGFLSDINPYSItMIE 705
Cdd:TIGR00440 399 DAAGKIttifCTYDNKTLGKEPADgrKVKGVIHWVSasSKYPTETRLYDRLFKVPNP----GAPDDFLSVINPESL-VIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1025395132 706 SALVDRSVGKAKVFDKFQFERVGYFSVDP-DSTSEKLVFNRTVTLKE 751
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
244-548 |
2.08e-158 |
|
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: 458.25 E-value: 2.08e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 244 QVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRPYAVTHASDNFQLL 323
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 324 YDLAVDLIRRGHAYVchqrgeelkghnvppspwrerpveeslllfdrmrkgmfaegevtlrmkmvmedgkmdpvayriky 403
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 404 tpHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKL 483
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025395132 484 VETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPR 548
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
244-544 |
2.63e-144 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 425.58 E-value: 2.63e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 244 QVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRP-YAVTHASDNFQL 322
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 323 LYDLAVDLIRRGHAYVCHQRGEELKGHNVP----PSPWRERPVEESLLLFDR-MRKGMFAEGEVTLRMKMVME-DGKM-D 395
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqealGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 396 PVAYRIKYTP---HHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYCPV-QWEYGRLNLT 471
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025395132 472 YTVVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQ-TTMEPHLLEACVREVLND 544
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
241-679 |
4.74e-85 |
|
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: 277.06 E-value: 4.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 241 TGGQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGY----RPYavtHA 316
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLdwdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 317 SDNFQLLYDLAVDLIRRGHAYVCHQRGEEL-------KGHNVPP---SPWRERPVEEslllfdrmRKGMFAEGE-VTLRM 385
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELealretqTAPGKPPrydGRCRDLSPEE--------LERMLAAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 386 KM-----VMED---GKM--------DPVAYRikytphhRTGdtwciYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYF 449
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 450 WLCNALDVYCPvqwEYGRLNLTY----TVVSKRKiiKLVetaivrdwddprlfTLTALRRRGFPPQAINNFCARVGVTVA 525
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK--GAV--------------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 526 --QTTMEPHLLEACVRevLNDTaPRAMAVLEPLKVTITNLPTNAQKEVR------VPDFPAN--EAKGSHVVPFSNT--- 592
Cdd:COG0008 279 ddQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNGPYIRALDDEelaellAPELPEAgiREDLERLVPLVRErak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 593 -----------IFIEQSDFREVMekgyKRLTPDQpvglrhagyvisVQRVIKDGCGNVCELEVscASSDSVekpKAFIQW 661
Cdd:COG0008 356 tlselaelarfFFIEREDEKAAK----KRLAPEE------------VRKVLKAALEVLEAVET--WDPETV---KGTIHW 414
|
490
....*....|....*...
gi 1025395132 662 VSDplQCEVRLyeRLFLH 679
Cdd:COG0008 415 VSA--EAGVKD--GLLFM 428
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
4-755 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 846.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 4 AVSIFMSIGLSEQKAKETLKNEALSSTLKKAIEQAQglLGSACiDKTAGTLLYNMVTRL--KDLNRLSFLTEYIITRKIT 81
Cdd:PLN02859 8 PLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAG--VTNGC-DKTVGNLLYTVATKYpaNALVHRPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 82 SELQLSAALDFLKSDPQENLDRLEFEATCGVGVVVTPEQIEDAVELIIRKHKDQLLAERYHFNMGILMGEARTALKWADG 161
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 162 KIVKNEVDMQVLHFLGPKTEADLEKKPKAAKPKAAekdmKIEQVSVENGK-------------FHKPGENYK-------T 221
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPA----KVEEKKVAVAAappseeelnpysiFPQPEENFKvhtevffS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 222 EGYVVTP-NTMTLLKKHLEETGGQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIR 300
Cdd:PLN02859 241 DGSVLRPsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 301 EMVEWLGYRPYAVTHASDNFQLLYDLAVDLIRRGHAYVCHQRGEELKGH--NVPPSPWRERPVEESLLLFDRMRKGMFAE 378
Cdd:PLN02859 321 EIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDMRRGLIEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 379 GEVTLRMKMVM--EDGKM-DPVAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNAL 455
Cdd:PLN02859 401 GKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 456 DVYCPVQWEYGRLNLTYTVVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTM-EPHLL 534
Cdd:PLN02859 481 GLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLiRMDRL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 535 EACVREVLNDTAPRAMAVLEPLKVTITNLPTNAQKEV---RVPDFPANEAKGSHVVPFSNTIFIEQSDFREVMEKGYKRL 611
Cdd:PLN02859 561 EHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 612 TPDQPVGLRHAGYVISVQRVIKDGCGNVCELEVSCASSDSVeKPKAFIQWVS------DPLQCEVRLYERLFlhkNPEDP 685
Cdd:PLN02859 641 APGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKT-KPKGVLHWVAepspgvEPLKVEVRLFDKLF---LSENP 716
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 686 AEVPAgFLSDINPYSITMIESALVDRSVGKAKVFDKFQFERVGYFSVDPDSTSEKLVFNRTVTLKEDPGK 755
Cdd:PLN02859 717 AELED-WLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
243-756 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 712.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 243 GQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRPYA-VTHASDNFQ 321
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSGeLRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 322 LLYDLAVDLIRRGHAYVCHQRGEELKGH----NVP--PSPWRERPVEESLLLFDRMRKGMFAEGEVTLRMKMVMEDGKM- 394
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIREYrgtlTEPgkNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNIn 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 395 --DPVAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYC-PVQWEYGRLNLT 471
Cdd:PRK05347 188 mrDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSRLNLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 472 YTVVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPRAMA 551
Cdd:PRK05347 268 YTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 552 VLEPLKVTITNLPTNAQKEVRVPDFPANEAKGSHVVPFSNTIFIEQSDFREVMEKGYKRLTPDQPVGLRHAgYVISVQRV 631
Cdd:PRK05347 348 VLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNA-YVIKCEEV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 632 IKDGCGNVCELEVSC-------ASSDSVeKPKAFIQWVS--DPLQCEVRLYERLFLHKNPEDPAEvpagFLSDINPYSIT 702
Cdd:PRK05347 427 VKDADGNITEIHCTYdpdtlsgNPADGR-KVKGTIHWVSaaHAVPAEVRLYDRLFTVPNPAAGKD----FLDFLNPDSLV 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1025395132 703 mIESALVDRSVGKAKVFDKFQFERVGYFSVDPDSTSEKLVFNRTVTLKEDPGKI 756
Cdd:PRK05347 502 -IKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
225-755 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 590.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 225 VVTPNTMTLLKKHLEETG--GQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREM 302
Cdd:PRK14703 10 LVSPNFITEIIEEDLEAGryPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 303 VEWLGYR-PYAVTHASDNFQLLYDLAVDLIRRGHAYVCHQRGEE---LKGhNVP----PSPWRERPVEESLLLFDRMRKG 374
Cdd:PRK14703 90 VRWLGFDwGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEireLRG-TVTepgtPSPYRDRSVEENLDLFRRMRAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 375 MFAEGEVTLRMKMVMEDGKM---DPVAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWL 451
Cdd:PRK14703 169 EFPDGAHVLRAKIDMSSPNMklrDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 452 CNALDVYC--PVQWEYGRLNLTYTVVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTM 529
Cdd:PRK14703 249 LDHLGPWPprPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 530 EPHLLEACVREVLNDTAPRAMAVLEPLKVTITNLPTNAQKEVRVPDFPANEAK-GSHVVPFSNTIFIEQSDFREVMEKGY 608
Cdd:PRK14703 329 DIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKeGSRKVPFTRELYIERDDFSEDPPKGF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 609 KRLTPDQPVGLRHAgYVISVQRVIKDGCGNVCELEV-----SCASSDSVEKPKAFIQWVS--DPLQCEVRLYERLFLHKN 681
Cdd:PRK14703 409 KRLTPGREVRLRGA-YIIRCDEVVRDADGAVTELRCtydpeSAKGEDTGRKAAGVIHWVSakHALPAEVRLYDRLFKVPQ 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025395132 682 PEdpaEVPAGFLSDINPYSITMIEsALVDRSVGKAKVFDKFQFERVGYFSVDP-DSTSEKLVFNRTVTLKEDPGK 755
Cdd:PRK14703 488 PE---AADEDFLEFLNPDSLRVAQ-GRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGA 558
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
245-751 |
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: 579.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 245 VRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRP-YAVTHASDNFQLL 323
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 324 YDLAVDLIRRGHAYVCHQRGEELK---GHNVPP---SPWRERPVEESLLLFDRMRKGMFAEGEVTLRMKMVMEDGKM--- 394
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 395 DPVAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYC-PVQWEYGRLNLTYT 473
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 474 VVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPRAMAVL 553
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 554 EPLKVTITNLPTNAQKeVRVPDFPANEAKGSHVVPFSNTIFIEQSDFREVMEKGYKRLTPDQPVGLRHAgYVISVQRVIK 633
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 634 DGCGNV----CELEVSCASSDSVE--KPKAFIQWVS--DPLQCEVRLYERLFLHKNPedpaEVPAGFLSDINPYSItMIE 705
Cdd:TIGR00440 399 DAAGKIttifCTYDNKTLGKEPADgrKVKGVIHWVSasSKYPTETRLYDRLFKVPNP----GAPDDFLSVINPESL-VIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1025395132 706 SALVDRSVGKAKVFDKFQFERVGYFSVDP-DSTSEKLVFNRTVTLKE 751
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
229-755 |
7.17e-179 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 524.16 E-value: 7.17e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 229 NTMTLLKKHLEETGGQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGY 308
Cdd:PTZ00437 36 NTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 309 RPYAVTHASDNFQLLYDLAVDLIRRGHAYVCHQRGEELKGH--NVPPSPWRERPVEESLLLFDRMRKGMFAEGEVTLRMK 386
Cdd:PTZ00437 116 KPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 387 MVMEDGK---MDPVAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYCPVQW 463
Cdd:PTZ00437 196 ADMKSDNpnmRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 464 EYGRLNLTYTVVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLN 543
Cdd:PTZ00437 276 EFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 544 DTAPRAMAVLEPLKVTITNLptNAQKEVRVPDFPANEAKGSHVVPFSNTIFIEQSDFR-EVMEKGYKRLTPD-QPVGLRH 621
Cdd:PTZ00437 356 ERCERRLMVIDPIKVVVDNW--KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKY 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 622 AGYVISVQ-RVIKDGCGNVCELEVSCASSDsveKPKAFIQWVSDP--LQCEVRLYERLFlhknPEDPAEVPAGFLSDINP 698
Cdd:PTZ00437 434 SGNVVCKGfEVDAAGQPSVIHVDIDFERKD---KPKTNISWVSATacTPVEVRLYNALL----KDDRAAIDPEFLKFIDE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025395132 699 YSiTMIESALVDRSVGKAKVFDKFQFERVGYFSVDPDSTSEKLVFNRTVTLKEDPGK 755
Cdd:PTZ00437 507 DS-EVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
244-548 |
2.08e-158 |
|
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: 458.25 E-value: 2.08e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 244 QVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRPYAVTHASDNFQLL 323
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 324 YDLAVDLIRRGHAYVchqrgeelkghnvppspwrerpveeslllfdrmrkgmfaegevtlrmkmvmedgkmdpvayriky 403
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 404 tpHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKL 483
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025395132 484 VETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPR 548
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
244-544 |
2.63e-144 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 425.58 E-value: 2.63e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 244 QVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRP-YAVTHASDNFQL 322
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 323 LYDLAVDLIRRGHAYVCHQRGEELKGHNVP----PSPWRERPVEESLLLFDR-MRKGMFAEGEVTLRMKMVME-DGKM-D 395
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqealGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 396 PVAYRIKYTP---HHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYCPV-QWEYGRLNLT 471
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025395132 472 YTVVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQ-TTMEPHLLEACVREVLND 544
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
243-733 |
4.55e-88 |
|
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: 287.87 E-value: 4.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 243 GQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRPYAVTHASDNFQL 322
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 323 LYDLAVDLIRRGHAYVCHQRGEELKGHNVP--PSPWRERPVEESLLLFDRMRKGMFAEGEVTLRMKMVMEDGK---MDPV 397
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRELRNRgeACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNpaiRDWV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 398 AYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEF--QSRRSSYFWLCNALDVYCPVQWEYGRLNLTYTVV 475
Cdd:TIGR00463 252 IFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 476 SKRKIIKLVETAIVrDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPRAMAVLEP 555
Cdd:TIGR00463 332 TSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNP 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 556 LKVTITNLPtnAQKEVRVPDFPANEAKGSHVVPFSNTIFIEQSDFREVMekgykrltpdQPVGLRHAGYVIsvqrvIKDG 635
Cdd:TIGR00463 411 VKIEIVGLP--EPKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRLMDAVNVI-----YSKK 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 636 CGNVCELEVSCASsdsvEKPKAFIQWVSDPLQCEVRLYerLFLHKNPEDPAEVPAGFLsdinpysitmiesalvdrsvgk 715
Cdd:TIGR00463 474 ELRYHSEGLEGAR----KLGKSIIHWLPAKDAVKVKVI--MPDASIVEGVIEADASEL---------------------- 525
|
490
....*....|....*...
gi 1025395132 716 aKVFDKFQFERVGYFSVD 733
Cdd:TIGR00463 526 -EVGDVVQFERFGFARLD 542
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
243-733 |
2.79e-87 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 290.47 E-value: 2.79e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 243 GQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRPYAVTHASDNFQL 322
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 323 LYDLAVDLIRRGHAYVC-----HQRGEELKGHNvppSPWRERPVEESLLLFDRMRKGMFAEGEVTLRMKMVMED--GKM- 394
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDdtpreQMRKERMDGIE---SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDpnKSLr 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 395 DPVAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYcPVQ-WEYGRLNLTYT 473
Cdd:PLN02907 369 DPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFSRLNFVYT 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 474 VVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPRAMAVL 553
Cdd:PLN02907 448 LLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 554 EPLKV--TITNLPtnAQKEVR-VPDFPANEAKGSHVVPFSNTIFIEQSDfREVMEKGykrltpdQPVGLRHAGYVIsVQR 630
Cdd:PLN02907 528 KEGRVllTLTDGP--ETPFVRiIPRHKKYEGAGKKATTFTNRIWLDYAD-AEAISEG-------EEVTLMDWGNAI-IKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 631 VIKDGCGNVCELEVSCASSDSVEKPKAFIQWVSD-PLQCEVRL--YERLFLHKNPEDPAEvpagFLSDINPysITMIES- 706
Cdd:PLN02907 597 ITKDEGGAVTALSGELHLEGSVKTTKLKLTWLPDtNELVPLSLveFDYLITKKKLEEDDN----FLDVLNP--CTKKETa 670
|
490 500
....*....|....*....|....*..
gi 1025395132 707 ALVDRSVGKAKVFDKFQFERVGYFSVD 733
Cdd:PLN02907 671 ALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
243-742 |
1.05e-86 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 285.70 E-value: 1.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 243 GQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYrPYAV--THASDNF 320
Cdd:PTZ00402 51 GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGV-SWDVgpTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 321 QLLYDLAVDLIRRGHAYVCHQRGEELKG--HNVPPSPWRERPVEESLLLFDRMRKGMfAEGEVT-LRMKMVMED---GKM 394
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNenkAMR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 395 DPVAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYCPVQWEYGRLNLTYTV 474
Cdd:PTZ00402 209 DPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 475 VSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPRAMAVLE 554
Cdd:PTZ00402 289 MSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 555 PLKVTITNLPTNAQKEVRVPDFPANEAKGSHVVPFSNTIFIEQSDFREVMEkgykrltpDQPVGLRHAG--YVISVQRVI 632
Cdd:PTZ00402 369 TLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVALLKE--------GDEVTLMDWGnaYIKNIRRSG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 633 KDGCgnVCELEVSCASSDSVEKPKAFIQWVSDPLQCEV---RLYERLFLHKNPeDPAEVPAGFLSDINPYSitmiESALV 709
Cdd:PTZ00402 441 EDAL--ITDADIVLHLEGDVKKTKFKLTWVPESPKAEVmelNEYDHLLTKKKP-DPEESIDDIIAPVTKYT----QEVYG 513
|
490 500 510
....*....|....*....|....*....|...
gi 1025395132 710 DRSVGKAKVFDKFQFERVGYFSVDPDSTSEKLV 742
Cdd:PTZ00402 514 EEALSVLKKGDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
241-679 |
4.74e-85 |
|
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: 277.06 E-value: 4.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 241 TGGQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGY----RPYavtHA 316
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLdwdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 317 SDNFQLLYDLAVDLIRRGHAYVCHQRGEEL-------KGHNVPP---SPWRERPVEEslllfdrmRKGMFAEGE-VTLRM 385
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELealretqTAPGKPPrydGRCRDLSPEE--------LERMLAAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 386 KM-----VMED---GKM--------DPVAYRikytphhRTGdtwciYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYF 449
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 450 WLCNALDVYCPvqwEYGRLNLTY----TVVSKRKiiKLVetaivrdwddprlfTLTALRRRGFPPQAINNFCARVGVTVA 525
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK--GAV--------------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 526 --QTTMEPHLLEACVRevLNDTaPRAMAVLEPLKVTITNLPTNAQKEVR------VPDFPAN--EAKGSHVVPFSNT--- 592
Cdd:COG0008 279 ddQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNGPYIRALDDEelaellAPELPEAgiREDLERLVPLVRErak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 593 -----------IFIEQSDFREVMekgyKRLTPDQpvglrhagyvisVQRVIKDGCGNVCELEVscASSDSVekpKAFIQW 661
Cdd:COG0008 356 tlselaelarfFFIEREDEKAAK----KRLAPEE------------VRKVLKAALEVLEAVET--WDPETV---KGTIHW 414
|
490
....*....|....*...
gi 1025395132 662 VSDplQCEVRLyeRLFLH 679
Cdd:COG0008 415 VSA--EAGVKD--GLLFM 428
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
243-743 |
3.67e-80 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 267.10 E-value: 3.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 243 GQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEK---EEEKYfTAIREMVEWLGYRPYAVTHASDN 319
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTkrpDPEAY-DMILEDLKWLGVKWDEVVIQSDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 320 FQLLYDLAVDLIRRGHAYVCHQRGEELKG--HNVPPSPWRERPVEESLLLFDRMRKGMFAEGEVTLRMKMVMEDGkmDP- 396
Cdd:PRK04156 179 LEIYYEYARKLIEMGGAYVCTCDPEEFKElrDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHP--NPs 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 397 ----VAYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQS--RRSSYFWLCNALDVycPVQWEYGRLNL 470
Cdd:PRK04156 257 vrdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntEKQRYIYDYFGWEY--PETIHYGRLKI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 471 TYTVVSKRKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPRAM 550
Cdd:PRK04156 335 EGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYF 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 551 AVLEPLKVTITNLPTnaqKEVRVPDFPANEAKGSHVVPFSNTIFIEQSDFREVMEkgykrltpdqPVGLRHAGYVisvqR 630
Cdd:PRK04156 415 FVRDPVELEIEGAEP---LEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAEGK----------MVRLMDLFNV----E 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 631 VIKDGCGnvcELEVSCASSDSVEKPKA-FIQWV--SDPLQCEVRlyerlflhknpedpaeVPAGFlsdinpysitmIESA 707
Cdd:PRK04156 478 ITGVSVD---KARYHSDDLEEARKNKApIIQWVpeDESVPVRVL----------------KPDGG-----------DIEG 527
|
490 500 510
....*....|....*....|....*....|....*.
gi 1025395132 708 LVDRSVGKAKVFDKFQFERVGYFSVDpDSTSEKLVF 743
Cdd:PRK04156 528 LAEPDVADLEVDDIVQFERFGFVRID-SVEDDEVVA 562
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
243-733 |
1.01e-73 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 248.77 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 243 GQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRPYAVTHASDNFQL 322
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 323 LYDLAVDLIRRGHAYVCHQRGEELKGHNV--PPSPWRERPVEESLLLFDRMRKGMFAEGEVTLRMKMVM--EDGKM-DPV 397
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERAdrAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMqsDNGTLrDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 398 AYRIKYTPHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYCPVQWEYGRLNLTYTVVSK 477
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 478 RKIIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPRAMAV--LEP 555
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkADH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 556 LKVTITNLPTNAQKEVRVPDF-PANEAKGSHVVPFSNTIFIEQSDFREVMekgykrlTPDQPVGLRHAgyVISVQRVikD 634
Cdd:PLN03233 330 TALTVTNADEEADFAFSETDChPKDPGFGKRAMRICDEVLLEKADTEDIQ-------LGEDIVLLRWG--VIEISKI--D 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 635 GcgnvcELEVSCASSDSVEKPKAFIQWVSD-PLQCEVRLYErlFLHKNPEDPAEVPAGFLSDINPYSITMIEsALVDRSV 713
Cdd:PLN03233 399 G-----DLEGHFIPDGDFKAAKKKISWIADvSDNIPVVLSE--FDNLIIKEKLEEDDKFEDFINPDTLAETD-VIGDAGL 470
|
490 500
....*....|....*....|
gi 1025395132 714 GKAKVFDKFQFERVGYFSVD 733
Cdd:PLN03233 471 KTLKEHDIIQLERRGFYRVD 490
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
2-161 |
1.73e-65 |
|
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: 214.35 E-value: 1.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 2 ADAVSIFMSIGLSEQKAKETLKNEALSSTLKKAIEQAQglLGSACiDKTAGTLLYNMVTRLKD--LNRLSFLTEYIITRK 79
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAG--VESGC-DKKQGNLLYTLATKLKGnaLPHRPYLVKYIVDGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 80 ITSELQLSAALDFLKSDPQENLDRLEFEATCGVGVVVTPEQIEDAVELIIRKHKDQLLAERYHFNMGILMGEART--ALK 157
Cdd:pfam04558 78 LKTTLQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKlpELK 157
|
....
gi 1025395132 158 WADG 161
Cdd:pfam04558 158 WADP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
546-733 |
2.73e-56 |
|
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: 190.18 E-value: 2.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 546 APRAMAVLEPLKVTITNLPTNAQKEVRVPDFPANEAKGSHVVPFSNTIFIEQSDFrevmekgyKRLTPDQPVGLRHAgYV 625
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDA-YN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 626 ISVQRVIKDGCGNVCELEVSCAsSDSVE---KPKA-FIQWVS--DPLQCEVRLYERLFLHKNPEDpaevpagFLsdINPY 699
Cdd:pfam03950 72 IKVTEVVKDEDGNVTELHCTYD-GDDLGgarKVKGkIIHWVSasDAVPAEVRLYDRLFKDEDDAD-------FL--LNPD 141
|
170 180 190
....*....|....*....|....*....|....
gi 1025395132 700 SITMIESALVDRSVGKAKVFDKFQFERVGYFSVD 733
Cdd:pfam03950 142 SLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
244-548 |
2.90e-45 |
|
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: 162.14 E-value: 2.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 244 QVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPE--KEEEKYFTAIREMVEWLGYRPYAVTHASDNFQ 321
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 322 LLYDLAVDLIRRGHAYVchqrgeelkghnvppspwrerpveeslllfdrmrkgmfaegevtlrmkmvmedgkmdpvayri 401
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 402 kytpHHRTGDTWCIYPTYDYTHCLCDSIENITHSLCTKEFQS--RRSSYFWLCNALDVycPVQWEYGRLNLTYTVVSKRK 479
Cdd:cd09287 98 ----HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntEKQRYIYEYFGWEY--PETIHWGRLKIEGGKLSTSK 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1025395132 480 IIKLVETAIVRDWDDPRLFTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEACVREVLNDTAPR 548
Cdd:cd09287 172 IRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
245-536 |
3.88e-45 |
|
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: 161.49 E-value: 3.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 245 VRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYR----PYavtHASDNF 320
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPY---RQSDRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 321 QLLYDLAVDLIRRGhayvchqrgeelkghnvppspwrerpveeslllfdrmrkgmfaegevtlrmkmvmedgkmdpvayr 400
Cdd:cd00418 79 DLYRAYAEELIKKG------------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 401 ikytphhrtgdtwcIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYFWLCNALDVYCPVQWEYGRLNLTY-TVVSKRK 479
Cdd:cd00418 93 --------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDgTKLSKRK 158
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025395132 480 IIKlvetaivrdwddprlfTLTALRRRGFPPQAINNFCARVGVTVAQTTMEPHLLEA 536
Cdd:cd00418 159 LNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEM 199
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
164-235 |
1.72e-23 |
|
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: 95.07 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 164 VKNEVDMQVLHFLGPKTEADL--------EKKPKAAKPKAAEKDMKIEQVSVEN-------GKFHKPGENYKTEGYVVTP 228
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLkkppkkkkKAKKKKAAKKKKKKAPIEEEENKRSmfsegflGKFHKPGENPKTDGYVVTE 80
|
....*..
gi 1025395132 229 NTMTLLK 235
Cdd:pfam04557 81 HTMRLLK 87
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
245-307 |
1.24e-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: 1.24e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025395132 245 VRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLG 307
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLG 64
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| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
239-363 |
2.46e-13 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 73.24 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 239 EETGGQVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLG----------- 307
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldwdegpdvgg 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025395132 308 -YRPYavtHASDNFQLLYDLAVDLIRRGHAYVCHQRGEEL-------KGHNVPP---SPWRERPVEE 363
Cdd:PLN02627 120 eYGPY---RQSERNAIYKQYAEKLLESGHVYPCFCTDEELeamkeeaELKKLPPrytGKWATASDEE 183
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
244-340 |
1.08e-08 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 57.17 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 244 QVRTRFPPEPNGILHIGHAKAINFNFGFAKANNGICFLRYDDTNPEKEEEKYFTAIREMVEWLGYRPYA-VTHASDNFQl 322
Cdd:PRK05710 5 PYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGpVLYQSQRHD- 83
|
90
....*....|....*....
gi 1025395132 323 LYDLAVD-LIRRGHAYVCH 340
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 ... |
247-349 |
1.44e-04 |
|
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: 42.47 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025395132 247 TRFPPEPNGILHIGHAKAINFNFGFAKANN-----GICFLRYDDTNPEKeeekyftaIREMVEWLGYRPYAVTHASDNFQ 321
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGGLI--------GDPANKKGENAKAFVERWIERIK 73
|
90 100 110
....*....|....*....|....*....|...
gi 1025395132 322 LLYDLAVD-LIRRGHAYVCHQR----GEELKGH 349
Cdd:cd00802 74 EDVEYMFLqAADFLLLYETECDihlgGSDQLGH 106
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
247-300 |
4.30e-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: 40.21 E-value: 4.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1025395132 247 TRFPPEPnGILHIGHAKAINFNFGFAkannGICFLRYDDTNPEKEEEKYFTAIR 300
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPHELEE 50
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