|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
5-775 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 877.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 5 LTLFTSIGLSEQKAKETMKNEALSSALkEAVTQAQRVhgASGVDKAMGTLLYNMASRLKdAKRL---AFLADSIVQRKIC 81
Cdd:PLN02859 9 LELFLKIGLDERTARNAIANNKVTSNL-TAVIHEAGV--TNGCDKTVGNLLYTVATKYP-ANALvhrPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 82 TELQLAAALDFVKSHPQDPINQKEFEEACGVGVVITPEQIEDAVESVIKKHKEQLLKERYHFNMGLLMGEARSALKWADG 161
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 162 KVIKNEVDMQVLHLLGPKTEADLEKKPKPQKAKvtenevKAKKEEVAVNGEVStgevKSLMEQLRGEALkFHKPGENFK- 240
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKPVKKKKEK------PAKVEEKKVAVAAA----PPSEEELNPYSI-FPQPEENFKv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 241 ------TEGYVVTP-NTMSLLKKHLDLTGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEE 313
Cdd:PLN02859 234 htevffSDGSVLRPsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 314 KYFTAIKDMVEWLGYKPYAVTHASDNFQQLYDLAVDLIRRGHAYVCHQRGEELKGH--NAPPSPWRDRPIEESLVLFERM 391
Cdd:PLN02859 314 EYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 392 KKGLFAEGEATLRMKMVM--EDGKM-DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSY 468
Cdd:PLN02859 394 RRGLIEEGKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 469 YWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTT 548
Cdd:PLN02859 474 YWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 549 T-EPHLLESCVRDVLNDTAPRAMAVLEPLKVTITNLPEDSQSDV---RVPDFPANEAKGSHMVPFTCTIFIEQSDFREVM 624
Cdd:PLN02859 554 LiRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKD 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 625 EKGYKRLTPEQPVGLRHAGYVISVQKVIKDAQGNVVELEVNcCRSETAEKPKAFIHWVS------KPLTCEVRLYERLFL 698
Cdd:PLN02859 634 SKDYYGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAE-YDPEKKTKPKGVLHWVAepspgvEPLKVEVRLFDKLFL 712
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079744115 699 hkhPEDPSEVPNgFLSDINPNSLQVISSALVDTSVKGAKVFDKFQFERVGYFSLDPDSTADKLIFNRTVTLKEDPGK 775
Cdd:PLN02859 713 ---SENPAELED-WLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
265-771 |
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: 593.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 265 IRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YAVTHASDNFQQL 343
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 344 YDLAVDLIRRGHAYVCHQRGEELK---GHNAPP---SPWRDRPIEESLVLFERMKKGLFAEGEATLRMKMVMEDGKM--- 414
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 415 DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYC-PVQWEYGRLNLTYT 493
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 494 VVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLNDTAPRAMAVL 573
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 574 EPLKVTITNLPEDSQSdVRVPDFPANEAKGSHMVPFTCTIFIEQSDFREVMEKGYKRLTPEQPVGLRHAgYVISVQKVIK 653
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 654 DAQGNVVELEVN------CCRSETAEKPKAFIHWVS--KPLTCEVRLYERLFlhkHPEDPSEvPNGFLSDINPNSLqVIS 725
Cdd:TIGR00440 399 DAAGKITTIFCTydnktlGKEPADGRKVKGVIHWVSasSKYPTETRLYDRLF---KVPNPGA-PDDFLSVINPESL-VIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1079744115 726 SALVDTSVKGAKVFDKFQFERVGYFSLDP-DSTADKLIFNRTVTLKE 771
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
264-568 |
5.83e-162 |
|
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: 468.27 E-value: 5.83e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYAVTHASDNFQQL 343
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 344 YDLAVDLIRRGHAYVchqrgeelkghnappspwrdrpieeslvlfermkkglfaegeatlrmkmvmedgkmdpvayriky 423
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 424 tpHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKL 503
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1079744115 504 VETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLNDTAPR 568
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
264-564 |
3.12e-149 |
|
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: 438.68 E-value: 3.12e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YAVTHASDNFQQ 342
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 343 LYDLAVDLIRRGHAYVCHQRGEELKGHN----APPSPWRDRPIEESLVLF-ERMKKGLFAEGEATLRMKMVME-DGKM-D 415
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEReeqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 416 PVAYRIKYTP---HHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPV-QWEYGRLNLT 491
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1079744115 492 YTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTT-EPHLLESCVRDVLND 564
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNrLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
261-699 |
4.60e-89 |
|
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: 288.23 E-value: 4.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 261 TGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK----PYavtHA 336
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 337 SDNFQQLYDLAVDLIRRGHAYVCHQRGEELKGHNA-------PP---SPWRDRPIEESlvlfERMKkglfAEGE-ATLRM 405
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALREtqtapgkPPrydGRCRDLSPEEL----ERML----AAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 406 KM-----VMED---GKM--------DPVAYRikytphhRTGdewciYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYY 469
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 470 WLCNALDVYCPvqwEYGRLNLTY----TVVSKRKiiklvetGVVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTV- 544
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKs 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 545 -SQTTTEPHLLESCVRdvLNDTaPRAMAVLEPLKVTITN------LPEDSQSDVRVPDFPAN--EAKGSHMVPFT----- 610
Cdd:COG0008 279 dDQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAgiREDLERLVPLVrerak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 611 ---------CTIFIEQSDFREVMekgyKRLTPEQpvglrhagyvisVQKVIKDAQGNVVELEvnccrSETAEKPKAFIHW 681
Cdd:COG0008 356 tlselaelaRFFFIEREDEKAAK----KRLAPEE------------VRKVLKAALEVLEAVE-----TWDPETVKGTIHW 414
|
490
....*....|....*...
gi 1079744115 682 VSKPLtcEVRLyeRLFLH 699
Cdd:COG0008 415 VSAEA--GVKD--GLLFM 428
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
5-775 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 877.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 5 LTLFTSIGLSEQKAKETMKNEALSSALkEAVTQAQRVhgASGVDKAMGTLLYNMASRLKdAKRL---AFLADSIVQRKIC 81
Cdd:PLN02859 9 LELFLKIGLDERTARNAIANNKVTSNL-TAVIHEAGV--TNGCDKTVGNLLYTVATKYP-ANALvhrPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 82 TELQLAAALDFVKSHPQDPINQKEFEEACGVGVVITPEQIEDAVESVIKKHKEQLLKERYHFNMGLLMGEARSALKWADG 161
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 162 KVIKNEVDMQVLHLLGPKTEADLEKKPKPQKAKvtenevKAKKEEVAVNGEVStgevKSLMEQLRGEALkFHKPGENFK- 240
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKPVKKKKEK------PAKVEEKKVAVAAA----PPSEEELNPYSI-FPQPEENFKv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 241 ------TEGYVVTP-NTMSLLKKHLDLTGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEE 313
Cdd:PLN02859 234 htevffSDGSVLRPsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 314 KYFTAIKDMVEWLGYKPYAVTHASDNFQQLYDLAVDLIRRGHAYVCHQRGEELKGH--NAPPSPWRDRPIEESLVLFERM 391
Cdd:PLN02859 314 EYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 392 KKGLFAEGEATLRMKMVM--EDGKM-DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSY 468
Cdd:PLN02859 394 RRGLIEEGKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 469 YWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTT 548
Cdd:PLN02859 474 YWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 549 T-EPHLLESCVRDVLNDTAPRAMAVLEPLKVTITNLPEDSQSDV---RVPDFPANEAKGSHMVPFTCTIFIEQSDFREVM 624
Cdd:PLN02859 554 LiRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKD 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 625 EKGYKRLTPEQPVGLRHAGYVISVQKVIKDAQGNVVELEVNcCRSETAEKPKAFIHWVS------KPLTCEVRLYERLFL 698
Cdd:PLN02859 634 SKDYYGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAE-YDPEKKTKPKGVLHWVAepspgvEPLKVEVRLFDKLFL 712
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079744115 699 hkhPEDPSEVPNgFLSDINPNSLQVISSALVDTSVKGAKVFDKFQFERVGYFSLDPDSTADKLIFNRTVTLKEDPGK 775
Cdd:PLN02859 713 ---SENPAELED-WLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
263-776 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 743.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYA-VTHASDNFQ 341
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSGeLRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 342 QLYDLAVDLIRRGHAYVCHQRGEELKGH----NAP--PSPWRDRPIEESLVLFERMKKGLFAEGEATLRMKMVMEDGKM- 414
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIREYrgtlTEPgkNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNIn 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 415 --DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYC-PVQWEYGRLNLT 491
Cdd:PRK05347 188 mrDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSRLNLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 492 YTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLNDTAPRAMA 571
Cdd:PRK05347 268 YTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 572 VLEPLKVTITNLPEDSQSDVRVPDFPANEAKGSHMVPFTCTIFIEQSDFREVMEKGYKRLTPEQPVGLRHAgYVISVQKV 651
Cdd:PRK05347 348 VLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNA-YVIKCEEV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 652 IKDAQGNVVELEvncC------RSETAE---KPKAFIHWVSKP--LTCEVRLYERLFLHKHPEDPSEvpngFLSDINPNS 720
Cdd:PRK05347 427 VKDADGNITEIH---CtydpdtLSGNPAdgrKVKGTIHWVSAAhaVPAEVRLYDRLFTVPNPAAGKD----FLDFLNPDS 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1079744115 721 LqVISSALVDTSVKGAKVFDKFQFERVGYFSLDPDSTADKLIFNRTVTLKEDPGKI 776
Cdd:PRK05347 500 L-VIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
259-775 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 609.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 259 DLTGG---QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK-PYAVT 334
Cdd:PRK14703 23 DLEAGrypRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 335 HASDNFQQLYDLAVDLIRRGHAYVCHQRGEE---LKGH-NAP--PSPWRDRPIEESLVLFERMKKGLFAEGEATLRMKMV 408
Cdd:PRK14703 103 YASDYFERMYAYAEQLIKMGLAYVDSVSEEEireLRGTvTEPgtPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKID 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 409 MEDGKM---DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYC--PVQW 483
Cdd:PRK14703 183 MSSPNMklrDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPprPRQY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 484 EYGRLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLN 563
Cdd:PRK14703 263 EFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 564 DTAPRAMAVLEPLKVTITNLPEDSQSDVRVPDFPANEAK-GSHMVPFTCTIFIEQSDFREVMEKGYKRLTPEQPVGLRHA 642
Cdd:PRK14703 343 RRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKeGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRGA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 643 gYVISVQKVIKDAQGNVVELEV-----NCCRSETAEKPKAFIHWVS--KPLTCEVRLYERLFLHKHPEDPSEvpnGFLSD 715
Cdd:PRK14703 423 -YIIRCDEVVRDADGAVTELRCtydpeSAKGEDTGRKAAGVIHWVSakHALPAEVRLYDRLFKVPQPEAADE---DFLEF 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1079744115 716 INPNSLQVIsSALVDTSVKGAKVFDKFQFERVGYFSLDP-DSTADKLIFNRTVTLKEDPGK 775
Cdd:PRK14703 499 LNPDSLRVA-QGRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGA 558
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
265-771 |
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: 593.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 265 IRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YAVTHASDNFQQL 343
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 344 YDLAVDLIRRGHAYVCHQRGEELK---GHNAPP---SPWRDRPIEESLVLFERMKKGLFAEGEATLRMKMVMEDGKM--- 414
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 415 DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYC-PVQWEYGRLNLTYT 493
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 494 VVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLNDTAPRAMAVL 573
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 574 EPLKVTITNLPEDSQSdVRVPDFPANEAKGSHMVPFTCTIFIEQSDFREVMEKGYKRLTPEQPVGLRHAgYVISVQKVIK 653
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 654 DAQGNVVELEVN------CCRSETAEKPKAFIHWVS--KPLTCEVRLYERLFlhkHPEDPSEvPNGFLSDINPNSLqVIS 725
Cdd:TIGR00440 399 DAAGKITTIFCTydnktlGKEPADGRKVKGVIHWVSasSKYPTETRLYDRLF---KVPNPGA-PDDFLSVINPESL-VIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1079744115 726 SALVDTSVKGAKVFDKFQFERVGYFSLDP-DSTADKLIFNRTVTLKE 771
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
249-775 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 540.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 249 NTMSLLKKHLDLTGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGY 328
Cdd:PTZ00437 36 NTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 329 KPYAVTHASDNFQQLYDLAVDLIRRGHAYVCHQRGEELKGH--NAPPSPWRDRPIEESLVLFERMKKGLFAEGEATLRMK 406
Cdd:PTZ00437 116 KPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 407 MVMEDGK---MDPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQW 483
Cdd:PTZ00437 196 ADMKSDNpnmRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 484 EYGRLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLN 563
Cdd:PTZ00437 276 EFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 564 DTAPRAMAVLEPLKVTITNLpeDSQSDVRVPDFPANEAKGSHMVPFTCTIFIEQSDFR-EVMEKGYKRLTP-EQPVGLRH 641
Cdd:PTZ00437 356 ERCERRLMVIDPIKVVVDNW--KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPgPRVVGLKY 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 642 AGYVISVQ-KVIKDAQGNVVELEVNCCRSetaEKPKAFIHWVSKP--LTCEVRLYERLFlhkhPEDPSEVPNGFLSDINP 718
Cdd:PTZ00437 434 SGNVVCKGfEVDAAGQPSVIHVDIDFERK---DKPKTNISWVSATacTPVEVRLYNALL----KDDRAAIDPEFLKFIDE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1079744115 719 NSlQVISSALVDTSVKGAKVFDKFQFERVGYFSLDPDSTADKLIFNRTVTLKEDPGK 775
Cdd:PTZ00437 507 DS-EVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
264-568 |
5.83e-162 |
|
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: 468.27 E-value: 5.83e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYAVTHASDNFQQL 343
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 344 YDLAVDLIRRGHAYVchqrgeelkghnappspwrdrpieeslvlfermkkglfaegeatlrmkmvmedgkmdpvayriky 423
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 424 tpHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKL 503
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1079744115 504 VETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLNDTAPR 568
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
264-564 |
3.12e-149 |
|
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: 438.68 E-value: 3.12e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YAVTHASDNFQQ 342
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 343 LYDLAVDLIRRGHAYVCHQRGEELKGHN----APPSPWRDRPIEESLVLF-ERMKKGLFAEGEATLRMKMVME-DGKM-D 415
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEReeqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 416 PVAYRIKYTP---HHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPV-QWEYGRLNLT 491
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1079744115 492 YTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTT-EPHLLESCVRDVLND 564
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNrLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
261-699 |
4.60e-89 |
|
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: 288.23 E-value: 4.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 261 TGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK----PYavtHA 336
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 337 SDNFQQLYDLAVDLIRRGHAYVCHQRGEELKGHNA-------PP---SPWRDRPIEESlvlfERMKkglfAEGE-ATLRM 405
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALREtqtapgkPPrydGRCRDLSPEEL----ERML----AAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 406 KM-----VMED---GKM--------DPVAYRikytphhRTGdewciYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYY 469
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 470 WLCNALDVYCPvqwEYGRLNLTY----TVVSKRKiiklvetGVVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTV- 544
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKs 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 545 -SQTTTEPHLLESCVRdvLNDTaPRAMAVLEPLKVTITN------LPEDSQSDVRVPDFPAN--EAKGSHMVPFT----- 610
Cdd:COG0008 279 dDQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAgiREDLERLVPLVrerak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 611 ---------CTIFIEQSDFREVMekgyKRLTPEQpvglrhagyvisVQKVIKDAQGNVVELEvnccrSETAEKPKAFIHW 681
Cdd:COG0008 356 tlselaelaRFFFIEREDEKAAK----KRLAPEE------------VRKVLKAALEVLEAVE-----TWDPETVKGTIHW 414
|
490
....*....|....*...
gi 1079744115 682 VSKPLtcEVRLyeRLFLH 699
Cdd:COG0008 415 VSAEA--GVKD--GLLFM 428
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
161-753 |
1.51e-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: 289.80 E-value: 1.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 161 GKVIKNEVDMQVlhllgpkteadlekkpkpqKAKVTENEVKAKKEEVavnGEVSTGEVKSLMEQLRGEALKfhkpgENFK 240
Cdd:TIGR00463 27 GAVMSNNPELRK-------------------KAKEVLEAVEAAVEEV---NSLSPEEQKELMKRLGLDIKK-----KEKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 241 TEGYVVTPntmsllkkhlDLTGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIK 320
Cdd:TIGR00463 80 RKGLRELP----------GAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 321 DMVEWLGYKPYAVTHASDNFQQLYDLAVDLIRRGHAYVCHQRGEELKG--HNAPPSPWRDRPIEESLVLFERMKKGLFAE 398
Cdd:TIGR00463 150 EDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRElrNRGEACHCRDRSVEENLERWEEMLEGKEEG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 399 GEATLRMKMVMEDGK---MDPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQA--RRSSYYWLCN 473
Cdd:TIGR00463 230 GSVVVRVKTDLKHKNpaiRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 474 ALDVYCPVQWEYGRLNLTYTVVSKRKiIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHL 553
Cdd:TIGR00463 310 GWEPPEFIHWGRLKIDDVRALSTSSA-RKGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 554 LESCVRDVLNDTAPRAMAVLEPLKVTITNLPEdsQSDVRVPDFPANEAKGSHMVPFTCTIFIEQSDFREVMekgykrltp 633
Cdd:TIGR00463 389 IYALNRKIIDEEARRYFFIWNPVKIEIVGLPE--PKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV--------- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 634 eQPVGLRHAGYVIsVQKviKDAQGNVVELEvnccrsETAEKPKAFIHWVSKPLTCEVRLyerlflhkhpedpsevpngfl 713
Cdd:TIGR00463 458 -EPVRLMDAVNVI-YSK--KELRYHSEGLE------GARKLGKSIIHWLPAKDAVKVKV--------------------- 506
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1079744115 714 sdINPNSLqvISSALVDTSVKGAKVFDKFQFERVGYFSLD 753
Cdd:TIGR00463 507 --IMPDAS--IVEGVIEADASELEVGDVVQFERFGFARLD 542
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
259-753 |
1.05e-87 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 292.01 E-value: 1.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 259 DLTG---GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYAVTH 335
Cdd:PLN02907 205 DLPGaeeGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTY 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 336 ASDNFQQLYDLAVDLIRRGHAYVC-----HQRGEELKGHNappSPWRDRPIEESLVLFERMKKGLFAEGEATLRMKMVME 410
Cdd:PLN02907 285 TSDYFPQLMEMAEKLIKEGKAYVDdtpreQMRKERMDGIE---SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQ 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 411 D--GKM-DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYcPVQ-WEYG 486
Cdd:PLN02907 362 DpnKSLrDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 487 RLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLNDTA 566
Cdd:PLN02907 441 RLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVC 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 567 PRAMAVLEPLKV--TITNLPEDSQSDVrVPDFPANEAKGSHMVPFTCTIFIEQSDfREVMEKGykrltpeQPVGLRHAGY 644
Cdd:PLN02907 521 PRHTAVLKEGRVllTLTDGPETPFVRI-IPRHKKYEGAGKKATTFTNRIWLDYAD-AEAISEG-------EEVTLMDWGN 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 645 VIsVQKVIKDAQGNVVEL--EVNCCRSETAEKPKafIHWVSK-PLTCEVRL--YERLFLHKHPEDPSEvpngFLSDINPN 719
Cdd:PLN02907 592 AI-IKEITKDEGGAVTALsgELHLEGSVKTTKLK--LTWLPDtNELVPLSLveFDYLITKKKLEEDDN----FLDVLNPC 664
|
490 500 510
....*....|....*....|....*....|....
gi 1079744115 720 SlQVISSALVDTSVKGAKVFDKFQFERVGYFSLD 753
Cdd:PLN02907 665 T-KKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
263-762 |
1.97e-84 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 280.31 E-value: 1.97e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYkPYAV--THASDNF 340
Cdd:PTZ00402 51 GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGV-SWDVgpTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 341 QQLYDLAVDLIRRGHAYVCHQRGEELKG--HNAPPSPWRDRPIEESLVLFERMKKGLfAEGEAT-LRMKMVMED---GKM 414
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNenkAMR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 415 DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTYTV 494
Cdd:PTZ00402 209 DPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 495 VSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLNDTAPRAMAVLE 574
Cdd:PTZ00402 289 MSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 575 PLKVTITNLPEDSQSDVRVPDFPANEAKGSHMVPFTCTIFIEQSDFREVMEKgykrltpeQPVGLRHAG--YVISVQKvi 652
Cdd:PTZ00402 369 TLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVALLKEG--------DEVTLMDWGnaYIKNIRR-- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 653 KDAQGNVVELEVNCCRSETAEKPKAFIHWVS---KPLTCEVRLYERLFLHKHPeDPSEVPNGFLSDINPNSLQVISSALV 729
Cdd:PTZ00402 439 SGEDALITDADIVLHLEGDVKKTKFKLTWVPespKAEVMELNEYDHLLTKKKP-DPEESIDDIIAPVTKYTQEVYGEEAL 517
|
490 500 510
....*....|....*....|....*....|...
gi 1079744115 730 DTSVKGakvfDKFQFERVGYFSLDPDSTADKLI 762
Cdd:PTZ00402 518 SVLKKG----DIIQLERRGYYIVDDVTPKKVLI 546
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
263-753 |
1.85e-77 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 260.55 E-value: 1.85e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEK---EEEKYfTAIKDMVEWLGYKPYAVTHASDN 339
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTkrpDPEAY-DMILEDLKWLGVKWDEVVIQSDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 340 FQQLYDLAVDLIRRGHAYVCHQRGEELKG--HNAPPSPWRDRPIEESLVLFERMKKGLFAEGEATLRMKMVMEDGkmDP- 416
Cdd:PRK04156 179 LEIYYEYARKLIEMGGAYVCTCDPEEFKElrDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHP--NPs 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 417 ----VAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQ--ARRSSYywlcnaldVYCPVQWEY----- 485
Cdd:PRK04156 257 vrdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--------IYDYFGWEYpetih 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 486 -GRLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLND 564
Cdd:PRK04156 329 yGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 565 TAPRAMAVLEPLKVTITNLPEDSqsdVRVPDFPANEAKGSHMVPFTCTIFIEQSDFREV------MEKGYKRLTPEQPVG 638
Cdd:PRK04156 409 IANRYFFVRDPVELEIEGAEPLE---AKIPLHPDRPERGEREIPVGGKVYVSSDDLEAEgkmvrlMDLFNVEITGVSVDK 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 639 LRHAGyvisvqkvikdaqgnvVELEVnccrsetAEKPKA-FIHWVSK--PLTCEVRLyerlflhkhpEDPSEVpNGFlsd 715
Cdd:PRK04156 486 ARYHS----------------DDLEE-------ARKNKApIIQWVPEdeSVPVRVLK----------PDGGDI-EGL--- 528
|
490 500 510
....*....|....*....|....*....|....*...
gi 1079744115 716 INPNslqvISSALVDTSVkgakvfdkfQFERVGYFSLD 753
Cdd:PRK04156 529 AEPD----VADLEVDDIV---------QFERFGFVRID 553
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
263-753 |
5.63e-75 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 252.62 E-value: 5.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYAVTHASDNFQQ 342
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 343 LYDLAVDLIRRGHAYVCHQRGEELKGHNA--PPSPWRDRPIEESLVLFERMKKGLFAEGEATLRMKMVM--EDGKM-DPV 417
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERAdrAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMqsDNGTLrDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 418 AYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTYTVVSK 497
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 498 RKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLNDTAPRAMAV--LEP 575
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkADH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 576 LKVTITNLPEDSQSDVRVPDF-PANEAKGSHMVPFTCTIFIEQSDFREVMekgykrlTPEQPVGLRHAgyVISVQKVIKD 654
Cdd:PLN03233 330 TALTVTNADEEADFAFSETDChPKDPGFGKRAMRICDEVLLEKADTEDIQ-------LGEDIVLLRWG--VIEISKIDGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 655 AQGNVVElevnccrSETAEKPKAFIHWVSKPLT-CEVRLYErlFLHKHPEDPSEVPNGFLSDINPNSlQVISSALVDTSV 733
Cdd:PLN03233 401 LEGHFIP-------DGDFKAAKKKISWIADVSDnIPVVLSE--FDNLIIKEKLEEDDKFEDFINPDT-LAETDVIGDAGL 470
|
490 500
....*....|....*....|
gi 1079744115 734 KGAKVFDKFQFERVGYFSLD 753
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 |
4.59e-69 |
|
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: 224.36 E-value: 4.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 2 ADTLTLFTSIGLSEQKAKETMKNEALSSALKEAVTQAQRVhgaSGVDKAMGTLLYNMASRLKDA--KRLAFLADSIVQRK 79
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVE---SGCDKKQGNLLYTLATKLKGNalPHRPYLVKYIVDGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 80 ICTELQLAAALDFVKSHPQDPINQKEFEEACGVGVVITPEQIEDAVESVIKKHKEQLLKERYHFNMGLLMGEAR--SALK 157
Cdd:pfam04558 78 LKTTLQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRklPELK 157
|
....
gi 1079744115 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 ... |
566-753 |
2.36e-58 |
|
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: 195.95 E-value: 2.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 566 APRAMAVLEPLKVTITNLPEDSQSDVRVPDFPANEAKGSHMVPFTCTIFIEQSDFrevmekgyKRLTPEQPVGLRHAgYV 645
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDA-YN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 646 ISVQKVIKDAQGNVVELEVNC--CRSETAEKPKA-FIHWVSK--PLTCEVRLYERLFLHKHPEDpsevpngFLsdINPNS 720
Cdd:pfam03950 72 IKVTEVVKDEDGNVTELHCTYdgDDLGGARKVKGkIIHWVSAsdAVPAEVRLYDRLFKDEDDAD-------FL--LNPDS 142
|
170 180 190
....*....|....*....|....*....|...
gi 1079744115 721 LQVISSALVDTSVKGAKVFDKFQFERVGYFSLD 753
Cdd:pfam03950 143 LKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
265-555 |
8.39e-46 |
|
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: 163.41 E-value: 8.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 265 IRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK----PYavtHASDNF 340
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPY---RQSDRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 341 QQLYDLAVDLIRRGhayvchqrgeelkghnappspwrdrpieeslvlfermkkglfaegeatlrmkmvmedgkmdpvayr 420
Cdd:cd00418 79 DLYRAYAEELIKKG------------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 421 ikytphhrtgdewcIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTY-TVVSKRK 499
Cdd:cd00418 93 --------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDgTKLSKRK 158
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1079744115 500 IIKlvetgvvrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLE 555
Cdd:cd00418 159 LNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEE 198
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
264-568 |
1.02e-44 |
|
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: 160.98 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPE--KEEEKYFTAIKDMVEWLGYKPYAVTHASDNFQ 341
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 342 QLYDLAVDLIRRGHAYVchqrgeelkghnappspwrdrpieeslvlfermkkglfaegeatlrmkmvmedgkmdpvayri 421
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 422 kytpHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQ--ARRSSYYWLCNALDVycPVQWEYGRLNLTYTVVSKRK 499
Cdd:cd09287 98 ----HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRYIYEYFGWEY--PETIHWGRLKIEGGKLSTSK 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1079744115 500 IIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVRDVLNDTAPR 568
Cdd:cd09287 172 IRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
164-255 |
3.79e-33 |
|
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: 122.42 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 164 IKNEVDMQVLHLLGPKTEADLEKKPKPQKAKVTENEVKAKKEEVAVNGEVSTGEVKSlmeqlRGEALKFHKPGENFKTEG 243
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPPKKKKKAKKKKAAKKKKKKAPIEEEENKRSMFS-----EGFLGKFHKPGENPKTDG 75
|
90
....*....|..
gi 1079744115 244 YVVTPNTMSLLK 255
Cdd:pfam04557 76 YVVTEHTMRLLK 87
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
265-327 |
7.03e-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: 69.15 E-value: 7.03e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079744115 265 IRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLG 327
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLG 64
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| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
261-383 |
5.75e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 69.00 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 261 TGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPE---KEEEKyfTAIKDMvEWLG---------- 327
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLArstKESEE--AVLRDL-KWLGldwdegpdvg 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079744115 328 --YKPYAVTHASDNFQQlydLAVDLIRRGHAYVCHQRGEEL-------KGHNAPP---SPWRDRPIEE 383
Cdd:PLN02627 119 geYGPYRQSERNAIYKQ---YAEKLLESGHVYPCFCTDEELeamkeeaELKKLPPrytGKWATASDEE 183
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|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
266-360 |
8.73e-07 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 51.39 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 266 RTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYA-VTHASDNFqQLY 344
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGpVLYQSQRH-DAY 85
|
90
....*....|....*..
gi 1079744115 345 DLAVD-LIRRGHAYVCH 360
Cdd:PRK05710 86 RAALDrLRAQGLVYPCF 102
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
267-369 |
7.72e-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: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079744115 267 TRFPPEPNGILHIGHAKAINFNFGYAKANN-----GICFLRYDDTNPekeeekyFTAIKDMVEWLGYKPYaVTHASDNFQ 341
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGG-------LIGDPANKKGENAKAF-VERWIERIK 73
|
90 100 110
....*....|....*....|....*....|...
gi 1079744115 342 QLYDLAVD-LIRRGHAYVCHQR----GEELKGH 369
Cdd:cd00802 74 EDVEYMFLqAADFLLLYETECDihlgGSDQLGH 106
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
267-317 |
1.21e-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: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1079744115 267 TRFPPEPnGILHIGHAKAINFNFGYAkannGICFLRYDDTNPEKEEEKYFT 317
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPHE 47
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