|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
8-776 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 778.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 8 IKLFQTIGLSEQKAKETLKNAQVTKHLKSAISEASKHGVLNNENGILLYHLASKVKVQIADKLPFMSESIVKKKLDTIQR 87
Cdd:PLN02859 9 LELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSKIKTPAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 88 VDAALNYFLSNIKESIDIKAFEDACGVGIEITQEQIKNAVNVIIEKNKNEIIEKRYRFNAGPLMQKIRNDLKWADGKLLK 167
Cdd:PLN02859 89 LEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADPKIVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 168 IEFDSQLFELLGEKTEADLMPIVKDGKNKQKSqekekkksdkekneiVKDKIDAQTISELMKTKVN----FHKPGENYKt 243
Cdd:PLN02859 169 KLIDKKLYELLGEKTAADNEKPVKKKKEKPAK---------------VEEKKVAVAAAPPSEEELNpysiFPQPEENFK- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 244 egyVVTE------------NTHKLLKEHLLITGGKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPE 311
Cdd:PLN02859 233 ---VHTEvffsdgsvlrpsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 312 KEEEKFFIGIREMVEWLGYKPNEITYSSDNFQQLYNWAVKLIEKGMAYVCHQTSDQMKGF--NPPPSPWRERPIEESLQL 389
Cdd:PLN02859 310 AEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 390 FQDMKDGLMEEGEATLRMKVTLEEGKQ---DPVAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSR 466
Cdd:PLN02859 390 FEDMRRGLIEEGKATLRMKQDMQNDNFnmyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 467 RSSYYWLCNAVDIYCPVQWEYGRLNVSYTVVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTG 546
Cdd:PLN02859 470 RASYYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITR 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 547 AQ-ATVDPEALEASVRDVLNITAPRHMVVLDPLKITISNFHGDSIsISV-----PNFPNEPEKGQHTITFNDVVYIEATD 620
Cdd:PLN02859 550 SDnSLIRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEV-IELdakrwPDAQNDDPSAFYKVPFSRVVYIERSD 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 621 FKENEEKGFRRLTPKQSVGLKHTGVVITFQSVEKDSNGRITNIIAKQEPvSDKNKPKAFIHWVSNPS------TASVRLY 694
Cdd:PLN02859 629 FRLKDSKDYYGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDP-EKKTKPKGVLHWVAEPSpgveplKVEVRLF 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 695 DRLFKHRNPedsNEVPNgFLSDINRDSKKEIV-AYIDSSLeKVSKPLEKMQFERIGFFCVDFDTKPNKVVFNRTVTLKED 773
Cdd:PLN02859 708 DKLFLSENP---AELED-WLEDLNPQSKEVISgAYAVPSL-KDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDS 782
|
...
gi 2322523171 774 SGK 776
Cdd:PLN02859 783 YGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
267-772 |
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: 584.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 267 VRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPN-EITYSSDNFQQL 345
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 346 YNWAVKLIEKGMAYVCHQTSDQMK---GFNPPP---SPWRERPIEESLQLFQDMKDGLMEEGEATLRMKVTLEEG---KQ 416
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPfpvMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 417 DPVAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYC-PVQWEYGRLNVSYT 495
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 496 VVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPRHMVVL 575
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 576 DPLKITISNFHGDSISISVPNFPNEPEKGQHTITFNDVVYIEATDFKENEEKGFRRLTPKQSVGLKHTgVVITFQSVEKD 655
Cdd:TIGR00440 321 DPVEVVIENLSDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 656 SNGRITNIIAKQEPV------SDKNKPKAFIHWVS--NPSTASVRLYDRLFKHRNPedsnEVPNGFLSDINRDSKKEIVA 727
Cdd:TIGR00440 400 AAGKITTIFCTYDNKtlgkepADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNP----GAPDDFLSVINPESLVIKQG 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2322523171 728 YIDSSLEKVSKPlEKMQFERIGFFCVDF-DTKPNKVVFNRTVTLKE 772
Cdd:TIGR00440 476 FMEHSLGDAVAN-KRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
266-570 |
9.21e-155 |
|
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: 449.78 E-value: 9.21e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 266 KVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNEITYSSDNFQQL 345
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 346 YNWAVKLIEKGMAYVchqtsdqmkgfnpppspwrerpieeslqlfqdmkdglmeegeatlrmkvtleegkqdpvayriky 425
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 426 vpHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYCPVQWEYGRLNVSYTVVSKRKIAKL 505
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2322523171 506 IDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPR 570
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
266-565 |
7.30e-136 |
|
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: 404.39 E-value: 7.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 266 KVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNE-ITYSSDNFQQ 344
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYgPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 345 LYNWAVKLIEKGMAYVCHQTSDQMKGFNPP----PSPWRERPIEESLQLFQ-DMKDGLMEEGEATLRMKVTLEEGKQ--D 417
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqealGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESPYVfrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 418 PVAYRIKYVP---HHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYCPV-QWEYGRLNVS 493
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2322523171 494 YTVVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQA-TVDPEALEASVRDVLN 565
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
263-586 |
3.36e-82 |
|
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: 270.13 E-value: 3.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 263 TGGKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNE-ITYSSDN 341
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 342 FQQLYNWAVKLIEKGMAYVCHQTSDQM-------KGFNPPP---SPWRERPIEEslqlfqdmKDGLMEEGE-ATLRMKVT 410
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELealretqTAPGKPPrydGRCRDLSPEE--------LERMLAAGEpPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 411 LEE--------GKQ--------DPVAYRikyvphhRTGdqwciYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLC 474
Cdd:COG0008 153 EEGvvfddlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 475 NAVDIYCPvqwEYGRLNVSY----TVVSKRKiaklideGIVsnwddprlfTLTALRRRGFPAEAINNFCAQMGVT--GAQ 548
Cdd:COG0008 221 EALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSksDDQ 281
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2322523171 549 ATVDPEALEA--SVRDVlnitaPRHMVVLDPLKITISNFH 586
Cdd:COG0008 282 EIFSLEELIEafDLDRV-----SRSPAVFDPVKLVWLNGP 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
8-776 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 778.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 8 IKLFQTIGLSEQKAKETLKNAQVTKHLKSAISEASKHGVLNNENGILLYHLASKVKVQIADKLPFMSESIVKKKLDTIQR 87
Cdd:PLN02859 9 LELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSKIKTPAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 88 VDAALNYFLSNIKESIDIKAFEDACGVGIEITQEQIKNAVNVIIEKNKNEIIEKRYRFNAGPLMQKIRNDLKWADGKLLK 167
Cdd:PLN02859 89 LEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADPKIVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 168 IEFDSQLFELLGEKTEADLMPIVKDGKNKQKSqekekkksdkekneiVKDKIDAQTISELMKTKVN----FHKPGENYKt 243
Cdd:PLN02859 169 KLIDKKLYELLGEKTAADNEKPVKKKKEKPAK---------------VEEKKVAVAAAPPSEEELNpysiFPQPEENFK- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 244 egyVVTE------------NTHKLLKEHLLITGGKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPE 311
Cdd:PLN02859 233 ---VHTEvffsdgsvlrpsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 312 KEEEKFFIGIREMVEWLGYKPNEITYSSDNFQQLYNWAVKLIEKGMAYVCHQTSDQMKGF--NPPPSPWRERPIEESLQL 389
Cdd:PLN02859 310 AEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 390 FQDMKDGLMEEGEATLRMKVTLEEGKQ---DPVAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSR 466
Cdd:PLN02859 390 FEDMRRGLIEEGKATLRMKQDMQNDNFnmyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 467 RSSYYWLCNAVDIYCPVQWEYGRLNVSYTVVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTG 546
Cdd:PLN02859 470 RASYYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITR 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 547 AQ-ATVDPEALEASVRDVLNITAPRHMVVLDPLKITISNFHGDSIsISV-----PNFPNEPEKGQHTITFNDVVYIEATD 620
Cdd:PLN02859 550 SDnSLIRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEV-IELdakrwPDAQNDDPSAFYKVPFSRVVYIERSD 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 621 FKENEEKGFRRLTPKQSVGLKHTGVVITFQSVEKDSNGRITNIIAKQEPvSDKNKPKAFIHWVSNPS------TASVRLY 694
Cdd:PLN02859 629 FRLKDSKDYYGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDP-EKKTKPKGVLHWVAEPSpgveplKVEVRLF 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 695 DRLFKHRNPedsNEVPNgFLSDINRDSKKEIV-AYIDSSLeKVSKPLEKMQFERIGFFCVDFDTKPNKVVFNRTVTLKED 773
Cdd:PLN02859 708 DKLFLSENP---AELED-WLEDLNPQSKEVISgAYAVPSL-KDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDS 782
|
...
gi 2322523171 774 SGK 776
Cdd:PLN02859 783 YGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
265-777 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 699.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 265 GKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPN-EITYSSDNFQ 343
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSgELRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 344 QLYNWAVKLIEKGMAYVCHQTSDQMK----GFNPP--PSPWRERPIEESLQLFQDMKDGLMEEGEATLRMKVTLEEGK-- 415
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIReyrgTLTEPgkNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNin 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 416 -QDPVAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYC-PVQWEYGRLNVS 493
Cdd:PRK05347 188 mRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSRLNLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 494 YTVVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPRHMV 573
Cdd:PRK05347 268 YTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 574 VLDPLKITISNF-HGDSISISVPNFPNEPEKGQHTITFNDVVYIEATDFKENEEKGFRRLTPKQSVGLKHtGVVITFQSV 652
Cdd:PRK05347 348 VLDPLKLVITNYpEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRN-AYVIKCEEV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 653 EKDSNGRITNIIA------KQEPVSDKNKPKAFIHWVS--NPSTASVRLYDRLFKHRNPEDSNEvpngFLSDINRDSKKE 724
Cdd:PRK05347 427 VKDADGNITEIHCtydpdtLSGNPADGRKVKGTIHWVSaaHAVPAEVRLYDRLFTVPNPAAGKD----FLDFLNPDSLVI 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2322523171 725 IVAYIDSSLEKVsKPLEKMQFERIGFFCVDFDTKPNKVVFNRTVTLKEDSGKI 777
Cdd:PRK05347 503 KQGFVEPSLADA-KPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
267-772 |
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: 584.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 267 VRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPN-EITYSSDNFQQL 345
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 346 YNWAVKLIEKGMAYVCHQTSDQMK---GFNPPP---SPWRERPIEESLQLFQDMKDGLMEEGEATLRMKVTLEEG---KQ 416
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPfpvMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 417 DPVAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYC-PVQWEYGRLNVSYT 495
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 496 VVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPRHMVVL 575
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 576 DPLKITISNFHGDSISISVPNFPNEPEKGQHTITFNDVVYIEATDFKENEEKGFRRLTPKQSVGLKHTgVVITFQSVEKD 655
Cdd:TIGR00440 321 DPVEVVIENLSDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 656 SNGRITNIIAKQEPV------SDKNKPKAFIHWVS--NPSTASVRLYDRLFKHRNPedsnEVPNGFLSDINRDSKKEIVA 727
Cdd:TIGR00440 400 AAGKITTIFCTYDNKtlgkepADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNP----GAPDDFLSVINPESLVIKQG 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2322523171 728 YIDSSLEKVSKPlEKMQFERIGFFCVDF-DTKPNKVVFNRTVTLKE 772
Cdd:TIGR00440 476 FMEHSLGDAVAN-KRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
265-776 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 566.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 265 GKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNE-ITYSSDNFQ 343
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEhLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 344 QLYNWAVKLIEKGMAYVCHQTSDQMK----GFNPP--PSPWRERPIEESLQLFQDMKDGLMEEGEATLRMKVTLEEGK-- 415
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEIRelrgTVTEPgtPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNmk 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 416 -QDPVAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYC--PVQWEYGRLNV 492
Cdd:PRK14703 190 lRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPprPRQYEFARLAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 493 SYTVVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPRHM 572
Cdd:PRK14703 270 GYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVM 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 573 VVLDPLKITISNFHGDSI-SISVPNFPNE-PEKGQHTITFNDVVYIEATDFKENEEKGFRRLTPKQSVGLKHTGvVITFQ 650
Cdd:PRK14703 350 AVLDPLKVVIENLPAGKVeELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRGAY-IIRCD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 651 SVEKDSNGRITNIIAKQEPVSDKN-----KPKAFIHWVSNPST--ASVRLYDRLFKHRNPEDSNEvpnGFLSDINRDSKK 723
Cdd:PRK14703 429 EVVRDADGAVTELRCTYDPESAKGedtgrKAAGVIHWVSAKHAlpAEVRLYDRLFKVPQPEAADE---DFLEFLNPDSLR 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2322523171 724 EIVAYIDSSLEKvSKPLEKMQFERIGFFCVD-FDTKPNKVVFNRTVTLKEDSGK 776
Cdd:PRK14703 506 VAQGRVEPAVRD-DPADTRYQFERQGYFWADpVDSRPDALVFNRIITLKDTWGA 558
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
251-776 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 536.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 251 NTHKLLKEHLLITGGKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGY 330
Cdd:PTZ00437 36 NTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 331 KPNEITYSSDNFQQLYNWAVKLIEKGMAYVCHQTSDQMKGF--NPPPSPWRERPIEESLQLFQDMKDGLMEEGEATLRMK 408
Cdd:PTZ00437 116 KPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 409 VTLEEGK---QDPVAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYCPVQW 485
Cdd:PTZ00437 196 ADMKSDNpnmRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 486 EYGRLNVSYTVVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLN 565
Cdd:PTZ00437 276 EFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 566 ITAPRHMVVLDPLKITISNFHGDSIsISVPNFPNEPEKGQHTITFNDVVYIEATDFK-ENEEKGFRRLTP-KQSVGLKHT 643
Cdd:PTZ00437 356 ERCERRLMVIDPIKVVVDNWKGERE-FECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPgPRVVGLKYS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 644 GVVITfQSVEKDSNGRITnIIAKQEPVSDKNKPKAFIHWVSNPSTASV--RLYDRLFKhrnpEDSNEVPNGFLSDINRDS 721
Cdd:PTZ00437 435 GNVVC-KGFEVDAAGQPS-VIHVDIDFERKDKPKTNISWVSATACTPVevRLYNALLK----DDRAAIDPEFLKFIDEDS 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2322523171 722 KKEIVAYIDSSLEKVsKPLEKMQFERIGFFCVDFDTKPNKVVFNRTVTLKEDSGK 776
Cdd:PTZ00437 509 EVVSHGYAEKGIENA-KHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
266-570 |
9.21e-155 |
|
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: 449.78 E-value: 9.21e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 266 KVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNEITYSSDNFQQL 345
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 346 YNWAVKLIEKGMAYVchqtsdqmkgfnpppspwrerpieeslqlfqdmkdglmeegeatlrmkvtleegkqdpvayriky 425
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 426 vpHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYCPVQWEYGRLNVSYTVVSKRKIAKL 505
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2322523171 506 IDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPR 570
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
266-565 |
7.30e-136 |
|
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: 404.39 E-value: 7.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 266 KVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNE-ITYSSDNFQQ 344
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYgPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 345 LYNWAVKLIEKGMAYVCHQTSDQMKGFNPP----PSPWRERPIEESLQLFQ-DMKDGLMEEGEATLRMKVTLEEGKQ--D 417
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqealGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESPYVfrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 418 PVAYRIKYVP---HHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYCPV-QWEYGRLNVS 493
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2322523171 494 YTVVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQA-TVDPEALEASVRDVLN 565
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDRKKLD 313
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
265-762 |
5.24e-94 |
|
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: 304.44 E-value: 5.24e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 265 GKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNEITYSSDNFQQ 344
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 345 LYNWAVKLIEKGMAYVCHQTSDQMKGF--NPPPSPWRERPIEESLQLFQDMKDGLMEEGEATLRMKVTLEEGK---QDPV 419
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRELrnRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNpaiRDWV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 420 AYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEF--QSRRSSYYWLCNAVDIYCPVQWEYGRLNVSYTVV 497
Cdd:TIGR00463 252 IFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 498 SKRKIaKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPRHMVVLDP 577
Cdd:TIGR00463 332 TSSAR-KGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNP 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 578 LKITISNFHGDSIsISVPNFPNEPEKGQHTITFNDVVYIEATDFKENeekgfrrltpKQSVGLKHTGVVITfqsVEKDSN 657
Cdd:TIGR00463 411 VKIEIVGLPEPKR-VERPLHPDHPEIGERVLILRGEIYVPKDDLEEG----------VEPVRLMDAVNVIY---SKKELR 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 658 gritniIAKQEPVSDKNKPKAFIHWVSNPSTASVRLYDrlFKHRNPEDSNEVpngflsdinrdskkeivayiDSSLEKVS 737
Cdd:TIGR00463 477 ------YHSEGLEGARKLGKSIIHWLPAKDAVKVKVIM--PDASIVEGVIEA--------------------DASELEVG 528
|
490 500
....*....|....*....|....*
gi 2322523171 738 KPLekmQFERIGFFCVDFDTKPNKV 762
Cdd:TIGR00463 529 DVV---QFERFGFARLDSADKDGMV 550
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
265-764 |
1.83e-91 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 297.92 E-value: 1.83e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 265 GKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPE--KEEEKFFIGIREMVEWLGYKPNEITYSSDNF 342
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDEVVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 343 QQLYNWAVKLIEKGMAYVCHQTSDQMKGF--NPPPSPWRERPIEESLQLFQDMKDGLMEEGEATLRMKVTLEEgkQDP-- 418
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKELrdAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEH--PNPsv 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 419 ---VAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQS--RRSSYywlcnavdIYCPVQWEY------ 487
Cdd:PRK04156 258 rdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntEKQRY--------IYDYFGWEYpetihy 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 488 GRLNVSYTVVSKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNIT 567
Cdd:PRK04156 330 GRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPI 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 568 APRHMVVLDPLKITISNfhGDSISISVPNFPNEPEKGQHTITFNDVVYIEATDFKEnEEKGFRrltpkqsvgLKHTGVVI 647
Cdd:PRK04156 410 ANRYFFVRDPVELEIEG--AEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEA-EGKMVR---------LMDLFNVE 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 648 tfqsVEKDSNGRITNIIAKQEpVSDKNKPKaFIHWVSNPSTASVRLydrlfkhRNPEdsNEVPNGFL-SDINRDSKKEIV 726
Cdd:PRK04156 478 ----ITGVSVDKARYHSDDLE-EARKNKAP-IIQWVPEDESVPVRV-------LKPD--GGDIEGLAePDVADLEVDDIV 542
|
490 500 510
....*....|....*....|....*....|....*...
gi 2322523171 727 ayidsslekvskplekmQFERIGFFCVDfDTKPNKVVF 764
Cdd:PRK04156 543 -----------------QFERFGFVRID-SVEDDEVVA 562
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
265-763 |
2.44e-90 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 296.10 E-value: 2.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 265 GKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYkPNEI--TYSSDNF 342
Cdd:PTZ00402 51 GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGV-SWDVgpTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 343 QQLYNWAVKLIEKGMAYVCHQTSDQMKG--FNPPPSPWRERPIEESLQLFQDMKDGLMEEGEATLRMKVTLE---EGKQD 417
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDnenKAMRD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 418 PVAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYCPVQWEYGRLNVSYTVV 497
Cdd:PTZ00402 210 PVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSVM 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 498 SKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPRHMVVLDP 577
Cdd:PTZ00402 290 SKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSNT 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 578 LKITIS-NFHGDSISISVPNFPNEPEKGQHTITFNDVVYIEATD---FKENEEkgfrrltpkqsVGLKHTGVVITFQSVE 653
Cdd:PTZ00402 370 LKVRCTvEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDvalLKEGDE-----------VTLMDWGNAYIKNIRR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 654 KDSNGRITNIIAKQEPVSDKNKPKAFIHWVSNPSTASV---RLYDRLFKHRNPeDSNEVPNGFLSDINRDSKKeivAYID 730
Cdd:PTZ00402 439 SGEDALITDADIVLHLEGDVKKTKFKLTWVPESPKAEVmelNEYDHLLTKKKP-DPEESIDDIIAPVTKYTQE---VYGE 514
|
490 500 510
....*....|....*....|....*....|...
gi 2322523171 731 SSLEKVSKPlEKMQFERIGFFCVDfDTKPNKVV 763
Cdd:PTZ00402 515 EALSVLKKG-DIIQLERRGYYIVD-DVTPKKVL 545
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
265-754 |
5.09e-90 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 298.56 E-value: 5.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 265 GKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNEITYSSDNFQQ 344
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 345 LYNWAVKLIEKGMAYVCHQTSDQMKG--FNPPPSPWRERPIEESLQLFQDMKDGlMEEG-EATLRMKVTLEEGK---QDP 418
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKerMDGIESKCRNNSVEENLRLWKEMIAG-SERGlQCCVRGKLDMQDPNkslRDP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 419 VAYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYcPVQ-WEYGRLNVSYTVV 497
Cdd:PLN02907 371 VYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFSRLNFVYTLL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 498 SKRKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPRHMVVLDP 577
Cdd:PLN02907 450 SKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKE 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 578 LKI--TISNFHGDSISISVPNFPNEPEKGQHTITFNDVVYIEATD---FKENEEkgfrrltpkqsVGLKHTGVVItFQSV 652
Cdd:PLN02907 530 GRVllTLTDGPETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADaeaISEGEE-----------VTLMDWGNAI-IKEI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 653 EKDSNGRITNIIAKQEPVSDKNKPKAFIHWVSN-PSTASVRL--YDRLFKHRNPEDSNEvpngFLSDINRDSKKEIVAYI 729
Cdd:PLN02907 598 TKDEGGAVTALSGELHLEGSVKTTKLKLTWLPDtNELVPLSLveFDYLITKKKLEEDDN----FLDVLNPCTKKETAALG 673
|
490 500
....*....|....*....|....*
gi 2322523171 730 DSSLEKVSKPlEKMQFERIGFFCVD 754
Cdd:PLN02907 674 DSNMRNLKRG-EIIQLERKGYYRCD 697
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
263-586 |
3.36e-82 |
|
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: 270.13 E-value: 3.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 263 TGGKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNE-ITYSSDN 341
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 342 FQQLYNWAVKLIEKGMAYVCHQTSDQM-------KGFNPPP---SPWRERPIEEslqlfqdmKDGLMEEGE-ATLRMKVT 410
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELealretqTAPGKPPrydGRCRDLSPEE--------LERMLAAGEpPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 411 LEE--------GKQ--------DPVAYRikyvphhRTGdqwciYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLC 474
Cdd:COG0008 153 EEGvvfddlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 475 NAVDIYCPvqwEYGRLNVSY----TVVSKRKiaklideGIVsnwddprlfTLTALRRRGFPAEAINNFCAQMGVT--GAQ 548
Cdd:COG0008 221 EALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSksDDQ 281
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2322523171 549 ATVDPEALEA--SVRDVlnitaPRHMVVLDPLKITISNFH 586
Cdd:COG0008 282 EIFSLEELIEafDLDRV-----SRSPAVFDPVKLVWLNGP 316
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
265-754 |
5.69e-79 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 263.41 E-value: 5.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 265 GKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNEITYSSDNFQQ 344
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 345 LYNWAVKLIEKGMAYVCHQTSDQMKG--FNPPPSPWRERPIEESLQLFQDMKDGLMEEGEATLRMKVTLEEGK---QDPV 419
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKerADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNgtlRDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 420 AYRIKYVPHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYCPVQWEYGRLNVSYTVVSK 499
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 500 RKIAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPRHMVV--LDP 577
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkADH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 578 LKITISNF--HGDSISISVPNFPNEPEKGQHTITFNDVVYIEATDFKEneekgfrrLTPKQSVGLKHTGvVITFQSVEKD 655
Cdd:PLN03233 330 TALTVTNAdeEADFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLLRWG-VIEISKIDGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 656 SNGRITniiakqePVSDKNKPKAFIHWVSNPSTAS-VRLY--DRLF-KHRNPEDSNevpngFLSDINRDSKKEIVAYIDS 731
Cdd:PLN03233 401 LEGHFI-------PDGDFKAAKKKISWIADVSDNIpVVLSefDNLIiKEKLEEDDK-----FEDFINPDTLAETDVIGDA 468
|
490 500
....*....|....*....|...
gi 2322523171 732 SLeKVSKPLEKMQFERIGFFCVD 754
Cdd:PLN03233 469 GL-KTLKEHDIIQLERRGFYRVD 490
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
6-163 |
2.99e-62 |
|
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: 205.87 E-value: 2.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 6 EDIKLFQTIGLSEQKAKETLKNAQVTKHLKSAISEASKHGVLNNENGILLYHLASKVKVQIADKLPFMSESIVKKKLDTI 85
Cdd:pfam04558 2 ELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 86 QRVDAALNYFLSNIKESIDIKAFEDACGVGIEITQEQIKNAVNVIIEKNKNEIIEKRYRFNAGPLMQKIRN--DLKWADG 163
Cdd:pfam04558 82 LQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKlpELKWADP 161
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
266-570 |
7.94e-53 |
|
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: 183.32 E-value: 7.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 266 KVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPE--KEEEKFFIGIREMVEWLGYKPNEITYSSDNFQ 343
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 344 QLYNWAVKLIEKGMAYVchqtsdqmkgfnpppspwrerpieeslqlfqdmkdglmeegeatlrmkvtleegkqdpvayri 423
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 424 kyvpHHRTGDQWCIYPTYDFTHCLCDSIEHITHSLCTKEFQS--RRSSYYWLCNAVDIycPVQWEYGRLNVSYTVVSKRK 501
Cdd:cd09287 98 ----HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntEKQRYIYEYFGWEY--PETIHWGRLKIEGGKLSTSK 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2322523171 502 IAKLIDEGIVSNWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQATVDPEALEASVRDVLNITAPR 570
Cdd:cd09287 172 IRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
266-565 |
2.52e-49 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 173.43 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 266 KVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNE-ITYSSDNFQQ 344
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEgPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 345 LYNWAVKLIEKGmayvchqtsdqmkgfnpppspwrerpieeslqlfqdmkdglmeegeatlrmkvtleegkqdpvayrik 424
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 425 yvphhrtgdqwcIYPTYDFTHCLCDSIEHITHSLCTKEFQSRRSSYYWLCNAVDIYCPVQWEYGRLNVSY-TVVSKRKIA 503
Cdd:cd00418 93 ------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDgTKLSKRKLN 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 504 KlidegivsnwddprlfTLTALRRRGFPAEAINNFCAQMGVT-----------------------GAQATVDPEALEASV 560
Cdd:cd00418 161 T----------------TLRALRRRGYLPEALRNYLALIGWSkpdghelftleemiaafsvervnSADATFDWAKLEWLN 224
|
....*
gi 2322523171 561 RDVLN 565
Cdd:cd00418 225 REYIR 229
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
568-754 |
1.32e-48 |
|
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: 169.37 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 568 APRHMVVLDPLKITISNF-HGDSISISVPNFPNEPEKGQHTITFNDVVYIEATDFKeneekgfrRLTPKQSVGLKHTGvV 646
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYpEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDFK--------RLAPGEEVRLMDAY-N 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 647 ITFQSVEKDSNGRITNIIAKQEP--VSDKNKPKA-FIHWVS--NPSTASVRLYDRLFKHRNPEDsnevpngFLsdINRDS 721
Cdd:pfam03950 72 IKVTEVVKDEDGNVTELHCTYDGddLGGARKVKGkIIHWVSasDAVPAEVRLYDRLFKDEDDAD-------FL--LNPDS 142
|
170 180 190
....*....|....*....|....*....|....
gi 2322523171 722 KKEIV-AYIDSSLEKVsKPLEKMQFERIGFFCVD 754
Cdd:pfam03950 143 LKVLTeGLAEPALANL-KPGDIVQFERIGYFRVD 175
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
167-257 |
2.52e-19 |
|
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: 83.13 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 167 KIEFDSQLFELLGEKTEADLMPIVKDGKNKQKSQEKEKKKsdkekneiVKDKIDAQTISELMKT---KVNFHKPGENYKT 243
Cdd:pfam04557 2 KNEVDEQILDLLGPKTEADLKKPPKKKKKAKKKKAAKKKK--------KKAPIEEEENKRSMFSegfLGKFHKPGENPKT 73
|
90
....*....|....
gi 2322523171 244 EGYVVTENTHKLLK 257
Cdd:pfam04557 74 DGYVVTEHTMRLLK 87
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
266-356 |
3.44e-11 |
|
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: 64.14 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 266 KVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPNEIT--------- 336
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPdvggpygpy 80
|
90 100
....*....|....*....|
gi 2322523171 337 YSSDNFQQLYNWAVKLIEKG 356
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
263-369 |
3.79e-09 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 59.76 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 263 TGGKVRTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPE---KEEEKFFigIREMvEWLG---------- 329
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLArstKESEEAV--LRDL-KWLGldwdegpdvg 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2322523171 330 --YKPneitYSSDNFQQLY-NWAVKLIEKGMAYVCHQTS---DQMK 369
Cdd:PLN02627 119 geYGP----YRQSERNAIYkQYAEKLLESGHVYPCFCTDeelEAMK 160
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
269-369 |
2.83e-07 |
|
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: 50.56 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 269 TRFPPEPNGILHIGHAKAININFGYAAA-----YGGTCNLRYDDTNP------------EKEEEKFFIG-IREMVEWLgy 330
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGligdpankkgenAKAFVERWIErIKEDVEYM-- 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 2322523171 331 kpneityssdnFQQLYNWAVKLIEKGMAYVChqTSDQMK 369
Cdd:cd00802 80 -----------FLQAADFLLLYETECDIHLG--GSDQLG 105
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
268-364 |
1.27e-06 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 51.00 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322523171 268 RTRFPPEPNGILHIGHAKAININFGYAAAYGGTCNLRYDDTNPEKEEEKFFIGIREMVEWLGYKPN-EITYSSDNFqQLY 346
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDgPVLYQSQRH-DAY 85
|
90
....*....|....*....
gi 2322523171 347 NWAV-KLIEKGMAYVCHQT 364
Cdd:PRK05710 86 RAALdRLRAQGLVYPCFCS 104
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
269-318 |
3.47e-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: 37.90 E-value: 3.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2322523171 269 TRFPPEPnGILHIGHAKAININFGYAaaygGTCNLRYDDTNPEKEEEKFF 318
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPH 46
|
|
| |
