|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
1-754 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 806.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 1 MEASVELFTSVGLSKLKAEETLKNKAIAARLAIIIHEARSLSdvEIDSGVGNLLYQIATE-----LRNQSKtsyLLQYVC 75
Cdd:PLN02859 5 SEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTN--GCDKTVGNLLYTVATKypanaLVHRPT---LLSYIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 76 RKEINNKSQLSAAMAYFVDNPTSPIDDVKFKAACGIGITVTPEETKAVVSQIINKHKNDILSCRYKFNFGTLIFEARDKL 155
Cdd:PLN02859 80 SSKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 156 KWADGRSVKSEIDSQVHALLGPKTAED---------KSSVKVIMTLSCKILKLTFSNSLScEYLIlnFHKPGENYK---- 222
Cdd:PLN02859 160 PWADPKIVKKLIDKKLYELLGEKTAADnekpvkkkkEKPAKVEEKKVAVAAAPPSEEELN-PYSI--FPQPEENFKvhte 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 223 ---TDGYVV-TNKTMDILQHHLNYTGGQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYF 298
Cdd:PLN02859 237 vffSDGSVLrPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 299 VGILEAVRWLGYEPYKVTHSSDYFEELYHYAIELINRDLAYVCHQSVDDIKGY--SPLPSPWRDRPIEESLILFEDMKNG 376
Cdd:PLN02859 317 DHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDMRRG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 377 KIDEGKATLRMKMTLEDGK---ADPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWL 453
Cdd:PLN02859 397 LIEEGKATLRMKQDMQNDNfnmYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 454 CNAVDVYCPVQWEYGRLNLPYTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQ-VTID 532
Cdd:PLN02859 477 LDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDnSLIR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 533 TQLLESCVREELNLTAPRIMAVLDPLKVSIVNFPEPKNLILSV---PDFPQDSSKGNHNIVFSNVIYIERGDFKKTAGEN 609
Cdd:PLN02859 557 MDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKD 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 610 FHRLTENQYVGLRHtGYAIMVQDIVMNDKN-NIEELLVVAKPISDIrKPKAFIHWVSE------PLTCEVRIYERLFKHA 682
Cdd:PLN02859 637 YYGLAPGKSVLLRY-AFPIKCTDVVLADDNeTVVEIRAEYDPEKKT-KPKGVLHWVAEpspgvePLKVEVRLFDKLFLSE 714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195998099 683 NPAEVPgGFLNDINENSLHVFGNALIDSTTANAAVGSQFQFERMGYFCVDRDSTRDKLVFNQIIKLREDFTK 754
Cdd:PLN02859 715 NPAELE-DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
247-752 |
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: 559.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 247 VRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEP-YKVTHSSDYFEEL 325
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 326 YHYAIELINRDLAYVCHQSVDDIKGYSPL------PSPWRDRPIEESLILFEDMKNGKIDEGKATLRMKMTLEDGKA--- 396
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTltdpgkNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 397 DPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYC-PVQWEYGRLNLPYT 475
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 476 VVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNLTAPRIMAVL 555
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 556 DPLKVSIVNFpEPKNLILSVPDFPQDSSKGNHNIVFSNVIYIERGDFKKTAGENFHRLTENQYVGLRHTgYAIMVQDIVM 635
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 636 NDKNNIEELL------VVAKPISDIRKPKAFIHWVS--EPLTCEVRIYERLFKHANPAEvPGGFLNDINENSLhVFGNAL 707
Cdd:TIGR00440 399 DAAGKITTIFctydnkTLGKEPADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNPGA-PDDFLSVINPESL-VIKQGF 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 195998099 708 IDSTTANAAVGSQFQFERMGYFCVD-RDSTRDKLVFNQIIKLREDF 752
Cdd:TIGR00440 477 MEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
246-550 |
5.48e-146 |
|
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: 426.67 E-value: 5.48e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 246 QVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEPYKVTHSSDYFEEL 325
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 326 YHYAIELINRDLAYVchqsvddikgysplpspwrdrpieeslilfedmkngkidegkatlrmkmtledgkadpvayrikf 405
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 406 tHHaRSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYCPVQWEYGRLNLPYTVVSKRKIVQL 485
Cdd:cd00807 96 -HH-RTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 195998099 486 IKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNLTAPR 550
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
246-545 |
2.37e-134 |
|
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: 399.77 E-value: 2.37e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 246 QVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEP-YKVTHSSDYFEE 324
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 325 LYHYAIELINRDLAYVCHQSVDDIKGY----SPLPSPWRDRPIEESLILF-EDMKNGKIDEGKATLRMKMTLEDGKA--D 397
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEreeqEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESPYVfrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 398 PVAYRIKFT---HHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYCPV-QWEYGRLNLP 473
Cdd:pfam00749 161 PVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 195998099 474 YTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQ-VTIDTQLLESCVREELN 545
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
243-571 |
8.22e-81 |
|
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: 265.89 E-value: 8.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 243 TGGQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYE----PYkvtHS 318
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 319 SDYFEELYHYAIELINRDLAYVCHQSVDDIK-------------GYSplpSPWRDRPIEEslilfedmKNGKIDEG-KAT 384
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEalretqtapgkppRYD---GRCRDLSPEE--------LERMLAAGePPV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 385 LRMKMTLED--------GKA--------DPVAYRikfthhaRSGnkwciYPTYDYTHCLCDSLEHITHSLCTKEFQSRRS 448
Cdd:COG0008 147 LRFKIPEEGvvfddlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 449 SYYWLCNAVDVYCPvqwEYGRLNLPY----TVVSKRkivqlikHGIVkswddprlfTLSALRRRGFPPAAINRFCAKVGV 524
Cdd:COG0008 215 RQIWLYEALGWEPP---EFAHLPLILgpdgTKLSKR-------KGAV---------TVSGLRRRGYLPEAIRNYLALLGW 275
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 195998099 525 TMA--QVTIDTQLLESCVreELNLTaPRIMAVLDPLKVSIVNFPEPKNL 571
Cdd:COG0008 276 SKSddQEIFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAL 321
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
1-754 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 806.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 1 MEASVELFTSVGLSKLKAEETLKNKAIAARLAIIIHEARSLSdvEIDSGVGNLLYQIATE-----LRNQSKtsyLLQYVC 75
Cdd:PLN02859 5 SEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTN--GCDKTVGNLLYTVATKypanaLVHRPT---LLSYIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 76 RKEINNKSQLSAAMAYFVDNPTSPIDDVKFKAACGIGITVTPEETKAVVSQIINKHKNDILSCRYKFNFGTLIFEARDKL 155
Cdd:PLN02859 80 SSKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 156 KWADGRSVKSEIDSQVHALLGPKTAED---------KSSVKVIMTLSCKILKLTFSNSLScEYLIlnFHKPGENYK---- 222
Cdd:PLN02859 160 PWADPKIVKKLIDKKLYELLGEKTAADnekpvkkkkEKPAKVEEKKVAVAAAPPSEEELN-PYSI--FPQPEENFKvhte 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 223 ---TDGYVV-TNKTMDILQHHLNYTGGQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYF 298
Cdd:PLN02859 237 vffSDGSVLrPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 299 VGILEAVRWLGYEPYKVTHSSDYFEELYHYAIELINRDLAYVCHQSVDDIKGY--SPLPSPWRDRPIEESLILFEDMKNG 376
Cdd:PLN02859 317 DHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDMRRG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 377 KIDEGKATLRMKMTLEDGK---ADPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWL 453
Cdd:PLN02859 397 LIEEGKATLRMKQDMQNDNfnmYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 454 CNAVDVYCPVQWEYGRLNLPYTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQ-VTID 532
Cdd:PLN02859 477 LDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDnSLIR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 533 TQLLESCVREELNLTAPRIMAVLDPLKVSIVNFPEPKNLILSV---PDFPQDSSKGNHNIVFSNVIYIERGDFKKTAGEN 609
Cdd:PLN02859 557 MDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKD 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 610 FHRLTENQYVGLRHtGYAIMVQDIVMNDKN-NIEELLVVAKPISDIrKPKAFIHWVSE------PLTCEVRIYERLFKHA 682
Cdd:PLN02859 637 YYGLAPGKSVLLRY-AFPIKCTDVVLADDNeTVVEIRAEYDPEKKT-KPKGVLHWVAEpspgvePLKVEVRLFDKLFLSE 714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195998099 683 NPAEVPgGFLNDINENSLHVFGNALIDSTTANAAVGSQFQFERMGYFCVDRDSTRDKLVFNQIIKLREDFTK 754
Cdd:PLN02859 715 NPAELE-DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
245-755 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 690.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 245 GQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEP-YKVTHSSDYFE 323
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWsGELRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 324 ELYHYAIELINRDLAYVCHQSVDDIKGY-----SP-LPSPWRDRPIEESLILFEDMKNGKIDEGKATLRMK-------MT 390
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIREYrgtltEPgKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKidmaspnIN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 391 LEDgkadPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYC-PVQWEYGR 469
Cdd:PRK05347 188 MRD----PVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 470 LNLPYTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNLTAP 549
Cdd:PRK05347 264 LNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 550 RIMAVLDPLKVSIVNFPEPKNLILSVPDFPQDSSKGNHNIVFSNVIYIERGDFKKTAGENFHRLTENQYVGLRHtGYAIM 629
Cdd:PRK05347 344 RAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRN-AYVIK 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 630 VQDIVMNDKNNIEELLVV------AKPISDIRKPKAFIHWVSEP--LTCEVRIYERLFKHANPAEVpGGFLNDINENSLH 701
Cdd:PRK05347 423 CEEVVKDADGNITEIHCTydpdtlSGNPADGRKVKGTIHWVSAAhaVPAEVRLYDRLFTVPNPAAG-KDFLDFLNPDSLV 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 195998099 702 VFgNALIDSTTANAAVGSQFQFERMGYFCVDRDSTRDKLVFNQIIKLREDFTKE 755
Cdd:PRK05347 502 IK-QGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
247-752 |
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: 559.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 247 VRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEP-YKVTHSSDYFEEL 325
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 326 YHYAIELINRDLAYVCHQSVDDIKGYSPL------PSPWRDRPIEESLILFEDMKNGKIDEGKATLRMKMTLEDGKA--- 396
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTltdpgkNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 397 DPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYC-PVQWEYGRLNLPYT 475
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 476 VVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNLTAPRIMAVL 555
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 556 DPLKVSIVNFpEPKNLILSVPDFPQDSSKGNHNIVFSNVIYIERGDFKKTAGENFHRLTENQYVGLRHTgYAIMVQDIVM 635
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 636 NDKNNIEELL------VVAKPISDIRKPKAFIHWVS--EPLTCEVRIYERLFKHANPAEvPGGFLNDINENSLhVFGNAL 707
Cdd:TIGR00440 399 DAAGKITTIFctydnkTLGKEPADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNPGA-PDDFLSVINPESL-VIKQGF 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 195998099 708 IDSTTANAAVGSQFQFERMGYFCVD-RDSTRDKLVFNQIIKLREDF 752
Cdd:TIGR00440 477 MEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
245-755 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 540.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 245 GQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYE-PYKVTHSSDYFE 323
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 324 ELYHYAIELINRDLAYVCHQSVDDIKGY-----SP-LPSPWRDRPIEESLILFEDMKNGKIDEGKATLRMKMTLEDGKA- 396
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEIRELrgtvtEPgTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMk 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 397 --DPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYC--PVQWEYGRLNL 472
Cdd:PRK14703 190 lrDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPprPRQYEFARLAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 473 PYTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNLTAPRIM 552
Cdd:PRK14703 270 GYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVM 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 553 AVLDPLKVSIVNFPEPKNLILSVPDFPQDSSK-GNHNIVFSNVIYIERGDFKKTAGENFHRLTENQYVGLRHtGYAIMVQ 631
Cdd:PRK14703 350 AVLDPLKVVIENLPAGKVEELDLPYWPHDVPKeGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRG-AYIIRCD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 632 DIVMNDKNNIEELLVV-----AKPISDIRKPKAFIHWVS--EPLTCEVRIYERLFKHANPAEVPGGFLNDINENSLHVFG 704
Cdd:PRK14703 429 EVVRDADGAVTELRCTydpesAKGEDTGRKAAGVIHWVSakHALPAEVRLYDRLFKVPQPEAADEDFLEFLNPDSLRVAQ 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 195998099 705 NaLIDSTTANAAVGSQFQFERMGYFCVD-RDSTRDKLVFNQIIKLREDFTKE 755
Cdd:PRK14703 509 G-RVEPAVRDDPADTRYQFERQGYFWADpVDSRPDALVFNRIITLKDTWGAR 559
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
232-754 |
1.15e-164 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 487.57 E-value: 1.15e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 232 TMDILQHHLNYTGGQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYE 311
Cdd:PTZ00437 37 TPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 312 PYKVTHSSDYFEELYHYAIELINRDLAYVCHQSVDDIKGY--SPLPSPWRDRPIEESLILFEDMKNGKIDEGKATLRMKM 389
Cdd:PTZ00437 117 PDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 390 TLEDGKA---DPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYCPVQWE 466
Cdd:PTZ00437 197 DMKSDNPnmrDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 467 YGRLNLPYTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNL 546
Cdd:PTZ00437 277 FSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 547 TAPRIMAVLDPLKVSIVNFpePKNLILSVPDFPQDSSKGNHNIVFSNVIYIERGDFKKTAGEN-FHRLTEN-QYVGLRHT 624
Cdd:PTZ00437 357 RCERRLMVIDPIKVVVDNW--KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRTEDNNSkFYGLAPGpRVVGLKYS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 625 GyaimvqDIVMN----DKNNIEELLVVAKPISDIRKPKAFIHWVSEP--LTCEVRIYERLFKHaNPAEVPGGFLNDINEN 698
Cdd:PTZ00437 435 G------NVVCKgfevDAAGQPSVIHVDIDFERKDKPKTNISWVSATacTPVEVRLYNALLKD-DRAAIDPEFLKFIDED 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 195998099 699 SlHVFGNALIDSTTANAAVGSQFQFERMGYFCVDRDSTRDKLVFNQIIKLREDFTK 754
Cdd:PTZ00437 508 S-EVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
246-550 |
5.48e-146 |
|
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: 426.67 E-value: 5.48e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 246 QVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEPYKVTHSSDYFEEL 325
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 326 YHYAIELINRDLAYVchqsvddikgysplpspwrdrpieeslilfedmkngkidegkatlrmkmtledgkadpvayrikf 405
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 406 tHHaRSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYCPVQWEYGRLNLPYTVVSKRKIVQL 485
Cdd:cd00807 96 -HH-RTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 195998099 486 IKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNLTAPR 550
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
246-545 |
2.37e-134 |
|
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: 399.77 E-value: 2.37e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 246 QVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEP-YKVTHSSDYFEE 324
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 325 LYHYAIELINRDLAYVCHQSVDDIKGY----SPLPSPWRDRPIEESLILF-EDMKNGKIDEGKATLRMKMTLEDGKA--D 397
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEreeqEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESPYVfrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 398 PVAYRIKFT---HHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYCPV-QWEYGRLNLP 473
Cdd:pfam00749 161 PVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 195998099 474 YTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQ-VTIDTQLLESCVREELN 545
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLD 313
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
245-732 |
1.08e-86 |
|
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: 284.41 E-value: 1.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 245 GQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEPYKVTHSSDYFEE 324
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 325 LYHYAIELINRDLAYVCHQSVDDIKGY--SPLPSPWRDRPIEESLILFEDMKNGKIDEGKATLRMKMtleDGKA------ 396
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRELrnRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKT---DLKHknpair 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 397 DPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEF--QSRRSSYYWLCNAVDVYCPVQWEYGRLNLPY 474
Cdd:TIGR00463 249 DWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 475 TVVSKRKIvQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNLTAPRIMAV 554
Cdd:TIGR00463 329 ALSTSSAR-KGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFI 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 555 LDPLKVSIVNFPEPKnlILSVPDFPQDSSKGNHNIVFSNVIYIERGDFkktaGENFHRLTENQYVGLRHTGYAIMVQdiv 634
Cdd:TIGR00463 408 WNPVKIEIVGLPEPK--RVERPLHPDHPEIGERVLILRGEIYVPKDDL----EEGVEPVRLMDAVNVIYSKKELRYH--- 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 635 mndKNNIEEllvvakpisDIRKPKAFIHWVSEpltcevriyerlfKHANPAEVpggflndINENSLHVFGnaLIDSTTAN 714
Cdd:TIGR00463 479 ---SEGLEG---------ARKLGKSIIHWLPA-------------KDAVKVKV-------IMPDASIVEG--VIEADASE 524
|
490
....*....|....*...
gi 195998099 715 AAVGSQFQFERMGYFCVD 732
Cdd:TIGR00463 525 LEVGDVVQFERFGFARLD 542
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
241-741 |
2.94e-85 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 281.85 E-value: 2.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 241 NYTGGQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYePYKV--THS 318
Cdd:PTZ00402 47 NAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGV-SWDVgpTYS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 319 SDYFEELYHYAIELINRDLAYVCHQSVDDIKG--YSPLPSPWRDRPIEESLILFEDMKNGKiDEGKAT-LRMKMTLED-G 394
Cdd:PTZ00402 126 SDYMDLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNeN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 395 KA--DPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYCPVQWEYGRLNL 472
Cdd:PTZ00402 205 KAmrDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNM 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 473 PYTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVT-----MAQVTI---DTQLLEScvreel 544
Cdd:PTZ00402 285 EYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSktvnfMEWSKLwyfNTQILDP------ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 545 nlTAPRIMAVLDPLKV-----SIVNFPEPKNLIlsvpdFPQDSSKGNHNIVFSNVIYIErgdfkktaGENFHRLTENQYV 619
Cdd:PTZ00402 359 --SVPRYTVVSNTLKVrctveGQIHLEACEKLL-----HKKVPDMGEKTYYKSDVIFLD--------AEDVALLKEGDEV 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 620 GLRHTGYAiMVQDIVMNDKNN-IEELLVVAKPISDIRKPKAFIHWVSE---PLTCEVRIYERLF--KHANPAEVPGGFLN 693
Cdd:PTZ00402 424 TLMDWGNA-YIKNIRRSGEDAlITDADIVLHLEGDVKKTKFKLTWVPEspkAEVMELNEYDHLLtkKKPDPEESIDDIIA 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 195998099 694 DINENSLHVFGnaliDSTTANAAVGSQFQFERMGYFCVDRDSTRDKLV 741
Cdd:PTZ00402 503 PVTKYTQEVYG----EEALSVLKKGDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
243-571 |
8.22e-81 |
|
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: 265.89 E-value: 8.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 243 TGGQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYE----PYkvtHS 318
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 319 SDYFEELYHYAIELINRDLAYVCHQSVDDIK-------------GYSplpSPWRDRPIEEslilfedmKNGKIDEG-KAT 384
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEalretqtapgkppRYD---GRCRDLSPEE--------LERMLAAGePPV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 385 LRMKMTLED--------GKA--------DPVAYRikfthhaRSGnkwciYPTYDYTHCLCDSLEHITHSLCTKEFQSRRS 448
Cdd:COG0008 147 LRFKIPEEGvvfddlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 449 SYYWLCNAVDVYCPvqwEYGRLNLPY----TVVSKRkivqlikHGIVkswddprlfTLSALRRRGFPPAAINRFCAKVGV 524
Cdd:COG0008 215 RQIWLYEALGWEPP---EFAHLPLILgpdgTKLSKR-------KGAV---------TVSGLRRRGYLPEAIRNYLALLGW 275
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 195998099 525 TMA--QVTIDTQLLESCVreELNLTaPRIMAVLDPLKVSIVNFPEPKNL 571
Cdd:COG0008 276 SKSddQEIFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAL 321
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
241-742 |
2.76e-78 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 262.09 E-value: 2.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 241 NYTGGQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPE---VEEEEYFVgILEAVRWLGYEPYKVTH 317
Cdd:PRK04156 96 NAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkrPDPEAYDM-ILEDLKWLGVKWDEVVI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 318 SSDYFEELYHYAIELINRDLAYVCHQSVDDIKGY--SPLPSPWRDRPIEESLILFEDMKNGKIDEGKATLRMKMTLEDgk 395
Cdd:PRK04156 175 QSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELrdAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEH-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 396 ADP-----VAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQS--RRSSYywlcnavdVYCPVQWEY- 467
Cdd:PRK04156 253 PNPsvrdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntEKQRY--------IYDYFGWEYp 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 468 -----GRLNLPYTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVRE 542
Cdd:PRK04156 325 etihyGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 543 ELNLTAPRIMAVLDPLKVSIVNFPEpknLILSVPDFPQDSSKGNHNIVFSNVIYIERGDFKKtAGENFhRLTEnqYVGLR 622
Cdd:PRK04156 405 LIDPIANRYFFVRDPVELEIEGAEP---LEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEA-EGKMV-RLMD--LFNVE 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 623 HTGyaimvqdivmndkNNIEELLVVAKPISDIRKPKA-FIHWV--SEPLTCEVRIyerlfkhANPAEVPGgflndinens 699
Cdd:PRK04156 478 ITG-------------VSVDKARYHSDDLEEARKNKApIIQWVpeDESVPVRVLK-------PDGGDIEG---------- 527
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 195998099 700 lhvfgnaLIDSTTANAAVGSQFQFERMGYFCVDrDSTRDKLVF 742
Cdd:PRK04156 528 -------LAEPDVADLEVDDIVQFERFGFVRID-SVEDDEVVA 562
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
245-733 |
2.07e-74 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 255.80 E-value: 2.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 245 GQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEPYKVTHSSDYFEE 324
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 325 LYHYAIELINRDLAYV--------CHQSVDDIKgysplpSPWRDRPIEESLILFEDMKNGKIDEGKATLRMKMTLEDGKA 396
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVddtpreqmRKERMDGIE------SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNK 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 397 ---DPVAYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYcPVQ-WEYGRLNL 472
Cdd:PLN02907 366 slrDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFSRLNF 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 473 PYTVVSKRKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFcakvgvtmaqvtidtqLLESCVREELNL------ 546
Cdd:PLN02907 445 VYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQF----------------ILSQGASKNLNLmewdkl 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 547 ----------TAPRIMAVLDPLKV--SIVNFPEpKNLILSVPDFPQDSSKGNHNIVFSNVIYIERGDFKKtagenfhrLT 614
Cdd:PLN02907 509 wtinkkiidpVCPRHTAVLKEGRVllTLTDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------IS 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 615 ENQYVGLRHTGYAImVQDIVMNDKNNIEELLVVAKPISDIRKPKAFIHW---VSEPLTCEVRIYERLFKHANPAEvPGGF 691
Cdd:PLN02907 580 EGEEVTLMDWGNAI-IKEITKDEGGAVTALSGELHLEGSVKTTKLKLTWlpdTNELVPLSLVEFDYLITKKKLEE-DDNF 657
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 195998099 692 LNDINENSLHVFGnALIDSTTANAAVGSQFQFERMGYFCVDR 733
Cdd:PLN02907 658 LDVLNPCTKKETA-ALGDSNMRNLKRGEIIQLERKGYYRCDA 698
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
245-733 |
5.18e-71 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 241.45 E-value: 5.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 245 GQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEPYKVTHSSDYFEE 324
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 325 LYHYAIELINRDLAYVCHQSVDDIKG--YSPLPSPWRDRPIEESLILFEDMKNGKIDEGKATLRMK--MTLEDGKA-DPV 399
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKerADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKidMQSDNGTLrDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 400 AYRIKFTHHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYCPVQWEYGRLNLPYTVVSK 479
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 480 RKIVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNLTAPRIMAV--LDP 557
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkADH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 558 LKVSIVNFPEPKNLILSVPDF-PQDSSKGNHNIVFSNVIYIERGDfkktagenfhrlTENQYVGlrhtgyaimvQDIVMN 636
Cdd:PLN03233 330 TALTVTNADEEADFAFSETDChPKDPGFGKRAMRICDEVLLEKAD------------TEDIQLG----------EDIVLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 637 DKNNIEellvVAK----------PISDIRKPKAFIHWVSEPLT-CEVRIYErlFKH---ANPAEVPGGFLNDINENSL-- 700
Cdd:PLN03233 388 RWGVIE----ISKidgdleghfiPDGDFKAAKKKISWIADVSDnIPVVLSE--FDNliiKEKLEEDDKFEDFINPDTLae 461
|
490 500 510
....*....|....*....|....*....|....
gi 195998099 701 -HVFGNALIDSTTANAAVgsqfQFERMGYFCVDR 733
Cdd:PLN03233 462 tDVIGDAGLKTLKEHDII----QLERRGFYRVDR 491
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
548-732 |
1.56e-53 |
|
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: 182.47 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 548 APRIMAVLDPLKVSIVNFPEPKNLILSVPDFPQDSSKGNHNIVFSNVIYIERGDFKktagenfhRLTENQYVGLRHtGYA 627
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDFK--------RLAPGEEVRLMD-AYN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 628 IMVQDIVMNDKNNIEELLVVAKP--ISDIRKPKA-FIHWVS--EPLTCEVRIYERLFKHANPAEvpggFLndINENSLHV 702
Cdd:pfam03950 72 IKVTEVVKDEDGNVTELHCTYDGddLGGARKVKGkIIHWVSasDAVPAEVRLYDRLFKDEDDAD----FL--LNPDSLKV 145
|
170 180 190
....*....|....*....|....*....|
gi 195998099 703 FGNALIDSTTANAAVGSQFQFERMGYFCVD 732
Cdd:pfam03950 146 LTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
2-160 |
6.90e-51 |
|
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: 174.67 E-value: 6.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 2 EASVELFTSVGLSKLKAEETLKNKAIAARLAIIIHEARSlsDVEIDSGVGNLLYQIATELRNQS--KTSYLLQYVCRKEI 79
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGV--ESGCDKKQGNLLYTLATKLKGNAlpHRPYLVKYIVDGKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 80 NNKSQLSAAMAYFVDNPTSPIDDVKFKAACGIGITVTPEETKAVVSQIINKHKNDILSCRYKFNFGTLIFEAR--DKLKW 157
Cdd:pfam04558 79 KTTLQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRklPELKW 158
|
...
gi 195998099 158 ADG 160
Cdd:pfam04558 159 ADP 161
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
247-545 |
1.59e-48 |
|
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: 170.73 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 247 VRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYE----PYKvthSSDYF 322
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPYR---QSDRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 323 EELYHYAIELINRDlayvchqsvddikgysplpspwrdrpieeslilfedmkngkidegkatlrmkmtledgkadpvayr 402
Cdd:cd00418 79 DLYRAYAEELIKKG------------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 403 ikfthharsgnkwcIYPTYDYTHCLCDSLEHITHSLCTKEFQSRRSSYYWLCNAVDVYCPVQWEYGRLNLPY-TVVSKRK 481
Cdd:cd00418 93 --------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDgTKLSKRK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 482 IVQlikhgivkswddprlfTLSALRRRGFPPAAINRFCAKVGVTMAQ-----------------------VTIDTQLLES 538
Cdd:cd00418 159 LNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDghelftleemiaafsvervnsadATFDWAKLEW 222
|
....*..
gi 195998099 539 CVREELN 545
Cdd:cd00418 223 LNREYIR 229
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
246-550 |
4.64e-45 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 161.75 E-value: 4.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 246 QVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEV--EEEEYFVGILEAVRWLGYEPYKVTHSSDYFE 323
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTkrPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 324 ELYHYAIELINRDLAYVchqsvddikgysplpspwrdrpieeslilfedmkngkidegkatlrmkmtledgkadpvayri 403
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 404 kfthHARSGNKWCIYPTYDYTHCLCDSLEHITHSLCTKEFQS--RRSSYYWLCNAVDVycPVQWEYGRLNLPYTVVSKRK 481
Cdd:cd09287 98 ----HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntEKQRYIYEYFGWEY--PETIHWGRLKIEGGKLSTSK 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195998099 482 IVQLIKHGIVKSWDDPRLFTLSALRRRGFPPAAINRFCAKVGVTMAQVTIDTQLLESCVREELNLTAPR 550
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 ... |
163-237 |
2.69e-17 |
|
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: 77.35 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 163 VKSEIDSQVHALLGPKTAED-------------KSSVKVIMTLSCKILKLTFSNSLScEYLILNFHKPGENYKTDGYVVT 229
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADlkkppkkkkkakkKKAAKKKKKKAPIEEEENKRSMFS-EGFLGKFHKPGENPKTDGYVVT 79
|
....*...
gi 195998099 230 NKTMDILQ 237
Cdd:pfam04557 80 EHTMRLLK 87
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
247-348 |
1.09e-16 |
|
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: 79.94 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 247 VRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLG------------YEPYK 314
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldwdegpdvggpYGPYR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 195998099 315 vthSSDYFeELYH-YAIELINRD-------LAYVchqsVDDI 348
Cdd:cd00808 82 ---QSERL-EIYRkYAEKLLEKGdgfptyhLANV----VDDH 115
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
246-355 |
1.01e-11 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 66.41 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 246 QVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLGYEPYK-VTHSSDYFeE 324
Cdd:PRK05710 5 PYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGpVLYQSQRH-D 83
|
90 100 110
....*....|....*....|....*....|..
gi 195998099 325 LYHYAIE-LINRDLAYVCHQSVDDIKGYSPLP 355
Cdd:PRK05710 84 AYRAALDrLRAQGLVYPCFCSRKEIAAAAPAP 115
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
243-341 |
7.46e-10 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 62.07 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 243 TGGQVRTRFPPEPNGILHIGHAKAINFNFCYAKANNGICFLRYDDTNPEVEEEEYFVGILEAVRWLG------------Y 310
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldwdegpdvggeY 121
|
90 100 110
....*....|....*....|....*....|.
gi 195998099 311 EPYKVTHSSDYFEElyhYAIELINRDLAYVC 341
Cdd:PLN02627 122 GPYRQSERNAIYKQ---YAEKLLESGHVYPC 149
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
249-339 |
3.08e-04 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 41.70 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195998099 249 TRFPPEPNGILHIGHAKAINFNFCYAKANN-----GICFLRYDDTNPeveeeeyFVGILEAVRWLGYEPYkVTHSSDYFE 323
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGG-------LIGDPANKKGENAKAF-VERWIERIK 73
|
90
....*....|....*.
gi 195998099 324 ELYHYAIELINRDLAY 339
Cdd:cd00802 74 EDVEYMFLQAADFLLL 89
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
249-298 |
8.07e-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: 36.75 E-value: 8.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 195998099 249 TRFPPEPnGILHIGHAKAInfnfCYAKANNGICFLRYDDTNPEVEEEEYF 298
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLI----CRAKGIADQCVVRIDDNPPVKVWQDPH 46
|
|
| |
