|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
10-777 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 836.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 10 FQALGMSEQKAKETLKNANVTKNLQLSLAAAGSATLSDGT-GMLIYHMATKLKPQTADHLPLLVRYIVEHKLDNTQRVDA 88
Cdd:PLN02859 12 FLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTvGNLLYTVATKYPANALVHRPTLLSYIVSSKIKTPAQLEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 89 ALEYLLKCGQSlnaNIDLQALEKECGVGVVVTPEQIERTVQAKIKASyKEALLEQRYHFNSFKILQDVRGELKWADAKSV 168
Cdd:PLN02859 92 AFSFFSSTGPE---SFDLNKFEEACGVGVVVSPEDIEAAVNEVFEEN-KEKILEQRYRTNVGDLLGQVRKRLPWADPKIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 169 KAAIDVEIFDLLGPKTEADL-KPQTKANDKP-KAAKPKAEVTPAAQTAEAASDGATTISELMKTKVHFhapgENFKADGY 246
Cdd:PLN02859 168 KKLIDKKLYELLGEKTAADNeKPVKKKKEKPaKVEEKKVAVAAAPPSEEELNPYSIFPQPEENFKVHT----EVFFSDGS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 247 VVTEH-TERLLKEHLARTGGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMV 325
Cdd:PLN02859 244 VLRPSnTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 326 EWLGYKPFKITYSSDNFQQLYEWAVVLINKGLAYVCHQKAEELKGFNPK--PSPWRERPIEESLRLFEDMKRGKIDEGAA 403
Cdd:PLN02859 324 EWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKkmNSPWRDRPIEESLKLFEDMRRGLIEEGKA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 404 TLRMKVTL--EEGKM-DPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIY 480
Cdd:PLN02859 404 TLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 481 CPVQWEYGRLNMNYALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVT---GAQIAVDpaMLE 557
Cdd:PLN02859 484 QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITrsdNSLIRMD--RLE 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 558 AAVRDVLNVTAPRRLVVLEPLKVTIKNFPHAAPVQLEV---PDFPQNPQQGTHKITLDKVIYIEQGDFKLEPEKGYRRLA 634
Cdd:PLN02859 562 HHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 635 PKQSVGLRHAgLVISVDEIVKDPATGQVVELICTSQPaEQAEKPKAFVQWVSQ------PIQLEVRLYEQLFkhkNPEDP 708
Cdd:PLN02859 642 PGKSVLLRYA-FPIKCTDVVLADDNETVVEIRAEYDP-EKKTKPKGVLHWVAEpspgvePLKVEVRLFDKLF---LSENP 716
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 709 NEVPgGFLSDISEQSMSVVV-AFADRALNQAKVYDKFQFERIGFFSVDPDTSANHLVFNRTVGLKEDAGK 777
Cdd:PLN02859 717 AELE-DWLEDLNPQSKEVISgAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
267-773 |
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: 553.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 267 VHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKP-FKITYSSDNFQQL 345
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 346 YEWAVVLINKGLAYVCHQKAEELKGF-----NP-KPSPWRERPIEESLRLFEDMKRGKIDEGAATLRMKVTLEEGKM--- 416
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYrgtltDPgKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 417 DPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYC-PVQWEYGRLNMNYA 495
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 496 LVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTAPRRLVVL 575
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 576 EPLKVTIKNFPHAAPVqLEVPDFPQNPQQGTHKITLDKVIYIEQGDFKLEPEKGYRRLAPKQSVGLRHAgLVISVDEIVK 655
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 656 DpATGQVVELICTSQP------AEQAEKPKAFVQWVS--QPIQLEVRLYEQLFKHKNPEDPNevpgGFLSDISEQSMSVV 727
Cdd:TIGR00440 399 D-AAGKITTIFCTYDNktlgkePADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNPGAPD----DFLSVINPESLVIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17864488 728 VAFADRALNQAKVYDKFQFERIGFFSVDP-DTSANHLVFNRTVGLKE 773
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
266-570 |
3.63e-159 |
|
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: 460.95 E-value: 3.63e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 266 KVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKPFKITYSSDNFQQL 345
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 346 YEWAVVLINKGLAYVchqkaeelkgfnpkpspwrerpieeslrlfedmkrgkidegaatlrmkvtleegkmdpvayrikf 425
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 426 isHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYCPVQWEYGRLNMNYALVSKRKIAKL 505
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17864488 506 ITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTAPR 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 |
2.04e-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: 405.93 E-value: 2.04e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 266 KVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKP-FKITYSSDNFQQ 344
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 345 LYEWAVVLINKGLAYVCHQKAEELKGFNP----KPSPWRERPIEESLRLF-EDMKRGKIDEGAATLRMKVTLEE--GKMD 417
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREeqeaLGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESpyVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 418 PVAYRIKFIS---HHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYCPV-QWEYGRLNMN 493
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864488 494 YALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQ-IAVDPAMLEAAVRDVLN 565
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
263-627 |
5.69e-79 |
|
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: 261.65 E-value: 5.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 263 TGGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKP-FKITYSSDN 341
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 342 FQQLYEWAVVLINKGLAYVCHQKAEEL---------KGFNPK-PSPWRERPIEE-----------SLRL--------FED 392
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEElermlaageppVLRFkipeegvvFDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 393 MKRGKIDEGAATLRmkvtleegkmDPVAYRikfiSHhrtGsdwciYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYW 472
Cdd:COG0008 161 LVRGEITFPNPNLR----------DPVLYR----AD---G-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIW 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 473 LCNALGIYCPvqwEYGRLNMNY----ALVSKRKIAKliteqivhdwddprlfTLTALRRRGFPAEAINNFCAQMGVT--G 546
Cdd:COG0008 219 LYEALGWEPP---EFAHLPLILgpdgTKLSKRKGAV----------------TVSGLRRRGYLPEAIRNYLALLGWSksD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 547 AQIAVDPAMLEAAVrDVLNVtaPRRLVVLEPLKVTIKNFPHAApvQLEVPDF-----PQNPQQGtHKITLDKVIYIEQGD 621
Cdd:COG0008 280 DQEIFSLEELIEAF-DLDRV--SRSPAVFDPVKLVWLNGPYIR--ALDDEELaellaPELPEAG-IREDLERLVPLVRER 353
|
....*.
gi 17864488 622 FKLEPE 627
Cdd:COG0008 354 AKTLSE 359
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
10-777 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 836.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 10 FQALGMSEQKAKETLKNANVTKNLQLSLAAAGSATLSDGT-GMLIYHMATKLKPQTADHLPLLVRYIVEHKLDNTQRVDA 88
Cdd:PLN02859 12 FLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTvGNLLYTVATKYPANALVHRPTLLSYIVSSKIKTPAQLEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 89 ALEYLLKCGQSlnaNIDLQALEKECGVGVVVTPEQIERTVQAKIKASyKEALLEQRYHFNSFKILQDVRGELKWADAKSV 168
Cdd:PLN02859 92 AFSFFSSTGPE---SFDLNKFEEACGVGVVVSPEDIEAAVNEVFEEN-KEKILEQRYRTNVGDLLGQVRKRLPWADPKIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 169 KAAIDVEIFDLLGPKTEADL-KPQTKANDKP-KAAKPKAEVTPAAQTAEAASDGATTISELMKTKVHFhapgENFKADGY 246
Cdd:PLN02859 168 KKLIDKKLYELLGEKTAADNeKPVKKKKEKPaKVEEKKVAVAAAPPSEEELNPYSIFPQPEENFKVHT----EVFFSDGS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 247 VVTEH-TERLLKEHLARTGGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMV 325
Cdd:PLN02859 244 VLRPSnTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 326 EWLGYKPFKITYSSDNFQQLYEWAVVLINKGLAYVCHQKAEELKGFNPK--PSPWRERPIEESLRLFEDMKRGKIDEGAA 403
Cdd:PLN02859 324 EWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKkmNSPWRDRPIEESLKLFEDMRRGLIEEGKA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 404 TLRMKVTL--EEGKM-DPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIY 480
Cdd:PLN02859 404 TLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 481 CPVQWEYGRLNMNYALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVT---GAQIAVDpaMLE 557
Cdd:PLN02859 484 QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITrsdNSLIRMD--RLE 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 558 AAVRDVLNVTAPRRLVVLEPLKVTIKNFPHAAPVQLEV---PDFPQNPQQGTHKITLDKVIYIEQGDFKLEPEKGYRRLA 634
Cdd:PLN02859 562 HHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 635 PKQSVGLRHAgLVISVDEIVKDPATGQVVELICTSQPaEQAEKPKAFVQWVSQ------PIQLEVRLYEQLFkhkNPEDP 708
Cdd:PLN02859 642 PGKSVLLRYA-FPIKCTDVVLADDNETVVEIRAEYDP-EKKTKPKGVLHWVAEpspgvePLKVEVRLFDKLF---LSENP 716
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 709 NEVPgGFLSDISEQSMSVVV-AFADRALNQAKVYDKFQFERIGFFSVDPDTSANHLVFNRTVGLKEDAGK 777
Cdd:PLN02859 717 AELE-DWLEDLNPQSKEVISgAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
265-778 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 697.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 265 GKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKPF-KITYSSDNFQ 343
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSgELRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 344 QLYEWAVVLINKGLAYVCHQKAEELK---------GfnpKPSPWRERPIEESLRLFEDMKRGKIDEGAATLRMKVTLEEG 414
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIReyrgtltepG---KNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 415 KM---DPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYC-PVQWEYGRL 490
Cdd:PRK05347 185 NInmrDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSRL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 491 NMNYALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTAPR 570
Cdd:PRK05347 265 NLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 571 RLVVLEPLKVTIKNFPHAAPVQLEVPDFPQNPQQGTHKITLDKVIYIEQGDFKLEPEKGYRRLAPKQSVGLRHAGlVISV 650
Cdd:PRK05347 345 AMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAY-VIKC 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 651 DEIVKDpATGQVVELICT------SQPAEQAEKPKAFVQWVS--QPIQLEVRLYEQLFKHKNPEDPNEvpggFLSDISEQ 722
Cdd:PRK05347 424 EEVVKD-ADGNITEIHCTydpdtlSGNPADGRKVKGTIHWVSaaHAVPAEVRLYDRLFTVPNPAAGKD----FLDFLNPD 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 17864488 723 SMSVVVAFADRALNQAKVYDKFQFERIGFFSVDPDTSANHLVFNRTVGLKEDAGKK 778
Cdd:PRK05347 499 SLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
236-777 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 560.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 236 APGENFKADGYVVTEHTERLLKehlARTGGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEE 315
Cdd:PRK14703 4 APRPRMLVSPNFITEIIEEDLE---AGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 316 KFFLAIKEMVEWLGYK-PFKITYSSDNFQQLYEWAVVLINKGLAYVCHQKAEELKGF-----NP-KPSPWRERPIEESLR 388
Cdd:PRK14703 81 EYVEAIKDDVRWLGFDwGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELrgtvtEPgTPSPYRDRSVEENLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 389 LFEDMKRGKIDEGAATLRMKVTLEEGKM---DPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQS 465
Cdd:PRK14703 161 LFRRMRAGEFPDGAHVLRAKIDMSSPNMklrDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 466 RRSSYYWLCNALGIYC--PVQWEYGRLNMNYALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMG 543
Cdd:PRK14703 241 NRAIYDWVLDHLGPWPprPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 544 VTGAQIAVDPAMLEAAVRDVLNVTAPRRLVVLEPLKVTIKNFPHAAPVQLEVPDFPQN-PQQGTHKITLDKVIYIEQGDF 622
Cdd:PRK14703 321 VAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 623 KLEPEKGYRRLAPKQSVGLRHAGlVISVDEIVKDpATGQVVELICTSQPAE-----QAEKPKAFVQWVS--QPIQLEVRL 695
Cdd:PRK14703 401 SEDPPKGFKRLTPGREVRLRGAY-IIRCDEVVRD-ADGAVTELRCTYDPESakgedTGRKAAGVIHWVSakHALPAEVRL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 696 YEQLFKHKNPEdpnEVPGGFLSDISEQSMSVVVAFADRALNQAKVYDKFQFERIGFFSVDP-DTSANHLVFNRTVGLKED 774
Cdd:PRK14703 479 YDRLFKVPQPE---AADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDT 555
|
...
gi 17864488 775 AGK 777
Cdd:PRK14703 556 WGA 558
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
267-773 |
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: 553.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 267 VHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKP-FKITYSSDNFQQL 345
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 346 YEWAVVLINKGLAYVCHQKAEELKGF-----NP-KPSPWRERPIEESLRLFEDMKRGKIDEGAATLRMKVTLEEGKM--- 416
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYrgtltDPgKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 417 DPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYC-PVQWEYGRLNMNYA 495
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 496 LVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTAPRRLVVL 575
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 576 EPLKVTIKNFPHAAPVqLEVPDFPQNPQQGTHKITLDKVIYIEQGDFKLEPEKGYRRLAPKQSVGLRHAgLVISVDEIVK 655
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 656 DpATGQVVELICTSQP------AEQAEKPKAFVQWVS--QPIQLEVRLYEQLFKHKNPEDPNevpgGFLSDISEQSMSVV 727
Cdd:TIGR00440 399 D-AAGKITTIFCTYDNktlgkePADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNPGAPD----DFLSVINPESLVIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17864488 728 VAFADRALNQAKVYDKFQFERIGFFSVDP-DTSANHLVFNRTVGLKE 773
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
251-777 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 536.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 251 HTERLLKEHLARTGGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGY 330
Cdd:PTZ00437 36 NTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 331 KPFKITYSSDNFQQLYEWAVVLINKGLAYVCHQKAEELKGF--NPKPSPWRERPIEESLRLFEDMKRGKIDEGAATLRMK 408
Cdd:PTZ00437 116 KPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 409 VTLEEGK---MDPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYCPVQW 485
Cdd:PTZ00437 196 ADMKSDNpnmRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 486 EYGRLNMNYALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLN 565
Cdd:PTZ00437 276 EFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 566 VTAPRRLVVLEPLKVTIKNFphAAPVQLEVPDFPQNPQQGTHKITLDKVIYIEQGDFKLEP-EKGYRRLAP-KQSVGLRH 643
Cdd:PTZ00437 356 ERCERRLMVIDPIKVVVDNW--KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRTEDnNSKFYGLAPgPRVVGLKY 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 644 AGLVI----SVDEivkdpaTGQVVeLICTSQPAEQAEKPKAFVQWVSQP--IQLEVRLYEQLFKhknpEDPNEVPGGFLS 717
Cdd:PTZ00437 434 SGNVVckgfEVDA------AGQPS-VIHVDIDFERKDKPKTNISWVSATacTPVEVRLYNALLK----DDRAAIDPEFLK 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 718 DISEQSMSVVVAFADRALNQAKVYDKFQFERIGFFSVDPDTSANHLVFNRTVGLKEDAGK 777
Cdd:PTZ00437 503 FIDEDSEVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
266-570 |
3.63e-159 |
|
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: 460.95 E-value: 3.63e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 266 KVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKPFKITYSSDNFQQL 345
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 346 YEWAVVLINKGLAYVchqkaeelkgfnpkpspwrerpieeslrlfedmkrgkidegaatlrmkvtleegkmdpvayrikf 425
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 426 isHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYCPVQWEYGRLNMNYALVSKRKIAKL 505
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17864488 506 ITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTAPR 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 |
2.04e-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: 405.93 E-value: 2.04e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 266 KVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKP-FKITYSSDNFQQ 344
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 345 LYEWAVVLINKGLAYVCHQKAEELKGFNP----KPSPWRERPIEESLRLF-EDMKRGKIDEGAATLRMKVTLEE--GKMD 417
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREeqeaLGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESpyVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 418 PVAYRIKFIS---HHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYCPV-QWEYGRLNMN 493
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864488 494 YALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQ-IAVDPAMLEAAVRDVLN 565
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLD 313
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
233-764 |
8.72e-92 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 299.96 E-value: 8.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 233 HFHAPGENFKADGYVVTEHTErllkehlartgGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEK 312
Cdd:PTZ00402 30 YFTAANANEENDKLQLTNAEE-----------GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 313 EEEKFFLAIKEMVEWLGYkPFKI--TYSSDNFQQLYEWAVVLINKGLAYVCHQKAEELKG--FNPKPSPWRERPIEESLR 388
Cdd:PTZ00402 99 EKEHFEQAILDDLATLGV-SWDVgpTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 389 LFEDMKRGKiDEGAAT-LRMKVTLE-EGKM--DPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQ 464
Cdd:PTZ00402 178 LWNEMKKGS-AEGQETcLRAKISVDnENKAmrDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYH 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 465 SRRSSYYWLCNALGIYCPVQWEYGRLNMNYALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGV 544
Cdd:PTZ00402 257 DRNDQYYWFCDALGIRKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGM 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 545 TGAQIAVDPAMLEAAVRDVLNVTAPRRLVVLEPLKV--TIKNFPHAApvQLEVPDFPQNPQQGTHKITLDKVIYIEQGDF 622
Cdd:PTZ00402 337 SKTVNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVrcTVEGQIHLE--ACEKLLHKKVPDMGEKTYYKSDVIFLDAEDV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 623 KLepekgyrrLAPKQSVGLRHAGLVIsVDEIVKDPATGQVVELICTSQPAEQAEKPKAFVQWVSQ---PIQLEVRLYEQL 699
Cdd:PTZ00402 415 AL--------LKEGDEVTLMDWGNAY-IKNIRRSGEDALITDADIVLHLEGDVKKTKFKLTWVPEspkAEVMELNEYDHL 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17864488 700 FKHKNPeDPNEVPGGFLSDISEQSMSVvvaFADRALNQAKVYDKFQFERIGFFSVDPDTSANHLV 764
Cdd:PTZ00402 486 LTKKKP-DPEESIDDIIAPVTKYTQEV---YGEEALSVLKKGDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
250-755 |
5.39e-88 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 288.26 E-value: 5.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 250 EHTERLLKEHLARTGGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLG 329
Cdd:TIGR00463 77 EKKRKGLRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 330 YKPFKITYSSDNFQQLYEWAVVLINKGLAYVCHQKAEELKGFNPK--PSPWRERPIEESLRLFEDMKRGKIDEGAATLRM 407
Cdd:TIGR00463 157 VKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRgeACHCRDRSVEENLERWEEMLEGKEEGGSVVVRV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 408 KVTLEEGK---MDPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEF--QSRRSSYYWLcnALGIYCP 482
Cdd:TIGR00463 237 KTDLKHKNpaiRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYR--YFGWEPP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 483 VQWEYGRLNMNY--ALVSKRKIaKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAV 560
Cdd:TIGR00463 315 EFIHWGRLKIDDvrALSTSSAR-KGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALN 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 561 RDVLNVTAPRRLVVLEPLKVTIKNFPhaAPVQLEVPDFPQNPQQGTHKITLDKVIYIEQGDFklepEKGyrrlapKQSVG 640
Cdd:TIGR00463 394 RKIIDEEARRYFFIWNPVKIEIVGLP--EPKRVERPLHPDHPEIGERVLILRGEIYVPKDDL----EEG------VEPVR 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 641 LRHAGLVIsVDEivkdpatgqvVELICTSQPAEQAEKPKA-FVQWVSQPIQLEVRLYEqlfkhknpEDPNEVPGgflsdi 719
Cdd:TIGR00463 462 LMDAVNVI-YSK----------KELRYHSEGLEGARKLGKsIIHWLPAKDAVKVKVIM--------PDASIVEG------ 516
|
490 500 510
....*....|....*....|....*....|....*.
gi 17864488 720 seqsmsvvvaFADRALNQAKVYDKFQFERIGFFSVD 755
Cdd:TIGR00463 517 ----------VIEADASELEVGDVVQFERFGFARLD 542
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
263-627 |
5.69e-79 |
|
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: 261.65 E-value: 5.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 263 TGGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKP-FKITYSSDN 341
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 342 FQQLYEWAVVLINKGLAYVCHQKAEEL---------KGFNPK-PSPWRERPIEE-----------SLRL--------FED 392
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEElermlaageppVLRFkipeegvvFDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 393 MKRGKIDEGAATLRmkvtleegkmDPVAYRikfiSHhrtGsdwciYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYW 472
Cdd:COG0008 161 LVRGEITFPNPNLR----------DPVLYR----AD---G-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIW 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 473 LCNALGIYCPvqwEYGRLNMNY----ALVSKRKIAKliteqivhdwddprlfTLTALRRRGFPAEAINNFCAQMGVT--G 546
Cdd:COG0008 219 LYEALGWEPP---EFAHLPLILgpdgTKLSKRKGAV----------------TVSGLRRRGYLPEAIRNYLALLGWSksD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 547 AQIAVDPAMLEAAVrDVLNVtaPRRLVVLEPLKVTIKNFPHAApvQLEVPDF-----PQNPQQGtHKITLDKVIYIEQGD 621
Cdd:COG0008 280 DQEIFSLEELIEAF-DLDRV--SRSPAVFDPVKLVWLNGPYIR--ALDDEELaellaPELPEAG-IREDLERLVPLVRER 353
|
....*.
gi 17864488 622 FKLEPE 627
Cdd:COG0008 354 AKTLSE 359
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
265-755 |
4.83e-78 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 266.20 E-value: 4.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 265 GKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKPFKITYSSDNFQQ 344
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 345 LYEWAVVLINKGLAYVCHQKAEELKG--FNPKPSPWRERPIEESLRLFEDMK-----------RGKIDEGA--ATLRmkv 409
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKerMDGIESKCRNNSVEENLRLWKEMIagserglqccvRGKLDMQDpnKSLR--- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 410 tleegkmDPVAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYcPVQ-WEYG 488
Cdd:PLN02907 369 -------DPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 489 RLNMNYALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTA 568
Cdd:PLN02907 441 RLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVC 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 569 PRRLVVLEPLKV--TIKNFPHAAPVQLeVPDFPQNPQQGTHKITLDKVIYIEQGDFKLepekgyrrLAPKQSVGLRHAGL 646
Cdd:PLN02907 521 PRHTAVLKEGRVllTLTDGPETPFVRI-IPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLMDWGN 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 647 VIsVDEIVKDPaTGQVVELICTSQPAEQAEKPKAFVQW---VSQPIQLEVRLYEQLFKHKNPEDPNEvpggFLSDISEQS 723
Cdd:PLN02907 592 AI-IKEITKDE-GGAVTALSGELHLEGSVKTTKLKLTWlpdTNELVPLSLVEFDYLITKKKLEEDDN----FLDVLNPCT 665
|
490 500 510
....*....|....*....|....*....|....*
gi 17864488 724 MSVVVAFAD---RALNQAKVydkFQFERIGFFSVD 755
Cdd:PLN02907 666 KKETAALGDsnmRNLKRGEI---IQLERKGYYRCD 697
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
265-755 |
4.86e-78 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 262.09 E-value: 4.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 265 GKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPE--KEEEKFFLAIKEMVEWLGYKPFKITYSSDNF 342
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDEVVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 343 QQLYEWAVVLINKGLAYVCHQKAEELKGF--NPKPSPWRERPIEESLRLFEDMKRGKIDEGAATLRMKVTLEEGkmDP-- 418
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKELrdAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHP--NPsv 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 419 ---VAYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQS--RRSSYywLCNALGIYCPVQWEYGRLNMN 493
Cdd:PRK04156 258 rdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntEKQRY--IYDYFGWEYPETIHYGRLKIE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 494 YALVSKRKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTAPRRLV 573
Cdd:PRK04156 336 GFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYFF 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 574 VLEPLKVTIKNFPhaaPVQLEVPDFPQNPQQGTHKITLDKVIYIEQGDfkLEPEKGYRRLapkqsvglrhAGLV-ISVDE 652
Cdd:PRK04156 416 VRDPVELEIEGAE---PLEAKIPLHPDRPERGEREIPVGGKVYVSSDD--LEAEGKMVRL----------MDLFnVEITG 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 653 IvkdpatgQVVELICTSQPAEQAEKPKA-FVQWV--SQPIQLEVRlyeqlfkhknpeDPNEvpggflsdiseqsmSVVVA 729
Cdd:PRK04156 481 V-------SVDKARYHSDDLEEARKNKApIIQWVpeDESVPVRVL------------KPDG--------------GDIEG 527
|
490 500
....*....|....*....|....*.
gi 17864488 730 FADRALNQAKVYDKFQFERIGFFSVD 755
Cdd:PRK04156 528 LAEPDVADLEVDDIVQFERFGFVRID 553
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
265-755 |
9.61e-73 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 246.85 E-value: 9.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 265 GKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKPFKITYSSDNFQQ 344
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 345 LYEWAVVLINKGLAYVCHQKAEELKG--FNPKPSPWRERPIEESLRLFEDMKRGKIDEGAATLRMKVTL--EEGKM-DPV 419
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKerADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMqsDNGTLrDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 420 AYRIKFISHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYCPVQWEYGRLNMNYALVSK 499
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 500 RKIAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTAPRRLVV--LEP 577
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkADH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 578 LKVTIKNFPHAAPVQLEVPDF-PQNPQQGTHKITLDKVIYIEQGDFKlepekgyrRLAPKQSVGLRHAGlVISVDEIVKD 656
Cdd:PLN03233 330 TALTVTNADEEADFAFSETDChPKDPGFGKRAMRICDEVLLEKADTE--------DIQLGEDIVLLRWG-VIEISKIDGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 657 pATGQVVelictsqPAEQAEKPKAFVQWVSQ-PIQLEVRLYE---QLFKHKNPEDPNevpggFLSDISEQSMSVVVAFAD 732
Cdd:PLN03233 401 -LEGHFI-------PDGDFKAAKKKISWIADvSDNIPVVLSEfdnLIIKEKLEEDDK-----FEDFINPDTLAETDVIGD 467
|
490 500
....*....|....*....|...
gi 17864488 733 RALNQAKVYDKFQFERIGFFSVD 755
Cdd:PLN03233 468 AGLKTLKEHDIIQLERRGFYRVD 490
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
4-165 |
7.44e-61 |
|
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: 202.41 E-value: 7.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 4 DDLIAKFQALGMSEQKAKETLKNANVTKNLQLSLAAAGSATLSD-GTGMLIYHMATKLKPQTADHLPLLVRYIVEHKLDN 82
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDkKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 83 TQRVDAALEYLLKcgqSLNANIDLQALEKECGVGVVVTPEQIERTVQAKIkASYKEALLEQRYHFNSFKILQDVRG--EL 160
Cdd:pfam04558 81 TLQVDAALKYLLK---KANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYI-EENKEEILEKRYRFNVGKLLGEVRKlpEL 156
|
....*
gi 17864488 161 KWADA 165
Cdd:pfam04558 157 KWADP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
568-755 |
9.07e-52 |
|
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: 177.85 E-value: 9.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 568 APRRLVVLEPLKVTIKNFPHAAPVQLEVPDFPQNPQQGTHKITLDKVIYIEQGDFKlepekgyrRLAPKQSVGLRHAGlV 647
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDFK--------RLAPGEEVRLMDAY-N 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 648 ISVDEIVKDpATGQVVELICTSQPA--EQAEKPKA-FVQWVS--QPIQLEVRLYEQLFKHKNPEDpnevpggFLsdISEQ 722
Cdd:pfam03950 72 IKVTEVVKD-EDGNVTELHCTYDGDdlGGARKVKGkIIHWVSasDAVPAEVRLYDRLFKDEDDAD-------FL--LNPD 141
|
170 180 190
....*....|....*....|....*....|....
gi 17864488 723 SMSVVV-AFADRALNQAKVYDKFQFERIGFFSVD 755
Cdd:pfam03950 142 SLKVLTeGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
266-570 |
3.18e-44 |
|
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: 159.17 E-value: 3.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 266 KVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYK----PFkitYSSDN 341
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPY---RQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 342 FQQLYEWAVVLINKGlayvchqkaeelkgfnpkpspwrerpieeslrlfedmkrgkidegaatlrmkvtleegkmdpvay 421
Cdd:cd00418 78 FDLYRAYAEELIKKG----------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 422 rikfishhrtgsdwcIYPTYDYTHCLCDSLEDITHSLCTKEFQSRRSSYYWLCNALGIYCPVQWEYGRLNMNYALV-SKR 500
Cdd:cd00418 93 ---------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKlSKR 157
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864488 501 KIAKliteqivhdwddprlfTLTALRRRGFPAEAINNFCAQMGVT---GAQIAVDPAMLEAAVRDVLNVTAPR 570
Cdd:cd00418 158 KLNT----------------TLRALRRRGYLPEALRNYLALIGWSkpdGHELFTLEEMIAAFSVERVNSADAT 214
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
266-570 |
4.89e-44 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 159.05 E-value: 4.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 266 KVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPE--KEEEKFFLAIKEMVEWLGYKPFKITYSSDNFQ 343
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 344 QLYEWAVVLINKGLAYVchqkaeelkgfnpkpspwrerpieeslrlfedmkrgkidegaatlrmkvtleegkmdpvayri 423
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 424 kfisHHRTGSDWCIYPTYDYTHCLCDSLEDITHSLCTKEFQS--RRSSYYWLCnaLGIYCPVQWEYGRLNMNYALVSKRK 501
Cdd:cd09287 98 ----HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntEKQRYIYEY--FGWEYPETIHWGRLKIEGGKLSTSK 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17864488 502 IAKLITEQIVHDWDDPRLFTLTALRRRGFPAEAINNFCAQMGVTGAQIAVDPAMLEAAVRDVLNVTAPR 570
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 ... |
168-257 |
1.98e-31 |
|
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: 117.41 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 168 VKAAIDVEIFDLLGPKTEADLKPQTKANDKPKAAKPKAEVTPAAQTAEAASDGATTISELmktKVHFHAPGENFKADGYV 247
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPPKKKKKAKKKKAAKKKKKKAPIEEEENKRSMFSEGF---LGKFHKPGENPKTDGYV 77
|
90
....*....|
gi 17864488 248 VTEHTERLLK 257
Cdd:pfam04557 78 VTEHTMRLLK 87
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
266-329 |
1.85e-09 |
|
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: 58.75 E-value: 1.85e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17864488 266 KVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLG 329
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLG 64
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
261-405 |
2.37e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 53.98 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 261 ARTGGKVHTRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPE---KEEEKFFLAikeMVEWLG-------- 329
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLArstKESEEAVLR---DLKWLGldwdegpd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 330 ----YKPFKITYSSDNFQQLyewAVVLINKGLAYVCHQKAEEL---------KGFNPK---------------------P 375
Cdd:PLN02627 117 vggeYGPYRQSERNAIYKQY---AEKLLESGHVYPCFCTDEELeamkeeaelKKLPPRytgkwatasdeevqaelakgtP 193
|
170 180 190
....*....|....*....|....*....|.
gi 17864488 376 SPWRER-PIEESLRLfEDMKRGKIDEGAATL 405
Cdd:PLN02627 194 YTYRFRvPKEGSVKI-DDLIRGEVSWNTDTL 223
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
268-348 |
2.48e-06 |
|
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: 47.86 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 268 HTRFPPEPNGILHIGHAKAININFGYAAAHD-----GVCYLRYDDTNP--EKEEEKFFLAIKEMVEwlgykpfkitYSSD 340
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGGliGDPANKKGENAKAFVE----------RWIE 70
|
....*...
gi 17864488 341 NFQQLYEW 348
Cdd:cd00802 71 RIKEDVEY 78
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
269-362 |
9.61e-06 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 48.31 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864488 269 TRFPPEPNGILHIGHAKAININFGYAAAHDGVCYLRYDDTNPEKEEEKFFLAIKEMVEWLGYKP-FKITYSSDNFqQLYE 347
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWdGPVLYQSQRH-DAYR 86
|
90
....*....|....*.
gi 17864488 348 WAV-VLINKGLAYVCH 362
Cdd:PRK05710 87 AALdRLRAQGLVYPCF 102
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
268-318 |
1.06e-04 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 42.14 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 17864488 268 HTRFPPEPnGILHIGHAKAININFGYAaahdGVCYLRYDDTNPEKEEEKFF 318
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPH 46
|
|
| |
