|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
5-775 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 862.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 5 LILFTSIGLSEQKAKETLKNEALSSALKEAITQAqnvtGVSE-VDKAMGMLLYSMASRLKDTKRV--AFLSENIAQRKIS 81
Cdd:PLN02859 9 LELFLKIGLDERTARNAIANNKVTSNLTAVIHEA----GVTNgCDKTVGNLLYTVATKYPANALVhrPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 82 TELQLAGALEFLMSHPHDPINQKEFEEACGVGVVITPEQIEDAVESVIKKHKEELLKERYHFNMGLLMREARGGLKWADG 161
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 162 KVIKNEVDMQVLHLLGPKTEADLEK---KTKAPKAKVAE-----NDVKPKKEELavngdattgEGMSLMEQLRgEALKFH 233
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKpvkKKKEKPAKVEEkkvavAAAPPSEEEL---------NPYSIFPQPE-ENFKVH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 234 KtgENYKTEGYVMTP-NTMSLLKKHLDYTGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEE 312
Cdd:PLN02859 235 T--EVFFSDGSVLRPsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 313 EKYFTAIKDMVEWLGYKPYQVTHASDNFQQLYDLAVDLIRRGHAYVCHQKGEELKGY--NAPPSPWKDRPIEESLLLFER 390
Cdd:PLN02859 313 KEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 391 MKKGLFAEGEATLRMKMVMEDGK---TDPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSS 467
Cdd:PLN02859 393 MRRGLIEEGKATLRMKQDMQNDNfnmYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRAS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 468 YYWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQT 547
Cdd:PLN02859 473 YYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 548 TT-EPHLLESCVREVLNDTAPRVMAVLEPLKVTIMNLPENTQSEV---RVPDFPANEAKGSHMVPFSRTIFIEQSDFREV 623
Cdd:PLN02859 553 SLiRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLK 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 624 MEKGYKRLTPEQPVGLRHAGYVISVQKVIKDTQGKVVEVEVNCCSSDAAeKPKAFIHWVSQ------PLQCEVRLYDRLF 697
Cdd:PLN02859 633 DSKDYYGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKT-KPKGVLHWVAEpspgvePLKVEVRLFDKLF 711
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105397357 698 LhkhPEDTSEVPNgFLSDINPDSLQVISSAFVDTSVKRAKVFDKFQFERLGYFSLDPDSTADKPVFNRTVTLKEDPGK 775
Cdd:PLN02859 712 L---SENPAELED-WLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
265-771 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 591.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 265 IRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YQVTHASDNFQQL 343
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 344 YDLAVDLIRRGHAYVCHQKGEELK---------GYNappSPWKDRPIEESLLLFERMKKGLFAEGEATLRMK-------M 407
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrgtltdpGKN---SPYRDRSIEENLALFEKMRDGKFKEGKAILRAKidmaspfP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 408 VMEdgktDPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYC-PVQWEYG 486
Cdd:TIGR00440 158 VMR----DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 487 RLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTA 566
Cdd:TIGR00440 234 RLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 567 PRVMAVLEPLKVTIMNLpENTQSEVRVPDFPANEAKGSHMVPFSRTIFIEQSDFREVMEKGYKRLTPEQPVGLRHAgYVI 646
Cdd:TIGR00440 314 PRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 647 SVQKVIKDTQGKVVEVEVN----CCSSDAAE--KPKAFIHWVS--QPLQCEVRLYDRLFLHKHPedtsEVPNGFLSDINP 718
Cdd:TIGR00440 392 KAERVEKDAAGKITTIFCTydnkTLGKEPADgrKVKGVIHWVSasSKYPTETRLYDRLFKVPNP----GAPDDFLSVINP 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2105397357 719 DSLqVISSAFVDTSVKRAKVFDKFQFERLGYFSLDP-DSTADKPVFNRTVTLKE 771
Cdd:TIGR00440 468 ESL-VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
264-568 |
3.76e-161 |
|
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: 465.96 E-value: 3.76e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYQVTHASDNFQQL 343
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 344 YDLAVDLIRRGHAYVchqkgeelkgynappspwkdrpieeslllfermkkglfaegeatlrmkmvmedgktdpvayriky 423
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 424 tpHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKL 503
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105397357 504 VETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTAPR 568
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
264-564 |
9.00e-148 |
|
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: 434.82 E-value: 9.00e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YQVTHASDNFQQ 342
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 343 LYDLAVDLIRRGHAYVCHQKGEELKGYN----APPSPWKDRPIEESLLLF-ERMKKGLFAEGEATLRMKMVMED--GKTD 415
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEReeqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESpyVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 416 PVAYRIKYTP---HHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPV-QWEYGRLNLT 491
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105397357 492 YTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTT-EPHLLESCVREVLND 564
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNrLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
261-699 |
5.38e-89 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 288.23 E-value: 5.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 261 TGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK----PYqvtHA 336
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 337 SDNFQQLYDLAVDLIRRGHAYVCHQKGEELKGYNA-------PP---SPWKDRPIEESlllfERMKkglfAEGE-ATLRM 405
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALREtqtapgkPPrydGRCRDLSPEEL----ERML----AAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 406 KM-----VMED---GKT--------DPVAYRikytphhRTGdewciYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYY 469
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 470 WLCNALDVYCPvqwEYGRLNLTY----TVVSKRKiiklvetGVVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTV- 544
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKs 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 545 -SQTTTEPHLLESCVRevLNDTaPRVMAVLEPLKVTIMN------LPENTQSEVRVPDFPAN--EAKGSHMVPFSRT--- 612
Cdd:COG0008 279 dDQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAgiREDLERLVPLVRErak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 613 -----------IFIEQSDFREVMekgyKRLTPEQpvglrhagyvisVQKVIKDTQGKVVEVEVncCSSDAAekpKAFIHW 681
Cdd:COG0008 356 tlselaelarfFFIEREDEKAAK----KRLAPEE------------VRKVLKAALEVLEAVET--WDPETV---KGTIHW 414
|
490
....*....|....*...
gi 2105397357 682 VSQplQCEVRlyDRLFLH 699
Cdd:COG0008 415 VSA--EAGVK--DGLLFM 428
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
5-775 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 862.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 5 LILFTSIGLSEQKAKETLKNEALSSALKEAITQAqnvtGVSE-VDKAMGMLLYSMASRLKDTKRV--AFLSENIAQRKIS 81
Cdd:PLN02859 9 LELFLKIGLDERTARNAIANNKVTSNLTAVIHEA----GVTNgCDKTVGNLLYTVATKYPANALVhrPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 82 TELQLAGALEFLMSHPHDPINQKEFEEACGVGVVITPEQIEDAVESVIKKHKEELLKERYHFNMGLLMREARGGLKWADG 161
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 162 KVIKNEVDMQVLHLLGPKTEADLEK---KTKAPKAKVAE-----NDVKPKKEELavngdattgEGMSLMEQLRgEALKFH 233
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKpvkKKKEKPAKVEEkkvavAAAPPSEEEL---------NPYSIFPQPE-ENFKVH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 234 KtgENYKTEGYVMTP-NTMSLLKKHLDYTGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEE 312
Cdd:PLN02859 235 T--EVFFSDGSVLRPsNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 313 EKYFTAIKDMVEWLGYKPYQVTHASDNFQQLYDLAVDLIRRGHAYVCHQKGEELKGY--NAPPSPWKDRPIEESLLLFER 390
Cdd:PLN02859 313 KEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 391 MKKGLFAEGEATLRMKMVMEDGK---TDPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSS 467
Cdd:PLN02859 393 MRRGLIEEGKATLRMKQDMQNDNfnmYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRAS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 468 YYWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQT 547
Cdd:PLN02859 473 YYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 548 TT-EPHLLESCVREVLNDTAPRVMAVLEPLKVTIMNLPENTQSEV---RVPDFPANEAKGSHMVPFSRTIFIEQSDFREV 623
Cdd:PLN02859 553 SLiRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLK 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 624 MEKGYKRLTPEQPVGLRHAGYVISVQKVIKDTQGKVVEVEVNCCSSDAAeKPKAFIHWVSQ------PLQCEVRLYDRLF 697
Cdd:PLN02859 633 DSKDYYGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKT-KPKGVLHWVAEpspgvePLKVEVRLFDKLF 711
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105397357 698 LhkhPEDTSEVPNgFLSDINPDSLQVISSAFVDTSVKRAKVFDKFQFERLGYFSLDPDSTADKPVFNRTVTLKEDPGK 775
Cdd:PLN02859 712 L---SENPAELED-WLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
263-776 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 753.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YQVTHASDNFQ 341
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWsGELRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 342 QLYDLAVDLIRRGHAYVCHQKGEELKGY----NAP--PSPWKDRPIEESLLLFERMKKGLFAEGEATLRMK-------MV 408
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIREYrgtlTEPgkNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKidmaspnIN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 409 MEDgktdPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYC-PVQWEYGR 487
Cdd:PRK05347 188 MRD----PVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 488 LNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTAP 567
Cdd:PRK05347 264 LNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 568 RVMAVLEPLKVTIMNLPENTQSEVRVPDFPANEAKGSHMVPFSRTIFIEQSDFREVMEKGYKRLTPEQPVGLRHAgYVIS 647
Cdd:PRK05347 344 RAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNA-YVIK 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 648 VQKVIKDTQGKVVEVEvncCSSDAA---------EKPKAFIHWVS--QPLQCEVRLYDRLFLHKHPEDTSEvpngFLSDI 716
Cdd:PRK05347 423 CEEVVKDADGNITEIH---CTYDPDtlsgnpadgRKVKGTIHWVSaaHAVPAEVRLYDRLFTVPNPAAGKD----FLDFL 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 717 NPDSLqVISSAFVDTSVKRAKVFDKFQFERLGYFSLDPDSTADKPVFNRTVTLKEDPGKI 776
Cdd:PRK05347 496 NPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
263-775 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 612.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK-PYQVTHASDNFQ 341
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 342 QLYDLAVDLIRRGHAYVCHQKGEELKGYNAP------PSPWKDRPIEESLLLFERMKKGLFAEGEATLRMKMVMEDGKT- 414
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEIRELRGTvtepgtPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMk 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 415 --DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYC--PVQWEYGRLNL 490
Cdd:PRK14703 190 lrDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPprPRQYEFARLAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 491 TYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTAPRVM 570
Cdd:PRK14703 270 GYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVM 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 571 AVLEPLKVTIMNLPENTQSEVRVPDFPANEAK-GSHMVPFSRTIFIEQSDFREVMEKGYKRLTPEQPVGLRHAgYVISVQ 649
Cdd:PRK14703 350 AVLDPLKVVIENLPAGKVEELDLPYWPHDVPKeGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRGA-YIIRCD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 650 KVIKDTQGKVVEVEvncC--------SSDAAEKPKAFIHWVS--QPLQCEVRLYDRLFLHKHPEDTSEvpnGFLSDINPD 719
Cdd:PRK14703 429 EVVRDADGAVTELR---CtydpesakGEDTGRKAAGVIHWVSakHALPAEVRLYDRLFKVPQPEAADE---DFLEFLNPD 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105397357 720 SLQVIsSAFVDTSVKRAKVFDKFQFERLGYFSLDP-DSTADKPVFNRTVTLKEDPGK 775
Cdd:PRK14703 503 SLRVA-QGRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGA 558
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
265-771 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 591.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 265 IRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YQVTHASDNFQQL 343
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 344 YDLAVDLIRRGHAYVCHQKGEELK---------GYNappSPWKDRPIEESLLLFERMKKGLFAEGEATLRMK-------M 407
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrgtltdpGKN---SPYRDRSIEENLALFEKMRDGKFKEGKAILRAKidmaspfP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 408 VMEdgktDPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYC-PVQWEYG 486
Cdd:TIGR00440 158 VMR----DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 487 RLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTA 566
Cdd:TIGR00440 234 RLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 567 PRVMAVLEPLKVTIMNLpENTQSEVRVPDFPANEAKGSHMVPFSRTIFIEQSDFREVMEKGYKRLTPEQPVGLRHAgYVI 646
Cdd:TIGR00440 314 PRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 647 SVQKVIKDTQGKVVEVEVN----CCSSDAAE--KPKAFIHWVS--QPLQCEVRLYDRLFLHKHPedtsEVPNGFLSDINP 718
Cdd:TIGR00440 392 KAERVEKDAAGKITTIFCTydnkTLGKEPADgrKVKGVIHWVSasSKYPTETRLYDRLFKVPNP----GAPDDFLSVINP 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2105397357 719 DSLqVISSAFVDTSVKRAKVFDKFQFERLGYFSLDP-DSTADKPVFNRTVTLKE 771
Cdd:TIGR00440 468 ESL-VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
249-775 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 536.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 249 NTMSLLKKHLDYTGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGY 328
Cdd:PTZ00437 36 NTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 329 KPYQVTHASDNFQQLYDLAVDLIRRGHAYVCHQKGEELKGY--NAPPSPWKDRPIEESLLLFERMKKGLFAEGEATLRMK 406
Cdd:PTZ00437 116 KPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 407 MVMEDGKT---DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQW 483
Cdd:PTZ00437 196 ADMKSDNPnmrDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 484 EYGRLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLN 563
Cdd:PTZ00437 276 EFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 564 DTAPRVMAVLEPLKVTIMNLpeNTQSEVRVPDFPANEAKGSHMVPFSRTIFIEQSDFR-EVMEKGYKRLTP-EQPVGLRH 641
Cdd:PTZ00437 356 ERCERRLMVIDPIKVVVDNW--KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPgPRVVGLKY 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 642 AGYVISVQ-KVIKDTQGKVVEVEVNCCSSDaaeKPKAFIHWVSQP--LQCEVRLYDRLFlhkhPEDTSEVPNGFLSDINP 718
Cdd:PTZ00437 434 SGNVVCKGfEVDAAGQPSVIHVDIDFERKD---KPKTNISWVSATacTPVEVRLYNALL----KDDRAAIDPEFLKFIDE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105397357 719 DSlQVISSAFVDTSVKRAKVFDKFQFERLGYFSLDPDSTADKPVFNRTVTLKEDPGK 775
Cdd:PTZ00437 507 DS-EVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
264-568 |
3.76e-161 |
|
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: 465.96 E-value: 3.76e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYQVTHASDNFQQL 343
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 344 YDLAVDLIRRGHAYVchqkgeelkgynappspwkdrpieeslllfermkkglfaegeatlrmkmvmedgktdpvayriky 423
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 424 tpHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTYTVVSKRKIIKL 503
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105397357 504 VETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTAPR 568
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
264-564 |
9.00e-148 |
|
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: 434.82 E-value: 9.00e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-YQVTHASDNFQQ 342
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 343 LYDLAVDLIRRGHAYVCHQKGEELKGYN----APPSPWKDRPIEESLLLF-ERMKKGLFAEGEATLRMKMVMED--GKTD 415
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEReeqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESpyVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 416 PVAYRIKYTP---HHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPV-QWEYGRLNLT 491
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105397357 492 YTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTT-EPHLLESCVREVLND 564
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNrLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
263-763 |
1.59e-89 |
|
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: 292.50 E-value: 1.59e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYQVTHASDNFQQ 342
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 343 LYDLAVDLIRRGHAYVCHQKGEELKGY--NAPPSPWKDRPIEESLLLFERMKKGLFAEGEATLRMKMVMEDGKT---DPV 417
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRELrnRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPairDWV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 418 AYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQA--RRSSYYWLCNALDVYCPVQWEYGRLNLTYTVV 495
Cdd:TIGR00463 252 IFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 496 SKRKiIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTAPRVMAVLEP 575
Cdd:TIGR00463 332 TSSA-RKGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNP 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 576 LKVTIMNLPEntQSEVRVPDFPANEAKGSHMVPFSRTIFIEQSDFREVMekgykrltpeQPVGLRHAGYVIsVQKVIKDT 655
Cdd:TIGR00463 411 VKIEIVGLPE--PKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRLMDAVNVI-YSKKELRY 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 656 QGKVVEVevnccssdAAEKPKAFIHWVSQPLQCEVRLydrlflhkhpedtsevpngflsdINPDSLqvISSAFVDTSVKR 735
Cdd:TIGR00463 478 HSEGLEG--------ARKLGKSIIHWLPAKDAVKVKV-----------------------IMPDAS--IVEGVIEADASE 524
|
490 500
....*....|....*....|....*...
gi 2105397357 736 AKVFDKFQFERLGYFSLDpdsTADKPVF 763
Cdd:TIGR00463 525 LEVGDVVQFERFGFARLD---SADKDGM 549
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
261-699 |
5.38e-89 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 288.23 E-value: 5.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 261 TGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK----PYqvtHA 336
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 337 SDNFQQLYDLAVDLIRRGHAYVCHQKGEELKGYNA-------PP---SPWKDRPIEESlllfERMKkglfAEGE-ATLRM 405
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALREtqtapgkPPrydGRCRDLSPEEL----ERML----AAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 406 KM-----VMED---GKT--------DPVAYRikytphhRTGdewciYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYY 469
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 470 WLCNALDVYCPvqwEYGRLNLTY----TVVSKRKiiklvetGVVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTV- 544
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKs 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 545 -SQTTTEPHLLESCVRevLNDTaPRVMAVLEPLKVTIMN------LPENTQSEVRVPDFPAN--EAKGSHMVPFSRT--- 612
Cdd:COG0008 279 dDQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAgiREDLERLVPLVRErak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 613 -----------IFIEQSDFREVMekgyKRLTPEQpvglrhagyvisVQKVIKDTQGKVVEVEVncCSSDAAekpKAFIHW 681
Cdd:COG0008 356 tlselaelarfFFIEREDEKAAK----KRLAPEE------------VRKVLKAALEVLEAVET--WDPETV---KGTIHW 414
|
490
....*....|....*...
gi 2105397357 682 VSQplQCEVRlyDRLFLH 699
Cdd:COG0008 415 VSA--EAGVK--DGLLFM 428
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
263-762 |
3.66e-85 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 285.46 E-value: 3.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYQVTHASDNFQQ 342
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 343 LYDLAVDLIRRGHAYVCHQKGEELKG--YNAPPSPWKDRPIEESLLLFERMKKGLFAEGEATLRMKMVMED-GKT--DPV 417
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKerMDGIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDpNKSlrDPV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 418 AYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYcPVQ-WEYGRLNLTYTVVS 496
Cdd:PLN02907 372 YYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFSRLNFVYTLLS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 497 KRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTAPRVMAVLEPL 576
Cdd:PLN02907 451 KRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEG 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 577 KV--TIMNLPENTqsEVR-VPDFPANEAKGSHMVPFSRTIFIEQSDfREVMEKGykrltpeQPVGLRHAGYVIsVQKVIK 653
Cdd:PLN02907 531 RVllTLTDGPETP--FVRiIPRHKKYEGAGKKATTFTNRIWLDYAD-AEAISEG-------EEVTLMDWGNAI-IKEITK 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 654 DTQGKVVEV--EVNCCSSDAAEKPKafIHW---VSQPLQCEVRLYDRLFLHKHPEDTSEvpngFLSDINPDSlQVISSAF 728
Cdd:PLN02907 600 DEGGAVTALsgELHLEGSVKTTKLK--LTWlpdTNELVPLSLVEFDYLITKKKLEEDDN----FLDVLNPCT-KKETAAL 672
|
490 500 510
....*....|....*....|....*....|....*
gi 2105397357 729 VDTSVKRAKVFDKFQFERLGYFSLD-PDSTADKPV 762
Cdd:PLN02907 673 GDSNMRNLKRGEIIQLERKGYYRCDaPFVRSSKPI 707
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
263-755 |
2.58e-84 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 279.92 E-value: 2.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYkPYQV--THASDNF 340
Cdd:PTZ00402 51 GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGV-SWDVgpTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 341 QQLYDLAVDLIRRGHAYVCHQKGEELKG--YNAPPSPWKDRPIEESLLLFERMKKGLfAEGEAT-LRMKMVMED---GKT 414
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNenkAMR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 415 DPVAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTYTV 494
Cdd:PTZ00402 209 DPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 495 VSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTAPRVMAVLE 574
Cdd:PTZ00402 289 MSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 575 PLKVTIMNLPENTQSEVRVPDFPANEAKGSHMVPFSRTIFIEQSDF------REV--MEKGYKRL----TPEQPVGLRHA 642
Cdd:PTZ00402 369 TLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVallkegDEVtlMDWGNAYIknirRSGEDALITDA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 643 GYVISVQKVIKDTQGKVVEVevnccssdaAEKPKAFIhwvsqplqCEVRLYDRLFLHKHPeDTSEVPNGFLSDINPDSLQ 722
Cdd:PTZ00402 449 DIVLHLEGDVKKTKFKLTWV---------PESPKAEV--------MELNEYDHLLTKKKP-DPEESIDDIIAPVTKYTQE 510
|
490 500 510
....*....|....*....|....*....|...
gi 2105397357 723 VISSAFVDTsVKRAkvfDKFQFERLGYFSLDPD 755
Cdd:PTZ00402 511 VYGEEALSV-LKKG---DIIQLERRGYYIVDDV 539
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
263-753 |
3.36e-78 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 262.48 E-value: 3.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEK---EEEKYfTAIKDMVEWLGYKPYQVTHASDN 339
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTkrpDPEAY-DMILEDLKWLGVKWDEVVIQSDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 340 FQQLYDLAVDLIRRGHAYVCHQKGEELKGY--NAPPSPWKDRPIEESLLLFERMKKGLFAEGEATLRMKMVMEDgkTDP- 416
Cdd:PRK04156 179 LEIYYEYARKLIEMGGAYVCTCDPEEFKELrdAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEH--PNPs 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 417 ----VAYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQ--ARRSSYywlcnaldVYCPVQWEY----- 485
Cdd:PRK04156 257 vrdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--------IYDYFGWEYpetih 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 486 -GRLNLTYTVVSKRKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLND 564
Cdd:PRK04156 329 yGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 565 TAPRVMAVLEPLKVTIMNLPEntqSEVRVPDFPANEAKGSHMVPFSRTIFIEQSDFREV------MEKGYKRLTPEQPVG 638
Cdd:PRK04156 409 IANRYFFVRDPVELEIEGAEP---LEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAEgkmvrlMDLFNVEITGVSVDK 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 639 LRHAGYvisvqkvikdtqgkvvevevnccSSDAAEKPKA-FIHWVsqplqcevrlydrlflhkhPEDTSeVPngfLSDIN 717
Cdd:PRK04156 486 ARYHSD-----------------------DLEEARKNKApIIQWV-------------------PEDES-VP---VRVLK 519
|
490 500 510
....*....|....*....|....*....|....*.
gi 2105397357 718 PDSLQVisSAFVDTSVKRAKVFDKFQFERLGYFSLD 753
Cdd:PRK04156 520 PDGGDI--EGLAEPDVADLEVDDIVQFERFGFVRID 553
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
263-762 |
1.91e-76 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 256.48 E-value: 1.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 263 GQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKPYQVTHASDNFQQ 342
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 343 LYDLAVDLIRRGHAYVCHQKGEELKGYNA--PPSPWKDRPIEESLLLFERMKKGLFAEGEATLRMKMVME-DGKT--DPV 417
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERAdrAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQsDNGTlrDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 418 AYRIKYTPHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTYTVVSK 497
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 498 RKIIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTAPRVMAV--LEP 575
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkADH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 576 LKVTIMNLPENTQSEVRVPDF-PANEAKGSHMVPFSRTIFIEQSDFREVMekgykrlTPEQPVGLRHAgyVISVQKVIKD 654
Cdd:PLN03233 330 TALTVTNADEEADFAFSETDChPKDPGFGKRAMRICDEVLLEKADTEDIQ-------LGEDIVLLRWG--VIEISKIDGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 655 TQGKVVEvevnccSSD--AAEKPKAFIHWVSQPLQCEVRLYDRLFLHKHPEDTsevpNGFLSDINPDSlQVISSAFVDTS 732
Cdd:PLN03233 401 LEGHFIP------DGDfkAAKKKISWIADVSDNIPVVLSEFDNLIIKEKLEED----DKFEDFINPDT-LAETDVIGDAG 469
|
490 500 510
....*....|....*....|....*....|.
gi 2105397357 733 VKRAKVFDKFQFERLGYFSLD-PDSTADKPV 762
Cdd:PLN03233 470 LKTLKEHDIIQLERRGFYRVDrPYMGEEKPL 500
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
2-161 |
2.02e-65 |
|
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N terminal to the catalytic domain of glutaminyl-tRNA synthetase (EC 6.1.1.18) in eukaryotes but not in Escherichia coli. This region is thought to bind RNA in a non-specific manner, enhancing interactions between the tRNA and enzyme, but is not essential for enzyme function.
Pssm-ID: 461353 Cd Length: 161 Bit Score: 214.35 E-value: 2.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 2 ADTLILFTSIGLSEQKAKETLKNEALSSALKEAITQAQNVtgvSEVDKAMGMLLYSMASRLKDT--KRVAFLSENIAQRK 79
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVE---SGCDKKQGNLLYTLATKLKGNalPHRPYLVKYIVDGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 80 ISTELQLAGALEFLMSHPHDPINQKEFEEACGVGVVITPEQIEDAVESVIKKHKEELLKERYHFNMGLLMREARGG--LK 157
Cdd:pfam04558 78 LKTTLQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKLpeLK 157
|
....
gi 2105397357 158 WADG 161
Cdd:pfam04558 158 WADP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
566-753 |
1.19e-60 |
|
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: 202.12 E-value: 1.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 566 APRVMAVLEPLKVTIMNLPENTQSEVRVPDFPANEAKGSHMVPFSRTIFIEQSDFrevmekgyKRLTPEQPVGLRHAgYV 645
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDA-YN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 646 ISVQKVIKDTQGKVVEVEVNC--CSSDAAEKPKA-FIHWVS--QPLQCEVRLYDRLFLHKHPEDtsevpngFLsdINPDS 720
Cdd:pfam03950 72 IKVTEVVKDEDGNVTELHCTYdgDDLGGARKVKGkIIHWVSasDAVPAEVRLYDRLFKDEDDAD-------FL--LNPDS 142
|
170 180 190
....*....|....*....|....*....|...
gi 2105397357 721 LQVISSAFVDTSVKRAKVFDKFQFERLGYFSLD 753
Cdd:pfam03950 143 LKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
265-574 |
8.23e-46 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 163.41 E-value: 8.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 265 IRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYK----PYqvtHASDNF 340
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPY---RQSDRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 341 QQLYDLAVDLIRRGhayvchqkgeelkgynappspwkdrpieeslllfermkkglfaegeatlrmkmvmedgktdpvayr 420
Cdd:cd00418 79 DLYRAYAEELIKKG------------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 421 ikytphhrtgdewcIYPTYDYTHCLCDSIENITHSLCTKEFQARRSSYYWLCNALDVYCPVQWEYGRLNLTY-TVVSKRK 499
Cdd:cd00418 93 --------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDgTKLSKRK 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105397357 500 IIKlvetgvvrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLE---SCVREVLNDTAPRV-MAVLE 574
Cdd:cd00418 159 LNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEmiaAFSVERVNSADATFdWAKLE 221
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
264-568 |
3.93e-45 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 162.14 E-value: 3.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 264 QIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPE--KEEEKYFTAIKDMVEWLGYKPYQVTHASDNFQ 341
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 342 QLYDLAVDLIRRGHAYVchqkgeelkgynappspwkdrpieeslllfermkkglfaegeatlrmkmvmedgktdpvayri 421
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 422 kytpHHRTGDEWCIYPTYDYTHCLCDSIENITHSLCTKEFQ--ARRSSYYWLCNALDVycPVQWEYGRLNLTYTVVSKRK 499
Cdd:cd09287 98 ----HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRYIYEYFGWEY--PETIHWGRLKIEGGKLSTSK 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105397357 500 IIKLVETGVVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVSQTTTEPHLLESCVREVLNDTAPR 568
Cdd:cd09287 172 IRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
164-255 |
1.20e-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: 118.18 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 164 IKNEVDMQVLHLLGPKTEADLEKKTKAPKAKVAENDVKPKKEELAVNGDATTGEGMSlmeqlRGEALKFHKTGENYKTEG 243
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPPKKKKKAKKKKAAKKKKKKAPIEEEENKRSMFS-----EGFLGKFHKPGENPKTDG 75
|
90
....*....|..
gi 2105397357 244 YVMTPNTMSLLK 255
Cdd:pfam04557 76 YVVTEHTMRLLK 87
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
265-327 |
7.03e-13 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 69.15 E-value: 7.03e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105397357 265 IRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLG 327
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLG 64
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
261-366 |
2.43e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 70.16 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 261 TGGQIRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPE---KEEEKyfTAIKDMvEWLG---------- 327
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLArstKESEE--AVLRDL-KWLGldwdegpdvg 118
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2105397357 328 --YKPYQVTHASDNFQQlydLAVDLIRRGHAYVCHQKGEEL 366
Cdd:PLN02627 119 geYGPYRQSERNAIYKQ---YAEKLLESGHVYPCFCTDEEL 156
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
266-360 |
9.94e-08 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 54.47 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 266 RTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRYDDTNPEKEEEKYFTAIKDMVEWLGYKP-----YQVTHasdnf 340
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWdgpvlYQSQR----- 81
|
90 100
....*....|....*....|.
gi 2105397357 341 QQLYDLAVD-LIRRGHAYVCH 360
Cdd:PRK05710 82 HDAYRAALDrLRAQGLVYPCF 102
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
267-350 |
8.08e-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: 40.54 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105397357 267 TRFPPEPNGILHIGHAKAINFNFGYAKANN-----GICFLRYDDTN-------------PEKEEEKYFTAIKDMVEWLGY 328
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGgligdpankkgenAKAFVERWIERIKEDVEYMFL 81
|
90 100
....*....|....*....|..
gi 2105397357 329 KPYQVTHASDNFQQLYDLAVDL 350
Cdd:cd00802 82 QAADFLLLYETECDIHLGGSDQ 103
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
267-317 |
1.23e-03 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 39.06 E-value: 1.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2105397357 267 TRFPPEPnGILHIGHAKAINFNFGYAkannGICFLRYDDTNPEKEEEKYFT 317
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPHE 47
|
|
| |
