|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
2-774 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 805.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 2 ATPDSLALFTGLGLSENKARETLKNEALSTQLREAATQAHQILGStiDKATGVLLYDLVSRLRDTRR--RSFLVSYIANK 79
Cdd:PLN02859 4 NSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGC--DKTVGNLLYTVATKYPANALvhRPTLLSYIVSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 80 KIHTGLQLSAALEYVRSHPQDPIDTKDFEQECGVGVVVTPEQIEEAVESTINKHQLQLLAERYRFNMGLLMGEARAALRW 159
Cdd:PLN02859 82 KIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 160 ADGKMIKNEVDMQVLHLLGPKMEADLVKKPKVAKArleetdrKTAKdvVEKGEVAGQTLSLMEQLRGEALKFHKPGENYK 239
Cdd:PLN02859 162 ADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKE-------KPAK--VEEKKVAVAAAPPSEEELNPYSIFPQPEENFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 240 -------TPGYVITPY-TMDLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEE 311
Cdd:PLN02859 233 vhtevffSDGSVLRPSnTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 312 AKFFTAIYDMVTWLGYTPYKVTYASDYFDQLYAWAVELIHGGLAYVCHQRVEELKGH--NPLPSPWRDRPKEESLLLFEA 389
Cdd:PLN02859 313 KEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 390 MRKGKFAEGEATLRMKLVM--EDGKM-DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSS 466
Cdd:PLN02859 393 MRRGLIEEGKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRAS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 467 YFWLCNALKVYCPVQWEYGRLNLHYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQT 546
Cdd:PLN02859 473 YYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 547 TM-EPHLLEACVRDVLNDAAPRAMAVLEPLQVVITNFPAPKPLDI---RVPNFPADETKGFHQVPFASTVFIERSDFKEE 622
Cdd:PLN02859 553 SLiRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLK 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 623 SEPGYKRLASGQPVGLRHtGYVIELQNIVRG-SSGCVERLEVTCRRADAgEKPKAFIHWVSQ------PLVCEIRLYECL 695
Cdd:PLN02859 633 DSKDYYGLAPGKSVLLRY-AFPIKCTDVVLAdDNETVVEIRAEYDPEKK-TKPKGVLHWVAEpspgvePLKVEVRLFDKL 710
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269954677 696 FqhkNPEDPVEVPgGFLSDLNPASLQVVEGALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGQIVFNRTVTLKEDPGK 774
Cdd:PLN02859 711 F---LSENPAELE-DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
264-770 |
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: 570.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 264 VRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTP-YKVTYASDYFDQL 342
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 343 YAWAVELIHGGLAYVCHQRVEELK---------GHNplpSPWRDRPKEESLLLFEAMRKGKFAEGEATLRMKLVMEDGKM 413
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrgtltdpGKN---SPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 414 ---DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYC-PVQWEYGRLNL 489
Cdd:TIGR00440 158 vmrDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 490 HYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPRAM 569
Cdd:TIGR00440 238 EGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 570 AVLEPLQVVITNFPAPKPLdIRVPNFPADETKGFHQVPFASTVFIERSDFKEESEPGYKRLASGQPVGLRHTgYVIELQN 649
Cdd:TIGR00440 318 AVIDPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAER 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 650 IVRGSSGCVERLEVT------CRRADAGEKPKAFIHWVS--QPLVCEIRLYECLFQHKNPedpvEVPGGFLSDLNPASLQ 721
Cdd:TIGR00440 396 VEKDAAGKITTIFCTydnktlGKEPADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNP----GAPDDFLSVINPESLV 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 269954677 722 VVEGaLVDCSVALAKPFDKFQFERLGYFSVDP-DSHQGQIVFNRTVTLKE 770
Cdd:TIGR00440 472 IKQG-FMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
263-567 |
1.60e-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: 462.11 E-value: 1.60e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTPYKVTYASDYFDQL 342
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 343 YAWAVELIHGGLAYVchqrveelkghnplpspwrdrpkeeslllfeamrkgkfaegeatlrmklvmedgkmdpvayrvky 422
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 423 tpHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYCPVQWEYGRLNLHYAVVSKRKILQL 502
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269954677 503 VAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPR 567
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
263-563 |
4.60e-153 |
|
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: 448.31 E-value: 4.60e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTP-YKVTYASDYFDQ 341
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 342 LYAWAVELIHGGLAYVCHQRVEELKGHNP----LPSPWRDRPKEESLLLF-EAMRKGKFAEGEATLRMKLVME-DGKM-D 414
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREeqeaLGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 415 PVAYRVKYTP---HHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYCPV-QWEYGRLNLH 490
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269954677 491 YAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQ-TTMEPHLLEACVRDVLND 563
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
260-682 |
3.48e-85 |
|
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: 277.83 E-value: 3.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 260 TGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYT----PYkvtYA 335
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 336 SDYFDQLYAWAVELIHGGLAYVCHQRVEEL---------KGHNPL-PSPWRDRPKEESlllfEAMRkgkfAEGE-ATLRM 404
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEEL----ERML----AAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 405 KL-----VMED---GKM--------DPVAYRVkytphhrTGdkwciYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYF 468
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 469 WLCNALKVYCPvqwEYGRLNLHY----AVVSKRKilqlvaaGAVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVA 544
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 545 --QTTMEPHLLEACVrDVlnDAAPRAMAVLEPLQVVITNFPAPKPLDIR------VPNFPAD--ETKGFHQVPF------ 608
Cdd:COG0008 279 ddQEIFSLEELIEAF-DL--DRVSRSPAVFDPVKLVWLNGPYIRALDDEelaellAPELPEAgiREDLERLVPLvrerak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 609 --------ASTVFIERSDfkeeSEPGYKRLASGqpvglrhtgyviELQNIVRGSSGCVERLEvtcrRADAgEKPKAFIHW 680
Cdd:COG0008 356 tlselaelARFFFIERED----EKAAKKRLAPE------------EVRKVLKAALEVLEAVE----TWDP-ETVKGTIHW 414
|
..
gi 269954677 681 VS 682
Cdd:COG0008 415 VS 416
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
2-774 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 805.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 2 ATPDSLALFTGLGLSENKARETLKNEALSTQLREAATQAHQILGStiDKATGVLLYDLVSRLRDTRR--RSFLVSYIANK 79
Cdd:PLN02859 4 NSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGC--DKTVGNLLYTVATKYPANALvhRPTLLSYIVSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 80 KIHTGLQLSAALEYVRSHPQDPIDTKDFEQECGVGVVVTPEQIEEAVESTINKHQLQLLAERYRFNMGLLMGEARAALRW 159
Cdd:PLN02859 82 KIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 160 ADGKMIKNEVDMQVLHLLGPKMEADLVKKPKVAKArleetdrKTAKdvVEKGEVAGQTLSLMEQLRGEALKFHKPGENYK 239
Cdd:PLN02859 162 ADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKE-------KPAK--VEEKKVAVAAAPPSEEELNPYSIFPQPEENFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 240 -------TPGYVITPY-TMDLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEE 311
Cdd:PLN02859 233 vhtevffSDGSVLRPSnTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 312 AKFFTAIYDMVTWLGYTPYKVTYASDYFDQLYAWAVELIHGGLAYVCHQRVEELKGH--NPLPSPWRDRPKEESLLLFEA 389
Cdd:PLN02859 313 KEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 390 MRKGKFAEGEATLRMKLVM--EDGKM-DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSS 466
Cdd:PLN02859 393 MRRGLIEEGKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRAS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 467 YFWLCNALKVYCPVQWEYGRLNLHYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQT 546
Cdd:PLN02859 473 YYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 547 TM-EPHLLEACVRDVLNDAAPRAMAVLEPLQVVITNFPAPKPLDI---RVPNFPADETKGFHQVPFASTVFIERSDFKEE 622
Cdd:PLN02859 553 SLiRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLK 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 623 SEPGYKRLASGQPVGLRHtGYVIELQNIVRG-SSGCVERLEVTCRRADAgEKPKAFIHWVSQ------PLVCEIRLYECL 695
Cdd:PLN02859 633 DSKDYYGLAPGKSVLLRY-AFPIKCTDVVLAdDNETVVEIRAEYDPEKK-TKPKGVLHWVAEpspgvePLKVEVRLFDKL 710
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269954677 696 FqhkNPEDPVEVPgGFLSDLNPASLQVVEGALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGQIVFNRTVTLKEDPGK 774
Cdd:PLN02859 711 F---LSENPAELE-DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
262-775 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 699.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTP-YKVTYASDYFD 340
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWsGELRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 341 QLYAWAVELIHGGLAYVCHQRVEELK---------GHNplpSPWRDRPKEESLLLFEAMRKGKFAEGEATLRMKLVMEDG 411
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIReyrgtltepGKN---SPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 412 KM---DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYC-PVQWEYGRL 487
Cdd:PRK05347 185 NInmrDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSRL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 488 NLHYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPR 567
Cdd:PRK05347 265 NLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 568 AMAVLEPLQVVITNFPAPKPLDIRVPNFPADETKGFHQVPFASTVFIERSDFKEESEPGYKRLASGQPVGLRHtGYVIEL 647
Cdd:PRK05347 345 AMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRN-AYVIKC 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 648 QNIVRGSSGCVerLEVTCR--------RADAGEKPKAFIHWVS--QPLVCEIRLYECLFQHKNPEDPVEvpggFLSDLNP 717
Cdd:PRK05347 424 EEVVKDADGNI--TEIHCTydpdtlsgNPADGRKVKGTIHWVSaaHAVPAEVRLYDRLFTVPNPAAGKD----FLDFLNP 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 269954677 718 ASLQVVEGaLVDCSVALAKPFDKFQFERLGYFSVDPDSHQGQIVFNRTVTLKEDPGKI 775
Cdd:PRK05347 498 DSLVIKQG-FVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
262-774 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 577.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYT-PYKVTYASDYFD 340
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 341 QLYAWAVELIHGGLAYVCHQRVEE---LKGH--NP-LPSPWRDRPKEESLLLFEAMRKGKFAEGEATLRMKLVMEDGKM- 413
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEireLRGTvtEPgTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMk 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 414 --DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYC--PVQWEYGRLNL 489
Cdd:PRK14703 190 lrDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPprPRQYEFARLAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 490 HYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPRAM 569
Cdd:PRK14703 270 GYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVM 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 570 AVLEPLQVVITNFPAPKPLDIRVPNFPADETK-GFHQVPFASTVFIERSDFKEESEPGYKRLASGQPVGLRHtGYVIELQ 648
Cdd:PRK14703 350 AVLDPLKVVIENLPAGKVEELDLPYWPHDVPKeGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRG-AYIIRCD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 649 NIVRGSSGCVERLEVT-----CRRADAGEKPKAFIHWVS--QPLVCEIRLYECLFQHKNPEdpvEVPGGFLSDLNPASLQ 721
Cdd:PRK14703 429 EVVRDADGAVTELRCTydpesAKGEDTGRKAAGVIHWVSakHALPAEVRLYDRLFKVPQPE---AADEDFLEFLNPDSLR 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 269954677 722 VVEGaLVDCSVALAKPFDKFQFERLGYFSVDP-DSHQGQIVFNRTVTLKEDPGK 774
Cdd:PRK14703 506 VAQG-RVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGA 558
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
264-770 |
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: 570.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 264 VRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTP-YKVTYASDYFDQL 342
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 343 YAWAVELIHGGLAYVCHQRVEELK---------GHNplpSPWRDRPKEESLLLFEAMRKGKFAEGEATLRMKLVMEDGKM 413
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrgtltdpGKN---SPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 414 ---DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYC-PVQWEYGRLNL 489
Cdd:TIGR00440 158 vmrDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 490 HYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPRAM 569
Cdd:TIGR00440 238 EGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 570 AVLEPLQVVITNFPAPKPLdIRVPNFPADETKGFHQVPFASTVFIERSDFKEESEPGYKRLASGQPVGLRHTgYVIELQN 649
Cdd:TIGR00440 318 AVIDPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAER 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 650 IVRGSSGCVERLEVT------CRRADAGEKPKAFIHWVS--QPLVCEIRLYECLFQHKNPedpvEVPGGFLSDLNPASLQ 721
Cdd:TIGR00440 396 VEKDAAGKITTIFCTydnktlGKEPADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNP----GAPDDFLSVINPESLV 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 269954677 722 VVEGaLVDCSVALAKPFDKFQFERLGYFSVDP-DSHQGQIVFNRTVTLKE 770
Cdd:TIGR00440 472 IKQG-FMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKD 520
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
241-774 |
6.34e-176 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 517.23 E-value: 6.34e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 241 PGYVITPytmDLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYD 320
Cdd:PTZ00437 32 PGCRNTP---ELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIME 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 321 MVTWLGYTPYKVTYASDYFDQLYAWAVELIHGGLAYVCHQRVEELKGH--NPLPSPWRDRPKEESLLLFEAMRKGKFAEG 398
Cdd:PTZ00437 109 MVKWMGWKPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 399 EATLRMKLVMEDGK---MDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALK 475
Cdd:PTZ00437 189 EATLRVKADMKSDNpnmRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 476 VYCPVQWEYGRLNLHYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEA 555
Cdd:PTZ00437 269 LWRPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLEN 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 556 CVRDVLNDAAPRAMAVLEPLQVVITNFPAPKplDIRVPNFPADETKGFHQVPFASTVFIERSDFK-EESEPGYKRLASG- 633
Cdd:PTZ00437 349 TLREDLDERCERRLMVIDPIKVVVDNWKGER--EFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGp 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 634 QPVGLRHTGYVI----ELQNIVRGSsgcVERLEVTCRRADageKPKAFIHWVSQP--LVCEIRLYECLFQhknpEDPVEV 707
Cdd:PTZ00437 427 RVVGLKYSGNVVckgfEVDAAGQPS---VIHVDIDFERKD---KPKTNISWVSATacTPVEVRLYNALLK----DDRAAI 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269954677 708 PGGFLSDLNPASLQVVEGaLVDCSVALAKPFDKFQFERLGYFSVDPDSHQGQIVFNRTVTLKEDPGK 774
Cdd:PTZ00437 497 DPEFLKFIDEDSEVVSHG-YAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
263-567 |
1.60e-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: 462.11 E-value: 1.60e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTPYKVTYASDYFDQL 342
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 343 YAWAVELIHGGLAYVchqrveelkghnplpspwrdrpkeeslllfeamrkgkfaegeatlrmklvmedgkmdpvayrvky 422
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 423 tpHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYCPVQWEYGRLNLHYAVVSKRKILQL 502
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269954677 503 VAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPR 567
Cdd:cd00807 174 VDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
263-563 |
4.60e-153 |
|
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: 448.31 E-value: 4.60e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTP-YKVTYASDYFDQ 341
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 342 LYAWAVELIHGGLAYVCHQRVEELKGHNP----LPSPWRDRPKEESLLLF-EAMRKGKFAEGEATLRMKLVME-DGKM-D 414
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREeqeaLGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 415 PVAYRVKYTP---HHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYCPV-QWEYGRLNLH 490
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269954677 491 YAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQ-TTMEPHLLEACVRDVLND 563
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
262-754 |
3.34e-85 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 282.24 E-value: 3.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGyTPYKV--TYASDYF 339
Cdd:PTZ00402 51 GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLG-VSWDVgpTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 340 DQLYAWAVELIHGGLAYVCHQRVEELKG--HNPLPSPWRDRPKEESLLLFEAMRKGKfAEGEAT-LRMKLVMED---GKM 413
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNenkAMR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 414 DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYCPVQWEYGRLNLHYAV 493
Cdd:PTZ00402 209 DPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 494 VSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPRAMAVLE 573
Cdd:PTZ00402 289 MSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 574 PLQVVIT-----NFPA-PKPLDIRVPNFpadETKGFHQvpfASTVFIERSDFkeesepgyKRLASGQPVGLRHTG--YVi 645
Cdd:PTZ00402 369 TLKVRCTvegqiHLEAcEKLLHKKVPDM---GEKTYYK---SDVIFLDAEDV--------ALLKEGDEVTLMDWGnaYI- 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 646 elQNIVR-GSSGCVERLEVTCRRADAGEKPKAFIHWVSQ---PLVCEIRLYECLFQHKNPeDPVEVPGGFLSDLNPASLQ 721
Cdd:PTZ00402 434 --KNIRRsGEDALITDADIVLHLEGDVKKTKFKLTWVPEspkAEVMELNEYDHLLTKKKP-DPEESIDDIIAPVTKYTQE 510
|
490 500 510
....*....|....*....|....*....|...
gi 269954677 722 VVEGAlvdcSVALAKPFDKFQFERLGYFSVDPD 754
Cdd:PTZ00402 511 VYGEE----ALSVLKKGDIIQLERRGYYIVDDV 539
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
260-682 |
3.48e-85 |
|
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: 277.83 E-value: 3.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 260 TGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYT----PYkvtYA 335
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 336 SDYFDQLYAWAVELIHGGLAYVCHQRVEEL---------KGHNPL-PSPWRDRPKEESlllfEAMRkgkfAEGE-ATLRM 404
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEEL----ERML----AAGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 405 KL-----VMED---GKM--------DPVAYRVkytphhrTGdkwciYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYF 468
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 469 WLCNALKVYCPvqwEYGRLNLHY----AVVSKRKilqlvaaGAVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVA 544
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 545 --QTTMEPHLLEACVrDVlnDAAPRAMAVLEPLQVVITNFPAPKPLDIR------VPNFPAD--ETKGFHQVPF------ 608
Cdd:COG0008 279 ddQEIFSLEELIEAF-DL--DRVSRSPAVFDPVKLVWLNGPYIRALDDEelaellAPELPEAgiREDLERLVPLvrerak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 609 --------ASTVFIERSDfkeeSEPGYKRLASGqpvglrhtgyviELQNIVRGSSGCVERLEvtcrRADAgEKPKAFIHW 680
Cdd:COG0008 356 tlselaelARFFFIERED----EKAAKKRLAPE------------EVRKVLKAALEVLEAVE----TWDP-ETVKGTIHW 414
|
..
gi 269954677 681 VS 682
Cdd:COG0008 415 VS 416
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
214-752 |
7.78e-84 |
|
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: 277.09 E-value: 7.78e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 214 AGQTLSLMEQLRGEALKFhKPGENYKtpgyVITPYTMDLLKQHLEITG---------GQVRTRFPPEPNGILHIGHAKAI 284
Cdd:TIGR00463 40 AKEVLEAVEAAVEEVNSL-SPEEQKE----LMKRLGLDIKKKEKKRKGlrelpgakmGEVVMRFAPNPSGPLHIGHARAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 285 NFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTPYKVTYASDYFDQLYAWAVELIHGGLAYVCHQRVEE 364
Cdd:TIGR00463 115 ILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 365 LKG--HNPLPSPWRDRPKEESLLLFEAMRKGKFAEGEATLRMKLVMEDGK---MDPVAYRVKYTPHHRTGDKWCIYPTYD 439
Cdd:TIGR00463 195 FRElrNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNpaiRDWVIFRIVKTPHPRTGDKYRVYPTMD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 440 YTHCLCDSIEHITHSLCTKEFQA--RRSSYFWLCNALKVycPVQWEYGRLNLH-YAVVSKRKILQLVAAGAVRDWDDPRL 516
Cdd:TIGR00463 275 FSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEP--PEFIHWGRLKIDdVRALSTSSARKGILRGEYSGWDDPRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 517 FTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPRAMAVLEPLQVVITNfpAPKPLDIRVPNFP 596
Cdd:TIGR00463 353 PTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVG--LPEPKRVERPLHP 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 597 ADETKGFHQVPFASTVFIERSDFKEESepgykrlasgQPVGLRHTGYVielqnIVRGSSGCVERLEVTCRRadagEKPKA 676
Cdd:TIGR00463 431 DHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRLMDAVNV-----IYSKKELRYHSEGLEGAR----KLGKS 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269954677 677 FIHWVSQPLVCEIRLyeCLFQHKNPEDPVEVPGGFLSdlnpaslqvvegalVDcsvalakpfDKFQFERLGYFSVD 752
Cdd:TIGR00463 492 IIHWLPAKDAVKVKV--IMPDASIVEGVIEADASELE--------------VG---------DVVQFERFGFARLD 542
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
262-752 |
2.39e-80 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 272.37 E-value: 2.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTPYKVTYASDYFDQ 341
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 342 LYAWAVELIHGGLAYVCHQRVEELKGH--NPLPSPWRDRPKEESLLLFEAMRKGKFAEGEATLRMKLVMED--GKM-DPV 416
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKErmDGIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDpnKSLrDPV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 417 AYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYcPVQ-WEYGRLNLHYAVVS 495
Cdd:PLN02907 372 YYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFSRLNFVYTLLS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 496 KRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPRAMAVLEPL 575
Cdd:PLN02907 451 KRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEG 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 576 QVVITNFPAPKPLDIR-VPNFPADETKGFHQVPFASTVFIERSDFKEESEpgykrlasGQPVGLRHTGYVIeLQNIVRGS 654
Cdd:PLN02907 531 RVLLTLTDGPETPFVRiIPRHKKYEGAGKKATTFTNRIWLDYADAEAISE--------GEEVTLMDWGNAI-IKEITKDE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 655 SGCVERLEVTCRRADAGEKPKAFIHWVSQ-PLVCEIRL--YECLFQHKNPEDPVEvpggFLSDLNPASlQVVEGALVDCS 731
Cdd:PLN02907 602 GGAVTALSGELHLEGSVKTTKLKLTWLPDtNELVPLSLveFDYLITKKKLEEDDN----FLDVLNPCT-KKETAALGDSN 676
|
490 500
....*....|....*....|.
gi 269954677 732 VALAKPFDKFQFERLGYFSVD 752
Cdd:PLN02907 677 MRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
262-752 |
6.13e-79 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 264.41 E-value: 6.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEK----EEAkfftaiYDMV----TWLGYTPYKVT 333
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTkrpdPEA------YDMIledlKWLGVKWDEVV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 334 YASDYFDQLYAWAVELIHGGLAYVCHQRVEELKG--HNPLPSPWRDRPKEESLLLFEAMRKGKFAEGEATLRMKLVMEDG 411
Cdd:PRK04156 174 IQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKElrDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHP 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 412 kmDP-----VAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQ--ARRSSYFWLCNALKVycPVQWEY 484
Cdd:PRK04156 254 --NPsvrdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRYIYDYFGWEY--PETIHY 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 485 GRLNLHYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDA 564
Cdd:PRK04156 330 GRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPI 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 565 APRAMAVLEPLQVVITNfpaPKPLDIRVPNFPADETKGFHQVPFASTVFIERSDFKEEsepgykrlasGQPVGLrhtgyv 644
Cdd:PRK04156 410 ANRYFFVRDPVELEIEG---AEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAE----------GKMVRL------ 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 645 IELQNIVRgSSGCVERLEVTCRRADAGEKPKA-FIHWVsqplvceirlyeclfqhknPED---PVEVpggflsdLNPASl 720
Cdd:PRK04156 471 MDLFNVEI-TGVSVDKARYHSDDLEEARKNKApIIQWV-------------------PEDesvPVRV-------LKPDG- 522
|
490 500 510
....*....|....*....|....*....|..
gi 269954677 721 QVVEGaLVDCSVALAKPFDKFQFERLGYFSVD 752
Cdd:PRK04156 523 GDIEG-LAEPDVADLEVDDIVQFERFGFVRID 553
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
262-752 |
1.27e-77 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 259.56 E-value: 1.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTPYKVTYASDYFDQ 341
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 342 LYAWAVELIHGGLAYVCHQRVEELKGH--NPLPSPWRDRPKEESLLLFEAMRKGKFAEGEATLRMKLVM--EDGKM-DPV 416
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKEraDRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMqsDNGTLrDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 417 AYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYCPVQWEYGRLNLHYAVVSK 496
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 497 RKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPRAMAVLEPLQ 576
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIDKADH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 577 VVITNFPAPKPLDIRVPN---FPADETKGFHQVPFASTVFIERSDFKEesepgykrLASGQPVGLRHTGyVIELQNIvrg 653
Cdd:PLN03233 330 TALTVTNADEEADFAFSEtdcHPKDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLLRWG-VIEISKI--- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 654 sSGCVERLEVTCRRADAGEKPKAFIHWVSQ--PLVceirLYEclFQHKNPEDPVEVPGGFLSDLNPASLQVVEgALVDCS 731
Cdd:PLN03233 398 -DGDLEGHFIPDGDFKAAKKKISWIADVSDniPVV----LSE--FDNLIIKEKLEEDDKFEDFINPDTLAETD-VIGDAG 469
|
490 500
....*....|....*....|.
gi 269954677 732 VALAKPFDKFQFERLGYFSVD 752
Cdd:PLN03233 470 LKTLKEHDIIQLERRGFYRVD 490
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
5-162 |
2.86e-64 |
|
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: 211.27 E-value: 2.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 5 DSLALFTGLGLSENKARETLKNEALSTQLREAATQAHqiLGSTIDKATGVLLYDLVSRLRDT--RRRSFLVSYIANKKIH 82
Cdd:pfam04558 2 ELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAG--VESGCDKKQGNLLYTLATKLKGNalPHRPYLVKYIVDGKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 83 TGLQLSAALEYVRSHPQDPIDTKDFEQECGVGVVVTPEQIEEAVESTINKHQLQLLAERYRFNMGLLMGEARA--ALRWA 160
Cdd:pfam04558 80 TTLQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKlpELKWA 159
|
..
gi 269954677 161 DG 162
Cdd:pfam04558 160 DP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
565-752 |
3.94e-59 |
|
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: 198.26 E-value: 3.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 565 APRAMAVLEPLQVVITNFPAPKPLDIRVPNFPADETKGFHQVPFASTVFIERSDFkeesepgyKRLASGQPVGLRHtGYV 644
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMD-AYN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 645 IELQNIVRGSSGCVERLEVTCRRADAGE--KPKA-FIHWVS--QPLVCEIRLYECLFQHKNPEDpvevpggFLsdLNPAS 719
Cdd:pfam03950 72 IKVTEVVKDEDGNVTELHCTYDGDDLGGarKVKGkIIHWVSasDAVPAEVRLYDRLFKDEDDAD-------FL--LNPDS 142
|
170 180 190
....*....|....*....|....*....|...
gi 269954677 720 LQVVEGALVDCSVALAKPFDKFQFERLGYFSVD 752
Cdd:pfam03950 143 LKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
263-567 |
1.54e-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: 163.29 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPE--KEEAKFFTAIYDMVTWLGYTPYKVTYASDYFD 340
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 341 QLYAWAVELIHGGLAYVchqrveelkghnplpspwrdrpkeeslllfeamrkgkfaegeatlrmklvmedgkmdpvayrv 420
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 421 kytpHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQ--ARRSSYFWLCNALKVycPVQWEYGRLNLHYAVVSKRK 498
Cdd:cd09287 98 ----HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRYIYEYFGWEY--PETIHWGRLKIEGGKLSTSK 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269954677 499 ILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPR 567
Cdd:cd09287 172 IRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
264-555 |
7.75e-45 |
|
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: 160.72 E-value: 7.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 264 VRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYT----PYkvtYASDYF 339
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPY---RQSDRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 340 DQLYAWAVELIHGGlayvchqrveelkghnplpspwrdrpkeeslllfeamrkgkfaegeatlrmklvmedgkmdpvayr 419
Cdd:cd00418 79 DLYRAYAEELIKKG------------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 420 vkytphhrtgdkwcIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYCPVQWEYGRLNLHYA-VVSKRK 498
Cdd:cd00418 93 --------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGtKLSKRK 158
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 269954677 499 ILQlvaagavrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEA 555
Cdd:cd00418 159 LNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEM 199
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
165-254 |
1.10e-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: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 165 IKNEVDMQVLHLLGPKMEADLVKKPKVAKarlEETDRKTAKDVVEKGEVAGQTLSLMEQLRGEALKFHKPGENYKTPGYV 244
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPPKKKK---KAKKKKAAKKKKKKAPIEEEENKRSMFSEGFLGKFHKPGENPKTDGYV 77
|
90
....*....|
gi 269954677 245 ITPYTMDLLK 254
Cdd:pfam04557 78 VTEHTMRLLK 87
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
264-353 |
2.63e-14 |
|
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: 73.00 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 264 VRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLG------------YTPYk 331
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldwdegpdvggpYGPY- 80
|
90 100
....*....|....*....|..
gi 269954677 332 vtYASDYFDQLYAWAVELIHGG 353
Cdd:cd00808 81 --RQSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
258-365 |
7.23e-11 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 65.53 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 258 EITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLG----------- 326
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldwdegpdvgg 119
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 269954677 327 -YTPYKVTYASDYFDQLyawAVELIHGGLAYVCHQRVEEL 365
Cdd:PLN02627 120 eYGPYRQSERNAIYKQY---AEKLLESGHVYPCFCTDEEL 156
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
263-359 |
6.62e-09 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 57.94 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269954677 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTPYK-VTYASDYFDq 341
Cdd:PRK05710 5 PYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGpVLYQSQRHD- 83
|
90
....*....|....*....
gi 269954677 342 LYAWAVE-LIHGGLAYVCH 359
Cdd:PRK05710 84 AYRAALDrLRAQGLVYPCF 102
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
266-310 |
4.64e-04 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 41.31 E-value: 4.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 269954677 266 TRFPPEPNGILHIGHAKAINFNFGYAKANN-----GICFLRFDDTNPEKE 310
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGGLIG 51
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
266-316 |
1.18e-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: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 269954677 266 TRFPPEPnGILHIGHAKAINFNFGYAkannGICFLRFDDTNPEKEEAKFFT 316
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPHE 47
|
|
| |
