|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
6-732 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 745.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 6 SLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGStiDKATGILLYGLASRLRDTRR--LSFLVSYIASKKIHT 83
Cdd:PLN02859 8 PLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGC--DKTVGNLLYTVATKYPANALvhRPTLLSYIVSSKIKT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 84 EPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGK 163
Cdd:PLN02859 86 PAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 164 MIKNEVDMQVLHLLGPKLEADLEK---KFKVAKARLEEtdrrtAKDVVENGETADQTLSlmeqlrgEALKFHKPGENYK- 239
Cdd:PLN02859 166 IVKKLIDKKLYELLGEKTAADNEKpvkKKKEKPAKVEE-----KKVAVAAAPPSEEELN-------PYSIFPQPEENFKv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 240 ------TPGYVVTPH-TMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEA 312
Cdd:PLN02859 234 htevffSDGSVLRPSnTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 313 KFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGH--NTLPSPWRDRPMEESLLLFEAM 390
Cdd:PLN02859 314 EYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 391 RKGKFSEGEATLRMKLVM--EDGKM-DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSY 467
Cdd:PLN02859 394 RRGLIEEGKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 468 FWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTT 547
Cdd:PLN02859 474 YWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 548 M-EPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQV---PNFPADETKGFHQVPFAPIVFIERTDFKEEP 623
Cdd:PLN02859 554 LiRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKD 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 624 EPGFKRLAWGQPVGLRHtGYVIELQHVVKGPS-GCVESLEVTCRRADAgEKPKAFIHWVSQ------PLMCEVRLYERLF 696
Cdd:PLN02859 634 SKDYYGLAPGKSVLLRY-AFPIKCTDVVLADDnETVVEIRAEYDPEKK-TKPKGVLHWVAEpspgvePLKVEVRLFDKLF 711
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370484858 697 qhkNPEDPTEVPgGFLSDLNL------------------------------------------LVFNRTVTLKEDPGK 732
Cdd:PLN02859 712 ---LSENPAELE-DWLEDLNPqskevisgayavpslkdakvgdrfqferlgyfavdkdstpekLVFNRTVTLKDSYGK 785
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
264-716 |
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: 532.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 264 VRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTP-YKVTYASDYFDQL 342
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 343 YAWAVELIRRGLAYVCHQRGEELK---GHNTLP---SPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKM--- 413
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 414 DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYC-PVQWEYGRLNLHYA 492
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 493 VVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVL 572
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 573 ESLRVIITNFPAAKSLdIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTgYVIELQHVVK 652
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370484858 653 GPSG------CVESLEVTCRRADAGEKPKAFIHWVS--QPLMCEVRLYERLFQHKNPEDPTevpgGFLSDLN 716
Cdd:TIGR00440 399 DAAGkittifCTYDNKTLGKEPADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNPGAPD----DFLSVIN 466
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
263-567 |
4.59e-164 |
|
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: 472.12 E-value: 4.59e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQL 342
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 343 YAWAVELIRRGLAYVchqrgeelkghntlpspwrdrpmeeslllfeamrkgkfsegeatlrmklvmedgkmdpvayrvky 422
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 423 tpHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQL 502
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370484858 503 VATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPR 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 |
5.11e-157 |
|
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: 457.17 E-value: 5.11e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTP-YKVTYASDYFDQ 341
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 342 LYAWAVELIRRGLAYVCHQRGEELKGHN----TLPSPWRDRPMEESLLLF-EAMRKGKFSEGEATLRMKLVME-DGKM-D 414
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEReeqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 415 PVAYRVKYTP---HHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV-QWEYGRLNLH 490
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370484858 491 YAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQ-TTMEPHLLEACVRDVLND 563
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
260-631 |
1.94e-82 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 269.74 E-value: 1.94e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 260 TGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYT----PYkvtYA 335
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 336 SDYFDQLYAWAVELIRRGLAYVCHQRGEEL---------KGHNTL-PSPWRDRPMEESlllfEAMRKgkfsEGE-ATLRM 404
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEEL----ERMLA----AGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 405 KL-----VMED---GKM--------DPVAYRVkytphhrTGdkwciYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYF 468
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 469 WLCNALDVYCPvqwEYGRLNLHY----AVVSKRKilqlvatGAVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVA 544
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 545 --QTTMEPHLLEACVRdvLNDTaPRAMAVLESLRVIITNFPAAKSLDIQ------VPNFPAD--ETKGFHQVPF------ 608
Cdd:COG0008 279 ddQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNGPYIRALDDEelaellAPELPEAgiREDLERLVPLvrerak 355
|
410 420 430
....*....|....*....|....*....|.
gi 1370484858 609 --------APIVFIERTDfkeePEPGFKRLA 631
Cdd:COG0008 356 tlselaelARFFFIERED----EKAAKKRLA 382
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
6-732 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 745.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 6 SLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGStiDKATGILLYGLASRLRDTRR--LSFLVSYIASKKIHT 83
Cdd:PLN02859 8 PLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGC--DKTVGNLLYTVATKYPANALvhRPTLLSYIVSSKIKT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 84 EPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGK 163
Cdd:PLN02859 86 PAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 164 MIKNEVDMQVLHLLGPKLEADLEK---KFKVAKARLEEtdrrtAKDVVENGETADQTLSlmeqlrgEALKFHKPGENYK- 239
Cdd:PLN02859 166 IVKKLIDKKLYELLGEKTAADNEKpvkKKKEKPAKVEE-----KKVAVAAAPPSEEELN-------PYSIFPQPEENFKv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 240 ------TPGYVVTPH-TMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEA 312
Cdd:PLN02859 234 htevffSDGSVLRPSnTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 313 KFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGH--NTLPSPWRDRPMEESLLLFEAM 390
Cdd:PLN02859 314 EYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEESLKLFEDM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 391 RKGKFSEGEATLRMKLVM--EDGKM-DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSY 467
Cdd:PLN02859 394 RRGLIEEGKATLRMKQDMqnDNFNMyDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 468 FWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTT 547
Cdd:PLN02859 474 YWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 548 M-EPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQV---PNFPADETKGFHQVPFAPIVFIERTDFKEEP 623
Cdd:PLN02859 554 LiRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKD 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 624 EPGFKRLAWGQPVGLRHtGYVIELQHVVKGPS-GCVESLEVTCRRADAgEKPKAFIHWVSQ------PLMCEVRLYERLF 696
Cdd:PLN02859 634 SKDYYGLAPGKSVLLRY-AFPIKCTDVVLADDnETVVEIRAEYDPEKK-TKPKGVLHWVAEpspgvePLKVEVRLFDKLF 711
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370484858 697 qhkNPEDPTEVPgGFLSDLNL------------------------------------------LVFNRTVTLKEDPGK 732
Cdd:PLN02859 712 ---LSENPAELE-DWLEDLNPqskevisgayavpslkdakvgdrfqferlgyfavdkdstpekLVFNRTVTLKDSYGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
262-733 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 639.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTP-YKVTYASDYFD 340
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWsGELRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 341 QLYAWAVELIRRGLAYVCHQRGEELKGHN-TL-----PSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKM- 413
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIREYRgTLtepgkNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNIn 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 414 --DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYC-PVQWEYGRLNLH 490
Cdd:PRK05347 188 mrDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSRLNLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 491 YAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMA 570
Cdd:PRK05347 268 YTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 571 VLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHtGYVIELQHV 650
Cdd:PRK05347 348 VLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRN-AYVIKCEEV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 651 VKGPSGCVesLEVTCR--------RADAGEKPKAFIHWVS--QPLMCEVRLYERLFQHKNPEDPTEvpggFLSDLN---- 716
Cdd:PRK05347 427 VKDADGNI--TEIHCTydpdtlsgNPADGRKVKGTIHWVSaaHAVPAEVRLYDRLFTVPNPAAGKD----FLDFLNpdsl 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1370484858 717 -------------------------------------LLVFNRTVTLKEDPGKV 733
Cdd:PRK05347 501 vikqgfvepsladakpedrfqferegyfcadkdstpgKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
264-716 |
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: 532.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 264 VRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTP-YKVTYASDYFDQL 342
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 343 YAWAVELIRRGLAYVCHQRGEELK---GHNTLP---SPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKM--- 413
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 414 DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYC-PVQWEYGRLNLHYA 492
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 493 VVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVL 572
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 573 ESLRVIITNFPAAKSLdIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTgYVIELQHVVK 652
Cdd:TIGR00440 321 DPVEVVIENLSDEYEL-ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNA-YVIKAERVEK 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370484858 653 GPSG------CVESLEVTCRRADAGEKPKAFIHWVS--QPLMCEVRLYERLFQHKNPEDPTevpgGFLSDLN 716
Cdd:TIGR00440 399 DAAGkittifCTYDNKTLGKEPADGRKVKGVIHWVSasSKYPTETRLYDRLFKVPNPGAPD----DFLSVIN 466
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
262-732 |
2.54e-176 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 523.52 E-value: 2.54e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYT-PYKVTYASDYFD 340
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 341 QLYAWAVELIRRGLAYVCHQRGEE---LKGHNTLP---SPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKM- 413
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEireLRGTVTEPgtpSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMk 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 414 --DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYC--PVQWEYGRLNL 489
Cdd:PRK14703 190 lrDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPprPRQYEFARLAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 490 HYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAM 569
Cdd:PRK14703 270 GYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVM 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 570 AVLESLRVIITNFPAAKSLDIQVPNFPADETK-GFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHtGYVIELQ 648
Cdd:PRK14703 350 AVLDPLKVVIENLPAGKVEELDLPYWPHDVPKeGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRG-AYIIRCD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 649 HVVKGPSGCVESLEVT-----CRRADAGEKPKAFIHWVS--QPLMCEVRLYERLFQHKNPEdptEVPGGFLSDLN----- 716
Cdd:PRK14703 429 EVVRDADGAVTELRCTydpesAKGEDTGRKAAGVIHWVSakHALPAEVRLYDRLFKVPQPE---AADEDFLEFLNpdslr 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1370484858 717 -------------------------------------LLVFNRTVTLKEDPGK 732
Cdd:PRK14703 506 vaqgrvepavrddpadtryqferqgyfwadpvdsrpdALVFNRIITLKDTWGA 558
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
263-567 |
4.59e-164 |
|
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: 472.12 E-value: 4.59e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQL 342
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 343 YAWAVELIRRGLAYVchqrgeelkghntlpspwrdrpmeeslllfeamrkgkfsegeatlrmklvmedgkmdpvayrvky 422
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 423 tpHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQL 502
Cdd:cd00807 96 --HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQL 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370484858 503 VATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPR 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 |
5.11e-157 |
|
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: 457.17 E-value: 5.11e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTP-YKVTYASDYFDQ 341
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 342 LYAWAVELIRRGLAYVCHQRGEELKGHN----TLPSPWRDRPMEESLLLF-EAMRKGKFSEGEATLRMKLVME-DGKM-D 414
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEReeqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMEsPYVFrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 415 PVAYRVKYTP---HHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV-QWEYGRLNLH 490
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370484858 491 YAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQ-TTMEPHLLEACVRDVLND 563
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
241-716 |
6.42e-155 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 461.76 E-value: 6.42e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 241 PGYVVTPHtmnLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICD 320
Cdd:PTZ00437 32 PGCRNTPE---LLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIME 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 321 MVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGH--NTLPSPWRDRPMEESLLLFEAMRKGKFSEG 398
Cdd:PTZ00437 109 MVKWMGWKPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 399 EATLRMKLVMEDGK---MDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALD 475
Cdd:PTZ00437 189 EATLRVKADMKSDNpnmRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 476 VYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEA 555
Cdd:PTZ00437 269 LWRPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLEN 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 556 CVRDVLNDTAPRAMAVLESLRVIITNFPAakSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFK-EEPEPGFKRLAWG- 633
Cdd:PTZ00437 349 TLREDLDERCERRLMVIDPIKVVVDNWKG--EREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGp 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 634 QPVGLRHTGYVIELQHVVKG---PSgcVESLEVTCRRADageKPKAFIHWVSQP--LMCEVRLYERLFQhknpEDPTEVP 708
Cdd:PTZ00437 427 RVVGLKYSGNVVCKGFEVDAagqPS--VIHVDIDFERKD---KPKTNISWVSATacTPVEVRLYNALLK----DDRAAID 497
|
....*...
gi 1370484858 709 GGFLSDLN 716
Cdd:PTZ00437 498 PEFLKFID 505
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
262-577 |
1.75e-84 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 279.15 E-value: 1.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGyTPYKV--TYASDYF 339
Cdd:PTZ00402 51 GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLG-VSWDVgpTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 340 DQLYAWAVELIRRGLAYVCHQRGEELKG--HNTLPSPWRDRPMEESLLLFEAMRKGKfSEGEAT-LRMKLVMED---GKM 413
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNenkAMR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 414 DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAV 493
Cdd:PTZ00402 209 DPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 494 VSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLE 573
Cdd:PTZ00402 289 MSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSN 368
|
....
gi 1370484858 574 SLRV 577
Cdd:PTZ00402 369 TLKV 372
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
260-631 |
1.94e-82 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 269.74 E-value: 1.94e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 260 TGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYT----PYkvtYA 335
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDwdegPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 336 SDYFDQLYAWAVELIRRGLAYVCHQRGEEL---------KGHNTL-PSPWRDRPMEESlllfEAMRKgkfsEGE-ATLRM 404
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEEL----ERMLA----AGEpPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 405 KL-----VMED---GKM--------DPVAYRVkytphhrTGdkwciYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYF 468
Cdd:COG0008 150 KIpeegvVFDDlvrGEItfpnpnlrDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 469 WLCNALDVYCPvqwEYGRLNLHY----AVVSKRKilqlvatGAVrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVA 544
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 545 --QTTMEPHLLEACVRdvLNDTaPRAMAVLESLRVIITNFPAAKSLDIQ------VPNFPAD--ETKGFHQVPF------ 608
Cdd:COG0008 279 ddQEIFSLEELIEAFD--LDRV-SRSPAVFDPVKLVWLNGPYIRALDDEelaellAPELPEAgiREDLERLVPLvrerak 355
|
410 420 430
....*....|....*....|....*....|.
gi 1370484858 609 --------APIVFIERTDfkeePEPGFKRLA 631
Cdd:COG0008 356 tlselaelARFFFIERED----EKAAKKRLA 382
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
262-625 |
3.11e-81 |
|
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: 269.39 E-value: 3.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQ 341
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 342 LYAWAVELIRRGLAYVCHQRGEELKG--HNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGK---MDPV 416
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRElrNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNpaiRDWV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 417 AYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQA--RRSSYFWLCNALDVycPVQWEYGRLNLH-YAV 493
Cdd:TIGR00463 252 IFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEP--PEFIHWGRLKIDdVRA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 494 VSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLE 573
Cdd:TIGR00463 330 LSTSSARKGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWN 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1370484858 574 SLRVIITNFPAAKslDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEP 625
Cdd:TIGR00463 410 PVKIEIVGLPEPK--RVERPLHPDHPEIGERVLILRGEIYVPKDDLEEGVEP 459
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
262-580 |
1.01e-77 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 264.28 E-value: 1.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQ 341
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 342 LYAWAVELIRRGLAYVC-----HQRGEELKGhntLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMED--GKM- 413
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDdtpreQMRKERMDG---IESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDpnKSLr 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 414 DPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYcPVQ-WEYGRLNLHYA 492
Cdd:PLN02907 369 DPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFSRLNFVYT 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 493 VVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVL 572
Cdd:PLN02907 448 LLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVL 527
|
....*...
gi 1370484858 573 ESLRVIIT 580
Cdd:PLN02907 528 KEGRVLLT 535
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
262-622 |
1.66e-76 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 257.09 E-value: 1.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPE--KEEAKFFTAICDMVAWLGYTPYKVTYASDYF 339
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDEVVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 340 DQLYAWAVELIRRGLAYVCHQRGEELKG--HNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGkmDP-- 415
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKElrDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHP--NPsv 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 416 ---VAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQ--ARRSSYFWLCNALDVycPVQWEYGRLNLH 490
Cdd:PRK04156 258 rdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRYIYDYFGWEY--PETIHYGRLKIE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 491 YAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMA 570
Cdd:PRK04156 336 GFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYFF 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1370484858 571 VLESLRVIITNfpaAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEE 622
Cdd:PRK04156 416 VRDPVELEIEG---AEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAE 464
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
262-621 |
1.59e-74 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 250.31 E-value: 1.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 262 GQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQ 341
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 342 LYAWAVELIRRGLAYVCHQRGEELKGH--NTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVM--EDGKM-DPV 416
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKEraDRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMqsDNGTLrDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 417 AYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSK 496
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 497 RKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLES-- 574
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIDKAdh 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1370484858 575 LRVIITNFP-AAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKE 621
Cdd:PLN03233 330 TALTVTNADeEADFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTED 377
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
5-162 |
2.09e-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: 213.58 E-value: 2.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 5 DSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQqtLGSTIDKATGILLYGLASRLRDT--RRLSFLVSYIASKKIH 82
Cdd:pfam04558 2 ELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAG--VESGCDKKQGNLLYTLATKLKGNalPHRPYLVKYIVDGKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 83 TEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAV--LKWA 160
Cdd:pfam04558 80 TTLQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKLpeLKWA 159
|
..
gi 1370484858 161 DG 162
Cdd:pfam04558 160 DP 161
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
263-567 |
1.45e-46 |
|
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: 165.60 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPE--KEEAKFFTAICDMVAWLGYTPYKVTYASDYFD 340
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 341 QLYAWAVELIRRGLAYVchqrgeelkghntlpspwrdrpmeeslllfeamrkgkfsegeatlrmklvmedgkmdpvayrv 420
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 421 kytpHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQ--ARRSSYFWLCNALDVycPVQWEYGRLNLHYAVVSKRK 498
Cdd:cd09287 98 ----HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRYIYEYFGWEY--PETIHWGRLKIEGGKLSTSK 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370484858 499 ILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPR 567
Cdd:cd09287 172 IRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
264-575 |
5.05e-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: 163.80 E-value: 5.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 264 VRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYT----PYkvtYASDYF 339
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPY---RQSDRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 340 DQLYAWAVELIRRGlayvchqrgeelkghntlpspwrdrpmeeslllfeamrkgkfsegeatlrmklvmedgkmdpvayr 419
Cdd:cd00418 79 DLYRAYAEELIKKG------------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 420 vkytphhrtgdkwcIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYA-VVSKRK 498
Cdd:cd00418 93 --------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGtKLSKRK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 499 ILQlvatgavrdwddprlfTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLE---ACVRDVLNDTAPR-AMAVLES 574
Cdd:cd00418 159 LNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEmiaAFSVERVNSADATfDWAKLEW 222
|
.
gi 1370484858 575 L 575
Cdd:cd00418 223 L 223
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
565-703 |
1.09e-40 |
|
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: 147.03 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 565 APRAMAVLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDfkeepepgFKRLAWGQPVGLRHtGYV 644
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIERED--------FKRLAPGEEVRLMD-AYN 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370484858 645 IELQHVVKGPSGCVESLEVTCRRADAGE--KPKA-FIHWVS--QPLMCEVRLYERLFQHKNPED 703
Cdd:pfam03950 72 IKVTEVVKDEDGNVTELHCTYDGDDLGGarKVKGkIIHWVSasDAVPAEVRLYDRLFKDEDDAD 135
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
165-254 |
1.45e-32 |
|
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: 120.87 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 165 IKNEVDMQVLHLLGPKLEADLEKKfkvAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYV 244
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKP---PKKKKKAKKKKAAKKKKKKAPIEEEENKRSMFSEGFLGKFHKPGENPKTDGYV 77
|
90
....*....|
gi 1370484858 245 VTPHTMNLLK 254
Cdd:pfam04557 78 VTEHTMRLLK 87
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
264-353 |
4.21e-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: 69.54 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 264 VRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLG------------YTPYk 331
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldwdegpdvggpYGPY- 80
|
90 100
....*....|....*....|..
gi 1370484858 332 vtYASDYFDQLYAWAVELIRRG 353
Cdd:cd00808 81 --RQSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
258-365 |
3.29e-11 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 66.30 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 258 EITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLG----------- 326
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldwdegpdvgg 119
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370484858 327 -YTPYKVTYASDYFDQLyawAVELIRRGLAYVCHQRGEEL 365
Cdd:PLN02627 120 eYGPYRQSERNAIYKQY---AEKLLESGHVYPCFCTDEEL 156
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
263-359 |
3.72e-10 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 61.79 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 263 QVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYK-VTYASDYFDq 341
Cdd:PRK05710 5 PYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGpVLYQSQRHD- 83
|
90
....*....|....*....
gi 1370484858 342 LYAWAVE-LIRRGLAYVCH 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 ... |
266-371 |
4.40e-05 |
|
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: 44.01 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484858 266 TRFPPEPNGILHIGHAKAINFNFGYAKANN-----GICFLRFDDTNPEKEEA--KFFTAICDMV-AWLGytPYKVTYASD 337
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGGLIGDPanKKGENAKAFVeRWIE--RIKEDVEYM 79
|
90 100 110
....*....|....*....|....*....|....
gi 1370484858 338 yFDQLYAWAVELIRRGLAYVChqrGEELKGHNTL 371
Cdd:cd00802 80 -FLQAADFLLLYETECDIHLG---GSDQLGHIEL 109
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
266-316 |
1.05e-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: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1370484858 266 TRFPPEPnGILHIGHAKAINFNFGYAkannGICFLRFDDTNPEKEEAKFFT 316
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPHE 47
|
|
| |
