|
Name |
Accession |
Description |
Interval |
E-value |
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
252-806 |
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: 880.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 252 VRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEP-WKITYSSDYFDEL 330
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 331 YGLAEVLINNNKGYICHCTAEDIKRGRGIKEDgtPGgerFACKHRDQSIELNLQEFRNMRDGKYKPGEAILRMKQDLGSP 410
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTD--PG---KNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 411 SPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVF-RPAQREYGRL 489
Cdd:TIGR00440 156 FPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 490 NITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRKYLEDTTPR 569
Cdd:TIGR00440 236 NLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 570 LMFVLDPVEVVVDNLTDDFeELATIPFRPGTPEFGERTVPFTNKFYIERSDFSENVdDKEFFRLTPNQSVgLIKVSHTVS 649
Cdd:TIGR00440 316 AMAVIDPVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEA-NKQYKRLVLGKEV-RLRNAYVIK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 650 FKSLEKDETGKIIRVHVNYDNKVE--EGTKPKKPKTYIQWVPVSSKYNsplrvVETRVHNQLFKSENPsSHPQGFLKDIN 727
Cdd:TIGR00440 393 AERVEKDAAGKITTIFCTYDNKTLgkEPADGRKVKGVIHWVSASSKYP-----TETRLYDRLFKVPNP-GAPDDFLSVIN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 728 PESeIVYKESVMEHNFGHVVKNSpwvvdsvknsefyvgedkeakevcRFQAMRVGYFTLD-KDSTADKVILNRIVSLKDA 806
Cdd:TIGR00440 467 PES-LVIKQGFMEHSLGDAVANK------------------------RFQFEREGYFCLDsKESTTEKVVFNRTVSLKDA 521
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
10-809 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 648.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 10 LFSQVGFEDNKVKEIVKNKKVSDSLSKLIKETPSDYQWNKSTRALVHNLASLIKGADLPKSDLIISGIINGNLKTSLQVD 89
Cdd:PLN02859 11 LFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSKIKTPAQLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 90 GAFKYVKANG-DASTVDGMNENSGVGIEVTEDQVRNYVMQYIQENKESIMKERYKLVPGI-FANVknLKELKWADPRSFK 167
Cdd:PLN02859 91 AAFSFFSSTGpESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDlLGQV--RKRLPWADPKIVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 168 PIIDQEILKLLGPKDERDLVKKKVKNNEKKKTTSAKKTSDDSATTGPKR----TMF----------NEGFLGDlhkvGE- 232
Cdd:PLN02859 169 KLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAAPPSEEElnpySIFpqpeenfkvhTEVFFSD----GSv 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 233 -NPQAYPELMKKHLE*TGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVS 311
Cdd:PLN02859 245 lRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 312 WLGFEPWKITYSSDYFDELYGLAEVLINNNKGYICHCTAEDIKRGRGIKEDgTPggerfackHRDQSIELNLQEFRNMRD 391
Cdd:PLN02859 325 WMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMN-SP--------WRDRPIEESLKLFEDMRR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 392 GKYKPGEAILRMKQDLGSPSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEW 471
Cdd:PLN02859 396 GLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYW 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 472 LCDQVHVFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTN-I 550
Cdd:PLN02859 476 LLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSlI 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 551 QVVRFESAIRKYLEDTTPRLMFVLDPVEVVVDNLTDD-FEEL--ATIPFRPGTPEFGERTVPFTNKFYIERSDFSENvDD 627
Cdd:PLN02859 556 RMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGeVIELdaKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLK-DS 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 628 KEFFRLTPNQSVGL-----IKVSHTVSfksleKDETGKIIRVHVNYDNKveegtKPKKPKTYIQWVPVSSKYNSPLRvVE 702
Cdd:PLN02859 635 KDYYGLAPGKSVLLryafpIKCTDVVL-----ADDNETVVEIRAEYDPE-----KKTKPKGVLHWVAEPSPGVEPLK-VE 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 703 TRVHNQLFKSENPSSHpQGFLKDINPESEIVYKESVMehnfghvvknspwvVDSVKNSEfyVGEdkeakevcRFQAMRVG 782
Cdd:PLN02859 704 VRLFDKLFLSENPAEL-EDWLEDLNPQSKEVISGAYA--------------VPSLKDAK--VGD--------RFQFERLG 758
|
810 820
....*....|....*....|....*..
gi 1069885398 783 YFTLDKDSTADKVILNRIVSLKDAASK 809
Cdd:PLN02859 759 YFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
251-565 |
5.42e-146 |
|
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: 431.36 E-value: 5.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEP-WKITYSSDYFDE 329
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 330 LYGLAEVLINNNKGYICHCTAEDIKRGRGIKedgtpggERFACKHRDQSIELNLQEF-RNMRDGKYKPGEAILRMKQDLG 408
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ-------EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 409 SPsPQMWDLIAYRVLNAP---HPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRP-AQR 484
Cdd:pfam00749 154 SP-YVFRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPpFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 485 EYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTS-TTNIQVVRFESAIRKYL 563
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKL 312
|
..
gi 1069885398 564 ED 565
Cdd:pfam00749 313 DW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
251-569 |
1.13e-144 |
|
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: 425.13 E-value: 1.13e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEPWKITYSSDYFDEL 330
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 331 YGLAEVLINNNKGYIchctaedikrgrgikedgtpggerfackhrdqsielnlqefrnmrdgkykpgeailrmkqdlgsp 410
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 411 spqmwdliayrvlnapHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGRLN 490
Cdd:cd00807 96 ----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLN 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1069885398 491 ITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRKYLEDTTPR 569
Cdd:cd00807 160 LTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
248-703 |
2.49e-83 |
|
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: 273.98 E-value: 2.49e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 248 TGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEpW--KITYSSD 325
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLD-WdeGPYYQSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 326 YFDELYGLAEVLINNNKGYICHCTAEDI--KRGRGIKEDGTPggeRFACKHRDQSIElnlqEFRNMRD-GKykpgEAILR 402
Cdd:COG0008 80 RFDIYYEYAEKLIEKGKAYVCFCTPEELeaLRETQTAPGKPP---RYDGRCRDLSPE----ELERMLAaGE----PPVLR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 403 MK--------QDLGS-----PSPQMWDLIAYRVlnaphprTGtkwkiYPTYDFTHCLVDSMENITHSLCTTEFYLSRESY 469
Cdd:COG0008 149 FKipeegvvfDDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 470 EWLCDQVHVFRPaqrEYGRLNIT----GTVLSKRKIAqlvdekfvrgwddprlFTLEAIRRRGVPPGAILSFINTLGVtt 545
Cdd:COG0008 217 IWLYEALGWEPP---EFAHLPLIlgpdGTKLSKRKGA----------------VTVSGLRRRGYLPEAIRNYLALLGW-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 546 STTNIQVVR-FESAIRKYLEDTTPRLMFVLDPVEVVVDNL----TDDFEELAT--IPFRP--GTPEFGERTVPFTNkfyi 616
Cdd:COG0008 276 SKSDDQEIFsLEELIEAFDLDRVSRSPAVFDPVKLVWLNGpyirALDDEELAEllAPELPeaGIREDLERLVPLVR---- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 617 ERSDF-SENVDDKEFFRLTPNQSVGLIKVshtvsfksLEKDETGKIIRVHVNYDNKVEEGTkPKKPKTYIQWVPVSS--- 692
Cdd:COG0008 352 ERAKTlSELAELARFFFIEREDEKAAKKR--------LAPEEVRKVLKAALEVLEAVETWD-PETVKGTIHWVSAEAgvk 422
|
490
....*....|...
gi 1069885398 693 --KYNSPLRVVET 703
Cdd:COG0008 423 dgLLFMPLRVALT 435
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
5-163 |
3.68e-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: 211.65 E-value: 3.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 5 EELTHLFSQVGFEDNKVKEIVKNKKVSDSLSKLIKETPSDYQWNKSTRALVHNLASLIKGADLPKSDLIISGIINGNLKT 84
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 85 SLQVDGAFKYV-KANGDASTVDGMNENSGVGIEVTEDQVRNYVMQYIQENKESIMKERY-KLVPGIFANVKNLKELKWAD 162
Cdd:pfam04558 81 TLQVDAALKYLlKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYrFNVGKLLGEVRKLPELKWAD 160
|
.
gi 1069885398 163 P 163
Cdd:pfam04558 161 P 161
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
166-244 |
7.71e-23 |
|
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: 93.14 E-value: 7.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 166 FKPIIDQEILKLLGPKDERDLVKK--KVKNNEKKKTTSAKKTSDDSATTGPKRTMFNEGFLGDLHKVGENPQAYPELMKK 243
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPpkKKKKAKKKKAAKKKKKKAPIEEEENKRSMFSEGFLGKFHKPGENPKTDGYVVTE 80
|
.
gi 1069885398 244 H 244
Cdd:pfam04557 81 H 81
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
252-806 |
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: 880.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 252 VRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEP-WKITYSSDYFDEL 330
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 331 YGLAEVLINNNKGYICHCTAEDIKRGRGIKEDgtPGgerFACKHRDQSIELNLQEFRNMRDGKYKPGEAILRMKQDLGSP 410
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTD--PG---KNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 411 SPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVF-RPAQREYGRL 489
Cdd:TIGR00440 156 FPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 490 NITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRKYLEDTTPR 569
Cdd:TIGR00440 236 NLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 570 LMFVLDPVEVVVDNLTDDFeELATIPFRPGTPEFGERTVPFTNKFYIERSDFSENVdDKEFFRLTPNQSVgLIKVSHTVS 649
Cdd:TIGR00440 316 AMAVIDPVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEA-NKQYKRLVLGKEV-RLRNAYVIK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 650 FKSLEKDETGKIIRVHVNYDNKVE--EGTKPKKPKTYIQWVPVSSKYNsplrvVETRVHNQLFKSENPsSHPQGFLKDIN 727
Cdd:TIGR00440 393 AERVEKDAAGKITTIFCTYDNKTLgkEPADGRKVKGVIHWVSASSKYP-----TETRLYDRLFKVPNP-GAPDDFLSVIN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 728 PESeIVYKESVMEHNFGHVVKNSpwvvdsvknsefyvgedkeakevcRFQAMRVGYFTLD-KDSTADKVILNRIVSLKDA 806
Cdd:TIGR00440 467 PES-LVIKQGFMEHSLGDAVANK------------------------RFQFEREGYFCLDsKESTTEKVVFNRTVSLKDA 521
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
10-809 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 648.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 10 LFSQVGFEDNKVKEIVKNKKVSDSLSKLIKETPSDYQWNKSTRALVHNLASLIKGADLPKSDLIISGIINGNLKTSLQVD 89
Cdd:PLN02859 11 LFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSKIKTPAQLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 90 GAFKYVKANG-DASTVDGMNENSGVGIEVTEDQVRNYVMQYIQENKESIMKERYKLVPGI-FANVknLKELKWADPRSFK 167
Cdd:PLN02859 91 AAFSFFSSTGpESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDlLGQV--RKRLPWADPKIVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 168 PIIDQEILKLLGPKDERDLVKKKVKNNEKKKTTSAKKTSDDSATTGPKR----TMF----------NEGFLGDlhkvGE- 232
Cdd:PLN02859 169 KLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAAPPSEEElnpySIFpqpeenfkvhTEVFFSD----GSv 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 233 -NPQAYPELMKKHLE*TGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVS 311
Cdd:PLN02859 245 lRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 312 WLGFEPWKITYSSDYFDELYGLAEVLINNNKGYICHCTAEDIKRGRGIKEDgTPggerfackHRDQSIELNLQEFRNMRD 391
Cdd:PLN02859 325 WMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMN-SP--------WRDRPIEESLKLFEDMRR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 392 GKYKPGEAILRMKQDLGSPSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEW 471
Cdd:PLN02859 396 GLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYW 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 472 LCDQVHVFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTN-I 550
Cdd:PLN02859 476 LLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSlI 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 551 QVVRFESAIRKYLEDTTPRLMFVLDPVEVVVDNLTDD-FEEL--ATIPFRPGTPEFGERTVPFTNKFYIERSDFSENvDD 627
Cdd:PLN02859 556 RMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGeVIELdaKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLK-DS 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 628 KEFFRLTPNQSVGL-----IKVSHTVSfksleKDETGKIIRVHVNYDNKveegtKPKKPKTYIQWVPVSSKYNSPLRvVE 702
Cdd:PLN02859 635 KDYYGLAPGKSVLLryafpIKCTDVVL-----ADDNETVVEIRAEYDPE-----KKTKPKGVLHWVAEPSPGVEPLK-VE 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 703 TRVHNQLFKSENPSSHpQGFLKDINPESEIVYKESVMehnfghvvknspwvVDSVKNSEfyVGEdkeakevcRFQAMRVG 782
Cdd:PLN02859 704 VRLFDKLFLSENPAEL-EDWLEDLNPQSKEVISGAYA--------------VPSLKDAK--VGD--------RFQFERLG 758
|
810 820
....*....|....*....|....*..
gi 1069885398 783 YFTLDKDSTADKVILNRIVSLKDAASK 809
Cdd:PLN02859 759 YFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
250-805 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 609.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 250 GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEpW--KITYSSDYF 327
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFD-WsgELRYASDYF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 328 DELYGLAEVLINNNKGYICHCTAEDIKRGRG-IKEDGTPGgerfacKHRDQSIELNLQEFRNMRDGKYKPGEAILRMKQD 406
Cdd:PRK05347 107 DQLYEYAVELIKKGKAYVDDLSAEEIREYRGtLTEPGKNS------PYRDRSVEENLDLFERMRAGEFPEGSAVLRAKID 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 407 LGSPSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHV-FRPAQRE 485
Cdd:PRK05347 181 MASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIpPHPRQYE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 486 YGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRKYLED 565
Cdd:PRK05347 261 FSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 566 TTPRLMFVLDPVEVVVDNLTDDFEELATIPFRPGTPEFGERTVPFTNKFYIERSDFSENvDDKEFFRLTPNQSVGLiKVS 645
Cdd:PRK05347 341 NAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEE-PPKKYFRLVPGKEVRL-RNA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 646 HTVSFKSLEKDETGKIIRVHVNYDNKVEEGTKPK--KPKTYIQWvpVSSKYNSPlrvVETRVHNQLFKSENPSShPQGFL 723
Cdd:PRK05347 419 YVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADgrKVKGTIHW--VSAAHAVP---AEVRLYDRLFTVPNPAA-GKDFL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 724 KDINPESEIVyKESVMEhnfghvvknsPWVvdsvknsefyvgedKEAKEVCRFQAMRVGYFTLDKDSTADKVILNRIVSL 803
Cdd:PRK05347 493 DFLNPDSLVI-KQGFVE----------PSL--------------ADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGL 547
|
..
gi 1069885398 804 KD 805
Cdd:PRK05347 548 RD 549
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
250-809 |
1.52e-178 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 531.99 E-value: 1.52e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 250 GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEpW--KITYSSDYF 327
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFD-WgeHLYYASDYF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 328 DELYGLAEVLINNNKGYICHCTAEDIKRGRG-IKEDGTPGgerfacKHRDQSIELNLQEFRNMRDGKYKPGEAILRMKQD 406
Cdd:PRK14703 109 ERMYAYAEQLIKMGLAYVDSVSEEEIRELRGtVTEPGTPS------PYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKID 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 407 LGSPSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVF--RPAQR 484
Cdd:PRK14703 183 MSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWppRPRQY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 485 EYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRKYLE 564
Cdd:PRK14703 263 EFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 565 DTTPRLMFVLDPVEVVVDNLTDDFEELATIPFRPG-TPEFGERTVPFTNKFYIERSDFSENvDDKEFFRLTPNQSVGLiK 643
Cdd:PRK14703 343 RRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHdVPKEGSRKVPFTRELYIERDDFSED-PPKGFKRLTPGREVRL-R 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 644 VSHTVSFKSLEKDETGKIIRVHVNYDNKVEEGTKP-KKPKTYIQWvpVSSKYNSPlrvVETRVHNQLFKSENPSSHPQGF 722
Cdd:PRK14703 421 GAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTgRKAAGVIHW--VSAKHALP---AEVRLYDRLFKVPQPEAADEDF 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 723 LKDINPESEIVYKesvmehnfgHVVKnsPWVVDSVKNSefyvgedkeakevcRFQAMRVGYFTLDK-DSTADKVILNRIV 801
Cdd:PRK14703 496 LEFLNPDSLRVAQ---------GRVE--PAVRDDPADT--------------RYQFERQGYFWADPvDSRPDALVFNRII 550
|
....*...
gi 1069885398 802 SLKDAASK 809
Cdd:PRK14703 551 TLKDTWGA 558
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
238-809 |
3.28e-174 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 513.76 E-value: 3.28e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 238 PELMKKHLE*TGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEP 317
Cdd:PTZ00437 38 PELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 318 WKITYSSDYFDELYGLAEVLINNNKGYICHCTAEDIKRGRGIKEDgTPggerfackHRDQSIELNLQEFRNMRDGKYKPG 397
Cdd:PTZ00437 118 DWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQRED-SP--------WRNRSVEENLLLFEHMRQGRYAEG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 398 EAILRMKQDLGSPSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVH 477
Cdd:PTZ00437 189 EATLRVKADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 478 VFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFES 557
Cdd:PTZ00437 269 LWRPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLEN 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 558 AIRKYLEDTTPRLMFVLDPVEVVVDNLtdDFEELATIPFRPGTPEFGERTVPFTNKFYIERSDFSENVDDKEFFRLTPNQ 637
Cdd:PTZ00437 349 TLREDLDERCERRLMVIDPIKVVVDNW--KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRTEDNNSKFYGLAPGP 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 638 SVGLIKVSHTVSFKSLEKDETGKIIRVHVNYDNKveegtKPKKPKTYIQWvpVSSKYNSPlrvVETRVHNQLFKSENPSS 717
Cdd:PTZ00437 427 RVVGLKYSGNVVCKGFEVDAAGQPSVIHVDIDFE-----RKDKPKTNISW--VSATACTP---VEVRLYNALLKDDRAAI 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 718 HPQgFLKDINPESEIVykesvmEHNFGHvvknspwvvdsvknsefyvGEDKEAKEVCRFQAMRVGYFTLDKDSTADKVIL 797
Cdd:PTZ00437 497 DPE-FLKFIDEDSEVV------SHGYAE-------------------KGIENAKHFESVQAERFGYFVVDPDTRPDHLVM 550
|
570
....*....|..
gi 1069885398 798 NRIVSLKDAASK 809
Cdd:PTZ00437 551 NRVLGLREDKEK 562
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
251-565 |
5.42e-146 |
|
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: 431.36 E-value: 5.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEP-WKITYSSDYFDE 329
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 330 LYGLAEVLINNNKGYICHCTAEDIKRGRGIKedgtpggERFACKHRDQSIELNLQEF-RNMRDGKYKPGEAILRMKQDLG 408
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ-------EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 409 SPsPQMWDLIAYRVLNAP---HPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRP-AQR 484
Cdd:pfam00749 154 SP-YVFRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPpFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 485 EYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTS-TTNIQVVRFESAIRKYL 563
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKL 312
|
..
gi 1069885398 564 ED 565
Cdd:pfam00749 313 DW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
251-569 |
1.13e-144 |
|
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: 425.13 E-value: 1.13e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEPWKITYSSDYFDEL 330
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 331 YGLAEVLINNNKGYIchctaedikrgrgikedgtpggerfackhrdqsielnlqefrnmrdgkykpgeailrmkqdlgsp 410
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 411 spqmwdliayrvlnapHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGRLN 490
Cdd:cd00807 96 ----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLN 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1069885398 491 ITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRKYLEDTTPR 569
Cdd:cd00807 160 LTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
250-701 |
6.50e-101 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 323.73 E-value: 6.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 250 GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAP--EYFESIKRMVSWLGFEPWKITYSSDYF 327
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPdpEAYDMILEDLKWLGVKWDEVVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 328 DELYGLAEVLINNNKGYICHCTAEDIKRgrgIKEDGTPggerfaCKHRDQSIELNLQEFRNMRDGKYKPGEAILRMKQDL 407
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKE---LRDAGKP------CPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 408 GSPSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESyewlcdQVHVFR------P 481
Cdd:PRK04156 251 EHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEK------QRYIYDyfgweyP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 482 AQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRK 561
Cdd:PRK04156 325 ETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 562 YLEDTTPRLMFVLDPVEVVVDNltdDFEELATIPFRPGTPEFGERTVPFTNKFYIERSDFsenVDDKEFFRLtpnqsVGL 641
Cdd:PRK04156 405 LIDPIANRYFFVRDPVELEIEG---AEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDL---EAEGKMVRL-----MDL 473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1069885398 642 IKVSHTvsfkslekdetgKIIRVHVNYDNK-VEEGTKPKKPktYIQWVPVSSKynSPLRVV 701
Cdd:PRK04156 474 FNVEIT------------GVSVDKARYHSDdLEEARKNKAP--IIQWVPEDES--VPVRVL 518
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
250-692 |
8.48e-94 |
|
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: 304.44 E-value: 8.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 250 GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEPWKITYSSDYFDE 329
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 330 LYGLAEVLINNNKGYICHCTAEDIKRgrgIKEDGTPggerfaCKHRDQSIELNLQEFRNMRDGKYKPGEAILRMKQDLGS 409
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRE---LRNRGEA------CHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 410 PSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGRL 489
Cdd:TIGR00463 243 KNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHWGRL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 490 NI--TGTVLSKRKIAQLVDEKFVrGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRKYLEDTT 567
Cdd:TIGR00463 323 KIddVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 568 PRLMFVLDPVEVVVDNLTDDFEELatIPFRPGTPEFGERTVPFTNKFYIERSDFSENvddKEFFRLTPNQSVGLIKVSHT 647
Cdd:TIGR00463 402 RRYFFIWNPVKIEIVGLPEPKRVE--RPLHPDHPEIGERVLILRGEIYVPKDDLEEG---VEPVRLMDAVNVIYSKKELR 476
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1069885398 648 VSFKSLEKDEtgkiirvhvnydnkveegtkpKKPKTYIQWVPVSS 692
Cdd:TIGR00463 477 YHSEGLEGAR---------------------KLGKSIIHWLPAKD 500
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
248-703 |
2.49e-83 |
|
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: 273.98 E-value: 2.49e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 248 TGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEpW--KITYSSD 325
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLD-WdeGPYYQSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 326 YFDELYGLAEVLINNNKGYICHCTAEDI--KRGRGIKEDGTPggeRFACKHRDQSIElnlqEFRNMRD-GKykpgEAILR 402
Cdd:COG0008 80 RFDIYYEYAEKLIEKGKAYVCFCTPEELeaLRETQTAPGKPP---RYDGRCRDLSPE----ELERMLAaGE----PPVLR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 403 MK--------QDLGS-----PSPQMWDLIAYRVlnaphprTGtkwkiYPTYDFTHCLVDSMENITHSLCTTEFYLSRESY 469
Cdd:COG0008 149 FKipeegvvfDDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 470 EWLCDQVHVFRPaqrEYGRLNIT----GTVLSKRKIAqlvdekfvrgwddprlFTLEAIRRRGVPPGAILSFINTLGVtt 545
Cdd:COG0008 217 IWLYEALGWEPP---EFAHLPLIlgpdGTKLSKRKGA----------------VTVSGLRRRGYLPEAIRNYLALLGW-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 546 STTNIQVVR-FESAIRKYLEDTTPRLMFVLDPVEVVVDNL----TDDFEELAT--IPFRP--GTPEFGERTVPFTNkfyi 616
Cdd:COG0008 276 SKSDDQEIFsLEELIEAFDLDRVSRSPAVFDPVKLVWLNGpyirALDDEELAEllAPELPeaGIREDLERLVPLVR---- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 617 ERSDF-SENVDDKEFFRLTPNQSVGLIKVshtvsfksLEKDETGKIIRVHVNYDNKVEEGTkPKKPKTYIQWVPVSS--- 692
Cdd:COG0008 352 ERAKTlSELAELARFFFIEREDEKAAKKR--------LAPEEVRKVLKAALEVLEAVETWD-PETVKGTIHWVSAEAgvk 422
|
490
....*....|...
gi 1069885398 693 --KYNSPLRVVET 703
Cdd:COG0008 423 dgLLFMPLRVALT 435
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
250-689 |
1.21e-81 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 276.61 E-value: 1.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 250 GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEPWKITYSSDYFDE 329
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 330 LYGLAEVLINNNKGYICHCTAEDIK--RGRGIKEdgtpggerfacKHRDQSIELNLQEFRNMRDGKYKPGEAILRMKQDL 407
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRkeRMDGIES-----------KCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDM 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 408 GSPSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCD-----QVHVFrpa 482
Cdd:PLN02907 361 QDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEdmglrKVHIW--- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 483 qrEYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGvttSTTNIQVVRFES--AIR 560
Cdd:PLN02907 438 --EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQG---ASKNLNLMEWDKlwTIN 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 561 KYLED-TTPRLMFVLDPVEVVVDnLTD--DFEELATIPFRPGTPEFGERTVPFTNKFYIERSDFSEnvddkeffrLTPNQ 637
Cdd:PLN02907 513 KKIIDpVCPRHTAVLKEGRVLLT-LTDgpETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA---------ISEGE 582
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1069885398 638 SVGLIKVSHTVsFKSLEKDETGKIIR----VHVnydnkveEGTKpKKPKTYIQWVP 689
Cdd:PLN02907 583 EVTLMDWGNAI-IKEITKDEGGAVTAlsgeLHL-------EGSV-KTTKLKLTWLP 629
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
250-620 |
1.03e-79 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 266.11 E-value: 1.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 250 GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEPWKITYSSDYFDE 329
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 330 LYGLAEVLINNNKGYICHCTAEDIKRGRGikedgtpggERFACKHRDQSIELNLQEFRNMRDGKYKPGEAILRMKQDLGS 409
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERA---------DRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 410 PSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGRL 489
Cdd:PLN03233 161 DNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 490 NITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRKYLEDTTPR 569
Cdd:PLN03233 241 NFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKR 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1069885398 570 LMFV--LDPVEVVVDNLTD--DFEELATiPFRPGTPEFGERTVPFTNKFYIERSD 620
Cdd:PLN03233 321 FMAIdkADHTALTVTNADEeaDFAFSET-DCHPKDPGFGKRAMRICDEVLLEKAD 374
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
232-773 |
2.02e-76 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 259.51 E-value: 2.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 232 ENPQAYPELMKKHLE*T-GGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMV 310
Cdd:PTZ00402 32 TAANANEENDKLQLTNAeEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 311 SWLGFePWKI--TYSSDYFDELYGLAEVLINNNKGYICHCTAEDIKRGRGikeDGTPggerfaCKHRDQSIELNLQEFRN 388
Cdd:PTZ00402 112 ATLGV-SWDVgpTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRF---DGVP------TKYRDISVEETKRLWNE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 389 MRDGKYKPGEAILRMKQDLGSPSPQMWDLIAYRVLNAPHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRES 468
Cdd:PTZ00402 182 MKKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 469 YEWLCDQVHVFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTT 548
Cdd:PTZ00402 262 YYWFCDALGIRKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 549 NIQVVRFESAIRKYLEDTTPRLMFVLDPVEV--VVDNLTDdfEELATIPFRPGTPEFGERTVPFTNKFYIERSDFSENVD 626
Cdd:PTZ00402 342 FMEWSKLWYFNTQILDPSVPRYTVVSNTLKVrcTVEGQIH--LEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVALLKE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 627 DKEFFRLtpNQSVGLIKVSHTVSFKSLEKDETgkiIRVHVNYDnkveegtkPKKPKTYIQWVPVSSKynspLRVVETRVH 706
Cdd:PTZ00402 420 GDEVTLM--DWGNAYIKNIRRSGEDALITDAD---IVLHLEGD--------VKKTKFKLTWVPESPK----AEVMELNEY 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069885398 707 NQLFKSENPSshPQGFLKDI-NPESEivYKESVMEHNFGHVVKNSPWVvdSVKNSEFYVGEDKEAKEV 773
Cdd:PTZ00402 483 DHLLTKKKPD--PEESIDDIiAPVTK--YTQEVYGEEALSVLKKGDII--QLERRGYYIVDDVTPKKV 544
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
5-163 |
3.68e-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: 211.65 E-value: 3.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 5 EELTHLFSQVGFEDNKVKEIVKNKKVSDSLSKLIKETPSDYQWNKSTRALVHNLASLIKGADLPKSDLIISGIINGNLKT 84
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 85 SLQVDGAFKYV-KANGDASTVDGMNENSGVGIEVTEDQVRNYVMQYIQENKESIMKERY-KLVPGIFANVKNLKELKWAD 162
Cdd:pfam04558 81 TLQVDAALKYLlKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYrFNVGKLLGEVRKLPELKWAD 160
|
.
gi 1069885398 163 P 163
Cdd:pfam04558 161 P 161
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
251-569 |
8.97e-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: 164.06 E-value: 8.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAP--EYFESIKRMVSWLGFEPWKITYSSDYFD 328
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 329 ELYGLAEVLINNNKGYIchctaedikrgrgikedgtpggerfackhrdqsielnlqefrnmrdgkykpgeailrmkqdlg 408
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 409 spspqmwdliayrvlnapHPRTGTKWKIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESyewlcdQVHVFR------PA 482
Cdd:cd09287 98 ------------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEK------QRYIYEyfgweyPE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 483 QREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAIRKY 562
Cdd:cd09287 154 TIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKL 233
|
....*..
gi 1069885398 563 LEDTTPR 569
Cdd:cd09287 234 IDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
251-544 |
4.80e-43 |
|
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: 156.09 E-value: 4.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEpW--KITYSSDYFD 328
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLD-WdeGPYRQSDRFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 329 ELYGLAEVLInnNKGyichctaedikrgrgikedgtpggerfackhrdqsielnlqefrnmrdgkykpgeailrmkqdlg 408
Cdd:cd00418 80 LYRAYAEELI--KKG----------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 409 spspqmwdliayrvlnaphprtgtkwkIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGR 488
Cdd:cd00418 93 ---------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPR 145
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1069885398 489 LNI-TGTVLSKRKIAQlvdekfvrgwddprlfTLEAIRRRGVPPGAILSFINTLGVT 544
Cdd:cd00418 146 LLLeDGTKLSKRKLNT----------------TLRALRRRGYLPEALRNYLALIGWS 186
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
568-787 |
5.04e-36 |
|
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: 133.94 E-value: 5.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 568 PRLMFVLDPVEVVVDNLTDDFEELATIPFRPGTPEFGERTVPFTNKFYIERSDfsenvddkeFFRLTPNQSVGL-----I 642
Cdd:pfam03950 2 PRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIERED---------FKRLAPGEEVRLmdaynI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 643 KVshtvsfKSLEKDETGKIIRVHVNYD-NKVEEGTKPKKPKtyIQWVPVSSKynsplRVVETRVHNQLFKSENPSshpqG 721
Cdd:pfam03950 73 KV------TEVVKDEDGNVTELHCTYDgDDLGGARKVKGKI--IHWVSASDA-----VPAEVRLYDRLFKDEDDA----D 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069885398 722 FLkdINPESEIVYKESVMEhnfghvvknspwvvDSVKNSEfyVGEdkeakevcRFQAMRVGYFTLD 787
Cdd:pfam03950 136 FL--LNPDSLKVLTEGLAE--------------PALANLK--PGD--------IVQFERIGYFRVD 175
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
166-244 |
7.71e-23 |
|
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: 93.14 E-value: 7.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 166 FKPIIDQEILKLLGPKDERDLVKK--KVKNNEKKKTTSAKKTSDDSATTGPKRTMFNEGFLGDLHKVGENPQAYPELMKK 243
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPpkKKKKAKKKKAAKKKKKKAPIEEEENKRSMFSEGFLGKFHKPGENPKTDGYVVTE 80
|
.
gi 1069885398 244 H 244
Cdd:pfam04557 81 H 81
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
251-317 |
8.78e-16 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 77.63 E-value: 8.78e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069885398 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEP 317
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDW 67
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
253-365 |
1.02e-13 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 72.58 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 253 RTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEpW--KITYSSDYFDeL 330
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLH-WdgPVLYQSQRHD-A 84
|
90 100 110
....*....|....*....|....*....|....*.
gi 1069885398 331 YGLA-EVLINNNKGYICHCTAEDIKRGRGIKEDGTP 365
Cdd:PRK05710 85 YRAAlDRLRAQGLVYPCFCSRKEIAAAAPAPPDGGG 120
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
246-361 |
5.20e-13 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 72.47 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 246 E*TGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHGGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFEpWKI----- 320
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLD-WDEgpdvg 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1069885398 321 ----TYSSDYFDELY-GLAEVLINNNKGYICHCTAEDIKRGRGIKE 361
Cdd:PLN02627 119 geygPYRQSERNAIYkQYAEKLLESGHVYPCFCTDEELEAMKEEAE 164
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
254-381 |
1.01e-07 |
|
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: 51.71 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069885398 254 TRFPPEPNGYLHIGHSKAIMVNFGYAKYH-----GGTCYLRFDDTNPEKEAPeyfesikRMVSWLGFEPWKITYSSDYFD 328
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYrklgyKVRCIALIDDAGGLIGDP-------ANKKGENAKAFVERWIERIKE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1069885398 329 ELYGLAEVLINNNKGYICHCTAEdikrgrgikedgtPGGERFAcKHRDQSIEL 381
Cdd:cd00802 75 DVEYMFLQAADFLLLYETECDIH-------------LGGSDQL-GHIELGLEL 113
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
254-308 |
4.18e-06 |
|
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: 45.99 E-value: 4.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1069885398 254 TRFPPEPnGYLHIGHSKAIMVNFGYAKYhggtCYLRFDDTNPEKEAPEYFESIKR 308
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIADQ----CVVRIDDNPPVKVWQDPHELEER 51
|
|
| |
