|
Name |
Accession |
Description |
Interval |
E-value |
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
252-807 |
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: 915.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 252 VRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKP-WKITYSSDYFDEL 330
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 331 YRLAEVLIKNGKAYVCHCTAEEIKRGRGIKEDgtPGgerYACKHRDQSIEQNLQEFRDMRDGKYKPGEAILRMKQDLNSP 410
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTD--PG---KNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 411 SPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVF-RPAQREYGRL 489
Cdd:TIGR00440 156 FPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 490 NITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKYLEDTTPR 569
Cdd:TIGR00440 236 NLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 570 LMFVLDPVEVVVDNLSDDYeELATIPYRPGTPEFGERTVPFTNKFYIERSDFSENVdDKEFFRLTPNQPVgLIKVSHTVS 649
Cdd:TIGR00440 316 AMAVIDPVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEA-NKQYKRLVLGKEV-RLRNAYVIK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 650 FKSLEKDEAGKIIRIHVNYDNKVE--EGSKPKKPKTYIQWVPISSKYNsplrvTETRVYNQLFKSENPsSHPEGFLKDIN 727
Cdd:TIGR00440 393 AERVEKDAAGKITTIFCTYDNKTLgkEPADGRKVKGVIHWVSASSKYP-----TETRLYDRLFKVPNP-GAPDDFLSVIN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 728 PESeVVYKESVMEHNFGDVVKNSpwvvdsvknsefyveedkdskevcRFQAMRVGYFTLD-KESTTSKVILNRIVSLKDA 806
Cdd:TIGR00440 467 PES-LVIKQGFMEHSLGDAVANK------------------------RFQFEREGYFCLDsKESTTEKVVFNRTVSLKDA 521
|
.
gi 398365535 807 T 807
Cdd:TIGR00440 522 T 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
9-809 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 660.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 9 QLFSQVGFEDKKVKEIVKNKKVSDSLYKLIKETPSDYQWNKSTRALVHNLASFVKGTDLPKSELIVNGIINGDLKTSLQV 88
Cdd:PLN02859 10 ELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSKIKTPAQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 89 DAAFKYVKANGEASTKMG-MNENSGVGIEITEDQVRNYVMQYIQENKERILTERYKLVPGI-FADVknLKELKWADPRSF 166
Cdd:PLN02859 90 EAAFSFFSSTGPESFDLNkFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDlLGQV--RKRLPWADPKIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 167 KPIIDQEVLKLLGPKDERDLIKKKTKNNEKKKTNSAKKSSD----------NSASSGPKR----TMFNEGFLGDlhkvGE 232
Cdd:PLN02859 168 KKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVaaappseeelNPYSIFPQPeenfKVHTEVFFSD----GS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 233 --NPQAYPELMKEHLEVTGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMV 310
Cdd:PLN02859 244 vlRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 311 SWLGFKPWKITYSSDYFDELYRLAEVLIKNGKAYVCHCTAEEIKRGRGIKEDgTPggeryackHRDQSIEQNLQEFRDMR 390
Cdd:PLN02859 324 EWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMN-SP--------WRDRPIEESLKLFEDMR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 391 DGKYKPGEAILRMKQDLNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYE 470
Cdd:PLN02859 395 RGLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 471 WLCDQVHVFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTN- 549
Cdd:PLN02859 475 WLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSl 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 550 IQVVRFESAVRKYLEDTTPRLMFVLDPVEVVVDNLSDD-YEEL--ATIPYRPGTPEFGERTVPFTNKFYIERSDFSENvD 626
Cdd:PLN02859 555 IRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGeVIELdaKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLK-D 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 627 DKEFFRLTPNQPVGL-----IKVSHTVsfkslEKDEAGKIIRIHVNYDnkveeGSKPKKPKTYIQWVPISSKYNSPLRVt 701
Cdd:PLN02859 634 SKDYYGLAPGKSVLLryafpIKCTDVV-----LADDNETVVEIRAEYD-----PEKKTKPKGVLHWVAEPSPGVEPLKV- 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 702 ETRVYNQLFKSENPSSHpEGFLKDINPESEVVYKESVMEHNFgdvvknspwvvdsvknsefyveedKDSKEVCRFQAMRV 781
Cdd:PLN02859 703 EVRLFDKLFLSENPAEL-EDWLEDLNPQSKEVISGAYAVPSL------------------------KDAKVGDRFQFERL 757
|
810 820
....*....|....*....|....*...
gi 398365535 782 GYFTLDKESTTSKVILNRIVSLKDATSK 809
Cdd:PLN02859 758 GYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
251-565 |
6.28e-152 |
|
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: 446.77 E-value: 6.28e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKP-WKITYSSDYFDE 329
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 330 LYRLAEVLIKNGKAYVCHCTAEEIKRGRGIKedgtpggERYACKHRDQSIEQNLQEF-RDMRDGKYKPGEAILRMKQDLN 408
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ-------EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 409 SPsPQMWDLIAYRVLNAP---HPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRP-AQR 484
Cdd:pfam00749 154 SP-YVFRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPpFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 485 EYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTS-TTNIQVVRFESAVRKYL 563
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKL 312
|
..
gi 398365535 564 ED 565
Cdd:pfam00749 313 DW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
251-569 |
8.48e-148 |
|
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: 432.83 E-value: 8.48e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKPWKITYSSDYFDEL 330
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 331 YRLAEVLIKNGKAYVchctaeeikrgrgikedgtpggeryackhrdqsieqnlqefrdmrdgkykpgeailrmkqdlnsp 410
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 411 spqmwdliayrvlnapHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGRLN 490
Cdd:cd00807 96 ----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLN 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365535 491 ITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKYLEDTTPR 569
Cdd:cd00807 160 LTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
248-703 |
1.47e-90 |
|
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: 292.85 E-value: 1.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 248 TGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKpW--KITYSSD 325
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLD-WdeGPYYQSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 326 YFDELYRLAEVLIKNGKAYVCHCTAEEI--KRGRGIKEDGTPggeRYACKHRDQSIEQnLQEFRDmrDGKykpgEAILRM 403
Cdd:COG0008 80 RFDIYYEYAEKLIEKGKAYVCFCTPEELeaLRETQTAPGKPP---RYDGRCRDLSPEE-LERMLA--AGE----PPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 404 K--------QDLNS-----PSPQMWDLIAYRVlnaphprTGtkwriYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYE 470
Cdd:COG0008 150 KipeegvvfDDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 471 WLCDQVHVFRPaqrEYGRLNIT----GTVLSKRKIAqlvdekfvrgwddprlFTLEAIRRRGVPPGAILSFINTLGVttS 546
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLIlgpdGTKLSKRKGA----------------VTVSGLRRRGYLPEAIRNYLALLGW--S 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 547 TTNIQVVR-FESAVRKYLEDTTPRLMFVLDPVEVVVDNL----SDDYEELAT--IPYRP--GTPEFGERTVPFTNkfyiE 617
Cdd:COG0008 277 KSDDQEIFsLEELIEAFDLDRVSRSPAVFDPVKLVWLNGpyirALDDEELAEllAPELPeaGIREDLERLVPLVR----E 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 618 RSDF-SENVDDKEFFRLTPNQPVGLIKVshtvsfksLEKDEAGKIIRIHVNYDNKVEEGSkPKKPKTYIQWVPISS---- 692
Cdd:COG0008 353 RAKTlSELAELARFFFIEREDEKAAKKR--------LAPEEVRKVLKAALEVLEAVETWD-PETVKGTIHWVSAEAgvkd 423
|
490
....*....|..
gi 398365535 693 -KYNSPLRVTET 703
Cdd:COG0008 424 gLLFMPLRVALT 435
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
5-163 |
5.07e-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: 213.96 E-value: 5.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 5 EELTQLFSQVGFEDKKVKEIVKNKKVSDSLYKLIKETPSDYQWNKSTRALVHNLASFVKGTDLPKSELIVNGIINGDLKT 84
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 85 SLQVDAAFKYV-KANGEASTKMGMNENSGVGIEITEDQVRNYVMQYIQENKERILTERY-KLVPGIFADVKNLKELKWAD 162
Cdd:pfam04558 81 TLQVDAALKYLlKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYrFNVGKLLGEVRKLPELKWAD 160
|
.
gi 398365535 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 |
1.91e-25 |
|
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: 100.46 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 166 FKPIIDQEVLKLLGPKDERDLIKK--KTKNNEKKKTNSAKKSSDNSASSGPKRTMFNEGFLGDLHKVGENPQAYPELMKE 243
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPpkKKKKAKKKKAAKKKKKKAPIEEEENKRSMFSEGFLGKFHKPGENPKTDGYVVTE 80
|
.
gi 398365535 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 ... |
252-807 |
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: 915.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 252 VRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKP-WKITYSSDYFDEL 330
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 331 YRLAEVLIKNGKAYVCHCTAEEIKRGRGIKEDgtPGgerYACKHRDQSIEQNLQEFRDMRDGKYKPGEAILRMKQDLNSP 410
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTD--PG---KNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 411 SPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVF-RPAQREYGRL 489
Cdd:TIGR00440 156 FPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 490 NITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKYLEDTTPR 569
Cdd:TIGR00440 236 NLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 570 LMFVLDPVEVVVDNLSDDYeELATIPYRPGTPEFGERTVPFTNKFYIERSDFSENVdDKEFFRLTPNQPVgLIKVSHTVS 649
Cdd:TIGR00440 316 AMAVIDPVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEA-NKQYKRLVLGKEV-RLRNAYVIK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 650 FKSLEKDEAGKIIRIHVNYDNKVE--EGSKPKKPKTYIQWVPISSKYNsplrvTETRVYNQLFKSENPsSHPEGFLKDIN 727
Cdd:TIGR00440 393 AERVEKDAAGKITTIFCTYDNKTLgkEPADGRKVKGVIHWVSASSKYP-----TETRLYDRLFKVPNP-GAPDDFLSVIN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 728 PESeVVYKESVMEHNFGDVVKNSpwvvdsvknsefyveedkdskevcRFQAMRVGYFTLD-KESTTSKVILNRIVSLKDA 806
Cdd:TIGR00440 467 PES-LVIKQGFMEHSLGDAVANK------------------------RFQFEREGYFCLDsKESTTEKVVFNRTVSLKDA 521
|
.
gi 398365535 807 T 807
Cdd:TIGR00440 522 T 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
9-809 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 660.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 9 QLFSQVGFEDKKVKEIVKNKKVSDSLYKLIKETPSDYQWNKSTRALVHNLASFVKGTDLPKSELIVNGIINGDLKTSLQV 88
Cdd:PLN02859 10 ELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSKIKTPAQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 89 DAAFKYVKANGEASTKMG-MNENSGVGIEITEDQVRNYVMQYIQENKERILTERYKLVPGI-FADVknLKELKWADPRSF 166
Cdd:PLN02859 90 EAAFSFFSSTGPESFDLNkFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDlLGQV--RKRLPWADPKIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 167 KPIIDQEVLKLLGPKDERDLIKKKTKNNEKKKTNSAKKSSD----------NSASSGPKR----TMFNEGFLGDlhkvGE 232
Cdd:PLN02859 168 KKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVaaappseeelNPYSIFPQPeenfKVHTEVFFSD----GS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 233 --NPQAYPELMKEHLEVTGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMV 310
Cdd:PLN02859 244 vlRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 311 SWLGFKPWKITYSSDYFDELYRLAEVLIKNGKAYVCHCTAEEIKRGRGIKEDgTPggeryackHRDQSIEQNLQEFRDMR 390
Cdd:PLN02859 324 EWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMN-SP--------WRDRPIEESLKLFEDMR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 391 DGKYKPGEAILRMKQDLNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYE 470
Cdd:PLN02859 395 RGLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 471 WLCDQVHVFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTN- 549
Cdd:PLN02859 475 WLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSl 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 550 IQVVRFESAVRKYLEDTTPRLMFVLDPVEVVVDNLSDD-YEEL--ATIPYRPGTPEFGERTVPFTNKFYIERSDFSENvD 626
Cdd:PLN02859 555 IRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGeVIELdaKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLK-D 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 627 DKEFFRLTPNQPVGL-----IKVSHTVsfkslEKDEAGKIIRIHVNYDnkveeGSKPKKPKTYIQWVPISSKYNSPLRVt 701
Cdd:PLN02859 634 SKDYYGLAPGKSVLLryafpIKCTDVV-----LADDNETVVEIRAEYD-----PEKKTKPKGVLHWVAEPSPGVEPLKV- 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 702 ETRVYNQLFKSENPSSHpEGFLKDINPESEVVYKESVMEHNFgdvvknspwvvdsvknsefyveedKDSKEVCRFQAMRV 781
Cdd:PLN02859 703 EVRLFDKLFLSENPAEL-EDWLEDLNPQSKEVISGAYAVPSL------------------------KDAKVGDRFQFERL 757
|
810 820
....*....|....*....|....*...
gi 398365535 782 GYFTLDKESTTSKVILNRIVSLKDATSK 809
Cdd:PLN02859 758 GYFAVDKDSTPEKLVFNRTVTLKDSYGK 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: 626.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 250 GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKpW--KITYSSDYF 327
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFD-WsgELRYASDYF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 328 DELYRLAEVLIKNGKAYVCHCTAEEIKRGRG-IKEDGTPGgeryacKHRDQSIEQNLQEFRDMRDGKYKPGEAILRMKQD 406
Cdd:PRK05347 107 DQLYEYAVELIKKGKAYVDDLSAEEIREYRGtLTEPGKNS------PYRDRSVEENLDLFERMRAGEFPEGSAVLRAKID 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 407 LNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHV-FRPAQRE 485
Cdd:PRK05347 181 MASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIpPHPRQYE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 486 YGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKYLED 565
Cdd:PRK05347 261 FSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 566 TTPRLMFVLDPVEVVVDNLSDDYEELATIPYRPGTPEFGERTVPFTNKFYIERSDFSENvDDKEFFRLTPNQPVGLiKVS 645
Cdd:PRK05347 341 NAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEE-PPKKYFRLVPGKEVRL-RNA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 646 HTVSFKSLEKDEAGKIIRIHVNYDNKVEEGSKPK--KPKTYIQWVpiSSKYNSPlrvTETRVYNQLFKSENPSShPEGFL 723
Cdd:PRK05347 419 YVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADgrKVKGTIHWV--SAAHAVP---AEVRLYDRLFTVPNPAA-GKDFL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 724 KDINPESEVVykesvmehnfgdvvknspwvvdsvknSEFYVEED-KDSKEVCRFQAMRVGYFTLDKESTTSKVILNRIVS 802
Cdd:PRK05347 493 DFLNPDSLVI--------------------------KQGFVEPSlADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVG 546
|
...
gi 398365535 803 LKD 805
Cdd:PRK05347 547 LRD 549
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
228-809 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 541.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 228 HKVGENPQAYPELMKEHLEV-TGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESI 306
Cdd:PRK14703 7 PRMLVSPNFITEIIEEDLEAgRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 307 KRMVSWLGFKpW--KITYSSDYFDELYRLAEVLIKNGKAYVCHCTAEEIKRGRG-IKEDGTPGgeryacKHRDQSIEQNL 383
Cdd:PRK14703 87 KDDVRWLGFD-WgeHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGtVTEPGTPS------PYRDRSVEENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 384 QEFRDMRDGKYKPGEAILRMKQDLNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFY 463
Cdd:PRK14703 160 DLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 464 LSRESYEWLCDQVHVF--RPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTL 541
Cdd:PRK14703 240 NNRAIYDWVLDHLGPWppRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 542 GVTTSTTNIQVVRFESAVRKYLEDTTPRLMFVLDPVEVVVDNLSDDYEELATIPYRPG-TPEFGERTVPFTNKFYIERSD 620
Cdd:PRK14703 320 GVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHdVPKEGSRKVPFTRELYIERDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 621 FSENvDDKEFFRLTPNQPVGLiKVSHTVSFKSLEKDEAGKIIRIHVNYD-NKVEEGSKPKKPKTYIQWVpiSSKYNSPlr 699
Cdd:PRK14703 400 FSED-PPKGFKRLTPGREVRL-RGAYIIRCDEVVRDADGAVTELRCTYDpESAKGEDTGRKAAGVIHWV--SAKHALP-- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 700 vTETRVYNQLFKSENPSSHPEGFLKDINPESEVVYKESVmehnfgdvvknSPWVVDsvknsefyveEDKDSkevcRFQAM 779
Cdd:PRK14703 474 -AEVRLYDRLFKVPQPEAADEDFLEFLNPDSLRVAQGRV-----------EPAVRD----------DPADT----RYQFE 527
|
570 580 590
....*....|....*....|....*....|.
gi 398365535 780 RVGYFTLDKE-STTSKVILNRIVSLKDATSK 809
Cdd:PRK14703 528 RQGYFWADPVdSRPDALVFNRIITLKDTWGA 558
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
238-809 |
3.43e-178 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 524.16 E-value: 3.43e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 238 PELMKEHLEVTGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKP 317
Cdd:PTZ00437 38 PELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 318 WKITYSSDYFDELYRLAEVLIKNGKAYVCHCTAEEIKRGRGIKEDgTPggeryackHRDQSIEQNLQEFRDMRDGKYKPG 397
Cdd:PTZ00437 118 DWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQRED-SP--------WRNRSVEENLLLFEHMRQGRYAEG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 398 EAILRMKQDLNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVH 477
Cdd:PTZ00437 189 EATLRVKADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 478 VFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFES 557
Cdd:PTZ00437 269 LWRPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLEN 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 558 AVRKYLEDTTPRLMFVLDPVEVVVDNLsdDYEELATIPYRPGTPEFGERTVPFTNKFYIERSDFSENVDDKEFFRLTPN- 636
Cdd:PTZ00437 349 TLREDLDERCERRLMVIDPIKVVVDNW--KGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRTEDNNSKFYGLAPGp 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 637 QPVGLiKVSHTVSFKSLEKDEAGKIIRIHVNYDNKveegsKPKKPKTYIQWVpiSSKYNSPLrvtETRVYNQLFKSENPS 716
Cdd:PTZ00437 427 RVVGL-KYSGNVVCKGFEVDAAGQPSVIHVDIDFE-----RKDKPKTNISWV--SATACTPV---EVRLYNALLKDDRAA 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 717 SHPEgFLKDINPESEVVykesvmehnfgdvvknspwvvdsvknSEFYVEED-KDSKEVCRFQAMRVGYFTLDKESTTSKV 795
Cdd:PTZ00437 496 IDPE-FLKFIDEDSEVV--------------------------SHGYAEKGiENAKHFESVQAERFGYFVVDPDTRPDHL 548
|
570
....*....|....
gi 398365535 796 ILNRIVSLKDATSK 809
Cdd:PTZ00437 549 VMNRVLGLREDKEK 562
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
251-565 |
6.28e-152 |
|
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: 446.77 E-value: 6.28e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKP-WKITYSSDYFDE 329
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 330 LYRLAEVLIKNGKAYVCHCTAEEIKRGRGIKedgtpggERYACKHRDQSIEQNLQEF-RDMRDGKYKPGEAILRMKQDLN 408
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ-------EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 409 SPsPQMWDLIAYRVLNAP---HPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRP-AQR 484
Cdd:pfam00749 154 SP-YVFRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPpFIH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 485 EYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTS-TTNIQVVRFESAVRKYL 563
Cdd:pfam00749 233 EYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKL 312
|
..
gi 398365535 564 ED 565
Cdd:pfam00749 313 DW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
251-569 |
8.48e-148 |
|
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: 432.83 E-value: 8.48e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKPWKITYSSDYFDEL 330
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 331 YRLAEVLIKNGKAYVchctaeeikrgrgikedgtpggeryackhrdqsieqnlqefrdmrdgkykpgeailrmkqdlnsp 410
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 411 spqmwdliayrvlnapHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGRLN 490
Cdd:cd00807 96 ----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLN 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365535 491 ITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKYLEDTTPR 569
Cdd:cd00807 160 LTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
247-693 |
3.52e-108 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 342.60 E-value: 3.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 247 VTGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAP--EYFESIKRMVSWLGFKPWKITYSS 324
Cdd:PRK04156 97 AEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPdpEAYDMILEDLKWLGVKWDEVVIQS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 325 DYFDELYRLAEVLIKNGKAYVCHCTAEEIKRgrgIKEDGTPggeryaCKHRDQSIEQNLQEFRDMRDGKYKPGEAILRMK 404
Cdd:PRK04156 177 DRLEIYYEYARKLIEMGGAYVCTCDPEEFKE---LRDAGKP------CPHRDKSPEENLELWEKMLDGEYKEGEAVVRVK 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 405 QDLNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESyewlcdQVHVFR---- 480
Cdd:PRK04156 248 TDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEK------QRYIYDyfgw 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 481 --PAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESA 558
Cdd:PRK04156 322 eyPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAI 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 559 VRKYLEDTTPRLMFVLDPVEVVVDNlsdDYEELATIPYRPGTPEFGERTVPFTNKFYIERSDFsenVDDKEFFRLtpnqp 638
Cdd:PRK04156 402 NRKLIDPIANRYFFVRDPVELEIEG---AEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDL---EAEGKMVRL----- 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365535 639 VGLIKVSHTvsfkslekdeagKIIRIHVNYDNK-VEEGSKPKKPktYIQWVPISSK 693
Cdd:PRK04156 471 MDLFNVEIT------------GVSVDKARYHSDdLEEARKNKAP--IIQWVPEDES 512
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
247-626 |
5.19e-98 |
|
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: 315.61 E-value: 5.19e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 247 VTGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKPWKITYSSDY 326
Cdd:TIGR00463 89 AKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 327 FDELYRLAEVLIKNGKAYVCHCTAEEIKRgrgIKEDGTPggeryaCKHRDQSIEQNLQEFRDMRDGKYKPGEAILRMKQD 406
Cdd:TIGR00463 169 IETYYDYTRKLIEMGKAYVCDCRPEEFRE---LRNRGEA------CHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 407 LNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREY 486
Cdd:TIGR00463 240 LKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHW 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 487 GRLNI--TGTVLSKRKIAQLVDEKFVrGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKYLE 564
Cdd:TIGR00463 320 GRLKIddVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIID 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365535 565 DTTPRLMFVLDPVEVVVDNLSDDYEELatIPYRPGTPEFGERTVPFTNKFYIERSDFSENVD 626
Cdd:TIGR00463 399 EEARRYFFIWNPVKIEIVGLPEPKRVE--RPLHPDHPEIGERVLILRGEIYVPKDDLEEGVE 458
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
248-703 |
1.47e-90 |
|
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: 292.85 E-value: 1.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 248 TGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKpW--KITYSSD 325
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLD-WdeGPYYQSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 326 YFDELYRLAEVLIKNGKAYVCHCTAEEI--KRGRGIKEDGTPggeRYACKHRDQSIEQnLQEFRDmrDGKykpgEAILRM 403
Cdd:COG0008 80 RFDIYYEYAEKLIEKGKAYVCFCTPEELeaLRETQTAPGKPP---RYDGRCRDLSPEE-LERMLA--AGE----PPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 404 K--------QDLNS-----PSPQMWDLIAYRVlnaphprTGtkwriYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYE 470
Cdd:COG0008 150 KipeegvvfDDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 471 WLCDQVHVFRPaqrEYGRLNIT----GTVLSKRKIAqlvdekfvrgwddprlFTLEAIRRRGVPPGAILSFINTLGVttS 546
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLIlgpdGTKLSKRKGA----------------VTVSGLRRRGYLPEAIRNYLALLGW--S 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 547 TTNIQVVR-FESAVRKYLEDTTPRLMFVLDPVEVVVDNL----SDDYEELAT--IPYRP--GTPEFGERTVPFTNkfyiE 617
Cdd:COG0008 277 KSDDQEIFsLEELIEAFDLDRVSRSPAVFDPVKLVWLNGpyirALDDEELAEllAPELPeaGIREDLERLVPLVR----E 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 618 RSDF-SENVDDKEFFRLTPNQPVGLIKVshtvsfksLEKDEAGKIIRIHVNYDNKVEEGSkPKKPKTYIQWVPISS---- 692
Cdd:COG0008 353 RAKTlSELAELARFFFIEREDEKAAKKR--------LAPEEVRKVLKAALEVLEAVETWD-PETVKGTIHWVSAEAgvkd 423
|
490
....*....|..
gi 398365535 693 -KYNSPLRVTET 703
Cdd:COG0008 424 gLLFMPLRVALT 435
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
250-689 |
1.67e-86 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 289.70 E-value: 1.67e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 250 GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKPWKITYSSDYFDE 329
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 330 LYRLAEVLIKNGKAYVCHCTAEEIK--RGRGIKEdgtpggeryacKHRDQSIEQNLQEFRDMRDGKYKPGEAILRMKQDL 407
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRkeRMDGIES-----------KCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDM 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 408 NSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCD-----QVHVFrpa 482
Cdd:PLN02907 361 QDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEdmglrKVHIW--- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 483 qrEYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKY 562
Cdd:PLN02907 438 --EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKI 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 563 LEDTTPRLMFVLDPVEVVVDnLSD--DYEELATIPYRPGTPEFGERTVPFTNKFYIERSDFSEnvddkeffrLTPNQPVG 640
Cdd:PLN02907 516 IDPVCPRHTAVLKEGRVLLT-LTDgpETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA---------ISEGEEVT 585
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 398365535 641 LIKVSHTVsFKSLEKDEAGKIIR----IHVnydnkveEGSKpKKPKTYIQWVP 689
Cdd:PLN02907 586 LMDWGNAI-IKEITKDEGGAVTAlsgeLHL-------EGSV-KTTKLKLTWLP 629
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
250-620 |
9.81e-84 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 276.89 E-value: 9.81e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 250 GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKPWKITYSSDYFDE 329
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 330 LYRLAEVLIKNGKAYVCHCTAEEIKRGRGikedgtpggERYACKHRDQSIEQNLQEFRDMRDGKYKPGEAILRMKQDLNS 409
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERA---------DRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 410 PSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGRL 489
Cdd:PLN03233 161 DNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 490 NITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKYLEDTTPR 569
Cdd:PLN03233 241 NFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKR 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 398365535 570 LMFV--LDPVEVVVDNLSDDYEEL-ATIPYRPGTPEFGERTVPFTNKFYIERSD 620
Cdd:PLN03233 321 FMAIdkADHTALTVTNADEEADFAfSETDCHPKDPGFGKRAMRICDEVLLEKAD 374
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
232-757 |
1.21e-81 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 273.38 E-value: 1.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 232 ENPQAYPElmKEHLEVTG---GKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKR 308
Cdd:PTZ00402 32 TAANANEE--NDKLQLTNaeeGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 309 MVSWLGFkPWKI--TYSSDYFDELYRLAEVLIKNGKAYVCHCTAEEIKRGRGikeDGTPggeryaCKHRDQSIEQNLQEF 386
Cdd:PTZ00402 110 DLATLGV-SWDVgpTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRF---DGVP------TKYRDISVEETKRLW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 387 RDMRDGKYKPGEAILRMKQDLNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSR 466
Cdd:PTZ00402 180 NEMKKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 467 ESYEWLCDQVHVFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTS 546
Cdd:PTZ00402 260 DQYYWFCDALGIRKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 547 TTNIQVVRFESAVRKYLEDTTPRLMFVLDPVEVVVDNLSDDYEELATIPYRPGTPEFGERTVPFTNKFYIERSDFSENVD 626
Cdd:PTZ00402 340 VNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVALLKE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 627 DKEFFRLTPNQpvGLIKVSHTVSFKSLEKDEAgkiIRIHVNYDnkveegskPKKPKTYIQWVPISSKynspLRVTETRVY 706
Cdd:PTZ00402 420 GDEVTLMDWGN--AYIKNIRRSGEDALITDAD---IVLHLEGD--------VKKTKFKLTWVPESPK----AEVMELNEY 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365535 707 NQLFKSENPSshPEGFLKDI-NPES----EVVYKESVMEHNFGDVV---KNSPWVVDSV 757
Cdd:PTZ00402 483 DHLLTKKKPD--PEESIDDIiAPVTkytqEVYGEEALSVLKKGDIIqleRRGYYIVDDV 539
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
5-163 |
5.07e-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: 213.96 E-value: 5.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 5 EELTQLFSQVGFEDKKVKEIVKNKKVSDSLYKLIKETPSDYQWNKSTRALVHNLASFVKGTDLPKSELIVNGIINGDLKT 84
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 85 SLQVDAAFKYV-KANGEASTKMGMNENSGVGIEITEDQVRNYVMQYIQENKERILTERY-KLVPGIFADVKNLKELKWAD 162
Cdd:pfam04558 81 TLQVDAALKYLlKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYrFNVGKLLGEVRKLPELKWAD 160
|
.
gi 398365535 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 |
5.74e-49 |
|
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: 172.92 E-value: 5.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAP--EYFESIKRMVSWLGFKPWKITYSSDYFD 328
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 329 ELYRLAEVLIKNGKAYVchctaeeikrgrgikedgtpggeryackhrdqsieqnlqefrdmrdgkykpgeailrmkqdln 408
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 409 spspqmwdliayrvlnapHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESyewlcdQVHVFR------PA 482
Cdd:cd09287 98 ------------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEK------QRYIYEyfgweyPE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 483 QREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKY 562
Cdd:cd09287 154 TIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKL 233
|
....*..
gi 398365535 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 |
2.77e-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: 156.48 E-value: 2.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKpW--KITYSSDYFD 328
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLD-WdeGPYRQSDRFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 329 ELYRLAEVLIKNGkayvchctaeeikrgrgikedgtpggeryackhrdqsieqnlqefrdmrdgkykpgeailrmkqdln 408
Cdd:cd00418 80 LYRAYAEELIKKG------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 409 spspqmwdliayrvlnaphprtgtkwrIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGR 488
Cdd:cd00418 93 ---------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPR 145
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365535 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 |
1.38e-37 |
|
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: 138.56 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 568 PRLMFVLDPVEVVVDNLSDDYEELATIPYRPGTPEFGERTVPFTNKFYIERSDfsenvddkeFFRLTPNQPVGL-----I 642
Cdd:pfam03950 2 PRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIERED---------FKRLAPGEEVRLmdaynI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 643 KVshtvsfKSLEKDEAGKIIRIHVNYD-NKVEEGSKPKKPKtyIQWVPISSKynsplRVTETRVYNQLFKSENpsshPEG 721
Cdd:pfam03950 73 KV------TEVVKDEDGNVTELHCTYDgDDLGGARKVKGKI--IHWVSASDA-----VPAEVRLYDRLFKDED----DAD 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365535 722 FLkdINPESEVVYKESVMEhnfgdvvknspwvvDSVKNSEfyvEEDkdskevcRFQAMRVGYFTLD 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 |
1.91e-25 |
|
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: 100.46 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 166 FKPIIDQEVLKLLGPKDERDLIKK--KTKNNEKKKTNSAKKSSDNSASSGPKRTMFNEGFLGDLHKVGENPQAYPELMKE 243
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPpkKKKKAKKKKAAKKKKKKAPIEEEENKRSMFSEGFLGKFHKPGENPKTDGYVVTE 80
|
.
gi 398365535 244 H 244
Cdd:pfam04557 81 H 81
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
253-378 |
7.03e-16 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 79.12 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 253 RTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKpW--KITYSSDYFDeL 330
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLH-WdgPVLYQSQRHD-A 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 398365535 331 YRLA-EVLIKNGKAYVCHCTAEEIKRGRGIKEDGTPggeRY--ACKHRDQS 378
Cdd:PRK05710 85 YRAAlDRLRAQGLVYPCFCSRKEIAAAAPAPPDGGG---IYpgTCRDLLHG 132
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
246-385 |
1.19e-15 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 80.56 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 246 EVTGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLG----------- 314
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldwdegpdvgg 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365535 315 -FKPwkitYSSDYFDELYR-LAEVLIKNGKAYVCHCTAEEIKRGRGI-KEDGTPggERYACKHRDQSIEQNLQE 385
Cdd:PLN02627 120 eYGP----YRQSERNAIYKqYAEKLLESGHVYPCFCTDEELEAMKEEaELKKLP--PRYTGKWATASDEEVQAE 187
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
251-341 |
2.34e-15 |
|
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: 76.47 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 251 KVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFK---------PWKIT 321
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDwdegpdvggPYGPY 80
|
90 100
....*....|....*....|.
gi 398365535 322 YSSDYFDeLYR-LAEVLIKNG 341
Cdd:cd00808 81 RQSERLE-IYRkYAEKLLEKG 100
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
254-349 |
7.21e-08 |
|
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: 52.10 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365535 254 TRFPPEPNGYLHIGHSKAIMVNFGYAKYHN-----GTCYLRFDDTNPEKEAPeyfesikRMVSWLGFKPWKITYSSDYFD 328
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGGLIGDP-------ANKKGENAKAFVERWIERIKE 74
|
90 100
....*....|....*....|.
gi 398365535 329 ELYRLAEVLIKNGKAYVCHCT 349
Cdd:cd00802 75 DVEYMFLQAADFLLLYETECD 95
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
254-308 |
4.52e-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: 4.52e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 398365535 254 TRFPPEPnGYLHIGHSKAIMVNFGYAKYhngtCYLRFDDTNPEKEAPEYFESIKR 308
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIADQ----CVVRIDDNPPVKVWQDPHELEER 51
|
|
| |
