|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
11-583 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1097.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 11 TPGSNDNAPRDFVRQIIREDLATGRHRAIRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFV 90
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 91 EGIKDDVRWLGYEWH-ELRHASDYFDVFYRAALKLIEDGKAYVDDLSADEVREYRGTLTEPGRNSPYRDRSIEENLDLFK 169
Cdd:PRK05347 82 DSIKEDVRWLGFDWSgELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 170 RMRAGEFADGSKTLRAKIDMASGNINLRDPALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRP 249
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 250 LYDWCVDNVDlaahpdlwqsvvqagleaMPAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRG 329
Cdd:PRK05347 242 LYDWVLDNLP------------------IPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 330 FTPAGLRLLIERLGISKQNSVIDYAILENCVREDLDATAPRRMAVLDPIKLTITNLPGNHEETLRFANHPKDESFGTREV 409
Cdd:PRK05347 304 YTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 410 PFGSTVWIEREDFAEVPPKGFKRLIPGGEVRLRGVGIVKCEEAVKDAAGDVVELRCTLDPDSRAGLPGADRKVKGTIHWV 489
Cdd:PRK05347 384 PFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 490 SARHAVAAEVRLYDRLFDVPAPDDESDgksWIEHINPEAKRIGRGWLEPAAAQAEPEQRFQFERLGYFVADRvDHRPDAP 569
Cdd:PRK05347 464 SAAHAVPAEVRLYDRLFTVPNPAAGKD---FLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADK-DSTPGKL 539
|
570
....*....|....
gi 2161680032 570 VFNRTVTLRDTWAR 583
Cdd:PRK05347 540 VFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
39-581 |
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: 680.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWH-ELRHASDYFDVF 117
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 118 YRAALKLIEDGKAYVDDLSADEVREYRGTLTEPGRNSPYRDRSIEENLDLFKRMRAGEFADGSKTLRAKIDMASGNINLR 197
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 198 DPALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVdlaahpdlwqsvvqagleA 277
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNI------------------H 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 278 MPAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSVIDYAILE 357
Cdd:TIGR00440 223 IFPRPAQYEFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 358 NCVREDLDATAPRRMAVLDPIKLTITNLPGNHeETLRFANHPKDESFGTREVPFGSTVWIEREDFAEVPPKGFKRLIPGG 437
Cdd:TIGR00440 303 SCIREDLNENAPRAMAVIDPVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 438 EVRLRGVGIVKCEEAVKDAAGDVVELRCTLDPDSRAGLPGADRKVKGTIHWVSARHAVAAEVRLYDRLFDVPAPDDESDg 517
Cdd:TIGR00440 382 EVRLRNAYVIKAERVEKDAAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDD- 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2161680032 518 ksWIEHINPEAKRIGRGWLEPAAAQAEPEQRFQFERLGYFVADRVDHRPDAPVFNRTVTLRDTW 581
Cdd:TIGR00440 461 --FLSVINPESLVIKQGFMEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
39-370 |
5.38e-129 |
|
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: 377.36 E-value: 5.38e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHELRHASDYFDVFY 118
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 119 RAALKLIEDGKAYVddlsadevreyrgtltepgrnspyrdrsieenldlfkrmragefadgsktlrakidmasgninlrd 198
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 199 palyrirkiaHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVDLAahpdlwqsvvqagleam 278
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY----------------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 279 paKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSVIDYAILEN 358
Cdd:cd00807 149 --RPHQWEFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEA 226
|
330
....*....|..
gi 2161680032 359 CVREDLDATAPR 370
Cdd:cd00807 227 CVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
39-365 |
6.40e-123 |
|
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: 365.10 E-value: 6.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHE-LRHASDYFDVF 117
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYgPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 118 YRAALKLIEDGKAYVDDLSADEVREYRGTLtePGRNSPYRDRSIEENLDLFKR-MRAGEFADGSKTLRAKIDMaSGNINL 196
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPM-ESPYVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 197 RDPALYRIR---KIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVDLaahpdlwqsvvqa 273
Cdd:pfam00749 159 RDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGW------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 274 gleamPAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSV-ID 352
Cdd:pfam00749 226 -----EPPPFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRL 300
|
330
....*....|...
gi 2161680032 353 YAILENCVREDLD 365
Cdd:pfam00749 301 SKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
39-509 |
2.95e-121 |
|
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: 366.43 E-value: 2.95e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHE-LRHASDYFDVF 117
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFDIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 118 YRAALKLIEDGKAYVDDLSADEVREYRGTLTEPGRNSPY----RDRSIEEnldLFKRMRAGEfadgSKTLRAKI------ 187
Cdd:COG0008 85 YEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE---LERMLAAGE----PPVLRFKIpeegvv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 188 --DMASG-----NINLRDPALYRirkiahqntGDAwpiYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCvdnvdl 260
Cdd:COG0008 158 fdDLVRGeitfpNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWL------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 261 aahpdlwqsvvqagLEAMPAKPRqiEFSRLNLSFC----ITSKRKlaqlvseGLVdgwddprmnTLRGLRRRGFTPAGLR 336
Cdd:COG0008 220 --------------YEALGWEPP--EFAHLPLILGpdgtKLSKRK-------GAV---------TVSGLRRRGYLPEAIR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 337 LLIERLGISKQNS--VIDYAILENCVreDLDATaPRRMAVLDPIKLTITNLPGNHE-ETLRFANH--PKDESFG-----T 406
Cdd:COG0008 268 NYLALLGWSKSDDqeIFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlDDEELAELlaPELPEAGiredlE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 407 REVPFG--------------STVWIEREDfaEVPPKgfKRLIPgGEVRlrgvgivkceeAVKDAAGDVVELRCTLDPDSr 472
Cdd:COG0008 345 RLVPLVreraktlselaelaRFFFIERED--EKAAK--KRLAP-EEVR-----------KVLKAALEVLEAVETWDPET- 407
|
490 500 510
....*....|....*....|....*....|....*..
gi 2161680032 473 aglpgadrkVKGTIHWVSArhavAAEVRlyDRLFDVP 509
Cdd:COG0008 408 ---------VKGTIHWVSA----EAGVK--DGLLFMP 429
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
11-583 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1097.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 11 TPGSNDNAPRDFVRQIIREDLATGRHRAIRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFV 90
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 91 EGIKDDVRWLGYEWH-ELRHASDYFDVFYRAALKLIEDGKAYVDDLSADEVREYRGTLTEPGRNSPYRDRSIEENLDLFK 169
Cdd:PRK05347 82 DSIKEDVRWLGFDWSgELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 170 RMRAGEFADGSKTLRAKIDMASGNINLRDPALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRP 249
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 250 LYDWCVDNVDlaahpdlwqsvvqagleaMPAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRG 329
Cdd:PRK05347 242 LYDWVLDNLP------------------IPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 330 FTPAGLRLLIERLGISKQNSVIDYAILENCVREDLDATAPRRMAVLDPIKLTITNLPGNHEETLRFANHPKDESFGTREV 409
Cdd:PRK05347 304 YTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 410 PFGSTVWIEREDFAEVPPKGFKRLIPGGEVRLRGVGIVKCEEAVKDAAGDVVELRCTLDPDSRAGLPGADRKVKGTIHWV 489
Cdd:PRK05347 384 PFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 490 SARHAVAAEVRLYDRLFDVPAPDDESDgksWIEHINPEAKRIGRGWLEPAAAQAEPEQRFQFERLGYFVADRvDHRPDAP 569
Cdd:PRK05347 464 SAAHAVPAEVRLYDRLFTVPNPAAGKD---FLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADK-DSTPGKL 539
|
570
....*....|....
gi 2161680032 570 VFNRTVTLRDTWAR 583
Cdd:PRK05347 540 VFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
9-585 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 830.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 9 ETTPGSNDNAPRDFVRQIIREDLATGRHRAIRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPE 88
Cdd:PRK14703 2 SDAPRPRMLVSPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 89 FVEGIKDDVRWLGYEWHE-LRHASDYFDVFYRAALKLIEDGKAYVDDLSADEVREYRGTLTEPGRNSPYRDRSIEENLDL 167
Cdd:PRK14703 82 YVEAIKDDVRWLGFDWGEhLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 168 FKRMRAGEFADGSKTLRAKIDMASGNINLRDPALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDH 247
Cdd:PRK14703 162 FRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 248 RPLYDWCVDNvdlaahpdlwqsvvqagLEAMPAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRR 327
Cdd:PRK14703 242 RAIYDWVLDH-----------------LGPWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 328 RGFTPAGLRLLIERLGISKQNSVIDYAILENCVREDLDATAPRRMAVLDPIKLTITNLPGNHEETLRFANHPKD-ESFGT 406
Cdd:PRK14703 305 RGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 407 REVPFGSTVWIEREDFAEVPPKGFKRLIPGGEVRLRGVGIVKCEEAVKDAAGDVVELRCTLDPDSRAGLPGAdRKVKGTI 486
Cdd:PRK14703 385 RKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTG-RKAAGVI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 487 HWVSARHAVAAEVRLYDRLFDVPAPDDESDGksWIEHINPEAKRIGRGWLEPAAAQAEPEQRFQFERLGYFVADRVDHRP 566
Cdd:PRK14703 464 HWVSAKHALPAEVRLYDRLFKVPQPEAADED--FLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRP 541
|
570
....*....|....*....
gi 2161680032 567 DAPVFNRTVTLRDTWARQA 585
Cdd:PRK14703 542 DALVFNRIITLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
39-581 |
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: 680.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWH-ELRHASDYFDVF 117
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 118 YRAALKLIEDGKAYVDDLSADEVREYRGTLTEPGRNSPYRDRSIEENLDLFKRMRAGEFADGSKTLRAKIDMASGNINLR 197
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 198 DPALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVdlaahpdlwqsvvqagleA 277
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNI------------------H 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 278 MPAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSVIDYAILE 357
Cdd:TIGR00440 223 IFPRPAQYEFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 358 NCVREDLDATAPRRMAVLDPIKLTITNLPGNHeETLRFANHPKDESFGTREVPFGSTVWIEREDFAEVPPKGFKRLIPGG 437
Cdd:TIGR00440 303 SCIREDLNENAPRAMAVIDPVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 438 EVRLRGVGIVKCEEAVKDAAGDVVELRCTLDPDSRAGLPGADRKVKGTIHWVSARHAVAAEVRLYDRLFDVPAPDDESDg 517
Cdd:TIGR00440 382 EVRLRNAYVIKAERVEKDAAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDD- 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2161680032 518 ksWIEHINPEAKRIGRGWLEPAAAQAEPEQRFQFERLGYFVADRVDHRPDAPVFNRTVTLRDTW 581
Cdd:TIGR00440 461 --FLSVINPESLVIKQGFMEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
41-581 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 530.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 41 TRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHELRHASDYFDVFYRA 120
Cdd:PLN02859 267 TRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 121 ALKLIEDGKAYVDDLSADEVREYRgtltEPGRNSPYRDRSIEENLDLFKRMRAGEFADGSKTLRAKIDMASGNINLRDPA 200
Cdd:PLN02859 347 AVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYDLI 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 201 LYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVDLaAHPDLWqsvvqagleampa 280
Cdd:PLN02859 423 AYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGL-YQPYVW------------- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 281 kprqiEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISK-QNSVIDYAILENC 359
Cdd:PLN02859 489 -----EYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRsDNSLIRMDRLEHH 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 360 VREDLDATAPRRMAVLDPIKLTITNLPGNHEETL---RFANHPKDESFGTREVPFGSTVWIEREDFAEVPPKGFKRLIPG 436
Cdd:PLN02859 564 IREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPG 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 437 GEVRLRGVGIVKCEEAV-KDAAGDVVELRCTLDPDSRAglpgadrKVKGTIHWVSA----RHAVAAEVRLYDRLFDVPAP 511
Cdd:PLN02859 644 KSVLLRYAFPIKCTDVVlADDNETVVEIRAEYDPEKKT-------KPKGVLHWVAEpspgVEPLKVEVRLFDKLFLSENP 716
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2161680032 512 DDESDgksWIEHINPEAKRIGRG-WLEPAAAQAEPEQRFQFERLGYFVADRvDHRPDAPVFNRTVTLRDTW 581
Cdd:PLN02859 717 AELED---WLEDLNPQSKEVISGaYAVPSLKDAKVGDRFQFERLGYFAVDK-DSTPEKLVFNRTVTLKDSY 783
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
42-579 |
8.07e-151 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 445.97 E-value: 8.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 42 RFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHELRHASDYFDVFYRAA 121
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHEFA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 122 LKLIEDGKAYVDDLSADEVREYRgtltEPGRNSPYRDRSIEENLDLFKRMRAGEFADGSKTLRAKIDMASGNINLRDPAL 201
Cdd:PTZ00437 135 VQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 202 YRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVdlaahpDLWqsvvqagleampaK 281
Cdd:PTZ00437 211 YRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEEL------NLW-------------R 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 282 PRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSVIDYAILENCVR 361
Cdd:PTZ00437 272 PHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 362 EDLDATAPRRMAVLDPIKLTITNLPGnhEETLRFANHPKDESFGTREVPFGSTVWIEREDF-AEVPPKGFKRLIPGGE-V 439
Cdd:PTZ00437 352 EDLDERCERRLMVIDPIKVVVDNWKG--EREFECPNHPRKPELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPGPRvV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 440 RLRGVGIVKCEEAVKDAAGDVVELRCTLDPDSRAglpgadrKVKGTIHWVSARHAVAAEVRLYDRLF--DVPAPDDEsdg 517
Cdd:PTZ00437 430 GLKYSGNVVCKGFEVDAAGQPSVIHVDIDFERKD-------KPKTNISWVSATACTPVEVRLYNALLkdDRAAIDPE--- 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2161680032 518 ksWIEHINPEAKRIGRGWLEPAAAQAEPEQRFQFERLGYFVADRvDHRPDAPVFNRTVTLRD 579
Cdd:PTZ00437 500 --FLKFIDEDSEVVSHGYAEKGIENAKHFESVQAERFGYFVVDP-DTRPDHLVMNRVLGLRE 558
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
39-370 |
5.38e-129 |
|
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: 377.36 E-value: 5.38e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHELRHASDYFDVFY 118
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 119 RAALKLIEDGKAYVddlsadevreyrgtltepgrnspyrdrsieenldlfkrmragefadgsktlrakidmasgninlrd 198
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 199 palyrirkiaHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVDLAahpdlwqsvvqagleam 278
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY----------------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 279 paKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSVIDYAILEN 358
Cdd:cd00807 149 --RPHQWEFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEA 226
|
330
....*....|..
gi 2161680032 359 CVREDLDATAPR 370
Cdd:cd00807 227 CVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
39-365 |
6.40e-123 |
|
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: 365.10 E-value: 6.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHE-LRHASDYFDVF 117
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYgPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 118 YRAALKLIEDGKAYVDDLSADEVREYRGTLtePGRNSPYRDRSIEENLDLFKR-MRAGEFADGSKTLRAKIDMaSGNINL 196
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPM-ESPYVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 197 RDPALYRIR---KIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVDLaahpdlwqsvvqa 273
Cdd:pfam00749 159 RDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGW------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 274 gleamPAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSV-ID 352
Cdd:pfam00749 226 -----EPPPFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRL 300
|
330
....*....|...
gi 2161680032 353 YAILENCVREDLD 365
Cdd:pfam00749 301 SKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
39-509 |
2.95e-121 |
|
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: 366.43 E-value: 2.95e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHE-LRHASDYFDVF 117
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFDIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 118 YRAALKLIEDGKAYVDDLSADEVREYRGTLTEPGRNSPY----RDRSIEEnldLFKRMRAGEfadgSKTLRAKI------ 187
Cdd:COG0008 85 YEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE---LERMLAAGE----PPVLRFKIpeegvv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 188 --DMASG-----NINLRDPALYRirkiahqntGDAwpiYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCvdnvdl 260
Cdd:COG0008 158 fdDLVRGeitfpNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWL------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 261 aahpdlwqsvvqagLEAMPAKPRqiEFSRLNLSFC----ITSKRKlaqlvseGLVdgwddprmnTLRGLRRRGFTPAGLR 336
Cdd:COG0008 220 --------------YEALGWEPP--EFAHLPLILGpdgtKLSKRK-------GAV---------TVSGLRRRGYLPEAIR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 337 LLIERLGISKQNS--VIDYAILENCVreDLDATaPRRMAVLDPIKLTITNLPGNHE-ETLRFANH--PKDESFG-----T 406
Cdd:COG0008 268 NYLALLGWSKSDDqeIFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlDDEELAELlaPELPEAGiredlE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 407 REVPFG--------------STVWIEREDfaEVPPKgfKRLIPgGEVRlrgvgivkceeAVKDAAGDVVELRCTLDPDSr 472
Cdd:COG0008 345 RLVPLVreraktlselaelaRFFFIERED--EKAAK--KRLAP-EEVR-----------KVLKAALEVLEAVETWDPET- 407
|
490 500 510
....*....|....*....|....*....|....*..
gi 2161680032 473 aglpgadrkVKGTIHWVSArhavAAEVRlyDRLFDVP 509
Cdd:COG0008 408 ---------VKGTIHWVSA----EAGVK--DGLLFMP 429
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
30-563 |
1.13e-101 |
|
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: 318.69 E-value: 1.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 30 DLATGRHRAIRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHELRH 109
Cdd:TIGR00463 85 ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 110 ASDYFDVFYRAALKLIEDGKAYVDDLSADEVREYRGTltepGRNSPYRDRSIEENLDLFKRMRAGEFADGSKTLRAKIDM 189
Cdd:TIGR00463 165 QSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 190 ASGNINLRDPALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDH--RPLYDWcvdnvdlaahpdlw 267
Cdd:TIGR00463 241 KHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNrrKQEYIY-------------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 268 qsvVQAGLEamPAKPRQIEFSRLNLSFCITSKRKLaQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQ 347
Cdd:TIGR00463 307 ---RYFGWE--PPEFIHWGRLKIDDVRALSTSSAR-KGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKIN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 348 NSVIDYAILENCVREDLDATAPRRMAVLDPIKLTITNLPGNHEETLRFanHPKDESFGTREVPFGSTVWIEREDFAEVPP 427
Cdd:TIGR00463 381 DVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRVERPL--HPDHPEIGERVLILRGEIYVPKDDLEEGVE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 428 kgfkrlipggEVRLRGVGIVKCEEAVKDAAGDvvelrctldpdsraGLPGADRKVKGTIHWVSARHAVAAEVrlydrlfd 507
Cdd:TIGR00463 459 ----------PVRLMDAVNVIYSKKELRYHSE--------------GLEGARKLGKSIIHWLPAKDAVKVKV-------- 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2161680032 508 vpapddesdgkswiehINPEAkRIGRGWLEPAAAQAEPEQRFQFERLGYFVADRVD 563
Cdd:TIGR00463 507 ----------------IMPDA-SIVEGVIEADASELEVGDVVQFERFGFARLDSAD 545
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
39-570 |
1.62e-101 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 323.21 E-value: 1.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHELRHASDYFDVFY 118
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLM 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 119 RAALKLIEDGKAYVDDLSADEVREYRGTLTEpgrnSPYRDRSIEENLDLFKRMRAGEFADGSKTLRAKIDMASGNINLRD 198
Cdd:PLN02907 294 EMAEKLIKEGKAYVDDTPREQMRKERMDGIE----SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRD 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 199 PALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCvdnvdlaahpdlwqsvvqagLEAM 278
Cdd:PLN02907 370 PVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRI--------------------LEDM 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 279 PAKPRQI-EFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSVIDYAILE 357
Cdd:PLN02907 430 GLRKVHIwEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLW 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 358 NCVREDLDATAPRRMAVLDPIK--LTITNLPGNhEETLRFANHPKDESFGTREVPFGSTVWIEREDfAEVPPKgfkrlip 435
Cdd:PLN02907 510 TINKKIIDPVCPRHTAVLKEGRvlLTLTDGPET-PFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD-AEAISE------- 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 436 GGEVRLRGVG--IVKceEAVKDAAGDVVELRCTLDpdsragLPGADRKVKGTIHWVSA-RHAVAAEVRLYDRLFDVPAPD 512
Cdd:PLN02907 581 GEEVTLMDWGnaIIK--EITKDEGGAVTALSGELH------LEGSVKTTKLKLTWLPDtNELVPLSLVEFDYLITKKKLE 652
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2161680032 513 DESDgksWIEHINPEAKRigrgwlePAAAQAEPEQR-------FQFERLGYFVADRVDHRPDAPV 570
Cdd:PLN02907 653 EDDN---FLDVLNPCTKK-------ETAALGDSNMRnlkrgeiIQLERKGYYRCDAPFVRSSKPI 707
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
39-570 |
2.00e-99 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 313.33 E-value: 2.00e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNP--GKEDPEFVEGIKDDVRWLGYEWHELRHASDYFDV 116
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPrtKRPDPEAYDMILEDLKWLGVKWDEVVIQSDRLEI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 117 FYRAALKLIEDGKAYVDDLSADEVREYRgtltEPGRNSPYRDRSIEENLDLFKRMRAGEFADGSKTLRAKIDMASGNINL 196
Cdd:PRK04156 182 YYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 197 RDPALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHslcTLEFEDH-------RPLYD---Wcvdnvdlaahpdl 266
Cdd:PRK04156 258 RDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTH---VLRGKDHidntekqRYIYDyfgW------------- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 267 wqsvvqagleampAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISK 346
Cdd:PRK04156 322 -------------EYPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 347 QNSVIDYAIL--ENcvREDLDATAPRRMAVLDPIKLTITNLPgnhEETLRFANHPKDESFGTREVPFGSTVWIEREDFAE 424
Cdd:PRK04156 389 TDATISWENLyaIN--RKLIDPIANRYFFVRDPVELEIEGAE---PLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEA 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 425 VppkgfkrlipGGEVRLRGVGIVKCEEAVKDAA---GDVVElrctldpdsraglpgADRKVKGTI-HWVSARHAVAAEVr 500
Cdd:PRK04156 464 E----------GKMVRLMDLFNVEITGVSVDKAryhSDDLE---------------EARKNKAPIiQWVPEDESVPVRV- 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 501 lydrlfdvpapddesdgkswiehINPEAKRIgRGWLEPAAAQAEPEQRFQFERLGyFVadRVDHRPDAPV 570
Cdd:PRK04156 518 -----------------------LKPDGGDI-EGLAEPDVADLEVDDIVQFERFG-FV--RIDSVEDDEV 560
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
39-570 |
8.77e-89 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 284.21 E-value: 8.77e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHELRHASDYFDVFY 118
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPIR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 119 RAALKLIEDGKAYVDDLSADEVREYRGTLTEpgrnSPYRDRSIEENLDLFKRMRAGEFADGSKTLRAKIDMASGNINLRD 198
Cdd:PLN03233 92 CYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLRD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 199 PALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVDLaahpdlwqsvvqagleam 278
Cdd:PLN03233 168 PVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGL------------------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 279 pAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSVIDYAILEN 358
Cdd:PLN03233 230 -RRPRIHAFARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 359 CVREDLDATAPRRMAV--LDPIKLTITNLP-GNHEETLRFANHPKDESFGTREVPFGSTVWIEREDfaevppkgFKRLIP 435
Cdd:PLN03233 309 ENKKEIDKRAKRFMAIdkADHTALTVTNADeEADFAFSETDCHPKDPGFGKRAMRICDEVLLEKAD--------TEDIQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 436 GGEVRLRGVGIVKCEEAVKDAAGDVVelrctldPDsraglpGADRKVKGTIHWVsARHAVAAEVRLYDrlFD--VPAPDD 513
Cdd:PLN03233 381 GEDIVLLRWGVIEISKIDGDLEGHFI-------PD------GDFKAAKKKISWI-ADVSDNIPVVLSE--FDnlIIKEKL 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2161680032 514 ESDGKsWIEHINP----EAKRIGRGWLEpaaaQAEPEQRFQFERLGYFVADRVDHRPDAPV 570
Cdd:PLN03233 445 EEDDK-FEDFINPdtlaETDVIGDAGLK----TLKEHDIIQLERRGFYRVDRPYMGEEKPL 500
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
41-565 |
7.21e-87 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 281.47 E-value: 7.21e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 41 TRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHE-LRHASDYFDVFYR 119
Cdd:PTZ00402 55 TRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVgPTYSSDYMDLMYE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 120 AALKLIEDGKAYVDDLSADEVREYRGTltepGRNSPYRDRSIEENLDLFKRMRAGEfADGSKT-LRAKIDMASGNINLRD 198
Cdd:PTZ00402 135 KAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNENKAMRD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 199 PALYRIRKIAHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVDLaahpdlwqsvvqagleam 278
Cdd:PTZ00402 210 PVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGI------------------ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 279 pAKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSVIDYAILEN 358
Cdd:PTZ00402 272 -RKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWY 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 359 CVREDLDATAPRRMAVLDPIKLTITNLPGNHEETLRFANHPKDESFGTREVPFGSTVWIEREDFAevppkgfkRLIPGGE 438
Cdd:PTZ00402 351 FNTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVA--------LLKEGDE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 439 VRLRGVGivkcEEAVKD-----AAGDVVELRCTLDPDsraglpGADRKVKGTIHWV-SARHAVAAEVRLYDRLFDVPAPD 512
Cdd:PTZ00402 423 VTLMDWG----NAYIKNirrsgEDALITDADIVLHLE------GDVKKTKFKLTWVpESPKAEVMELNEYDHLLTKKKPD 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2161680032 513 DESDGKSWIEHINPEAKRIgrgWLEPAAAQAEPEQRFQFERLGYFVADRVDHR 565
Cdd:PTZ00402 493 PEESIDDIIAPVTKYTQEV---YGEEALSVLKKGDIIQLERRGYYIVDDVTPK 542
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
368-560 |
1.10e-73 |
|
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: 232.93 E-value: 1.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 368 APRRMAVLDPIKLTITNLPGNHEETLRFANHPKDESFGTREVPFGSTVWIEREDfaevppkgFKRLIPGGEVRLRGVGIV 447
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIERED--------FKRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 448 KCEEAVKDAAGDVVELRCTLDPDSRAGlpgaDRKVKG-TIHWVSARHAVAAEVRLYDRLFDVPAPDDESdgkswiehINP 526
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGG----ARKVKGkIIHWVSASDAVPAEVRLYDRLFKDEDDADFL--------LNP 140
|
170 180 190
....*....|....*....|....*....|....*
gi 2161680032 527 EA-KRIGRGWLEPAAAQAEPEQRFQFERLGYFVAD 560
Cdd:pfam03950 141 DSlKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
39-365 |
6.91e-53 |
|
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: 180.36 E-value: 6.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHE-LRHASDYFDVF 117
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEgPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 118 YRAALKLIEDGkayvddlsadevreyrgtltepgrnspyrdrsieenldlfkrmragefadgsktlrakidmasgninlr 197
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 198 dpalyrirkiahqntgdawpIYPMYDFAHALSDAVEGITHSLCTLEFEDHRPLYDWCVDNVDLAAhpdlwqsvvqaglea 277
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEP--------------- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 278 mpakPRQIEFSRLNLSFC-ITSKRKLAqlvseglvdgwddprmNTLRGLRRRGFTPAGLRLLIERLGISK---------- 346
Cdd:cd00418 138 ----PRFYHFPRLLLEDGtKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKpdghelftle 197
|
330 340 350
....*....|....*....|....*....|..
gi 2161680032 347 -------------QNSVIDYAILENCVREDLD 365
Cdd:cd00418 198 emiaafsvervnsADATFDWAKLEWLNREYIR 229
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
39-370 |
1.23e-42 |
|
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: 152.89 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 39 IRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNP--GKEDPEFVEGIKDDVRWLGYEWHELRHASDYFDV 116
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 117 FYRAALKLIEDGKAYVddlsadevreyrgtltepgrnspyrdrsieenldlfkrmragefadgsktlrakidmasgninl 196
Cdd:cd09287 82 YYEYARKLIEMGGAYV---------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 197 rdpalyrirkiaHQNTGDAWPIYPMYDFAHALSDAVEGITHSLCTLEFED----HRPLYDWcvdnvdlaahpdlwqsvvq 272
Cdd:cd09287 98 ------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEY------------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 273 AGLEampaKPRQIEFSRLNLSFCITSKRKLAQLVSEGLVDGWDDPRMNTLRGLRRRGFTPAGLRLLIERLGISKQNSVID 352
Cdd:cd09287 147 FGWE----YPETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATIS 222
|
330
....*....|....*...
gi 2161680032 353 YAILENCVREDLDATAPR 370
Cdd:cd09287 223 WENLYAINRKLIDPRANR 240
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
38-134 |
1.33e-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: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 38 AIRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHE-LRHASDY--- 113
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgPDVGGPYgpy 80
|
90 100 110
....*....|....*....|....*....|....
gi 2161680032 114 -----FDVFYRAALKLIEDGKAY--------VDD 134
Cdd:cd00808 81 rqserLEIYRKYAEKLLEKGDGFptyhlanvVDD 114
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
40-131 |
1.60e-14 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 74.50 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 40 RTRFPPEPNGYLHIGHAKAICLNFGIAREFGG-WCnLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWH-ELRHASDYFDVf 117
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGrWL-LRIEDIDPPREVPGAADAILADLEWLGLHWDgPVLYQSQRHDA- 84
|
90
....*....|....*
gi 2161680032 118 YRAAL-KLIEDGKAY 131
Cdd:PRK05710 85 YRAALdRLRAQGLVY 99
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
38-249 |
5.19e-11 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 65.15 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 38 AIRTRFPPEPNGYLHIGHAKAICLNFGIAREFGGWCNLRLDDTNPGKEDPEFVEGIKDDVRWLGYEWHE----------L 107
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgpdvggeygpY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 108 RHaSDYFDVFYRAALKLIEDGKAYVDDLSADEVREYRGTLTEPGRNSPYRdrsieenldlfkrmraGEFADGSKtlrAKI 187
Cdd:PLN02627 125 RQ-SERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYT----------------GKWATASD---EEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 188 D--MASGNinlrdPALYRIR-------KI----------AHQNTGDAWPI----YPMYDFAHALSDAVEGITHslcTLEF 244
Cdd:PLN02627 185 QaeLAKGT-----PYTYRFRvpkegsvKIddlirgevswNTDTLGDFVLLrsngQPVYNFCVAVDDATMGITH---VIRA 256
|
....*
gi 2161680032 245 EDHRP 249
Cdd:PLN02627 257 EEHLP 261
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
41-100 |
3.50e-10 |
|
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: 58.26 E-value: 3.50e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2161680032 41 TRFPPEPNGYLHIGHAKAICLNFGIAR--EFGGW---CNLRLDDTNPGKEDP-------------EFVEGIKDDVRWL 100
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQayRKLGYkvrCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM 79
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
41-104 |
1.44e-08 |
|
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: 52.54 E-value: 1.44e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2161680032 41 TRFPPEPnGYLHIGHAKAICLNFGIArefgGWCNLRLDDTNPGK------EDPEFVEGIKDDVRWLGYEW 104
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDF 66
|
|
| |
