|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
12-609 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1075.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 12 DASAEPHRPGNFLRGIIERDLEAGTYAgrrhagspgdaahhagapldaaKIRTRFPPEPNGYLHVGHAKSICLNFGLARD 91
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASGKHT----------------------RVHTRFPPEPNGYLHIGHAKSICLNFGLAQD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 92 YGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQGrdpahpetpveHLYYASDYFDFMYRAAEALVTAGFAYVDEQS 171
Cdd:PRK05347 60 YGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSG-----------ELRYASDYFDQLYEYAVELIKKGKAYVDDLS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 172 AEQMRATRGDFNTPGTDSPFRSRTPAENLARFRAMRDGQLADGAAVLRARIDMASPNINLRDPAIYRIKRATHHNTGDTW 251
Cdd:PRK05347 129 AEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 252 CIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTlctlgLLAQPRPHQHEFARLNLTYVVTSKRKLKQLVDEG 331
Cdd:PRK05347 209 CIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDN-----LPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 332 HVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATLDAALRDDLEGKAPRAMAVLDPLKLKLTNWAEvf 411
Cdd:PRK05347 284 HVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPE-- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 412 gsaDHLEPCHAPAHPHLPELGSREFTLGPEVWIERDDFAEQPPKGFFRLFPGNKVRLKYGVVVECSGCEKDADGRIVAVL 491
Cdd:PRK05347 362 ---GQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIH 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 492 ATVVPDTKSGtPGADAVKVKGTITWVGVHEAVPAELRLYDRLFTEAQPDaGGRDFLTVLNPDSRRVAAGYVEASVGRVMP 571
Cdd:PRK05347 439 CTYDPDTLSG-NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPNPA-AGKDFLDFLNPDSLVIKQGFVEPSLADAKP 516
|
570 580 590
....*....|....*....|....*....|....*...
gi 124259282 572 ESRLQFERHGYFVADsKAHRTGQPVFNRITGLKDSWGK 609
Cdd:PRK05347 517 EDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
62-607 |
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: 650.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 62 IRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQGRdpahpetpveh 141
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 142 LYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDFNTPGTDSPFRSRTPAENLARFRAMRDGQLADGAAVLRAR 221
Cdd:TIGR00440 70 IRYSSDYFDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 222 IDMASPNINLRDPAIYRIKRATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTLCTlgllaQ 301
Cdd:TIGR00440 150 IDMASPFPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHI-----F 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 302 PRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATLDAA 381
Cdd:TIGR00440 225 PRPAQYEFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESC 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 382 LRDDLEGKAPRAMAVLDPLKLKLTNWaevfgsADHLEPCHAPAHPHLPELGSREFTLGPEVWIERDDFAEQPPKGFFRLF 461
Cdd:TIGR00440 305 IREDLNENAPRAMAVIDPVEVVIENL------SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 462 PGNKVRLKYGVVVECSGCEKDADGRIVAVLATVVPDTKSGTPgADAVKVKGTITWVGVHEAVPAELRLYDRLFTEAQPDA 541
Cdd:TIGR00440 379 LGKEVRLRNAYVIKAERVEKDAAGKITTIFCTYDNKTLGKEP-ADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGA 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124259282 542 gGRDFLTVLNPDSRRVAAGYVEASVGRVMPESRLQFERHGYFVADSKAHRTGQPVFNRITGLKDSW 607
Cdd:TIGR00440 458 -PDDFLSVINPESLVIKQGFMEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
61-392 |
4.12e-135 |
|
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: 393.93 E-value: 4.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWqgrdpahpetpvE 140
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP------------Y 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 HLYYASDYFDFMYRAAEALVTAGFAYVdeqsaeqmratrgdfntpgtdspfrsrtpaenlarframrdgqladgaavlra 220
Cdd:cd00807 69 KVTYASDYFDQLYEYAEQLIKKGKAYV----------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 221 ridmaspninlrdpaiyrikratHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTLctlGLla 300
Cdd:cd00807 96 -----------------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL---RL-- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 301 qPRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATLDA 380
Cdd:cd00807 148 -YRPHQWEFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEA 226
|
330
....*....|..
gi 124259282 381 ALRDDLEGKAPR 392
Cdd:cd00807 227 CVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
61-387 |
4.53e-125 |
|
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: 371.27 E-value: 4.53e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQGRdpahpetpve 140
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 hLYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDfnTPGTDSPFRSRTPAENLARF-RAMRDGQLADGAAVLR 219
Cdd:pfam00749 71 -PYYQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREE--QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 220 ARIDMASPnINLRDPAIYRIK---RATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTLCtl 296
Cdd:pfam00749 148 AKIPMESP-YVFRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 297 gllAQPRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSW-IDY 375
Cdd:pfam00749 225 ---WEPPPFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLS 301
|
330
....*....|..
gi 124259282 376 ATLDAALRDDLE 387
Cdd:pfam00749 302 KSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
61-585 |
5.92e-122 |
|
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: 368.74 E-value: 5.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQgrdpahpetpvE 140
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWD-----------E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 HLYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDFNTPGT----DSPFRSRTPAEnLARFRAmrdgqlADGAA 216
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKppryDGRCRDLSPEE-LERMLA------AGEPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 217 VLRARI--------DMAS-----PNINLRDPAIYRIkrathhnTGdtwciYPMYTYAHPIEDALEGITHSICTLEFEDQR 283
Cdd:COG0008 146 VLRFKIpeegvvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 284 PFYDWLLDtlcTLGLlaqPRPhqhEFARLNLTY----VVTSKRKlkqlvdeGHVdgwddprmpTLVGLRRRGYTPDSIQL 359
Cdd:COG0008 214 PRQIWLYE---ALGW---EPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRN 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 360 FCERIGVSKDYSW--IDYATLDAALrdDLEGKaPRAMAVLDPLKLKLTNWAEVFG-SADHLepcHAPAHPHLPELGSREF 436
Cdd:COG0008 269 YLALLGWSKSDDQeiFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlDDEEL---AELLAPELPEAGIRED 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 437 -------------------TLGPEVWIERDDfaEQPPKGffRLFPGNkVRlkygvvvecsgcekdadgRIVAVLATVVPD 497
Cdd:COG0008 343 lerlvplvreraktlselaELARFFFIERED--EKAAKK--RLAPEE-VR------------------KVLKAALEVLEA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 498 TKSGTPGAdavkVKGTITWvgvheaVPAELRLYDRLFteAQPdaggrdfltvlnpdsRRVA--AGYVEASVGRVMP---E 572
Cdd:COG0008 400 VETWDPET----VKGTIHW------VSAEAGVKDGLL--FMP---------------LRVAltGRTVEPSLFDVLEllgK 452
|
570
....*....|...
gi 124259282 573 SRLqFERHGYFVA 585
Cdd:COG0008 453 ERV-FERLGYAID 464
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
12-609 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1075.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 12 DASAEPHRPGNFLRGIIERDLEAGTYAgrrhagspgdaahhagapldaaKIRTRFPPEPNGYLHVGHAKSICLNFGLARD 91
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASGKHT----------------------RVHTRFPPEPNGYLHIGHAKSICLNFGLAQD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 92 YGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQGrdpahpetpveHLYYASDYFDFMYRAAEALVTAGFAYVDEQS 171
Cdd:PRK05347 60 YGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSG-----------ELRYASDYFDQLYEYAVELIKKGKAYVDDLS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 172 AEQMRATRGDFNTPGTDSPFRSRTPAENLARFRAMRDGQLADGAAVLRARIDMASPNINLRDPAIYRIKRATHHNTGDTW 251
Cdd:PRK05347 129 AEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 252 CIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTlctlgLLAQPRPHQHEFARLNLTYVVTSKRKLKQLVDEG 331
Cdd:PRK05347 209 CIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDN-----LPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 332 HVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATLDAALRDDLEGKAPRAMAVLDPLKLKLTNWAEvf 411
Cdd:PRK05347 284 HVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPE-- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 412 gsaDHLEPCHAPAHPHLPELGSREFTLGPEVWIERDDFAEQPPKGFFRLFPGNKVRLKYGVVVECSGCEKDADGRIVAVL 491
Cdd:PRK05347 362 ---GQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIH 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 492 ATVVPDTKSGtPGADAVKVKGTITWVGVHEAVPAELRLYDRLFTEAQPDaGGRDFLTVLNPDSRRVAAGYVEASVGRVMP 571
Cdd:PRK05347 439 CTYDPDTLSG-NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPNPA-AGKDFLDFLNPDSLVIKQGFVEPSLADAKP 516
|
570 580 590
....*....|....*....|....*....|....*...
gi 124259282 572 ESRLQFERHGYFVADsKAHRTGQPVFNRITGLKDSWGK 609
Cdd:PRK05347 517 EDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
12-609 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 800.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 12 DASAEPHRPG---NFLRGIIERDLEAGTYAgrrhagspgdaahhagapldaaKIRTRFPPEPNGYLHVGHAKSICLNFGL 88
Cdd:PRK14703 1 MSDAPRPRMLvspNFITEIIEEDLEAGRYP----------------------RVVTRFPPEPNGYLHIGHAKSILLNFGI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 89 ARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQgrdpahpetpvEHLYYASDYFDFMYRAAEALVTAGFAYVD 168
Cdd:PRK14703 59 ARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWG-----------EHLYYASDYFERMYAYAEQLIKMGLAYVD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 169 EQSAEQMRATRGDFNTPGTDSPFRSRTPAENLARFRAMRDGQLADGAAVLRARIDMASPNINLRDPAIYRIKRATHHNTG 248
Cdd:PRK14703 128 SVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 249 DTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTLctlgLLAQPRPHQHEFARLNLTYVVTSKRKLKQLV 328
Cdd:PRK14703 208 DEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHL----GPWPPRPRQYEFARLALGYTVMSKRKLRELV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 329 DEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATLDAALRDDLEGKAPRAMAVLDPLKLKLTNWa 408
Cdd:PRK14703 284 EEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENL- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 409 evfgSADHLEPCHAPAHPH-LPELGSREFTLGPEVWIERDDFAEQPPKGFFRLFPGNKVRLKYGVVVECSGCEKDADGRI 487
Cdd:PRK14703 363 ----PAGKVEELDLPYWPHdVPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 488 VAVLATVVPDTKSGTPgaDAVKVKGTITWVGVHEAVPAELRLYDRLFTEAQPDAGGRDFLTVLNPDSRRVAAGYVEASVG 567
Cdd:PRK14703 439 TELRCTYDPESAKGED--TGRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEAADEDFLEFLNPDSLRVAQGRVEPAVR 516
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 124259282 568 RVMPESRLQFERHGYFVADSKAHRTGQPVFNRITGLKDSWGK 609
Cdd:PRK14703 517 DDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGA 558
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
62-607 |
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: 650.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 62 IRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQGRdpahpetpveh 141
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 142 LYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDFNTPGTDSPFRSRTPAENLARFRAMRDGQLADGAAVLRAR 221
Cdd:TIGR00440 70 IRYSSDYFDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 222 IDMASPNINLRDPAIYRIKRATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTLCTlgllaQ 301
Cdd:TIGR00440 150 IDMASPFPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHI-----F 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 302 PRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATLDAA 381
Cdd:TIGR00440 225 PRPAQYEFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESC 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 382 LRDDLEGKAPRAMAVLDPLKLKLTNWaevfgsADHLEPCHAPAHPHLPELGSREFTLGPEVWIERDDFAEQPPKGFFRLF 461
Cdd:TIGR00440 305 IREDLNENAPRAMAVIDPVEVVIENL------SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 462 PGNKVRLKYGVVVECSGCEKDADGRIVAVLATVVPDTKSGTPgADAVKVKGTITWVGVHEAVPAELRLYDRLFTEAQPDA 541
Cdd:TIGR00440 379 LGKEVRLRNAYVIKAERVEKDAAGKITTIFCTYDNKTLGKEP-ADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGA 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124259282 542 gGRDFLTVLNPDSRRVAAGYVEASVGRVMPESRLQFERHGYFVADSKAHRTGQPVFNRITGLKDSW 607
Cdd:TIGR00440 458 -PDDFLSVINPESLVIKQGFMEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
61-609 |
5.02e-159 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 475.02 E-value: 5.02e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGfdWQgrdpahpetPVE 140
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WE---------PFK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 hLYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDFntpgTDSPFRSRTPAENLARFRAMRDGQLADGAAVLRA 220
Cdd:PLN02859 333 -ITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKK----MNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRM 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 221 RIDMASPNINLRDPAIYRIKRATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDtlcTLGLLa 300
Cdd:PLN02859 408 KQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLD---SLGLY- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 301 qpRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSK-DYSWIDYATLD 379
Cdd:PLN02859 484 --QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRsDNSLIRMDRLE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 380 AALRDDLEGKAPRAMAVLDPLKLKLTNWaevfgSADHLEPCHAPAHPHLPELGSREFTLGP---EVWIERDDFAEQPPKG 456
Cdd:PLN02859 562 HHIREELNKTAPRTMVVLHPLKVVITNL-----ESGEVIELDAKRWPDAQNDDPSAFYKVPfsrVVYIERSDFRLKDSKD 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 457 FFRLFPGNKVRLKYGVVVECSG-CEKDADGRIVAVLATVVPDTKSgtpgadavKVKGTITWV-----GVhEAVPAELRLY 530
Cdd:PLN02859 637 YYGLAPGKSVLLRYAFPIKCTDvVLADDNETVVEIRAEYDPEKKT--------KPKGVLHWVaepspGV-EPLKVEVRLF 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 531 DRLFTEAQPdAGGRDFLTVLNPDSRRVAAG-YVEASVGRVMPESRLQFERHGYFVADsKAHRTGQPVFNRITGLKDSWGK 609
Cdd:PLN02859 708 DKLFLSENP-AELEDWLEDLNPQSKEVISGaYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
49-605 |
5.51e-154 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 454.83 E-value: 5.51e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 49 AAHHAgapLDAAKIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGF--D 126
Cdd:PTZ00437 42 EKHEA---VTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 127 WqgrdpahpetpvehLYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDFNtpgtDSPFRSRTPAENLARFRAM 206
Cdd:PTZ00437 119 W--------------VTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQRE----DSPWRNRSVEENLLLFEHM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 207 RDGQLADGAAVLRARIDMASPNINLRDPAIYRIKRATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFY 286
Cdd:PTZ00437 181 RQGRYAEGEATLRVKADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 287 DWLLDTLCTLgllaqpRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGV 366
Cdd:PTZ00437 261 FWLLEELNLW------RPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 367 SKDYSWIDYATLDAALRDDLEGKAPRAMAVLDPLKLKLTNWaevfgSADHLEPChaPAHPHLPELGSREFTLGPEVWIER 446
Cdd:PTZ00437 335 TRSMNVIQISMLENTLREDLDERCERRLMVIDPIKVVVDNW-----KGEREFEC--PNHPRKPELGSRKVMFTDTFYVDR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 447 DDF-AEQPPKGFFRLFPGNK-VRLKYGVVVECSGCEKDADGRIVAVLATVVPDTKSgtpgadavKVKGTITWVGVHEAVP 524
Cdd:PTZ00437 408 SDFrTEDNNSKFYGLAPGPRvVGLKYSGNVVCKGFEVDAAGQPSVIHVDIDFERKD--------KPKTNISWVSATACTP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 525 AELRLYDRLFTEAQPdAGGRDFLTVLNPDSRRVAAGYVEASVGRVMPESRLQFERHGYFVADSKAhRTGQPVFNRITGLK 604
Cdd:PTZ00437 480 VEVRLYNALLKDDRA-AIDPEFLKFIDEDSEVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDT-RPDHLVMNRVLGLR 557
|
.
gi 124259282 605 D 605
Cdd:PTZ00437 558 E 558
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
61-392 |
4.12e-135 |
|
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: 393.93 E-value: 4.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWqgrdpahpetpvE 140
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP------------Y 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 HLYYASDYFDFMYRAAEALVTAGFAYVdeqsaeqmratrgdfntpgtdspfrsrtpaenlarframrdgqladgaavlra 220
Cdd:cd00807 69 KVTYASDYFDQLYEYAEQLIKKGKAYV----------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 221 ridmaspninlrdpaiyrikratHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTLctlGLla 300
Cdd:cd00807 96 -----------------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL---RL-- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 301 qPRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATLDA 380
Cdd:cd00807 148 -YRPHQWEFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEA 226
|
330
....*....|..
gi 124259282 381 ALRDDLEGKAPR 392
Cdd:cd00807 227 CVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
61-387 |
4.53e-125 |
|
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: 371.27 E-value: 4.53e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQGRdpahpetpve 140
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 hLYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDfnTPGTDSPFRSRTPAENLARF-RAMRDGQLADGAAVLR 219
Cdd:pfam00749 71 -PYYQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREE--QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 220 ARIDMASPnINLRDPAIYRIK---RATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTLCtl 296
Cdd:pfam00749 148 AKIPMESP-YVFRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 297 gllAQPRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSW-IDY 375
Cdd:pfam00749 225 ---WEPPPFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLS 301
|
330
....*....|..
gi 124259282 376 ATLDAALRDDLE 387
Cdd:pfam00749 302 KSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
61-585 |
5.92e-122 |
|
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: 368.74 E-value: 5.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQgrdpahpetpvE 140
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWD-----------E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 HLYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDFNTPGT----DSPFRSRTPAEnLARFRAmrdgqlADGAA 216
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKppryDGRCRDLSPEE-LERMLA------AGEPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 217 VLRARI--------DMAS-----PNINLRDPAIYRIkrathhnTGdtwciYPMYTYAHPIEDALEGITHSICTLEFEDQR 283
Cdd:COG0008 146 VLRFKIpeegvvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 284 PFYDWLLDtlcTLGLlaqPRPhqhEFARLNLTY----VVTSKRKlkqlvdeGHVdgwddprmpTLVGLRRRGYTPDSIQL 359
Cdd:COG0008 214 PRQIWLYE---ALGW---EPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRN 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 360 FCERIGVSKDYSW--IDYATLDAALrdDLEGKaPRAMAVLDPLKLKLTNWAEVFG-SADHLepcHAPAHPHLPELGSREF 436
Cdd:COG0008 269 YLALLGWSKSDDQeiFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlDDEEL---AELLAPELPEAGIRED 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 437 -------------------TLGPEVWIERDDfaEQPPKGffRLFPGNkVRlkygvvvecsgcekdadgRIVAVLATVVPD 497
Cdd:COG0008 343 lerlvplvreraktlselaELARFFFIERED--EKAAKK--RLAPEE-VR------------------KVLKAALEVLEA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 498 TKSGTPGAdavkVKGTITWvgvheaVPAELRLYDRLFteAQPdaggrdfltvlnpdsRRVA--AGYVEASVGRVMP---E 572
Cdd:COG0008 400 VETWDPET----VKGTIHW------VSAEAGVKDGLL--FMP---------------LRVAltGRTVEPSLFDVLEllgK 452
|
570
....*....|...
gi 124259282 573 SRLqFERHGYFVA 585
Cdd:COG0008 453 ERV-FERLGYAID 464
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
33-609 |
6.81e-103 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 327.45 E-value: 6.81e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 33 EAGTYAGRRHAGSP--------------GDAAHHAGAP---LDAA---KIRTRFPPEPNGYLHVGHAKSICLNFGLARDY 92
Cdd:PLN02907 165 VTAAYVGKRGAGKPaaakskekvadagkADGAKDKGSFevdLPGAeegKVCTRFPPEPSGYLHIGHAKAALLNQYFARRY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 93 GGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWqgrdpahpetpvEHLYYASDYFDFMYRAAEALVTAGFAYVDEQSA 172
Cdd:PLN02907 245 KGKLIVRFDDTNPSKESDEFVENILKDIETLGIKY------------DAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 173 EQMRATRGDfntpGTDSPFRSRTPAENLARFRAMRDGQLADGAAVLRARIDMASPNINLRDPAIYRIKRATHHNTGDTWC 252
Cdd:PLN02907 313 EQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 253 IYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDtlcTLGLlaqPRPHQHEFARLNLTYVVTSKRKLKQLVDEGH 332
Cdd:PLN02907 389 VYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILE---DMGL---RKVHIWEFSRLNFVYTLLSKRKLQWFVDNGK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 333 VDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYS---WIDYATLDAALRDDLegkAPRAMAVLDPLK--LKLTNW 407
Cdd:PLN02907 463 VEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNlmeWDKLWTINKKIIDPV---CPRHTAVLKEGRvlLTLTDG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 408 AEvfgsadhlEP--CHAPAHPHLPELGSREFTLGPEVWIERDDfAEQPPKgffrlfpGNKVRL-KYG--VVVEcsgCEKD 482
Cdd:PLN02907 540 PE--------TPfvRIIPRHKKYEGAGKKATTFTNRIWLDYAD-AEAISE-------GEEVTLmDWGnaIIKE---ITKD 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 483 ADGRIVAVLATVVPDtksgtpgADAVKVKGTITWVG-VHEAVPAELRLYDRLFTEAQPDAgGRDFLTVLNPDSRRVAAGY 561
Cdd:PLN02907 601 EGGAVTALSGELHLE-------GSVKTTKLKLTWLPdTNELVPLSLVEFDYLITKKKLEE-DDNFLDVLNPCTKKETAAL 672
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 124259282 562 VEASVGRVMPESRLQFERHGYFVADSKAHRTGQPV--FNRITGLKDSWGK 609
Cdd:PLN02907 673 GDSNMRNLKRGEIIQLERKGYYRCDAPFVRSSKPIvlFAIPDGRQQKSGK 722
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
59-586 |
1.30e-95 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 302.70 E-value: 1.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 59 AAKIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFdwqgrdpahpeTP 138
Cdd:PLN03233 9 AGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEI-----------KP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 139 vEHLYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDfntpGTDSPFRSRTPAENLARFRAMRDGQLADGAAVL 218
Cdd:PLN03233 78 -DSVSFTSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERAD----RAESKHRNQSPEEALEMFKEMCSGKEEGGAWCL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 219 RARIDMASPNINLRDPAIYRIKRATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTlctlgl 298
Cdd:PLN03233 153 RAKIDMQSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKA------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 299 LAQPRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATL 378
Cdd:PLN03233 227 LGLRRPRIHAFARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 379 DAALRDDLEGKAPRAMAV--LDPLKLKLTNWAEvfgsADHLEPCHAPAHPHLPELGSREFTLGPEVWIERDDFAEqppkg 456
Cdd:PLN03233 307 WAENKKEIDKRAKRFMAIdkADHTALTVTNADE----EADFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTED----- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 457 ffrLFPGNKVRLKYGVVVECSGCEKDADGRIVavlatvvpdtksgtPGADAVKVKGTITWVG-VHEAVPAELRLYDRLFT 535
Cdd:PLN03233 378 ---IQLGEDIVLLRWGVIEISKIDGDLEGHFI--------------PDGDFKAAKKKISWIAdVSDNIPVVLSEFDNLII 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 124259282 536 EA--QPDAGGRDFltvLNPDSRRVAAGYVEASVGRVMPESRLQFERHGYFVAD 586
Cdd:PLN03233 441 KEklEEDDKFEDF---INPDTLAETDVIGDAGLKTLKEHDIIQLERRGFYRVD 490
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
61-588 |
2.01e-94 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 300.59 E-value: 2.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWqgrdpahpetpvE 140
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKW------------D 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 HLYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDfntpGTDSPFRSRTPAENLARFRAMRDGQLADGAAVLRA 220
Cdd:TIGR00463 161 EVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 221 RIDMASPNINLRDPAIYRIKRATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFED--QRPFYDWLLdtlctLGL 298
Cdd:TIGR00463 237 KTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRY-----FGW 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 299 LAqPRPHQHEFARLNLTYVVTSKRKLKQLVDeGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATL 378
Cdd:TIGR00463 312 EP-PEFIHWGRLKIDDVRALSTSSARKGILR-GEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 379 DAALRDDLEGKAPRAMAVLDPLKLKLTNwaevfgsADHLEPCHAPAHPHLPELGSREFTLGPEVWIERDDFAEQPpkgff 458
Cdd:TIGR00463 390 YALNRKIIDEEARRYFFIWNPVKIEIVG-------LPEPKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV----- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 459 rlfpgNKVRLK--YGVVVEcsgcEKDADgrivavlatVVPDTKSGtpgaDAVKVKGTITWVGVHEAVPAElrlydrlfte 536
Cdd:TIGR00463 458 -----EPVRLMdaVNVIYS----KKELR---------YHSEGLEG----ARKLGKSIIHWLPAKDAVKVK---------- 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 124259282 537 aqpdaggrdfltVLNPDSRRvAAGYVEASVGRVMPESRLQFERHGYFVADSK 588
Cdd:TIGR00463 506 ------------VIMPDASI-VEGVIEADASELEVGDVVQFERFGFARLDSA 544
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
61-587 |
1.28e-92 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 297.26 E-value: 1.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQgrdpAHPEtpve 140
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD----VGPT---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 hlyYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDfntpGTDSPFRSRTPAENLARFRAMRDGQLADGAAVLRA 220
Cdd:PTZ00402 124 ---YSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 221 RIDMASPNINLRDPAIYRIKRATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTLctlGLla 300
Cdd:PTZ00402 197 KISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDAL---GI-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 301 qPRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATLDA 380
Cdd:PTZ00402 272 -RKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWY 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 381 ALRDDLEGKAPRAMAVLDPLKLKLTnwaeVFGSAdHLEPCHAPAHPHLPELGSREFTLGPEVWIERDDFAeqppkgffRL 460
Cdd:PTZ00402 351 FNTQILDPSVPRYTVVSNTLKVRCT----VEGQI-HLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVA--------LL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 461 FPGNKVRL-----KYGVVVECSGcekdADGRIVAvlATVVPDtksgtPGADAVKVKGTITWVGVH-EAVPAELRLYDRLF 534
Cdd:PTZ00402 418 KEGDEVTLmdwgnAYIKNIRRSG----EDALITD--ADIVLH-----LEGDVKKTKFKLTWVPESpKAEVMELNEYDHLL 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 124259282 535 TEAQPDAgGRDFLTVLNPDSRRVAAGYVEASVGRVMPESRLQFERHGYFVADS 587
Cdd:PTZ00402 487 TKKKPDP-EESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDD 538
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
61-588 |
5.52e-86 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 278.66 E-value: 5.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPE--KEEQEYVDAIVDAVKWLGFDWqgrdpahpetp 138
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKW----------- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 139 vEHLYYASDYFDFMYRAAEALVTAGFAYVDEQSAEQMRATRGDfntpGTDSPFRSRTPAENLARFRAMRDGQLADGAAVL 218
Cdd:PRK04156 170 -DEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 219 RARIDMASPNINLRDPAIYRIKRATHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFED----QRPFYD---Wlld 291
Cdd:PRK04156 245 RVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYDyfgW--- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 292 tlctlgllaqPRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYS 371
Cdd:PRK04156 322 ----------EYPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDA 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 372 WIDYATLDAALRDDLEGKAPRAMAVLDPLKLKLTNWAEVFGsadhlepcHAPAHPHLPELGSREFTLGPEVWIERDDFAE 451
Cdd:PRK04156 392 TISWENLYAINRKLIDPIANRYFFVRDPVELEIEGAEPLEA--------KIPLHPDRPERGEREIPVGGKVYVSSDDLEA 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 452 QppkgffrlfpGNKVRLKYGVVVECSGCEKDAdgrivavlATVVPDTksgtpgADAVKVKGT--ITWVGVHEAVPAELRl 529
Cdd:PRK04156 464 E----------GKMVRLMDLFNVEITGVSVDK--------ARYHSDD------LEEARKNKApiIQWVPEDESVPVRVL- 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 124259282 530 ydrlfteaQPDAGgrdfltvlnpdsrrVAAGYVEASVGRVMPESRLQFERHGYFVADSK 588
Cdd:PRK04156 519 --------KPDGG--------------DIEGLAEPDVADLEVDDIVQFERFGFVRIDSV 555
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
390-586 |
1.57e-60 |
|
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: 199.03 E-value: 1.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 390 APRAMAVLDPLKLKLTNWAEvfgsaDHLEPCHAPAHPHLPELGSREFTLGPEVWIERDDFaeqppkgfFRLFPGNKVRLK 469
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPE-----GQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 470 YGVVVECSGCEKDADGRIVAVLATVVPDTKSGtpgadAVKVKG-TITWVGVHEAVPAELRLYDRLFTEAQpdaggrDFLT 548
Cdd:pfam03950 68 DAYNIKVTEVVKDEDGNVTELHCTYDGDDLGG-----ARKVKGkIIHWVSASDAVPAEVRLYDRLFKDED------DADF 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 124259282 549 VLNPDSRRVAA-GYVEASVGRVMPESRLQFERHGYFVAD 586
Cdd:pfam03950 137 LLNPDSLKVLTeGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
61-406 |
3.04e-59 |
|
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: 197.69 E-value: 3.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWQgrdpahpetpvE 140
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWD-----------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 141 HLYYASDYFDFMYRAAEALVTAGfayvdeqsaeqmratrgdfntpgtdspfrsrtpaenlarframrdgqladgaavlra 220
Cdd:cd00418 70 GPYRQSDRFDLYRAYAEELIKKG--------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 221 ridmaspninlrdpaiyrikrathhntgdtwcIYPMYTYAHPIEDALEGITHSICTLEFEDQRPFYDWLLDTlctlglLA 300
Cdd:cd00418 93 --------------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEA------LG 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 301 QPRPHQHEFARLNLTY-VVTSKRKLKqlvdeghvdgwddprmPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWIDYATLD 379
Cdd:cd00418 135 WEPPRFYHFPRLLLEDgTKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEE 198
|
330 340
....*....|....*....|....*..
gi 124259282 380 AALRDDLEGKAPrAMAVLDPLKLKLTN 406
Cdd:cd00418 199 MIAAFSVERVNS-ADATFDWAKLEWLN 224
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
61-392 |
5.34e-41 |
|
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: 149.04 E-value: 5.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPE--KEEQEYVDAIVDAVKWLGFDWqgrdpahpetp 138
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKW----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 139 vEHLYYASDYFDFMYRAAEALVTAGFAYVdeqsaeqmratrgdfntpgtdspfrsrtpaenlarframrdgqladgaavl 218
Cdd:cd09287 70 -DEVVIASDRIELYYEYARKLIEMGGAYV--------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 219 raridmaspninlrdpaiyrikratHHNTGDTWCIYPMYTYAHPIEDALEGITHSICTLEFED----QRPFYDWLldtlc 294
Cdd:cd09287 98 -------------------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEYF----- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 295 tlgllAQPRPHQHEFARLNLTYVVTSKRKLKQLVDEGHVDGWDDPRMPTLVGLRRRGYTPDSIQLFCERIGVSKDYSWID 374
Cdd:cd09287 148 -----GWEYPETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATIS 222
|
330
....*....|....*...
gi 124259282 375 YATLDAALRDDLEGKAPR 392
Cdd:cd09287 223 WENLYAINRKLIDPRANR 240
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
61-163 |
2.44e-19 |
|
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: 87.64 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 61 KIRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDW-QGRDPAHPETPv 139
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWdEGPDVGGPYGP- 79
|
90 100
....*....|....*....|....*
gi 124259282 140 ehlYYASDYFDfMYR-AAEALVTAG 163
Cdd:cd00808 80 ---YRQSERLE-IYRkYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
30-274 |
6.21e-15 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 77.86 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 30 RDLEAGTYAGRRHAGSPGDAAHHAGAPLDAAK---IRTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPE 106
Cdd:PLN02627 11 RLLPELAPPFLRRSRSSRRRFSVRAAAAGESKggpVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 107 KEEQEYVDAIVDAVKWLGFDW-QGRDPAHPETPvehlYYASDYFDFMYRAAEALVTAGFAY----VDEQsAEQMRATRGD 181
Cdd:PLN02627 91 RSTKESEEAVLRDLKWLGLDWdEGPDVGGEYGP----YRQSERNAIYKQYAEKLLESGHVYpcfcTDEE-LEAMKEEAEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 182 FN-TPGTDSPFRSRTPAE---NLA-------RFRAMRDGqladgaavlRARID-----MASPNIN-LRDPAIYRikrath 244
Cdd:PLN02627 166 KKlPPRYTGKWATASDEEvqaELAkgtpytyRFRVPKEG---------SVKIDdlirgEVSWNTDtLGDFVLLR------ 230
|
250 260 270
....*....|....*....|....*....|
gi 124259282 245 hNTGdtwciYPMYTYAHPIEDALEGITHSI 274
Cdd:PLN02627 231 -SNG-----QPVYNFCVAVDDATMGITHVI 254
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
63-166 |
3.68e-13 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 70.26 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 63 RTRFPPEPNGYLHVGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIVDAVKWLGFDWqgrdpahpETPVehl 142
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHW--------DGPV--- 75
|
90 100
....*....|....*....|....*
gi 124259282 143 YYASDYFDfMYRAA-EALVTAGFAY 166
Cdd:PRK05710 76 LYQSQRHD-AYRAAlDRLRAQGLVY 99
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
64-162 |
4.45e-09 |
|
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: 55.18 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124259282 64 TRFPPEPNGYLHVGHAKSICLNFGLARD-----YGGVCHLRFDDTNPEKEEQ-------------EYVDAIVDAVKWLgF 125
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM-F 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 124259282 126 DWQGRDPAHPETPVEHLYYASDyFDFMYRAAEALVTA 162
Cdd:cd00802 81 LQAADFLLLYETECDIHLGGSD-QLGHIELGLELLKK 116
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
64-129 |
2.24e-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: 52.16 E-value: 2.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124259282 64 TRFPPEPnGYLHVGHAKSICLNFGLArdygGVCHLRFDDTNPEKEEQ------EYVDAIVDAVKWLGFDWQG 129
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQdpheleERKESIEEDISVCGEDFQQ 68
|
|
| |
