|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
44-533 |
0e+00 |
|
glutamyl-tRNA synthetase, bacterial 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 bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 700.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 44 PVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLI 123
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 124 YDKYVKILLSSGKAYRCFCSKERLNDLRHsaMELKPPSMASYDRCCAHLGEEEIKSKLAQGIPFTVRFKSPERY-PTFTD 202
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLRE--EQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAvVSFND 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 203 LLHGQINLQPQVNfndkryDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIP 282
Cdd:TIGR00464 159 QVRGEITFQNSEL------DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 283 LLTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDlaskkHECFSMEELETIFNLNGLTKGNAKVDDKK 362
Cdd:TIGR00464 233 MILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDD-----QEFFSLEELIEIFSLNRVSKSPAKFDWKK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 363 LWFFNKHFLQKriLNPSTLRELVDDIMPSLesiYNTSTISREKVAKILLNCGGSLSRINDFHDEFYYFFEKPKYNDNDAV 442
Cdd:TIGR00464 308 LQWLNAHYIKE--LPDEELFELLDPHLKSL---VNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 443 TKFLSKNESRHIAHLLKKLGQFQEGTdAQEVESMVETMYYENGFSRKVTYQAMRFALAGCHPGAKIAAMIDILGIKESNK 522
Cdd:TIGR00464 383 KKHLKKNVKEVLEALKKKLQALEEWT-ADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIK 461
|
490
....*....|.
gi 6324540 523 RLSEglQFLQR 533
Cdd:TIGR00464 462 RLKA--QFIAA 470
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
44-532 |
1.58e-169 |
|
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: 487.76 E-value: 1.58e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 44 PVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLI 123
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 124 YDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSMasYDRCCAHLGEEEIKSKLAQGIPFTVRFKSPERYPTFTDL 203
Cdd:COG0008 84 YYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPR--YDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 204 LHGQINlqpqvnFNDKRYDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIPL 283
Cdd:COG0008 162 VRGEIT------FPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 284 LTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDlaskkHECFSMEELETIFNLNGLTKGNAKVDDKKL 363
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDD-----QEIFSLEELIEAFDLDRVSRSPAVFDPVKL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 364 WFFNKHFLQKriLNPSTLRELVddiMPSLEsiyntSTISREKVAKILLNCGGSLSRINDFHDEFYYFFEKPkyNDNDAVT 443
Cdd:COG0008 311 VWLNGPYIRA--LDDEELAELL---APELP-----EAGIREDLERLVPLVRERAKTLSELAELARFFFIER--EDEKAAK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 444 KFLSKNESR----HIAHLLKKLGQFqegtDAQEVESMVETMYYENGFSRKVTYQAMRFALAGCHPGAKIAAMIDILGIKE 519
Cdd:COG0008 379 KRLAPEEVRkvlkAALEVLEAVETW----DPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKER 454
|
490
....*....|...
gi 6324540 520 SNKRLSEGLQFLQ 532
Cdd:COG0008 455 VFERLGYAIDKLA 467
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
44-365 |
6.33e-156 |
|
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: 447.15 E-value: 6.33e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 44 PVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLI 123
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 124 YDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSMASYDRCCAHLGEEEIKSKLAQGIPFTVRFKSPERYP-TFTD 202
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMESPyVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 203 LLHGQINLQPQVnfndkrYDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIP 282
Cdd:pfam00749 161 PVRGRIKFTPQE------IHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 283 LLTTVGDKKLSKRKGDMS--ISDLKRQGVLPEALINFCALFGWSPPrdlasKKHECFSMEELETIFNLNGLTKGNAKVDD 360
Cdd:pfam00749 235 LRLNLDGTKLSKRKLSWSvdISQVKGWGDPREATLNGLRRRGWTPE-----GIREFFTREGVIKSFDVNRLSKSLEAFDR 309
|
....*
gi 6324540 361 KKLWF 365
Cdd:pfam00749 310 KKLDW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
45-373 |
5.25e-125 |
|
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: 365.76 E-value: 5.25e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDE--------TPIK 116
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 117 QSERKLIYDKYVKILLSSGkayrcfcskerlndlrhsamelkppsmasydrccahlgeeeiksklaqgipftvrfksper 196
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 197 yptftdllhgqinlqpqvnfndkryddlilvksDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACP 276
Cdd:cd00808 101 ---------------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPP 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 277 KFIHIPLLTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDlaskkHECFSMEELETIFNLNGLTKGNA 356
Cdd:cd00808 148 KFAHLPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDG-----EEFFTLEELIELFDLERVSKSPA 222
|
330
....*....|....*..
gi 6324540 357 KVDDKKLWFFNKHFLQK 373
Cdd:cd00808 223 IFDPEKLDWLNGQYIRE 239
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
44-369 |
6.73e-88 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 280.86 E-value: 6.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 44 PVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETP--------I 115
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygpY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 116 KQSERKLIYDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELK-PPSmasYDRCCAHLGEEEIKSKLAQGIPFTVRFKSP 194
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKlPPR---YTGKWATASDEEVQAELAKGTPYTYRFRVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 195 -ERYPTFTDLLHGQinlqpqVNFNDKRYDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGW 273
Cdd:PLN02627 202 kEGSVKIDDLIRGE------VSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 274 ACPKFIHIPLLTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDlaskkHECFSMEELETIFNLNGLTK 353
Cdd:PLN02627 276 PMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTE-----NEIFTLEELVEKFSIDRINK 350
|
330
....*....|....*..
gi 6324540 354 GNAKVDDKKL-WFFNKH 369
Cdd:PLN02627 351 SGAVFDSTKLkWMNGQH 367
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
44-533 |
0e+00 |
|
glutamyl-tRNA synthetase, bacterial 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 bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 700.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 44 PVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLI 123
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 124 YDKYVKILLSSGKAYRCFCSKERLNDLRHsaMELKPPSMASYDRCCAHLGEEEIKSKLAQGIPFTVRFKSPERY-PTFTD 202
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLRE--EQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAvVSFND 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 203 LLHGQINLQPQVNfndkryDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIP 282
Cdd:TIGR00464 159 QVRGEITFQNSEL------DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 283 LLTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDlaskkHECFSMEELETIFNLNGLTKGNAKVDDKK 362
Cdd:TIGR00464 233 MILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDD-----QEFFSLEELIEIFSLNRVSKSPAKFDWKK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 363 LWFFNKHFLQKriLNPSTLRELVDDIMPSLesiYNTSTISREKVAKILLNCGGSLSRINDFHDEFYYFFEKPKYNDNDAV 442
Cdd:TIGR00464 308 LQWLNAHYIKE--LPDEELFELLDPHLKSL---VNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 443 TKFLSKNESRHIAHLLKKLGQFQEGTdAQEVESMVETMYYENGFSRKVTYQAMRFALAGCHPGAKIAAMIDILGIKESNK 522
Cdd:TIGR00464 383 KKHLKKNVKEVLEALKKKLQALEEWT-ADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIK 461
|
490
....*....|.
gi 6324540 523 RLSEglQFLQR 533
Cdd:TIGR00464 462 RLKA--QFIAA 470
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
44-532 |
1.58e-169 |
|
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: 487.76 E-value: 1.58e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 44 PVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLI 123
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 124 YDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSMasYDRCCAHLGEEEIKSKLAQGIPFTVRFKSPERYPTFTDL 203
Cdd:COG0008 84 YYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPR--YDGRCRDLSPEELERMLAAGEPPVLRFKIPEEGVVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 204 LHGQINlqpqvnFNDKRYDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIPL 283
Cdd:COG0008 162 VRGEIT------FPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 284 LTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDlaskkHECFSMEELETIFNLNGLTKGNAKVDDKKL 363
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDD-----QEIFSLEELIEAFDLDRVSRSPAVFDPVKL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 364 WFFNKHFLQKriLNPSTLRELVddiMPSLEsiyntSTISREKVAKILLNCGGSLSRINDFHDEFYYFFEKPkyNDNDAVT 443
Cdd:COG0008 311 VWLNGPYIRA--LDDEELAELL---APELP-----EAGIREDLERLVPLVRERAKTLSELAELARFFFIER--EDEKAAK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 444 KFLSKNESR----HIAHLLKKLGQFqegtDAQEVESMVETMYYENGFSRKVTYQAMRFALAGCHPGAKIAAMIDILGIKE 519
Cdd:COG0008 379 KRLAPEEVRkvlkAALEVLEAVETW----DPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKER 454
|
490
....*....|...
gi 6324540 520 SNKRLSEGLQFLQ 532
Cdd:COG0008 455 VFERLGYAIDKLA 467
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
44-365 |
6.33e-156 |
|
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: 447.15 E-value: 6.33e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 44 PVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLI 123
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 124 YDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSMASYDRCCAHLGEEEIKSKLAQGIPFTVRFKSPERYP-TFTD 202
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMESPyVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 203 LLHGQINLQPQVnfndkrYDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIP 282
Cdd:pfam00749 161 PVRGRIKFTPQE------IHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 283 LLTTVGDKKLSKRKGDMS--ISDLKRQGVLPEALINFCALFGWSPPrdlasKKHECFSMEELETIFNLNGLTKGNAKVDD 360
Cdd:pfam00749 235 LRLNLDGTKLSKRKLSWSvdISQVKGWGDPREATLNGLRRRGWTPE-----GIREFFTREGVIKSFDVNRLSKSLEAFDR 309
|
....*
gi 6324540 361 KKLWF 365
Cdd:pfam00749 310 KKLDW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
45-373 |
5.25e-125 |
|
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: 365.76 E-value: 5.25e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDE--------TPIK 116
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 117 QSERKLIYDKYVKILLSSGkayrcfcskerlndlrhsamelkppsmasydrccahlgeeeiksklaqgipftvrfksper 196
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 197 yptftdllhgqinlqpqvnfndkryddlilvksDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACP 276
Cdd:cd00808 101 ---------------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPP 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 277 KFIHIPLLTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDlaskkHECFSMEELETIFNLNGLTKGNA 356
Cdd:cd00808 148 KFAHLPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDG-----EEFFTLEELIELFDLERVSKSPA 222
|
330
....*....|....*..
gi 6324540 357 KVDDKKLWFFNKHFLQK 373
Cdd:cd00808 223 IFDPEKLDWLNGQYIRE 239
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
44-369 |
6.73e-88 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 280.86 E-value: 6.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 44 PVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETP--------I 115
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygpY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 116 KQSERKLIYDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELK-PPSmasYDRCCAHLGEEEIKSKLAQGIPFTVRFKSP 194
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKlPPR---YTGKWATASDEEVQAELAKGTPYTYRFRVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 195 -ERYPTFTDLLHGQinlqpqVNFNDKRYDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGW 273
Cdd:PLN02627 202 kEGSVKIDDLIRGE------VSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 274 ACPKFIHIPLLTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDlaskkHECFSMEELETIFNLNGLTK 353
Cdd:PLN02627 276 PMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTE-----NEIFTLEELVEKFSIDRINK 350
|
330
....*....|....*..
gi 6324540 354 GNAKVDDKKL-WFFNKH 369
Cdd:PLN02627 351 SGAVFDSTKLkWMNGQH 367
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
41-331 |
7.26e-79 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 249.38 E-value: 7.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 41 PSLPVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSER 120
Cdd:PRK05710 2 TMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 121 KLIYDKYVKILLSSGKAYRCFCSKERLNDLRHSamelkPPSMA-SYDRCCAHLGeeeikskLAQGIPFTVRFKSPERYPT 199
Cdd:PRK05710 82 HDAYRAALDRLRAQGLVYPCFCSRKEIAAAAPA-----PPDGGgIYPGTCRDLL-------HGPRNPPAWRLRVPDAVIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 200 FTDLLHGQI--NLQPQVnfndkryDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPK 277
Cdd:PRK05710 150 FDDRLQGRQhqDLALAV-------GDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPR 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6324540 278 FIHIPLLTTVGDKKLSKRKGDMSISDLKRQGVLPEALinfcALFGWSPPRDLAS 331
Cdd:PRK05710 223 YLHLPLVLNADGQKLSKQNGAPALDAAGPLPVLAAAL----RFLGQPPPAADAS 272
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
45-330 |
3.89e-74 |
|
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274810 Cd Length: 271 Bit Score: 236.28 E-value: 3.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLIY 124
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 125 DKYVKILLSSGKAYRCFCSKERLNDLRHSAmelkppsmASYDRCCAHLgeeeikSKLAQGIPFTVRFKSPERYPTFTDLL 204
Cdd:TIGR03838 81 QAALDRLLAAGLAYPCQCTRKEIAAARDGG--------GIYPGTCRNG------LPGRPGRPAAWRLRVPDGVIAFDDRL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 205 HG--QINLQPQVnfndkryDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIP 282
Cdd:TIGR03838 147 QGpqQQDLAAAV-------GDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLP 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6324540 283 LLTTVGDKKLSKRKGDMSISDLKRQGVLPEALinfcALFGWSPPRDLA 330
Cdd:TIGR03838 220 LVVNADGEKLSKQNGAPALDDSRPLPALLAAL----RFLGLPPPPELA 263
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
45-373 |
8.21e-73 |
|
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: 231.21 E-value: 8.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLIY 124
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 125 DKYVkillssgkayrcfcskERLndlrhsamelkppsmasydrccahlgeeeikskLAQGIpftvrfksperyptftdll 204
Cdd:cd00418 82 RAYA----------------EEL---------------------------------IKKGG------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 205 hgqinlqpqvnfndkryddlilvksdkLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIPLL 284
Cdd:cd00418 94 ---------------------------YPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRL 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 285 TTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDlaskkHECFSMEELETIFNLNGLTKGNAKVDDKKLW 364
Cdd:cd00418 147 LLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDG-----HELFTLEEMIAAFSVERVNSADATFDWAKLE 221
|
....*....
gi 6324540 365 FFNKHFLQK 373
Cdd:cd00418 222 WLNREYIRE 230
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
36-317 |
1.45e-42 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 160.02 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 36 KEDIH--PSLP------VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTD--QKRLIEGAEENIYEILKW 105
Cdd:PRK04156 85 KEEKKglPPLPnaekgkVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKW 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 106 CNINYDETpIKQSERKLIYDKYVKILLSSGKAYRCFCSKERLNDLRHSAMEL----KPP--SMASYDRccahLGEEEIKS 179
Cdd:PRK04156 165 LGVKWDEV-VIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCphrdKSPeeNLELWEK----MLDGEYKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 180 KLAqgipfTVRFKsperyptfTDLLHGQINLQPQVNFndkRYDD----LILVKSDKLPTYHLANVVDDHLMGITHVIRGE 255
Cdd:PRK04156 240 GEA-----VVRVK--------TDLEHPNPSVRDWVAF---RIVKtphpRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGK 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324540 256 EWLPSTPKHIALYNAFGWACPKFIHI-------PLLTTVGDKKLSKRKGDMSISD--------LKRQGVLPEALINF 317
Cdd:PRK04156 304 DHIDNTEKQRYIYDYFGWEYPETIHYgrlkiegFVLSTSKIRKGIEEGEYSGWDDprlptlraLRRRGILPEAIREL 380
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
45-373 |
5.18e-38 |
|
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: 146.89 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIkQSERKLIY 124
Cdd:TIGR00463 94 VVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVY-QSDRIETY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 125 DKYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSMASYDRCcaHLGEEEIKSKLAQGiPFTVRFKSPERY--PTFTD 202
Cdd:TIGR00463 173 YDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENL--ERWEEMLEGKEEGG-SVVVRVKTDLKHknPAIRD 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 203 LLHGQINLQPQVNFNDKR--YddlilvksdklPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIH 280
Cdd:TIGR00463 250 WVIFRIVKTPHPRTGDKYrvY-----------PTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIH 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 281 IPLLTTVGDKKLSkrkgdmsiSDLKRQGVLPEALInfcalfGWSPPR--DLASKKHECFSMEELETIFNLNGLTKGNAKV 358
Cdd:TIGR00463 319 WGRLKIDDVRALS--------TSSARKGILRGEYS------GWDDPRlpTLRAIRRRGIRPEAIRKFMLSIGVKINDVTM 384
|
330
....*....|....*
gi 6324540 359 DDKKLWFFNKHFLQK 373
Cdd:TIGR00463 385 SWKNIYALNRKIIDE 399
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
44-317 |
1.86e-31 |
|
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: 121.69 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 44 PVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTD--QKRLIEGAEENIYEILKWCNINYDETPIkQSERK 121
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDprTKRPDPEAYDMIPEDLEWLGVKWDEVVI-ASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 122 LIYDKYVKILLSSGKAYrcfcskerlndlrhsamelKPPSMASYDRCcahlgeeeiksklaqgipftvrfksperyptft 201
Cdd:cd09287 80 ELYYEYARKLIEMGGAY-------------------VHPRTGSKYRV--------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 202 dllhgqinlqpqvnfndkryddlilvksdkLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHI 281
Cdd:cd09287 108 ------------------------------WPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHW 157
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 6324540 282 PLLtTVGDKKLSK---RKGDMS-------------ISDLKRQGVLPEALINF 317
Cdd:cd09287 158 GRL-KIEGGKLSTskiRKGIESgeyegwddprlptLRALRRRGIRPEAIRDF 208
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
45-385 |
3.73e-15 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 78.47 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSER-KLI 123
Cdd:PTZ00402 53 VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYmDLM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 124 YDKyVKILLSSGKAYRCFCSKERLNDLRHSAMELK--PPSMASYDRCCahlgeEEIKSKLAQGIPFTVRFKSPERYP--T 199
Cdd:PTZ00402 133 YEK-AEELIKKGLAYCDKTPREEMQKCRFDGVPTKyrDISVEETKRLW-----NEMKKGSAEGQETCLRAKISVDNEnkA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 200 FTDLLHGQINLQPQVNFNdkryddlilVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACP--- 276
Cdd:PTZ00402 207 MRDPVIYRVNLTPHARQG---------TKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPive 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 277 KFIHIPLLTTVgdkkLSKRKgdmsISDLKRQGVLPealinfcalfGWSPPR--DLASKKHECFSMEELETIFNLNGLTKG 354
Cdd:PTZ00402 278 DFSRLNMEYSV----MSKRK----LTQLVDTHVVD----------GWDDPRfpTVRALVRRGLKMEALRQFVQEQGMSKT 339
|
330 340 350
....*....|....*....|....*....|.
gi 6324540 355 NAKVDDKKLWFFNkhflqKRILNPSTLRELV 385
Cdd:PTZ00402 340 VNFMEWSKLWYFN-----TQILDPSVPRYTV 365
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
45-382 |
2.89e-13 |
|
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: 69.59 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLIY 124
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 125 DKYVKiLLSSGKAYrcfcskerlndlrhsamelkppsmasydrccAHlgeeeiksklaqgipftvrfksperyptftdll 204
Cdd:cd00807 82 EYAEQ-LIKKGKAY-------------------------------VH--------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 205 hgqinlqPQVNFNDKRYddlilvksdklPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPK---FIHI 281
Cdd:cd00807 97 -------HRTGDKWCIY-----------PTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHqweFSRL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 282 PLLTTVgdkkLSKRK-------GDMS---------ISDLKRQGVLPEALINFCALFgwspprdlaskkhecfsmeeleti 345
Cdd:cd00807 159 NLTYTV----MSKRKllqlvdeGYVDgwddprlptLRGLRRRGVTPEAIRQFILRQ------------------------ 210
|
330 340 350
....*....|....*....|....*....|....*..
gi 6324540 346 fnlnGLTKGNAKVDDKKLWFFNkhflqKRILNPSTLR 382
Cdd:cd00807 211 ----GVSKADSTIDWDKLEACV-----RKDLNPTAPR 238
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
45-296 |
3.75e-12 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 68.50 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLIY 124
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPIR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 125 DkYVKILLSSGKAYRCFCSKERLN----DLRHSAMELKPPSMA--SYDRCCAhlGEEEiksklaqGIPFTVRFK--SPER 196
Cdd:PLN03233 92 C-YAIILIEEGLAYMDDTPQEEMKkeraDRAESKHRNQSPEEAleMFKEMCS--GKEE-------GGAWCLRAKidMQSD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 197 YPTFTDLLHGQINLQP--QVNFNDKRYddlilvksdklPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWA 274
Cdd:PLN03233 162 NGTLRDPVLFRQNTTPhhRSGTAYKAY-----------PTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR 230
|
250 260
....*....|....*....|....*
gi 6324540 275 CPK---FIHIPLLTTVgdkkLSKRK 296
Cdd:PLN03233 231 RPRihaFARMNFMNTV----LSKRK 251
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
45-322 |
1.43e-10 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 63.97 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKrlIEGAE--ENIYEILKWCNINYDETPIKQS---E 119
Cdd:PRK14703 32 VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPE--TEDTEyvEAIKDDVRWLGFDWGEHLYYASdyfE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 120 RklIYDkYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSmaSY-DRccahlgeeeiksKLAQGIPFTVRFKSPErYP 198
Cdd:PRK14703 110 R--MYA-YAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPS--PYrDR------------SVEENLDLFRRMRAGE-FP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 199 TFTDLLHGQINL-QPQVNFNDKryddlILVK---------SDK---LPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHI 265
Cdd:PRK14703 172 DGAHVLRAKIDMsSPNMKLRDP-----LLYRirhahhyrtGDEwciYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYD 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324540 266 ALYNAFGWACPK-----FIHIPLLTTVgdkkLSKRK------GDM----------SISDLKRQGVLPEALINFCALFG 322
Cdd:PRK14703 247 WVLDHLGPWPPRprqyeFARLALGYTV----MSKRKlrelveEGYvsgwddprmpTIAGQRRRGVTPEAIRDFADQIG 320
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
45-257 |
3.77e-08 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 56.27 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRliEGAE--ENIYEILKWCNINYDetpikqserKL 122
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSK--ESDEfvENILKDIETLGIKYD---------AV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 123 IY--DKYVKI------LLSSGKAYRCFCSKERLNDLRHSAMELKppsmasydrCCAHLGEE------EIKSKLAQGIPFT 188
Cdd:PLN02907 283 TYtsDYFPQLmemaekLIKEGKAYVDDTPREQMRKERMDGIESK---------CRNNSVEEnlrlwkEMIAGSERGLQCC 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324540 189 VRFK----SPERypTFTDLLHGQINLQP--QVNFNDKRYddlilvksdklPTYHLANVVDDHLMGITHVIRGEEW 257
Cdd:PLN02907 354 VRGKldmqDPNK--SLRDPVYYRCNPTPhhRIGSKYKVY-----------PTYDFACPFVDALEGVTHALRSSEY 415
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
45-318 |
6.34e-08 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 55.54 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 45 VRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWC-----NINYDETPIKQse 119
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMgwepfKITYTSDYFQE-- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 120 rklIYDKYVKiLLSSGKAYRCFCSKERLNDLRHSAMElKP----PSMASYDrccahLGEEEIKSKLAQGiPFTVRFKSPE 195
Cdd:PLN02859 343 ---LYELAVE-LIRRGHAYVDHQTPEEIKEYREKKMN-SPwrdrPIEESLK-----LFEDMRRGLIEEG-KATLRMKQDM 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 196 RYPTFT--DLLHGQINLQPQVNFNDKR--YddlilvksdklPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAF 271
Cdd:PLN02859 412 QNDNFNmyDLIAYRIKFTPHPHAGDKWciY-----------PSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL 480
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324540 272 GWACP---KFIHIPLLTTVgdkkLSKRKGD----------------MSISDLKRQGVLPEALINFC 318
Cdd:PLN02859 481 GLYQPyvwEYSRLNVTNTV----MSKRKLNrlvtekyvdgwddprlLTLAGLRRRGVTPTAINAFC 542
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
383-528 |
1.23e-07 |
|
Anticodon binding domain; This entry represents the anticodon binding domain found at the C-terminus of the class-I glutamyl tRNA synthetase enzyme.
Pssm-ID: 466020 [Multi-domain] Cd Length: 148 Bit Score: 51.04 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 383 ELVDDIMPSLESiYNTSTISREKVAKILLNCGGSLSRINDFHDEFYYFFEKPKYNDNDAVTKFLSKNESRHIAHLLKKL- 461
Cdd:pfam19269 1 ELAELALPYLEE-AGLDGLDDEYLKKVVPLLKERAETLSELAELADFFFELPLEYDEEAYAKKKMKTNKEESLEVLQELl 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324540 462 GQFQEGTD--AQEVESMVETMYYENGFSRKVTYQAMRFALAGCHPGAKIAAMIDILGIKESNKRLSEGL 528
Cdd:pfam19269 80 PRLEALEDwtAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
48-322 |
1.60e-06 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 50.75 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 48 RFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKrliegAEENIY-----EILKWCNINYDETPIKQSERKL 122
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPE-----TEEQVYidaimEMVKWMGWKPDWVTFSSDYFDQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 123 IYDKYVKiLLSSGKAYRCFCSKERLNDLRHSaMELKPPSMASYDRCCAHLgEEEIKSKLAQGiPFTVRFKSPERY--PTF 200
Cdd:PTZ00437 130 LHEFAVQ-LIKDGKAYVDHSTPDELKQQREQ-REDSPWRNRSVEENLLLF-EHMRQGRYAEG-EATLRVKADMKSdnPNM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 201 TDLLHGQINLQPQVNFNDKR--YddlilvksdklPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKF 278
Cdd:PTZ00437 206 RDFIAYRVKYVEHPHAKDKWciY-----------PSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHV 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324540 279 IHIPLLTTVGdKKLSKRKGD----------------MSISDLKRQGVLPEALINFCALFG 322
Cdd:PTZ00437 275 WEFSRLNVTG-SLLSKRKINvlvrkgivrgfddprlLTLAGMRRRGYTPAAINRFCELVG 333
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
35-86 |
7.09e-05 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 45.48 E-value: 7.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324540 35 IKEDI----HPSlpVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDT 86
Cdd:PRK05347 18 IDEDLasgkHTR--VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDT 71
|
|
| |
