|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
36-521 |
1.35e-162 |
|
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: 469.66 E-value: 1.35e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 36 TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDEsprqggpaGPY 115
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE--------GPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 116 YQSQRLALYAQATEALLKSGAAYPCFCSPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLATDPKPAIRFRLEEAV 195
Cdd:COG0008 76 YQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 196 PAFQDLVYGWTQHEVASVeGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLP 275
Cdd:COG0008 156 VVFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 276 LLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFN 355
Cdd:COG0008 235 LILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 356 RLHLRRLVSSEtqrphlveklqglVKEAFGSELQDRDVLDpaYMERILLLRQGHISRLQDLVsPVYSYLWTRP--AVHRA 433
Cdd:COG0008 315 GPYIRALDDEE-------------LAELLAPELPEAGIRE--DLERLVPLVRERAKTLSELA-ELARFFFIERedEKAAK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 434 ELGASSEKLDVIaKHLLGLLERPGlSLTQDVVNRELKKLSEGLeGTKHSSVMKLLRMALSGQLQGPPVAEMMVSLGPEEV 513
Cdd:COG0008 379 KRLAPEEVRKVL-KAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERV 455
|
....*...
gi 226958334 514 RERIQKVL 521
Cdd:COG0008 456 FERLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
36-519 |
2.92e-155 |
|
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: 451.04 E-value: 2.92e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 36 TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDEsprqggpaGPY 115
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 116 YQSQRLALYAQATEALLKSGAAYPCFCSPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLATDPKPAIRFRL-EEA 194
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 195 VPAFQDLVYGwtQHEVASVE-GDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAH 273
Cdd:TIGR00464 153 VVSFNDQVRG--EITFQNSElDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 274 LPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPE 353
Cdd:TIGR00464 231 LPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 354 FNRLHLRRLvSSETQRPHLVEKLQGLVkeafgselqDRDVLDPAYMERILLLRQGHISRLQDLVSPVYSYL-----WTRP 428
Cdd:TIGR00464 311 LNAHYIKEL-PDEELFELLDPHLKSLV---------NTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFedkkeVDED 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 429 AVHRAELGASSEKLDVIAKHLLGLLERpglslTQDVVNRELKKLSEgLEGTKHSSVMKLLRMALSGQLQGPPVAEMMVSL 508
Cdd:TIGR00464 381 AFKKHLKKNVKEVLEALKKKLQALEEW-----TADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKGHGPDLAQILELI 454
|
490
....*....|.
gi 226958334 509 GPEEVRERIQK 519
Cdd:TIGR00464 455 GKTESIKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
36-361 |
1.72e-129 |
|
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: 376.54 E-value: 1.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 36 TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDESPRQGGPAGPY 115
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 116 YQSQRLALYAQATEALLKSGaaypcfcspqrlellkkealrsrqtprydnrcrnlsqaqvaqklatdpkpairfrleeav 195
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 196 pafqdlvygwtqhevasvegdpvilksDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLP 275
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 276 LLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFN 355
Cdd:cd00808 154 LILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233
|
....*.
gi 226958334 356 RLHLRR 361
Cdd:cd00808 234 GQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
37-351 |
1.58e-105 |
|
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: 318.11 E-value: 1.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDEsprqggpaGPYY 116
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 117 QSQRLALYAQATEALLKSGAAYPCFCSPQRLELLKK--EALRSRQTPRYDNRCRNLSQAQVAQKLATDPKPAIRFRL-EE 193
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREeqEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIpME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 194 AVPAFQDLVYGwtQHEVASVEGDP-VILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFA 272
Cdd:pfam00749 154 SPYVFRDPVRG--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 273 HLPLLLNRDGSKLSKRQGDI--FLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEK 350
Cdd:pfam00749 232 HEYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKK 311
|
.
gi 226958334 351 L 351
Cdd:pfam00749 312 L 312
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
8-509 |
2.18e-99 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 310.13 E-value: 2.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 8 LLLAGPHVGALGHRVGRREASL-----GPDPGVTVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSR 82
Cdd:PLN02627 12 LLPELAPPFLRRSRSSRRRFSVraaaaGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 83 LVPGAAENIEDMLEWAGIPPDESPRQGGPAGPYYQSQRLALYAQATEALLKSGAAYPCFCSPQRLELLKKEALRSRQTPR 162
Cdd:PLN02627 92 STKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 163 YDNRCRNLSQAQVAQKLATDPKPAIRFRL-EEAVPAFQDLVYGwtqhEV---ASVEGDPVILKSDGFPTYHLACVVDDHH 238
Cdd:PLN02627 172 YTGKWATASDEEVQAELAKGTPYTYRFRVpKEGSVKIDDLIRG----EVswnTDTLGDFVLLRSNGQPVYNFCVAVDDAT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 239 MSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGF 318
Cdd:PLN02627 248 MGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWND 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 319 AENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFNRLHLRRLvSSETQRPHLVEKL--QGLVKEAFGSELQdrdvldp 396
Cdd:PLN02627 328 GTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQHLRLL-PEEELVKLVGERWksAGILKESDGSFVK------- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 397 aymERILLLRQGhISRLQDLVSPVYSYLwtrpAVHRAELGASSEKLDVIAKHLLGLLE------RPGlSLTQDV------ 464
Cdd:PLN02627 400 ---EAVELLKDG-IELVTDADKELLNLL----SYPLAATLSSPEAKTVVEDNFSEVADaliaayDSG-ELAAALeeghdg 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 226958334 465 ----VNRELKKLsegleGTKHSSVMKLLRMALSGQLQGPPVAEMMVSLG 509
Cdd:PLN02627 471 wqkwVKAFGKAL-----KRKGKRLFMPLRVALTGKMHGPDVGESLVLLH 514
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
36-521 |
1.35e-162 |
|
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: 469.66 E-value: 1.35e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 36 TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDEsprqggpaGPY 115
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE--------GPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 116 YQSQRLALYAQATEALLKSGAAYPCFCSPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLATDPKPAIRFRLEEAV 195
Cdd:COG0008 76 YQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 196 PAFQDLVYGWTQHEVASVeGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLP 275
Cdd:COG0008 156 VVFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 276 LLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFN 355
Cdd:COG0008 235 LILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 356 RLHLRRLVSSEtqrphlveklqglVKEAFGSELQDRDVLDpaYMERILLLRQGHISRLQDLVsPVYSYLWTRP--AVHRA 433
Cdd:COG0008 315 GPYIRALDDEE-------------LAELLAPELPEAGIRE--DLERLVPLVRERAKTLSELA-ELARFFFIERedEKAAK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 434 ELGASSEKLDVIaKHLLGLLERPGlSLTQDVVNRELKKLSEGLeGTKHSSVMKLLRMALSGQLQGPPVAEMMVSLGPEEV 513
Cdd:COG0008 379 KRLAPEEVRKVL-KAALEVLEAVE-TWDPETVKGTIHWVSAEA-GVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERV 455
|
....*...
gi 226958334 514 RERIQKVL 521
Cdd:COG0008 456 FERLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
36-519 |
2.92e-155 |
|
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: 451.04 E-value: 2.92e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 36 TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDEsprqggpaGPY 115
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 116 YQSQRLALYAQATEALLKSGAAYPCFCSPQRLELLKKEALRSRQTPRYDNRCRNLSQAQVAQKLATDPKPAIRFRL-EEA 194
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIpQEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 195 VPAFQDLVYGwtQHEVASVE-GDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAH 273
Cdd:TIGR00464 153 VVSFNDQVRG--EITFQNSElDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 274 LPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPE 353
Cdd:TIGR00464 231 LPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 354 FNRLHLRRLvSSETQRPHLVEKLQGLVkeafgselqDRDVLDPAYMERILLLRQGHISRLQDLVSPVYSYL-----WTRP 428
Cdd:TIGR00464 311 LNAHYIKEL-PDEELFELLDPHLKSLV---------NTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFedkkeVDED 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 429 AVHRAELGASSEKLDVIAKHLLGLLERpglslTQDVVNRELKKLSEgLEGTKHSSVMKLLRMALSGQLQGPPVAEMMVSL 508
Cdd:TIGR00464 381 AFKKHLKKNVKEVLEALKKKLQALEEW-----TADEVKSAIKQIAE-ELGLKGKKVFMPLRLALTGKGHGPDLAQILELI 454
|
490
....*....|.
gi 226958334 509 GPEEVRERIQK 519
Cdd:TIGR00464 455 GKTESIKRLKA 465
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
36-361 |
1.72e-129 |
|
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: 376.54 E-value: 1.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 36 TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDESPRQGGPAGPY 115
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 116 YQSQRLALYAQATEALLKSGaaypcfcspqrlellkkealrsrqtprydnrcrnlsqaqvaqklatdpkpairfrleeav 195
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 196 pafqdlvygwtqhevasvegdpvilksDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLP 275
Cdd:cd00808 101 ---------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 276 LLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFN 355
Cdd:cd00808 154 LILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233
|
....*.
gi 226958334 356 RLHLRR 361
Cdd:cd00808 234 GQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
37-351 |
1.58e-105 |
|
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: 318.11 E-value: 1.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDEsprqggpaGPYY 116
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 117 QSQRLALYAQATEALLKSGAAYPCFCSPQRLELLKK--EALRSRQTPRYDNRCRNLSQAQVAQKLATDPKPAIRFRL-EE 193
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREeqEALGSPSRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIpME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 194 AVPAFQDLVYGwtQHEVASVEGDP-VILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFA 272
Cdd:pfam00749 154 SPYVFRDPVRG--RIKFTPQEIHDrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 273 HLPLLLNRDGSKLSKRQGDI--FLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEK 350
Cdd:pfam00749 232 HEYLRLNLDGTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKK 311
|
.
gi 226958334 351 L 351
Cdd:pfam00749 312 L 312
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
8-509 |
2.18e-99 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 310.13 E-value: 2.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 8 LLLAGPHVGALGHRVGRREASL-----GPDPGVTVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSR 82
Cdd:PLN02627 12 LLPELAPPFLRRSRSSRRRFSVraaaaGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 83 LVPGAAENIEDMLEWAGIPPDESPRQGGPAGPYYQSQRLALYAQATEALLKSGAAYPCFCSPQRLELLKKEALRSRQTPR 162
Cdd:PLN02627 92 STKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 163 YDNRCRNLSQAQVAQKLATDPKPAIRFRL-EEAVPAFQDLVYGwtqhEV---ASVEGDPVILKSDGFPTYHLACVVDDHH 238
Cdd:PLN02627 172 YTGKWATASDEEVQAELAKGTPYTYRFRVpKEGSVKIDDLIRG----EVswnTDTLGDFVLLRSNGQPVYNFCVAVDDAT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 239 MSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLPLLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGF 318
Cdd:PLN02627 248 MGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWND 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 319 AENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFNRLHLRRLvSSETQRPHLVEKL--QGLVKEAFGSELQdrdvldp 396
Cdd:PLN02627 328 GTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQHLRLL-PEEELVKLVGERWksAGILKESDGSFVK------- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 397 aymERILLLRQGhISRLQDLVSPVYSYLwtrpAVHRAELGASSEKLDVIAKHLLGLLE------RPGlSLTQDV------ 464
Cdd:PLN02627 400 ---EAVELLKDG-IELVTDADKELLNLL----SYPLAATLSSPEAKTVVEDNFSEVADaliaayDSG-ELAAALeeghdg 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 226958334 465 ----VNRELKKLsegleGTKHSSVMKLLRMALSGQLQGPPVAEMMVSLG 509
Cdd:PLN02627 471 wqkwVKAFGKAL-----KRKGKRLFMPLRVALTGKMHGPDVGESLVLLH 514
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
40-339 |
3.57e-86 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 267.87 E-value: 3.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 40 RFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDESPRqggpagpyYQSQ 119
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVL--------YQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 120 RLALYAQATEALLKSGAAYPCFCSpqRLELLKKEALRSRQTPRYDNRCRNLSQAQvaqklatDPKPAIRFRLEEAVPAFQ 199
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCS--RKEIAAAAPAPPDGGGIYPGTCRDLLHGP-------RNPPAWRLRVPDAVIAFD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 200 DLVYGWTQHEVASVEGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLPLLLN 279
Cdd:PRK05710 152 DRLQGRQHQDLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLN 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226958334 280 RDGSKLSKRQGDIFLehfAATGFLPeALLDIITNCG-SGFAENQMGRTL-PELITQFDLTRI 339
Cdd:PRK05710 232 ADGQKLSKQNGAPAL---DAAGPLP-VLAAALRFLGqPPPAADASVEELlAQAVAHWDLTRL 289
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
37-290 |
1.80e-83 |
|
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: 259.78 E-value: 1.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDESPRqggpagpyY 116
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVV--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 117 QSQRLALYAQATEALLKSGAAYPCFCSpqRLELlkkeALRSRQTPRYDNRCRNLSQAQVAQKlatdpkPAIRFRLEEAVP 196
Cdd:TIGR03838 73 QSQRHALYQAALDRLLAAGLAYPCQCT--RKEI----AAARDGGGIYPGTCRNGLPGRPGRP------AAWRLRVPDGVI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 197 AFQDLVYGWTQHEVASVEGDPVILKSDGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLPL 276
Cdd:TIGR03838 141 AFDDRLQGPQQQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPL 220
|
250
....*....|....
gi 226958334 277 LLNRDGSKLSKRQG 290
Cdd:TIGR03838 221 VVNADGEKLSKQNG 234
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
36-360 |
8.55e-66 |
|
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: 212.72 E-value: 8.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 36 TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDEsprqggpaGPY 115
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 116 YQSQRLALYAQATEALLKSGaaypcfcspqrlellkkealrsrqtprydnrcrnlsqaqvaqklatdpkpairfrleeav 195
Cdd:cd00418 73 RQSDRFDLYRAYAEELIKKG------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 196 pafqdlvygwtqhevasvegdpvilksdGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLP 275
Cdd:cd00418 93 ----------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFP 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 276 LLLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAENQMGRTLPELITQFDLTRITCHSALLDLEKLPEFN 355
Cdd:cd00418 145 RLLLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWLN 224
|
....*
gi 226958334 356 RLHLR 360
Cdd:cd00418 225 REYIR 229
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
25-315 |
1.16e-45 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 168.49 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 25 REASLGPDPGV---TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTD--QSRLVPGAAENIEDMLEWAG 99
Cdd:PRK04156 87 EKKGLPPLPNAekgKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 100 IPPDESprqggpagpYYQSQRLALYAQATEALLKSGAAYPCFCSPQRLELLK--KEALRSRQTPRYDNRCR-------NL 170
Cdd:PRK04156 167 VKWDEV---------VIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRdaGKPCPHRDKSPEENLELwekmldgEY 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 171 SQAQVAQKLATD---PKPAIR----FRLEEavpafqdlvygwTQHevaSVEGDPVILksdgFPTYHLACVVDDHHMSISH 243
Cdd:PRK04156 238 KEGEAVVRVKTDlehPNPSVRdwvaFRIVK------------TPH---PRVGDKYRV----WPTYNFAVAVDDHLLGVTH 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 244 VLRGSEWLVSTSKHLLLYQALGWQPPQFAH---LPLllnrDGSKLSK---RQG----------DIFLEHFAAT---GFLP 304
Cdd:PRK04156 299 VLRGKDHIDNTEKQRYIYDYFGWEYPETIHygrLKI----EGFVLSTskiRKGieegeysgwdDPRLPTLRALrrrGILP 374
|
330
....*....|.
gi 226958334 305 EALLDIITNCG 315
Cdd:PRK04156 375 EAIRELIIEVG 385
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
37-323 |
1.34e-37 |
|
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: 145.74 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDESprqggpagpYY 116
Cdd:TIGR00463 94 VVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEV---------VY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 117 QSQRLALYAQATEALLKSGAAYPCFCSPqrlELLKKEALRSRQTPRYDNRCRN------------LSQAQVAQKLATD-- 182
Cdd:TIGR00463 165 QSDRIETYYDYTRKLIEMGKAYVCDCRP---EEFRELRNRGEACHCRDRSVEEnlerweemlegkEEGGSVVVRVKTDlk 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 183 -PKPAIR----FRLEEavpafqdlvygwTQHEVAsveGDPVILksdgFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKH 257
Cdd:TIGR00463 242 hKNPAIRdwviFRIVK------------TPHPRT---GDKYRV----YPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 258 LLLYQALGWQPPQFAHLPLLLNRDGSKLS---KRQGDI-------------FLEHFAATGFLPEALLDIITNCGSGFAEN 321
Cdd:TIGR00463 303 EYIYRYFGWEPPEFIHWGRLKIDDVRALStssARKGILrgeysgwddprlpTLRAIRRRGIRPEAIRKFMLSIGVKINDV 382
|
..
gi 226958334 322 QM 323
Cdd:TIGR00463 383 TM 384
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
37-315 |
8.02e-35 |
|
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: 130.93 E-value: 8.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTD--QSRLVPGAAENIEDMLEWAGIPPDESprqggpagp 114
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDprTKRPDPEAYDMIPEDLEWLGVKWDEV--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 115 YYQSQRLALYAQATEALLKSGAAYpcfcspqrlellkkealrsrQTPRYDNRCRnlsqaqvaqklatdpkpairfrleea 194
Cdd:cd09287 73 VIASDRIELYYEYARKLIEMGGAY--------------------VHPRTGSKYR-------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 195 vpafqdlVYgwtqhevasvegdpvilksdgfPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHL 274
Cdd:cd09287 107 -------VW----------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHW 157
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 226958334 275 PlLLNRDGSKLSK---RQG----------DIFLEHFAA---TGFLPEALLDIITNCG 315
Cdd:cd09287 158 G-RLKIEGGKLSTskiRKGiesgeyegwdDPRLPTLRAlrrRGIRPEAIRDFIIEVG 213
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
37-250 |
1.81e-15 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 79.38 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDESPrqggpagpyY 116
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVT---------Y 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 117 QSQRLALYAQATEALLKSGAAYpcfcspqrLELLKKEALRSRQTPRYDNRCRNLSqaqVAQKL-------ATDPKP---A 186
Cdd:PLN02907 285 TSDYFPQLMEMAEKLIKEGKAY--------VDDTPREQMRKERMDGIESKCRNNS---VEENLrlwkemiAGSERGlqcC 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 187 IRFRLEEAVP--AFQDLVY----GWTQHEVASvegdpvilKSDGFPTYHLACVVDDHHMSISHVLRGSEW 250
Cdd:PLN02907 354 VRGKLDMQDPnkSLRDPVYyrcnPTPHHRIGS--------KYKVYPTYDFACPFVDALEGVTHALRSSEY 415
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
30-302 |
3.25e-15 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 78.13 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 30 GPDPGVTVrVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDESPrqg 109
Cdd:PLN03233 6 GAIAGQIV-TRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVS--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 110 gpagpyYQSQRLALYAQATEALLKSGAAYpcfcspqrLELLKKEALRSRQTPRYDNRCRNLSQaqvaqklatdpkpairf 189
Cdd:PLN03233 82 ------FTSDYFEPIRCYAIILIEEGLAY--------MDDTPQEEMKKERADRAESKHRNQSP----------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 190 rlEEAVPAFQDLVYG------W---TQHEVASVEG---DPVILKSD------------GFPTYHLACVVDDHHMSISHVL 245
Cdd:PLN03233 131 --EEALEMFKEMCSGkeeggaWclrAKIDMQSDNGtlrDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHAL 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 226958334 246 RGSEWLVSTSKHLLLYQALGWQPPQFaHLPLLLNRDGSKLSKRQGDIFLEHFAATGF 302
Cdd:PLN03233 209 RTTEYDDRDAQFFWIQKALGLRRPRI-HAFARMNFMNTVLSKRKLTWFVDNGHVTGW 264
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
36-138 |
7.75e-15 |
|
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: 74.21 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 36 TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDESprqggpagpY 115
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV---------T 71
|
90 100
....*....|....*....|....*.
gi 226958334 116 YQS---QRLALYAqatEALLKSGAAY 138
Cdd:cd00807 72 YASdyfDQLYEYA---EQLIKKGKAY 94
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
10-289 |
9.40e-15 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 76.92 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 10 LAGPHVGALGHRVGRREASLGPDPGVTVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAE 89
Cdd:PTZ00402 26 LSNTYFTAANANEENDKLQLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 90 NIEDMLEWAGIPPDesprqggpAGPYYQSQRLALYAQATEALLKSGAAYpcfCSpqrlellkkealrsrQTPRYDnrcrn 169
Cdd:PTZ00402 106 AILDDLATLGVSWD--------VGPTYSSDYMDLMYEKAEELIKKGLAY---CD---------------KTPREE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 170 lsqaqvAQKLATDPKPAiRFR---LEEAVPAFQDLVYGWTQHEVASVEG------------DPVIL------------KS 222
Cdd:PTZ00402 155 ------MQKCRFDGVPT-KYRdisVEETKRLWNEMKKGSAEGQETCLRAkisvdnenkamrDPVIYrvnltpharqgtKY 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226958334 223 DGFPTYHLACVVDDHHMSISHVLRGSEWLVSTSKHLLLYQALGWQPPQFAHLPlLLNRDGSKLSKRQ 289
Cdd:PTZ00402 228 KAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFS-RLNMEYSVMSKRK 293
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
389-521 |
1.35e-14 |
|
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: 71.07 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 389 QDRDVLDPAYMERILLLRQGHISRLQDLVSPVYSYLW------TRPAVHRAELGASSEKLDVIAKhLLGLLErpGLS-LT 461
Cdd:pfam19269 13 AGLDGLDDEYLKKVVPLLKERAETLSELAELADFFFElpleydEEAYAKKKMKTNKEESLEVLQE-LLPRLE--ALEdWT 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 462 QDVVNRELKKLSEGLeGTKHSSVMKLLRMALSGQLQGPPVAEMMVSLGPEEVRERIQKVL 521
Cdd:pfam19269 90 AEALEAALKALAEEL-GVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
40-340 |
1.19e-10 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 63.85 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 40 RFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDESPRqggpAGPYYQSq 119
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTF----SSDYFDQ- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 120 rlaLYAQATEaLLKSGAAYPCFCSPQRLellkKEALRSRQTPRYDNRC--------RNLSQAQVAQKLATdpkPAIRFRL 191
Cdd:PTZ00437 130 ---LHEFAVQ-LIKDGKAYVDHSTPDEL----KQQREQREDSPWRNRSveenlllfEHMRQGRYAEGEAT---LRVKADM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 192 EEAVPAFQDLVygwtQHEVASVEGDPVILKSDGFPTYHLA-CVVDDHHmSISHVLRGSEWLVSTSKHLLLYQALG-WQPP 269
Cdd:PTZ00437 199 KSDNPNMRDFI----AYRVKYVEHPHAKDKWCIYPSYDFThCLIDSLE-DIDYSLCTLEFETRRESYFWLLEELNlWRPH 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226958334 270 --QFAHlpllLNRDGSKLSKRQGDIFLEHFAATGFLPEALLDIITNCGSGFAenqmgrtlPELITQF-DLTRIT 340
Cdd:PTZ00437 274 vwEFSR----LNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYT--------PAAINRFcELVGIT 335
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
34-157 |
3.19e-07 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 53.22 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 34 GVTVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDqsrlvPGAA-----ENIEDMLEWAGIPPDESPRq 108
Cdd:PLN02859 262 GGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEkkeyiDHIEEIVEWMGWEPFKITY- 335
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 226958334 109 ggpAGPYYQsqrlALYAQATEaLLKSGAAYPCFCSPQRLELLKKEALRS 157
Cdd:PLN02859 336 ---TSDYFQ----ELYELAVE-LIRRGHAYVDHQTPEEIKEYREKKMNS 376
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
37-138 |
4.32e-07 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 52.80 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAENIEDMLEWAGIPPDEsprqggpaGPYY 116
Cdd:PRK14703 32 VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGE--------HLYY 103
|
90 100
....*....|....*....|..
gi 226958334 117 QSQRLALYAQATEALLKSGAAY 138
Cdd:PRK14703 104 ASDYFERMYAYAEQLIKMGLAY 125
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
36-144 |
1.34e-04 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 44.71 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958334 36 TVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDT-----DQsRLVpgaaENIEDMLEWAGIPPDESPRQgg 110
Cdd:PRK05347 29 RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTnpekeDQ-EYV----DSIKEDVRWLGFDWSGELRY-- 101
|
90 100 110
....*....|....*....|....*....|....
gi 226958334 111 pAGPYYQSqrlaLYAQAtEALLKSGAAYPCFCSP 144
Cdd:PRK05347 102 -ASDYFDQ----LYEYA-VELIKKGKAYVDDLSA 129
|
|
| |
