|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-480 |
0e+00 |
|
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: 631.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 1 MSVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLD 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 81 LYKAAVQQLLDSGKAYRCYCTEAELEALRESQRARNEAPRYDNRHRDLTPEQEAAFQAEGREAVIRFRIDDDrEIAWTDL 160
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEE-GVVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 161 VRDRVVWKGSDLgGDMVIARRSpagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAHTPL 240
Cdd:COG0008 162 VRGEITFPNPNL-RDPVLYRAD-----GYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 241 ILNKEGRKLSKRDGVTSISDFQNLGYLPEAIANYMTLLGWSPVEGmDERFSLAEAATVFDFDRVNKAGAKFDWDKLNWLN 320
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDD-QEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 321 SQVIKEKSASELVALLQPFWSKAGVDTaaypaaWLEELATLLGPSLVTLTDIVGQSQLFFsQGIELQEDAIAQLGQAGSK 400
Cdd:COG0008 315 GPYIRALDDEELAELLAPELPEAGIRE------DLERLVPLVRERAKTLSELAELARFFF-IEREDEKAAKKRLAPEEVR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 401 AVLQQILEALPS-EALTLEVAKGLIDQAVKAAGVKKGIGMRSLRAALMGSMQGPDLLTSWVLLHQAgQAQPRLQAAIAAA 479
Cdd:COG0008 388 KVLKAALEVLEAvETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKE-RVFERLGYAIDKL 466
|
.
gi 499563239 480 Q 480
Cdd:COG0008 467 A 467
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
2-479 |
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: 619.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 2 SVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLDL 81
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 82 YKAAVQQLLDSGKAYRCYCTEAELEALRESQRARNEAPRYDNRHRDLTPEQEAAFQAEGREAVIRFRIDDDREIAWTDLV 161
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 162 RDRVVWKGSDLgGDMVIARRSpagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAHTPLI 241
Cdd:TIGR00464 161 RGEITFQNSEL-DDFVILRSD-----GSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 242 LNKEGRKLSKRDGVTSISDFQNLGYLPEAIANYMTLLGWSPVeGMDERFSLAEAATVFDFDRVNKAGAKFDWDKLNWLNS 321
Cdd:TIGR00464 235 LDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPP-DDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 322 QVIKEKSASELVALLQPFW-SKAGVDTAAYPAawLEELATLLGPSLVTLTDIVGQSQLFFSQGIELQEDAIAQLGQAGSK 400
Cdd:TIGR00464 314 HYIKELPDEELFELLDPHLkSLVNTDTLNREQ--LAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLKKNVK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 401 AVLQQILEALPS-EALTLEVAKGLIDQAVKAAGVKKGIGMRSLRAALMGSMQGPDLLTSWVLLhQAGQAQPRLQAAIAAA 479
Cdd:TIGR00464 392 EVLEALKKKLQAlEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELI-GKTESIKRLKAQFIAA 470
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-469 |
1.25e-144 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 424.92 E-value: 1.25e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 2 SVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGP--------F 73
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygpY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 74 YQTQRLDLYKAAVQQLLDSGKAYRCYCTEAELEALRESQRARNEAPRYDNRHRDLTPEQEAAFQAEGREAVIRFRIDDDR 153
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 154 EIAWTDLVRDRVVWKgSDLGGDMVIARRSpagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVP 233
Cdd:PLN02627 205 SVKIDDLIRGEVSWN-TDTLGDFVLLRSN-----GQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 234 EFAHTPLILNKEGRKLSKRDGVTSISDFQNLGYLPEAIANYMTLLGWSpvEGMD-ERFSLAEAATVFDFDRVNKAGAKFD 312
Cdd:PLN02627 279 RFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN--DGTEnEIFTLEELVEKFSIDRINKSGAVFD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 313 WDKLNWLNSQVIKEKSASELVALLQPFWSKAGVDTAAyPAAWLEELATLLGPSLVTLTDIVGQSQLFFSQGIElqedaiA 392
Cdd:PLN02627 357 STKLKWMNGQHLRLLPEEELVKLVGERWKSAGILKES-DGSFVKEAVELLKDGIELVTDADKELLNLLSYPLA------A 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 393 QLGQAGSKAVLQQ--------ILEALPSEALTLEVAKGLID--QAVKAAGVKKGIGMRSL----RAALMGSMQGPDLLTS 458
Cdd:PLN02627 430 TLSSPEAKTVVEDnfsevadaLIAAYDSGELAAALEEGHDGwqKWVKAFGKALKRKGKRLfmplRVALTGKMHGPDVGES 509
|
490
....*....|.
gi 499563239 459 WVLLHQAGQAQ 469
Cdd:PLN02627 510 LVLLHKAGTPD 520
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-326 |
3.95e-128 |
|
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: 371.53 E-value: 3.95e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 2 SVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDE--------GPF 73
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 74 YQTQRLDLYKAAVQQLLDSGkayrcycteaelealresqrarneaprydnrhrdltpeqeaafqaegreavirfridddr 153
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 154 eiawtdlvrdrvvwkgsdlggdmviarrspagtIGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVP 233
Cdd:cd00808 101 ---------------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPP 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 234 EFAHTPLILNKEGRKLSKRDGVTSISDFQNLGYLPEAIANYMTLLGWSPVEGmDERFSLAEAATVFDFDRVNKAGAKFDW 313
Cdd:cd00808 148 KFAHLPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDG-EEFFTLEELIELFDLERVSKSPAIFDP 226
|
330
....*....|...
gi 499563239 314 DKLNWLNSQVIKE 326
Cdd:cd00808 227 EKLDWLNGQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-318 |
2.13e-127 |
|
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: 372.81 E-value: 2.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLDLY 82
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 83 KAAVQQLLDSGKAYRCYCTEAELEALRESQRARNEA--PRYDNRHRDLTPEQEAAFQAEGREAVIRFRIDDDREIAWTDL 160
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMESPYVFRDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 161 VRDRVVWKGSDLggDMVIARRSPagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAHTPL 240
Cdd:pfam00749 162 VRGRIKFTPQEI--HDRTGVKWD----GYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 241 ILNKEGRKLSKRDGVTS--ISDFQNLGYLPEAIANYMTLLGWSPvEGMDERFSLAEAATVFDFDRVNKAGAKFDWDKLNW 318
Cdd:pfam00749 236 RLNLDGTKLSKRKLSWSvdISQVKGWGDPREATLNGLRRRGWTP-EGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-480 |
0e+00 |
|
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: 631.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 1 MSVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLD 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 81 LYKAAVQQLLDSGKAYRCYCTEAELEALRESQRARNEAPRYDNRHRDLTPEQEAAFQAEGREAVIRFRIDDDrEIAWTDL 160
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEE-GVVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 161 VRDRVVWKGSDLgGDMVIARRSpagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAHTPL 240
Cdd:COG0008 162 VRGEITFPNPNL-RDPVLYRAD-----GYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 241 ILNKEGRKLSKRDGVTSISDFQNLGYLPEAIANYMTLLGWSPVEGmDERFSLAEAATVFDFDRVNKAGAKFDWDKLNWLN 320
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDD-QEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 321 SQVIKEKSASELVALLQPFWSKAGVDTaaypaaWLEELATLLGPSLVTLTDIVGQSQLFFsQGIELQEDAIAQLGQAGSK 400
Cdd:COG0008 315 GPYIRALDDEELAELLAPELPEAGIRE------DLERLVPLVRERAKTLSELAELARFFF-IEREDEKAAKKRLAPEEVR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 401 AVLQQILEALPS-EALTLEVAKGLIDQAVKAAGVKKGIGMRSLRAALMGSMQGPDLLTSWVLLHQAgQAQPRLQAAIAAA 479
Cdd:COG0008 388 KVLKAALEVLEAvETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKE-RVFERLGYAIDKL 466
|
.
gi 499563239 480 Q 480
Cdd:COG0008 467 A 467
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
2-479 |
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: 619.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 2 SVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLDL 81
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 82 YKAAVQQLLDSGKAYRCYCTEAELEALRESQRARNEAPRYDNRHRDLTPEQEAAFQAEGREAVIRFRIDDDREIAWTDLV 161
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 162 RDRVVWKGSDLgGDMVIARRSpagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAHTPLI 241
Cdd:TIGR00464 161 RGEITFQNSEL-DDFVILRSD-----GSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 242 LNKEGRKLSKRDGVTSISDFQNLGYLPEAIANYMTLLGWSPVeGMDERFSLAEAATVFDFDRVNKAGAKFDWDKLNWLNS 321
Cdd:TIGR00464 235 LDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPP-DDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 322 QVIKEKSASELVALLQPFW-SKAGVDTAAYPAawLEELATLLGPSLVTLTDIVGQSQLFFSQGIELQEDAIAQLGQAGSK 400
Cdd:TIGR00464 314 HYIKELPDEELFELLDPHLkSLVNTDTLNREQ--LAELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLKKNVK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 401 AVLQQILEALPS-EALTLEVAKGLIDQAVKAAGVKKGIGMRSLRAALMGSMQGPDLLTSWVLLhQAGQAQPRLQAAIAAA 479
Cdd:TIGR00464 392 EVLEALKKKLQAlEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELI-GKTESIKRLKAQFIAA 470
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-469 |
1.25e-144 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 424.92 E-value: 1.25e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 2 SVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGP--------F 73
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPdvggeygpY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 74 YQTQRLDLYKAAVQQLLDSGKAYRCYCTEAELEALRESQRARNEAPRYDNRHRDLTPEQEAAFQAEGREAVIRFRIDDDR 153
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 154 EIAWTDLVRDRVVWKgSDLGGDMVIARRSpagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVP 233
Cdd:PLN02627 205 SVKIDDLIRGEVSWN-TDTLGDFVLLRSN-----GQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 234 EFAHTPLILNKEGRKLSKRDGVTSISDFQNLGYLPEAIANYMTLLGWSpvEGMD-ERFSLAEAATVFDFDRVNKAGAKFD 312
Cdd:PLN02627 279 RFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN--DGTEnEIFTLEELVEKFSIDRINKSGAVFD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 313 WDKLNWLNSQVIKEKSASELVALLQPFWSKAGVDTAAyPAAWLEELATLLGPSLVTLTDIVGQSQLFFSQGIElqedaiA 392
Cdd:PLN02627 357 STKLKWMNGQHLRLLPEEELVKLVGERWKSAGILKES-DGSFVKEAVELLKDGIELVTDADKELLNLLSYPLA------A 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 393 QLGQAGSKAVLQQ--------ILEALPSEALTLEVAKGLID--QAVKAAGVKKGIGMRSL----RAALMGSMQGPDLLTS 458
Cdd:PLN02627 430 TLSSPEAKTVVEDnfsevadaLIAAYDSGELAAALEEGHDGwqKWVKAFGKALKRKGKRLfmplRVALTGKMHGPDVGES 509
|
490
....*....|.
gi 499563239 459 WVLLHQAGQAQ 469
Cdd:PLN02627 510 LVLLHKAGTPD 520
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-326 |
3.95e-128 |
|
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: 371.53 E-value: 3.95e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 2 SVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDE--------GPF 73
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 74 YQTQRLDLYKAAVQQLLDSGkayrcycteaelealresqrarneaprydnrhrdltpeqeaafqaegreavirfridddr 153
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 154 eiawtdlvrdrvvwkgsdlggdmviarrspagtIGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVP 233
Cdd:cd00808 101 ---------------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPP 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 234 EFAHTPLILNKEGRKLSKRDGVTSISDFQNLGYLPEAIANYMTLLGWSPVEGmDERFSLAEAATVFDFDRVNKAGAKFDW 313
Cdd:cd00808 148 KFAHLPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDG-EEFFTLEELIELFDLERVSKSPAIFDP 226
|
330
....*....|...
gi 499563239 314 DKLNWLNSQVIKE 326
Cdd:cd00808 227 EKLDWLNGQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-318 |
2.13e-127 |
|
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: 372.81 E-value: 2.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLDLY 82
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 83 KAAVQQLLDSGKAYRCYCTEAELEALRESQRARNEA--PRYDNRHRDLTPEQEAAFQAEGREAVIRFRIDDDREIAWTDL 160
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMESPYVFRDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 161 VRDRVVWKGSDLggDMVIARRSPagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAHTPL 240
Cdd:pfam00749 162 VRGRIKFTPQEI--HDRTGVKWD----GYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 241 ILNKEGRKLSKRDGVTS--ISDFQNLGYLPEAIANYMTLLGWSPvEGMDERFSLAEAATVFDFDRVNKAGAKFDWDKLNW 318
Cdd:pfam00749 236 RLNLDGTKLSKRKLSWSvdISQVKGWGDPREATLNGLRRRGWTP-EGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
3-326 |
2.22e-98 |
|
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: 295.54 E-value: 2.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLDLY 82
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 83 KAAVQQLLDSGkayrcycteaelealresqrarneaprydnrhrdltpeqeaafqaegreavirfridddreiawtdlvr 162
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 163 drvvwkgsdlggdmviarrspagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAHTPLIL 242
Cdd:cd00418 93 -------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLL 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 243 NKEGRKLSKRDGVTSISDFQNLGYLPEAIANYMTLLGWSPVEGMDErFSLAEAATVFDFDRVNKAGAKFDWDKLNWLNSQ 322
Cdd:cd00418 148 LEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHEL-FTLEEMIAAFSVERVNSADATFDWAKLEWLNRE 226
|
....
gi 499563239 323 VIKE 326
Cdd:cd00418 227 YIRE 230
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-304 |
1.84e-91 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 280.20 E-value: 1.84e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 1 MSVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLD 80
Cdd:PRK05710 4 TPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 81 LYKAAVQQLLDSGKAYRCYCTEAELEALreSQRARNEAPRYDNRHRDLTPEQEAAFqaegreaVIRFRIdDDREIAWTDL 160
Cdd:PRK05710 84 AYRAALDRLRAQGLVYPCFCSRKEIAAA--APAPPDGGGIYPGTCRDLLHGPRNPP-------AWRLRV-PDAVIAFDDR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 161 VRDRVVwkgSDLG---GDMVIARRSpagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAH 237
Cdd:PRK05710 154 LQGRQH---QDLAlavGDFVLRRAD-----GLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLH 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499563239 238 TPLILNKEGRKLSKRDGVTSIsdfqNLGYLPEAIANYMTLLGWSPVEGM-DERFSLAEAATVFDFDRV 304
Cdd:PRK05710 226 LPLVLNADGQKLSKQNGAPAL----DAAGPLPVLAAALRFLGQPPPAADaSVEELLAQAVAHWDLTRL 289
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
3-294 |
4.72e-87 |
|
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: 267.87 E-value: 4.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLDLY 82
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 83 KAAVQQLLDSGKAYRCYCTEAELealresQRARNEAPRYDNRHRDLTPEqeaafqAEGREAVIRFRIdDDREIAWTDLVR 162
Cdd:TIGR03838 81 QAALDRLLAAGLAYPCQCTRKEI------AAARDGGGIYPGTCRNGLPG------RPGRPAAWRLRV-PDGVIAFDDRLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 163 DRVVWKGSDLGGDMVIARRSpagtiGQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAHTPLIL 242
Cdd:TIGR03838 148 GPQQQDLAAAVGDFVLRRAD-----GLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499563239 243 NKEGRKLSKRDGVTSISDFQNLGYLPEAianyMTLLGWSPVEGMDeRFSLAE 294
Cdd:TIGR03838 223 NADGEKLSKQNGAPALDDSRPLPALLAA----LRFLGLPPPPELA-AASPAE 269
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
3-324 |
1.74e-52 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 186.21 E-value: 1.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSE---YtDNILTGLQWLGLNWDEgPFYQTQRL 79
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPDpeaY-DMILEDLKWLGVKWDE-VVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 80 DLYKAAVQQLLDSGKAYRCYCTEAELEALRESQRArneAPrydnrHRDLTPEQ---------EAAFQaEGrEAVIRFRid 150
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKP---CP-----HRDKSPEEnlelwekmlDGEYK-EG-EAVVRVK-- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 151 ddreiawTDL------VRDrvvWkgsdlggdmVIAR--RSPAGTIGQ-----PLYNLAVVVDDIDMTISHVIRGEDHIAN 217
Cdd:PRK04156 248 -------TDLehpnpsVRD---W---------VAFRivKTPHPRVGDkyrvwPTYNFAVAVDDHLLGVTHVLRGKDHIDN 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 218 TAKQILLYEALGAAVPEFAHTPlILNKEGRKLSK---RDGVTS-------------ISDFQNLGYLPEAIANYMTLLGws 281
Cdd:PRK04156 309 TEKQRYIYDYFGWEYPETIHYG-RLKIEGFVLSTskiRKGIEEgeysgwddprlptLRALRRRGILPEAIRELIIEVG-- 385
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 499563239 282 pvegmderfslaeaatvfdfdrVNKAGAKFDWDKLNWLNSQVI 324
Cdd:PRK04156 386 ----------------------VKETDATISWENLYAINRKLI 406
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
3-328 |
2.90e-40 |
|
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: 152.28 E-value: 2.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEgPFYQTQRLDLY 82
Cdd:TIGR00463 94 VVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDE-VVYQSDRIETY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 83 KAAVQQLLDSGKAYRCYCTEAELEALRESQRArneaprydNRHRDLTPEQ-----EAAFQA--EGREAVIRFRID-DDRE 154
Cdd:TIGR00463 173 YDYTRKLIEMGKAYVCDCRPEEFRELRNRGEA--------CHCRDRSVEEnlerwEEMLEGkeEGGSVVVRVKTDlKHKN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 155 IAWTDLVRDRVVWKGSDLGGDMVIArrspagtigQPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPE 234
Cdd:TIGR00463 245 PAIRDWVIFRIVKTPHPRTGDKYRV---------YPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 235 FAHTPLILNKEGRKLS---KRDGVT-------------SISDFQNLGYLPEAIANYMTLLGwspvegmderfslaeaatv 298
Cdd:TIGR00463 316 FIHWGRLKIDDVRALStssARKGILrgeysgwddprlpTLRAIRRRGIRPEAIRKFMLSIG------------------- 376
|
330 340 350
....*....|....*....|....*....|
gi 499563239 299 fdfdrVNKAGAKFDWDKLNWLNSQVIKEKS 328
Cdd:TIGR00463 377 -----VKINDVTMSWKNIYALNRKIIDEEA 401
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
3-293 |
3.07e-40 |
|
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: 144.80 E-value: 3.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRS--EYTDNILTGLQWLGLNWDEgPFYQTQRLD 80
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDE-VVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 81 LYKAAVQQLLDSGKAYrcycteaelealresqrarnEAPRYDNRHRdltpeqeaafqaegreavirfridddreiawtdl 160
Cdd:cd09287 81 LYYEYARKLIEMGGAY--------------------VHPRTGSKYR---------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 161 vrdrvVWkgsdlggdmviarrspagtigqPLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALGAAVPEFAHTPl 240
Cdd:cd09287 107 -----VW----------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWG- 158
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499563239 241 ILNKEGRKLSK---RDGVTS-------------ISDFQNLGYLPEAIANYMTLLGWSPVegmDERFSLA 293
Cdd:cd09287 159 RLKIEGGKLSTskiRKGIESgeyegwddprlptLRALRRRGIRPEAIRDFIIEVGVKQT---DATISWE 224
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
3-96 |
1.20e-19 |
|
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: 87.69 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEgPFYQTQRLD-L 81
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYK-VTYASDYFDqL 80
|
90
....*....|....*
gi 499563239 82 YKAAVqQLLDSGKAY 96
Cdd:cd00807 81 YEYAE-QLIKKGKAY 94
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
3-252 |
4.92e-19 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 90.02 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLDLY 82
Cdd:PTZ00402 53 VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDLM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 83 KAAVQQLLDSGKAYrCYCTEAElealrESQRAR-NEAPrydNRHRDLTPEQEAAF-------QAEGREAVIRFRIDDDRE 154
Cdd:PTZ00402 133 YEKAEELIKKGLAY-CDKTPRE-----EMQKCRfDGVP---TKYRDISVEETKRLwnemkkgSAEGQETCLRAKISVDNE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 155 iawTDLVRDRVVWKGSdlggdMVIARRSPAGTIGQPLYNLAV-VVDDIDmTISHVIRGEDHIANTAKQILLYEALGAAVP 233
Cdd:PTZ00402 204 ---NKAMRDPVIYRVN-----LTPHARQGTKYKAYPTYDFCCpIIDSVE-GVTHALRTNEYHDRNDQYYWFCDALGIRKP 274
|
250 260
....*....|....*....|..
gi 499563239 234 ---EFAHtpliLNKEGRKLSKR 252
Cdd:PTZ00402 275 iveDFSR----LNMEYSVMSKR 292
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
331-462 |
5.20e-18 |
|
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: 80.70 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 331 ELVALLQPFWSKAGVDTAAYPaaWLEELATLLGPSLVTLTDIVGQSQLFFSQGIELQEDAIAQ----LGQAGSKAVLQQI 406
Cdd:pfam19269 1 ELAELALPYLEEAGLDGLDDE--YLKKVVPLLKERAETLSELAELADFFFELPLEYDEEAYAKkkmkTNKEESLEVLQEL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 499563239 407 LEALPS-EALTLEVAKGLIDQAVKAAGVKKGIGMRSLRAALMGSMQGPDLLTSWVLL 462
Cdd:pfam19269 79 LPRLEAlEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEIL 135
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
3-279 |
1.29e-16 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 82.85 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLDLY 82
Cdd:PRK14703 32 VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASDYFERM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 83 KAAVQQLLDSGKAYRCYCTEaelEALREsQRARNEAPRYDNRHRDLTPEQ--------EAAFQAEGrEAVIRFRIDddrE 154
Cdd:PRK14703 112 YAYAEQLIKMGLAYVDSVSE---EEIRE-LRGTVTEPGTPSPYRDRSVEEnldlfrrmRAGEFPDG-AHVLRAKID---M 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 155 IAWTDLVRDRVVWKgsdlggdmviARRSPAGTIGQ-----PLYNLAVVVDDIDMTISHVIRGEDHIANTAKQILLYEALG 229
Cdd:PRK14703 184 SSPNMKLRDPLLYR----------IRHAHHYRTGDewciyPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLG 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499563239 230 AAVP-----EFAHTPL---ILNK-------EGRKLSKRDG--VTSISDFQNLGYLPEAIANYMTLLG 279
Cdd:PRK14703 254 PWPPrprqyEFARLALgytVMSKrklrelvEEGYVSGWDDprMPTIAGQRRRGVTPEAIRDFADQIG 320
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
3-252 |
4.37e-16 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 80.44 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPfYQTQRLDLY 82
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVS-FTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 83 KAAVQQLLDSGKAYRCYCTEAELEALResqrarneAPRYDNRHRDLTPEQEAAF-------QAEGREAVIRFRIDDDREi 155
Cdd:PLN03233 91 RCYAIILIEEGLAYMDDTPQEEMKKER--------ADRAESKHRNQSPEEALEMfkemcsgKEEGGAWCLRAKIDMQSD- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 156 awTDLVRDRVVWKgsdlgGDMVIARRSPAGTIGQPLYNLAV-VVDDIDmTISHVIRGEDHIANTAKQILLYEALGAAVPE 234
Cdd:PLN03233 162 --NGTLRDPVLFR-----QNTTPHHRSGTAYKAYPTYDLACpIVDSIE-GVTHALRTTEYDDRDAQFFWIQKALGLRRPR 233
|
250
....*....|....*...
gi 499563239 235 FaHTPLILNKEGRKLSKR 252
Cdd:PLN03233 234 I-HAFARMNFMNTVLSKR 250
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
3-150 |
2.06e-15 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 79.00 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPF---YQTQRL 79
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYtsdYFPQLM 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499563239 80 DLykaaVQQLLDSGKAyrcYCTEAELEALRESQRARNEAprydnRHRDLTPEQEAAFQAE-------GREAVIRFRID 150
Cdd:PLN02907 294 EM----AEKLIKEGKA---YVDDTPREQMRKERMDGIES-----KCRNNSVEENLRLWKEmiagserGLQCCVRGKLD 359
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
6-150 |
2.61e-14 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 75.40 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 6 RIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLDLYKAA 85
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHEFA 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499563239 86 VqQLLDSGKAYRCYCTEAELEALRESqraRNEAPrYDNRHRD----LTPEQEAAFQAEGrEAVIRFRID 150
Cdd:PTZ00437 135 V-QLIKDGKAYVDHSTPDELKQQREQ---REDSP-WRNRSVEenllLFEHMRQGRYAEG-EATLRVKAD 197
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
2-150 |
1.12e-13 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 73.21 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 2 SVRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGLNWDEGPFYQTQRLD- 80
Cdd:PRK05347 29 RVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSGELRYASDYFDq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 81 LYKAAVqQLLDSGKAYRCycteaEL--EALREsQRARNEAPRYDNRHRDLTPEQEAA-FQ-------AEGrEAVIRFRID 150
Cdd:PRK05347 109 LYEYAV-ELIKKGKAYVD-----DLsaEEIRE-YRGTLTEPGKNSPYRDRSVEENLDlFErmragefPEG-SAVLRAKID 180
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
3-113 |
1.66e-12 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 69.79 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499563239 3 VRVRIAPSPTGNLHIGTARTAVFNWLFARRHQGQFILRIEDTDLERSRSEYTDNILTGLQWLGlnWDegPFYQTQRLD-- 80
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WE--PFKITYTSDyf 340
|
90 100 110
....*....|....*....|....*....|....*
gi 499563239 81 --LYKAAVqQLLDSGKAYRCYCTEAELEALRESQR 113
Cdd:PLN02859 341 qeLYELAV-ELIRRGHAYVDHQTPEEIKEYREKKM 374
|
|
| |
