|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
2-494 |
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: 607.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 2 ANDSIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEgpdkpgey 81
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 82 GPYRQSERFDIYKPYIQQLLDEGKAYKSYRTEDELEADREAQRARHEMPHYEYEYAGMSDDEIkdamAKAEAKGLKPVIR 161
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEEL----ERMLAAGEPPVLR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 162 FHVPAHKTyAWDDMVKGKVSFDSDTIgGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWT 241
Cdd:COG0008 149 FKIPEEGV-VFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 242 PPKFGHMSLIISKDtGKKLSKRDETVlqFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPA 321
Cdd:COG0008 227 PPEFAHLPLILGPD-GTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 322 TFDKKKLEWINNQYVKTSDEDVVVDLAlqqliaagnIPENPDAKTLEWARQLINLYKRQMSYMAQINDMASVFFQEPEKI 401
Cdd:COG0008 304 VFDPVKLVWLNGPYIRALDDEELAELL---------APELPEAGIREDLERLVPLVRERAKTLSELAELARFFFIEREDE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 402 SgEALDEISNDTAPVVLKEFSERIKKLPIFDKVKILKTIKDIQKDTGIKGRKLWMPIRIAVTHEMHGPELPESIELVGRD 481
Cdd:COG0008 375 K-AAKKRLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKE 453
|
490
....*....|...
gi 1655147397 482 KTLKHVAQTLAQL 494
Cdd:COG0008 454 RVFERLGYAIDKL 466
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
5-485 |
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: 553.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 5 SIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEgpdkpgeyGPY 84
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 85 RQSERFDIYKPYIQQLLDEGKAYKSYRTEDELEADREAQRARHEMPHYEYEYAGMSDDEIKdamaKAEAKGLKPVIRFHV 164
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIE----NKLAKGIPPVVRFKI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 165 PAHKTYAWDDMVKGKVSFDSDTIgGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPPK 244
Cdd:TIGR00464 149 PQEAVVSFNDQVRGEITFQNSEL-DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 245 FGHMSLIISKDtGKKLSKRDETvlQFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPATFD 324
Cdd:TIGR00464 228 FAHLPMILDED-GKKLSKRDGA--TSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 325 KKKLEWINNQYVKTSDEDVVVDLALQQLIAAGNIpENPDAKTLewaRQLINLYKRQMSYMAQINDMASVFFQEPEKISGE 404
Cdd:TIGR00464 305 WKKLQWLNAHYIKELPDEELFELLDPHLKSLVNT-DTLNREQL---AELLLLFKERLKTLKEIAELIRLFFEDKKEVDED 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 405 ALDEISNDTAPVVLKEFSERIKKLPIFDKVKILKTIKDIQKDTGIKGRKLWMPIRIAVTHEMHGPELPESIELVGRDKTL 484
Cdd:TIGR00464 381 AFKKHLKKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESI 460
|
.
gi 1655147397 485 K 485
Cdd:TIGR00464 461 K 461
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
5-480 |
5.32e-156 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 454.58 E-value: 5.32e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 5 SIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEGPDKPGEYGPY 84
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 85 RQSERFDIYKPYIQQLLDEGKAYKSYRTEDELEADREAQRARHEMPHYEYEYAGMSDDEIKDAMakaeAKGLKPVIRFHV 164
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAEL----AKGTPYTYRFRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 165 PAHKTYAWDDMVKGKVSFDSDTIgGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPPK 244
Cdd:PLN02627 201 PKEGSVKIDDLIRGEVSWNTDTL-GDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 245 FGHMSLIISKDTgKKLSKRDETVlqFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPATFD 324
Cdd:PLN02627 280 FAHVSLILAPDR-SKLSKRHGAT--SVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 325 KKKLEWINNQYVKTSDEDVVVDLALQQLIAAGNIPENpdakTLEWARQLINLYKRQMSYMAQINDMASVFFQEPEK---I 401
Cdd:PLN02627 357 STKLKWMNGQHLRLLPEEELVKLVGERWKSAGILKES----DGSFVKEAVELLKDGIELVTDADKELLNLLSYPLAatlS 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 402 SGEALDEISNDTAPVVLK--------EFSERIKKLPifDKVKilKTIKDIQKDTGIKGRKLWMPIRIAVTHEMHGPELPE 473
Cdd:PLN02627 433 SPEAKTVVEDNFSEVADAliaaydsgELAAALEEGH--DGWQ--KWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGE 508
|
....*..
gi 1655147397 474 SIELVGR 480
Cdd:PLN02627 509 SLVLLHK 515
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
6-330 |
3.05e-137 |
|
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: 398.23 E-value: 3.05e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 6 IRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDegpdkpgeYGPYR 85
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 86 QSERFDIYKPYIQQLLDEGKAYKSYRTEDELEADREAQRARHE--MPHYEYEYAGMSDDEikdaMAKAEAKGLKPVIRFH 163
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSpsRDRYDEENLHLFEEE----MKKGSAEGGPATVRAK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 164 VPAHKTYAWDDMVKGKVSFDSDTIgGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPP 243
Cdd:pfam00749 150 IPMESPYVFRDPVRGRIKFTPQEI-HDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 244 KFGHMSLIISkDTGKKLSKRDETVLQFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPATF 323
Cdd:pfam00749 229 PFIHEYLRLN-LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAF 307
|
....*..
gi 1655147397 324 DKKKLEW 330
Cdd:pfam00749 308 DRKKLDW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
5-338 |
1.42e-133 |
|
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: 386.17 E-value: 1.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 5 SIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEGPDKPGEYGPY 84
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 85 RQSERFDIYKPYIQQLLDEGkayksyrtedeleadreaqrarhemphyeyeyagmsddeikdamakaeakglkpvirfhv 164
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 165 pahktyawddmvkgkvsfdsdtiggdfvivkaDGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPPK 244
Cdd:cd00808 101 --------------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPK 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 245 FGHMSLIISKDtGKKLSKRDETVlqFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPATFD 324
Cdd:cd00808 149 FAHLPLILNPD-GKKLSKRKGDT--SISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFD 225
|
330
....*....|....
gi 1655147397 325 KKKLEWINNQYVKT 338
Cdd:cd00808 226 PEKLDWLNGQYIRE 239
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
2-494 |
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: 607.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 2 ANDSIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEgpdkpgey 81
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 82 GPYRQSERFDIYKPYIQQLLDEGKAYKSYRTEDELEADREAQRARHEMPHYEYEYAGMSDDEIkdamAKAEAKGLKPVIR 161
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEEL----ERMLAAGEPPVLR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 162 FHVPAHKTyAWDDMVKGKVSFDSDTIgGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWT 241
Cdd:COG0008 149 FKIPEEGV-VFDDLVRGEITFPNPNL-RDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 242 PPKFGHMSLIISKDtGKKLSKRDETVlqFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPA 321
Cdd:COG0008 227 PPEFAHLPLILGPD-GTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 322 TFDKKKLEWINNQYVKTSDEDVVVDLAlqqliaagnIPENPDAKTLEWARQLINLYKRQMSYMAQINDMASVFFQEPEKI 401
Cdd:COG0008 304 VFDPVKLVWLNGPYIRALDDEELAELL---------APELPEAGIREDLERLVPLVRERAKTLSELAELARFFFIEREDE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 402 SgEALDEISNDTAPVVLKEFSERIKKLPIFDKVKILKTIKDIQKDTGIKGRKLWMPIRIAVTHEMHGPELPESIELVGRD 481
Cdd:COG0008 375 K-AAKKRLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKE 453
|
490
....*....|...
gi 1655147397 482 KTLKHVAQTLAQL 494
Cdd:COG0008 454 RVFERLGYAIDKL 466
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
5-485 |
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: 553.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 5 SIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEgpdkpgeyGPY 84
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 85 RQSERFDIYKPYIQQLLDEGKAYKSYRTEDELEADREAQRARHEMPHYEYEYAGMSDDEIKdamaKAEAKGLKPVIRFHV 164
Cdd:TIGR00464 73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIE----NKLAKGIPPVVRFKI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 165 PAHKTYAWDDMVKGKVSFDSDTIgGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPPK 244
Cdd:TIGR00464 149 PQEAVVSFNDQVRGEITFQNSEL-DDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 245 FGHMSLIISKDtGKKLSKRDETvlQFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPATFD 324
Cdd:TIGR00464 228 FAHLPMILDED-GKKLSKRDGA--TSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 325 KKKLEWINNQYVKTSDEDVVVDLALQQLIAAGNIpENPDAKTLewaRQLINLYKRQMSYMAQINDMASVFFQEPEKISGE 404
Cdd:TIGR00464 305 WKKLQWLNAHYIKELPDEELFELLDPHLKSLVNT-DTLNREQL---AELLLLFKERLKTLKEIAELIRLFFEDKKEVDED 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 405 ALDEISNDTAPVVLKEFSERIKKLPIFDKVKILKTIKDIQKDTGIKGRKLWMPIRIAVTHEMHGPELPESIELVGRDKTL 484
Cdd:TIGR00464 381 AFKKHLKKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESI 460
|
.
gi 1655147397 485 K 485
Cdd:TIGR00464 461 K 461
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
5-480 |
5.32e-156 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 454.58 E-value: 5.32e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 5 SIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEGPDKPGEYGPY 84
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 85 RQSERFDIYKPYIQQLLDEGKAYKSYRTEDELEADREAQRARHEMPHYEYEYAGMSDDEIKDAMakaeAKGLKPVIRFHV 164
Cdd:PLN02627 125 RQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAEL----AKGTPYTYRFRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 165 PAHKTYAWDDMVKGKVSFDSDTIgGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPPK 244
Cdd:PLN02627 201 PKEGSVKIDDLIRGEVSWNTDTL-GDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 245 FGHMSLIISKDTgKKLSKRDETVlqFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPATFD 324
Cdd:PLN02627 280 FAHVSLILAPDR-SKLSKRHGAT--SVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 325 KKKLEWINNQYVKTSDEDVVVDLALQQLIAAGNIPENpdakTLEWARQLINLYKRQMSYMAQINDMASVFFQEPEK---I 401
Cdd:PLN02627 357 STKLKWMNGQHLRLLPEEELVKLVGERWKSAGILKES----DGSFVKEAVELLKDGIELVTDADKELLNLLSYPLAatlS 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 402 SGEALDEISNDTAPVVLK--------EFSERIKKLPifDKVKilKTIKDIQKDTGIKGRKLWMPIRIAVTHEMHGPELPE 473
Cdd:PLN02627 433 SPEAKTVVEDNFSEVADAliaaydsgELAAALEEGH--DGWQ--KWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGE 508
|
....*..
gi 1655147397 474 SIELVGR 480
Cdd:PLN02627 509 SLVLLHK 515
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
6-330 |
3.05e-137 |
|
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: 398.23 E-value: 3.05e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 6 IRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDegpdkpgeYGPYR 85
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 86 QSERFDIYKPYIQQLLDEGKAYKSYRTEDELEADREAQRARHE--MPHYEYEYAGMSDDEikdaMAKAEAKGLKPVIRFH 163
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSpsRDRYDEENLHLFEEE----MKKGSAEGGPATVRAK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 164 VPAHKTYAWDDMVKGKVSFDSDTIgGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPP 243
Cdd:pfam00749 150 IPMESPYVFRDPVRGRIKFTPQEI-HDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 244 KFGHMSLIISkDTGKKLSKRDETVLQFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPATF 323
Cdd:pfam00749 229 PFIHEYLRLN-LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAF 307
|
....*..
gi 1655147397 324 DKKKLEW 330
Cdd:pfam00749 308 DRKKLDW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
5-338 |
1.42e-133 |
|
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: 386.17 E-value: 1.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 5 SIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEGPDKPGEYGPY 84
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 85 RQSERFDIYKPYIQQLLDEGkayksyrtedeleadreaqrarhemphyeyeyagmsddeikdamakaeakglkpvirfhv 164
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 165 pahktyawddmvkgkvsfdsdtiggdfvivkaDGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPPK 244
Cdd:cd00808 101 --------------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPK 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 245 FGHMSLIISKDtGKKLSKRDETVlqFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPATFD 324
Cdd:cd00808 149 FAHLPLILNPD-GKKLSKRKGDT--SISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFD 225
|
330
....*....|....
gi 1655147397 325 KKKLEWINNQYVKT 338
Cdd:cd00808 226 PEKLDWLNGQYIRE 239
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
6-337 |
2.29e-82 |
|
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: 254.70 E-value: 2.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 6 IRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEGPdkpgeygpYR 85
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGP--------YR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 86 QSERFDIYKPYIQQLLDEGkayksyrtedeleadreaqrarhemphyeyeyagmsddeikdamakaeakglkpvirfhvp 165
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 166 ahktyawddmvkgkvsfdsdtiggdfvivkadGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPPKF 245
Cdd:cd00418 93 --------------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRF 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 246 GHMSLIISKDtGKKLSKRDetVLQFIEQYRKLGYLPDALLNFIILLGWSPVGEDEIYSLKELVKMYDEKRLSKSPATFDK 325
Cdd:cd00418 141 YHFPRLLLED-GTKLSKRK--LNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDW 217
|
330
....*....|..
gi 1655147397 326 KKLEWINNQYVK 337
Cdd:cd00418 218 AKLEWLNREYIR 229
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-264 |
1.88e-71 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 228.97 E-value: 1.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 1 MANDSIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDeGPdkpge 80
Cdd:PRK05710 1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWD-GP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 81 ygPYRQSERFDIYKPYIQQLLDEGKAYKSYRTEDELeadreaQRARHEMPHYEYEYAGMSDDEIKDAMAkaeakglKPVI 160
Cdd:PRK05710 75 --VLYQSQRHDAYRAALDRLRAQGLVYPCFCSRKEI------AAAAPAPPDGGGIYPGTCRDLLHGPRN-------PPAW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 161 RFHVPaHKTYAWDDMVKGKVSFDSDTIGGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGW 240
Cdd:PRK05710 140 RLRVP-DAVIAFDDRLQGRQHQDLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGL 218
|
250 260
....*....|....*....|....
gi 1655147397 241 TPPKFGHMSLIISKDtGKKLSKRD 264
Cdd:PRK05710 219 PTPRYLHLPLVLNAD-GQKLSKQN 241
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
9-264 |
6.12e-68 |
|
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: 218.95 E-value: 6.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 9 RYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEGPDkpgeygpyRQSE 88
Cdd:TIGR03838 4 RFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVV--------YQSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 89 RFDIYKPYIQQLLDEGKAYKSYRTEdeleadREAQRARHEMPHyeyeYAGMSDDEIKDAMAKAEAkglkpvIRFHVPaHK 168
Cdd:TIGR03838 76 RHALYQAALDRLLAAGLAYPCQCTR------KEIAAARDGGGI----YPGTCRNGLPGRPGRPAA------WRLRVP-DG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 169 TYAWDDMVKGKVSFDSDTIGGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPPKFGHM 248
Cdd:TIGR03838 139 VIAFDDRLQGPQQQDLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHL 218
|
250
....*....|....*.
gi 1655147397 249 SLIISKDtGKKLSKRD 264
Cdd:TIGR03838 219 PLVVNAD-GEKLSKQN 233
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
3-292 |
7.65e-49 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 176.58 E-value: 7.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 3 NDSIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTD--TKRNVADGEKSQLDNLRWLGLDWDEgpdkpge 80
Cdd:PRK04156 99 KGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWDE------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 81 ygPYRQSERFDIYKPYIQQLLDEGKAYKSYRTEDELeadREAQRARHEMPHYE-------YEYAGMSDDEIKDAMAkaea 153
Cdd:PRK04156 172 --VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEF---KELRDAGKPCPHRDkspeenlELWEKMLDGEYKEGEA---- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 154 kglkpVIRFHV-PAHKTYAWDDMVKGKVSFDSDTIGGDFVIVkadgIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQL 232
Cdd:PRK04156 243 -----VVRVKTdLEHPNPSVRDWVAFRIVKTPHPRVGDKYRV----WPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQR 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655147397 233 MVYEAFGWTPPK---FGHMSL---IISKDTGKKL------SKRDETVLQFIEQYRKLGYLPDALLNFIILLG 292
Cdd:PRK04156 314 YIYDYFGWEYPEtihYGRLKIegfVLSTSKIRKGieegeySGWDDPRLPTLRALRRRGILPEAIRELIIEVG 385
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
6-307 |
4.60e-44 |
|
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: 155.20 E-value: 4.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 6 IRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGE--KSQLDNLRWLGLDWDEgpdkpgeygP 83
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEayDMIPEDLEWLGVKWDE---------V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 84 YRQSERFDIYKPYIQQLLDEGKAYKSYRTEDeleadreaqrarhemphyeyeyagmsddeikdamakaeakglkpvirfh 163
Cdd:cd09287 73 VIASDRIELYYEYARKLIEMGGAYVHPRTGS------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 164 vpahKTYAWddmvkgkvsfdsdtiggdfvivkadgiPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPP 243
Cdd:cd09287 104 ----KYRVW---------------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYP 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655147397 244 K---FGHMSL---IISKDTGKK------LSKRDETVLQFIEQYRKLGYLPDALLNFIILLGWSPVgeDEIYSLKEL 307
Cdd:cd09287 153 EtihWGRLKIeggKLSTSKIRKgiesgeYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQT--DATISWENL 226
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
4-292 |
1.05e-39 |
|
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: 151.13 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 4 DSIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEgpdkpgeygP 83
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDE---------V 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 84 YRQSERFDIYKPYIQQLLDEGKAYKSYRTEDELeadREAQRARHEMPHYEyeyAGMSDD-EIKDAMAKAEAKGLKPVIRF 162
Cdd:TIGR00463 163 VYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEF---RELRNRGEACHCRD---RSVEENlERWEEMLEGKEEGGSVVVRV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 163 HVP-AHKTYAWDDMVKGKVSFDSDTIGGDFVIVkadgIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWT 241
Cdd:TIGR00463 237 KTDlKHKNPAIRDWVIFRIVKTPHPRTGDKYRV----YPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWE 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655147397 242 PPKFGHMSLIISKDTGKKLSKR-------------DETVLQFIEQYRKLGYLPDALLNFIILLG 292
Cdd:TIGR00463 313 PPEFIHWGRLKIDDVRALSTSSarkgilrgeysgwDDPRLPTLRAIRRRGIRPEAIRKFMLSIG 376
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
344-485 |
3.24e-22 |
|
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: 92.64 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 344 VVDLALQQLIAAGNIPENPdaktlEWARQLINLYKRQMSYMAQINDMASVFFQEPEKISGEALDEISN----DTAPVVLK 419
Cdd:pfam19269 2 LAELALPYLEEAGLDGLDD-----EYLKKVVPLLKERAETLSELAELADFFFELPLEYDEEAYAKKKMktnkEESLEVLQ 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655147397 420 EFSERIKKLPIFDKVKILKTIKDIQKDTGIKGRKLWMPIRIAVTHEMHGPELPESIELVGRDKTLK 485
Cdd:pfam19269 77 ELLPRLEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLA 142
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
3-292 |
1.45e-17 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 85.93 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 3 NDSIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEgpdkpgeyG 82
Cdd:PRK14703 29 YPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGE--------H 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 83 PYRQSERFDIYKPYIQQLLDEGKAYKSYRTEDELeadREaQRARHEMPHYEYEYA------------GMSDDEIKDA--- 147
Cdd:PRK14703 101 LYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEI---RE-LRGTVTEPGTPSPYRdrsveenldlfrRMRAGEFPDGahv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 148 ------MAKAEAKGLKPV---IRfHVPAHKTyawddmvkgkvsfdsdtiGGDFVIVkadgiPTYNFAVVLDDHLMKISHV 218
Cdd:PRK14703 177 lrakidMSSPNMKLRDPLlyrIR-HAHHYRT------------------GDEWCIY-----PMYDFAHPLEDAIEGVTHS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 219 FRGDDHVANTPKQLMVYEAFGWTPPK-----FGHMSL---IISKD------TGKKLSKRDETVLQFIEQYRKLGYLPDAL 284
Cdd:PRK14703 233 ICTLEFENNRAIYDWVLDHLGPWPPRprqyeFARLALgytVMSKRklrelvEEGYVSGWDDPRMPTIAGQRRRGVTPEAI 312
|
....*...
gi 1655147397 285 LNFIILLG 292
Cdd:PRK14703 313 RDFADQIG 320
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
9-266 |
1.50e-15 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 79.24 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 9 RYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEGPDKPGEYgpyrqse 88
Cdd:PTZ00402 56 RFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDY------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 89 rFDIYKPYIQQLLDEGKAYKSYRTEDELeadreaQRARHEMPHYEYEYAGMSDD-EIKDAMAKAEAKGLKPVIRFHVPA- 166
Cdd:PTZ00402 129 -MDLMYEKAEELIKKGLAYCDKTPREEM------QKCRFDGVPTKYRDISVEETkRLWNEMKKGSAEGQETCLRAKISVd 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 167 HKTYAWDDMVKGKVSFDSDTIGGdfviVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTPP--- 243
Cdd:PTZ00402 202 NENKAMRDPVIYRVNLTPHARQG----TKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPive 277
|
250 260
....*....|....*....|...
gi 1655147397 244 KFGHMSLIISKDTGKKLSKRDET 266
Cdd:PTZ00402 278 DFSRLNMEYSVMSKRKLTQLVDT 300
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
6-261 |
1.66e-14 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 75.82 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 6 IRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDwdegPDKPGeygpyR 85
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK----PDSVS-----F 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 86 QSERFDIYKPYIQQLLDEGKAYKSYRTEDELE---ADREAQRARHEMPHYEYEYAGMsddeikdaMAKAEAKGLKPVIRF 162
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKkerADRAESKHRNQSPEEALEMFKE--------MCSGKEEGGAWCLRA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 163 HVPAHKTyawDDMVKGKVSFDSDTIGGDFVIVKADGIPTYNFAVVLDDHLMKISHVFRGDDHVANTPKQLMVYEAFGWTP 242
Cdd:PLN03233 155 KIDMQSD---NGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRR 231
|
250 260
....*....|....*....|..
gi 1655147397 243 PK---FGHMSLIISKDTGKKLS 261
Cdd:PLN03233 232 PRihaFARMNFMNTVLSKRKLT 253
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
6-107 |
4.19e-12 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 68.60 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 6 IRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGLDWDEgpdkpGEYgpyr 85
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDA-----VTY---- 284
|
90 100
....*....|....*....|..
gi 1655147397 86 QSERFDIYKPYIQQLLDEGKAY 107
Cdd:PLN02907 285 TSDYFPQLMEMAEKLIKEGKAY 306
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
9-292 |
3.83e-11 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 65.39 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 9 RYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDTKRNVADGEKSQLDNLRWLGldWDegPDkpgeYGPYrQSE 88
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMG--WK--PD----WVTF-SSD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 89 RFDIYKPYIQQLLDEGKAYKSYRTEDELEADREaqrARHEMP-----------HYEYEYAGMSDDEIKDAMAKAEAKGLK 157
Cdd:PTZ00437 126 YFDQLHEFAVQLIKDGKAYVDHSTPDELKQQRE---QREDSPwrnrsveenllLFEHMRQGRYAEGEATLRVKADMKSDN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 158 PVIRfhvpahktyawdDMVKGKVSFDSDTIGGDfvivKADGIPTYNFAVVLDDHLMKISHVF-------RGDDHVAnTPK 230
Cdd:PTZ00437 203 PNMR------------DFIAYRVKYVEHPHAKD----KWCIYPSYDFTHCLIDSLEDIDYSLctlefetRRESYFW-LLE 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655147397 231 QLMVYEAFGWtppKFGHMSLiiskdTGKKLSKR--------------DETVLQFIEQYRKLGYLPDALLNFIILLG 292
Cdd:PTZ00437 266 ELNLWRPHVW---EFSRLNV-----TGSLLSKRkinvlvrkgivrgfDDPRLLTLAGMRRRGYTPAAINRFCELVG 333
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
3-107 |
2.70e-09 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 59.35 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 3 NDSIRVRYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTD-TKRNVadgE--KSQLDNLRWLGLDWDEgpdkpg 79
Cdd:PRK05347 27 HTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNpEKEDQ---EyvDSIKEDVRWLGFDWSG------ 97
|
90 100
....*....|....*....|....*....
gi 1655147397 80 eyGPYRQSERFD-IYKpYIQQLLDEGKAY 107
Cdd:PRK05347 98 --ELRYASDYFDqLYE-YAVELIKKGKAY 123
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
9-124 |
1.44e-05 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 47.83 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 9 RYAPSPTGHLHIGNARTALFNYLFARHYKGKFIIRIEDTDtkrnvADGEKSQ-LDNL----RWLGldWDegpdkpgeygP 83
Cdd:PLN02859 268 RFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEKKEyIDHIeeivEWMG--WE----------P 330
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1655147397 84 YRQSERFDiykpYIQQLLD-------EGKAYKSYRTEDELEADREAQR 124
Cdd:PLN02859 331 FKITYTSD----YFQELYElavelirRGHAYVDHQTPEEIKEYREKKM 374
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
8-58 |
6.60e-04 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 40.16 E-value: 6.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655147397 8 VRYAPSPTGHLHIGNARTALFNYLFAR-----HYKGKFIIRIEDTDTKRNVADGEK 58
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQayrklGYKVRCIALIDDAGGLIGDPANKK 57
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
12-263 |
8.44e-04 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 42.06 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 12 PSPTGHLHIGNARTALFNYLFARHYK--GKFIIR---IEDTDTkrnvadgeksQLDNL-----RWlGLDWDEGPDKPGEY 81
Cdd:COG0018 125 ANPTKPLHVGHLRGAVIGDALARILEaaGYDVTRenyINDAGT----------QIGKLalsleRY-GEEEIEPESKPDGY 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 82 G--PYRqseRFDIYKPYIQQLLDEGKAYKsyrteDELEA-DREAQRARHEMphYEYEYAGMSDD---------------- 142
Cdd:COG0018 194 LgdLYV---KFHKEYEEDPELEDIARELL-----AKLEPgDEEALELWKKA--VDWSLEEIKEDlkrlgvefdvwfsess 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655147397 143 -----EIKDAMAKAEAKGLkpvirfhvpahkTYaWDDmvkGKVSFDSDTIGG--DFVIVKADGIPTY------------- 202
Cdd:COG0018 264 lydsgAVEEVVEELKEKGL------------LY-ESD---GALWVRLTEFGDdkDRVLVKSDGTYTYfttdiayhlykfe 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655147397 203 --NFAVVLD----DHlmkishvfrgDDHVantpKQLM-VYEAFGWTPPK------FGHMSLiisKDtGKKLSKR 263
Cdd:COG0018 328 ryGFDRVIYvvgaDQ----------HGHF----KRLFaALKALGYDPAKdlehllFGMVNL---RD-GEKMSTR 383
|
|
| |
