|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-481 |
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: 646.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 1 MSDRIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDEsvdkdngy 80
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 81 GPYRQSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGEMPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVP 160
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 161 QNQTySFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFG 240
Cdd:COG0008 153 EEGV-VFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 241 HMSLIVNEERKKLSKRDGQIlqFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQK 320
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 321 LAWVNNQYMKQKDTETVFQLALPHLIKANLipevpseedLSWGRKLIALYQKEMSYAGEIVPLSEMFFKEmPALGEEEQQ 400
Cdd:COG0008 310 LVWLNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIE-REDEKAAKK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 401 VINGEQVPELMTHLFSKLEVLEPFEAAEIKKTIKEVQKETGIKGKQLFMPIRVAVTGQMHGPELPNTIEVLGKEKVLNRL 480
Cdd:COG0008 380 RLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERL 459
|
.
gi 447206538 481 K 481
Cdd:COG0008 460 G 460
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
5-481 |
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: 608.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 5 IRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDEsvdkdngyGPYR 84
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 85 QSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGEMPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVPQNQT 164
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 165 YSFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHMSL 244
Cdd:TIGR00464 154 VSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 245 IVNEERKKLSKRDGqiLQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLAWV 324
Cdd:TIGR00464 234 ILDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 325 NNQYMKQKDTETVFQLALPHLiKANLIPEVPSEEDLswgRKLIALYQKEMSYAGEIVPLSEMFFKEMPALGEEEQQVING 404
Cdd:TIGR00464 312 NAHYIKELPDEELFELLDPHL-KSLVNTDTLNREQL---AELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLK 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447206538 405 EQVPELMTHLFSKLEVLEPFEAAEIKKTIKEVQKETGIKGKQLFMPIRVAVTGQMHGPELPNTIEVLGKEKVLNRLK 481
Cdd:TIGR00464 388 KNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLK 464
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
5-474 |
2.21e-153 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 447.27 E-value: 2.21e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 5 IRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVDKDNGYGPYR 84
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 85 QSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGEMPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVPQNQT 164
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEGS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 165 YSFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHMSL 244
Cdd:PLN02627 206 VKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 245 IVNEERKKLSKRDGQilQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLAWV 324
Cdd:PLN02627 286 ILAPDRSKLSKRHGA--TSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWM 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 325 NNQYMKQKDTETVFQLALPHLIKANLIpevpSEEDLSWGRKLIALYQKEMsyagEIV-----PLSEMFFKEMPA-LGEEE 398
Cdd:PLN02627 364 NGQHLRLLPEEELVKLVGERWKSAGIL----KESDGSFVKEAVELLKDGI----ELVtdadkELLNLLSYPLAAtLSSPE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 399 QQVINGEQVPELMTHLFSKLEVLEPFEAAE-----IKKTIKEVQKETGIKGKQLFMPIRVAVTGQMHGPELPNTIEVLGK 473
Cdd:PLN02627 436 AKTVVEDNFSEVADALIAAYDSGELAAALEeghdgWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGESLVLLHK 515
|
.
gi 447206538 474 E 474
Cdd:PLN02627 516 A 516
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
5-323 |
7.40e-149 |
|
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: 427.51 E-value: 7.40e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 5 IRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDesvdkdngYGPYR 84
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 85 QSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGE--MPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVPQN 162
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSpsRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 163 QTYSFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHM 242
Cdd:pfam00749 154 SPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 243 SLIVNEERKKLSKRDGQILQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLA 322
Cdd:pfam00749 234 YLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
.
gi 447206538 323 W 323
Cdd:pfam00749 314 W 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
5-331 |
6.16e-137 |
|
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: 394.26 E-value: 6.16e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 5 IRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVDKDNGYGPYR 84
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 85 QSERQHIYQPLIDQLLAedkaykcymteeeleaereaqiargempryggqhahlteeqrqqfeaegrqpsirfrvpqnqt 164
Cdd:cd00808 82 QSERLEIYRKYAEKLLE--------------------------------------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 165 ysfddmvkgnisfdsngigdwvivKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHMSL 244
Cdd:cd00808 99 ------------------------KGDGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 245 IVNEERKKLSKRDGQilQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLAWV 324
Cdd:cd00808 155 ILNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWL 232
|
....*..
gi 447206538 325 NNQYMKQ 331
Cdd:cd00808 233 NGQYIRE 239
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-481 |
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: 646.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 1 MSDRIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDEsvdkdngy 80
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 81 GPYRQSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGEMPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVP 160
Cdd:COG0008 73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 161 QNQTySFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFG 240
Cdd:COG0008 153 EEGV-VFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 241 HMSLIVNEERKKLSKRDGQIlqFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQK 320
Cdd:COG0008 232 HLPLILGPDGTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 321 LAWVNNQYMKQKDTETVFQLALPHLIKANLipevpseedLSWGRKLIALYQKEMSYAGEIVPLSEMFFKEmPALGEEEQQ 400
Cdd:COG0008 310 LVWLNGPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERAKTLSELAELARFFFIE-REDEKAAKK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 401 VINGEQVPELMTHLFSKLEVLEPFEAAEIKKTIKEVQKETGIKGKQLFMPIRVAVTGQMHGPELPNTIEVLGKEKVLNRL 480
Cdd:COG0008 380 RLAPEEVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERL 459
|
.
gi 447206538 481 K 481
Cdd:COG0008 460 G 460
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
5-481 |
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: 608.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 5 IRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDEsvdkdngyGPYR 84
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 85 QSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGEMPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVPQNQT 164
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 165 YSFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHMSL 244
Cdd:TIGR00464 154 VSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 245 IVNEERKKLSKRDGqiLQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLAWV 324
Cdd:TIGR00464 234 ILDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 325 NNQYMKQKDTETVFQLALPHLiKANLIPEVPSEEDLswgRKLIALYQKEMSYAGEIVPLSEMFFKEMPALGEEEQQVING 404
Cdd:TIGR00464 312 NAHYIKELPDEELFELLDPHL-KSLVNTDTLNREQL---AELLLLFKERLKTLKEIAELIRLFFEDKKEVDEDAFKKHLK 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447206538 405 EQVPELMTHLFSKLEVLEPFEAAEIKKTIKEVQKETGIKGKQLFMPIRVAVTGQMHGPELPNTIEVLGKEKVLNRLK 481
Cdd:TIGR00464 388 KNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLK 464
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
5-474 |
2.21e-153 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 447.27 E-value: 2.21e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 5 IRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVDKDNGYGPYR 84
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 85 QSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGEMPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVPQNQT 164
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEGS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 165 YSFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHMSL 244
Cdd:PLN02627 206 VKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 245 IVNEERKKLSKRDGQilQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLAWV 324
Cdd:PLN02627 286 ILAPDRSKLSKRHGA--TSVGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWM 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 325 NNQYMKQKDTETVFQLALPHLIKANLIpevpSEEDLSWGRKLIALYQKEMsyagEIV-----PLSEMFFKEMPA-LGEEE 398
Cdd:PLN02627 364 NGQHLRLLPEEELVKLVGERWKSAGIL----KESDGSFVKEAVELLKDGI----ELVtdadkELLNLLSYPLAAtLSSPE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 399 QQVINGEQVPELMTHLFSKLEVLEPFEAAE-----IKKTIKEVQKETGIKGKQLFMPIRVAVTGQMHGPELPNTIEVLGK 473
Cdd:PLN02627 436 AKTVVEDNFSEVADALIAAYDSGELAAALEeghdgWQKWVKAFGKALKRKGKRLFMPLRVALTGKMHGPDVGESLVLLHK 515
|
.
gi 447206538 474 E 474
Cdd:PLN02627 516 A 516
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
5-323 |
7.40e-149 |
|
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: 427.51 E-value: 7.40e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 5 IRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDesvdkdngYGPYR 84
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD--------YGPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 85 QSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGE--MPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVPQN 162
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSpsRDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 163 QTYSFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHM 242
Cdd:pfam00749 154 SPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 243 SLIVNEERKKLSKRDGQILQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLA 322
Cdd:pfam00749 234 YLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
.
gi 447206538 323 W 323
Cdd:pfam00749 314 W 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
5-331 |
6.16e-137 |
|
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: 394.26 E-value: 6.16e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 5 IRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVDKDNGYGPYR 84
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 85 QSERQHIYQPLIDQLLAedkaykcymteeeleaereaqiargempryggqhahlteeqrqqfeaegrqpsirfrvpqnqt 164
Cdd:cd00808 82 QSERLEIYRKYAEKLLE--------------------------------------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 165 ysfddmvkgnisfdsngigdwvivKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHMSL 244
Cdd:cd00808 99 ------------------------KGDGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 245 IVNEERKKLSKRDGQilQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLAWV 324
Cdd:cd00808 155 ILNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWL 232
|
....*..
gi 447206538 325 NNQYMKQ 331
Cdd:cd00808 233 NGQYIRE 239
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
4-331 |
1.52e-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: 255.09 E-value: 1.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 4 RIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDEsvdkdngyGPY 83
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDE--------GPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 84 RQSERQHIYQPLIDQLLaedkaykcymteeeleaereaqiargempryggqhahlteeqrqqfeaegrqpsirfrvpqnq 163
Cdd:cd00418 73 RQSDRFDLYRAYAEELI--------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 164 tysfddmvkgnisfdsngigdwvivKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHMS 243
Cdd:cd00418 90 -------------------------KKGGYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFP 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 244 LIVNEERKKLSKRDGQilQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLAW 323
Cdd:cd00418 145 RLLLEDGTKLSKRKLN--TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEW 222
|
....*...
gi 447206538 324 VNNQYMKQ 331
Cdd:cd00418 223 LNREYIRE 230
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
8-258 |
3.14e-73 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 233.20 E-value: 3.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 8 RYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVdkdngygpYRQSE 87
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPV--------LYQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 88 RQHIYQPLIDQLLAEDKAYKCYMTeeeleaerEAQIARGEM------PRYGGQHAHLTEEQRqqfeaegRQPSIRFRVPq 161
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCS--------RKEIAAAAPappdggGIYPGTCRDLLHGPR-------NPPAWRLRVP- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 162 NQTYSFDDMVKGNISFDSNG-IGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFG 240
Cdd:PRK05710 145 DAVIAFDDRLQGRQHQDLALaVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYL 224
|
250
....*....|....*...
gi 447206538 241 HMSLIVNEERKKLSKRDG 258
Cdd:PRK05710 225 HLPLVLNADGQKLSKQNG 242
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
8-291 |
2.46e-71 |
|
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: 227.42 E-value: 2.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 8 RYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVDkdngygpyRQSE 87
Cdd:TIGR03838 4 RFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVV--------YQSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 88 RQHIYQPLIDQLLAEDKAYKCYMTeeeleaerEAQIA--RGEMPRYGG--QHAHLteeqrqqfEAEGRQPSIRFRVPqNQ 163
Cdd:TIGR03838 76 RHALYQAALDRLLAAGLAYPCQCT--------RKEIAaaRDGGGIYPGtcRNGLP--------GRPGRPAAWRLRVP-DG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 164 TYSFDDMVKGNISFDSNG-IGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHM 242
Cdd:TIGR03838 139 VIAFDDRLQGPQQQDLAAaVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHL 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 447206538 243 SLIVNEERKKLSKRDG-QILqfieqyrDLGYLPEALFNFIALLGWSPEGE 291
Cdd:TIGR03838 219 PLVVNADGEKLSKQNGaPAL-------DDSRPLPALLAALRFLGLPPPPE 261
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
3-285 |
1.28e-42 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 158.86 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 3 DRIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTD--KKRNLEDGETSQFDNLKWLGLDWDESvdkdngy 80
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWDEV------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 81 gpYRQSERQHIYQPLIDQLLAEDKAYKCYMTEeeleaereaqiargempryggqhahltEEQRqQFEAEGRQPSIRFRVP 160
Cdd:PRK04156 173 --VIQSDRLEIYYEYARKLIEMGGAYVCTCDP---------------------------EEFK-ELRDAGKPCPHRDKSP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 161 QNQTYSFDDMVKG-------------NISFDSNGIGDWV---IVK----KDGI-----PTYNFAVAIDDHYMQISDVIRG 215
Cdd:PRK04156 223 EENLELWEKMLDGeykegeavvrvktDLEHPNPSVRDWVafrIVKtphpRVGDkyrvwPTYNFAVAVDDHLLGVTHVLRG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 216 DDHISNTPKQIMIYEAFGWEPPR---FGHMSLivneERKKLSKrdGQILQFIEQY----------------RDLGYLPEA 276
Cdd:PRK04156 303 KDHIDNTEKQRYIYDYFGWEYPEtihYGRLKI----EGFVLST--SKIRKGIEEGeysgwddprlptlralRRRGILPEA 376
|
....*....
gi 447206538 277 LFNFIALLG 285
Cdd:PRK04156 377 IRELIIEVG 385
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
4-288 |
2.08e-39 |
|
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: 142.49 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 4 RIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQF--DNLKWLGLDWDESvdkdngyg 81
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEAYDMipEDLEWLGVKWDEV-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 82 pYRQSERQHIYQPLIDQLLAEDKAYKcymteeeleaereaqiargeMPRYGGqhahlteeqrqqfeaegrqpsiRFRVpq 161
Cdd:cd09287 73 -VIASDRIELYYEYARKLIEMGGAYV--------------------HPRTGS----------------------KYRV-- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 162 nqtysfddmvkgnisfdsngigdWvivkkdgiPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGH 241
Cdd:cd09287 108 -----------------------W--------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIH 156
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 242 MSLIVNE-------------ERKKLSKRDGQILQFIEQYRDLGYLPEALFNFIALLGWSP 288
Cdd:cd09287 157 WGRLKIEggklstskirkgiESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQ 216
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
3-285 |
7.08e-34 |
|
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: 134.18 E-value: 7.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 3 DRIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVdkdngygp 82
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVV-------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 83 yRQSERQHIYQPLIDQLLAEDKAYKCYMTeeeleaereaqiargempryggqhahlTEEQRqQFEAEGRQPSIRFRVPQN 162
Cdd:TIGR00463 164 -YQSDRIETYYDYTRKLIEMGKAYVCDCR---------------------------PEEFR-ELRNRGEACHCRDRSVEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 163 QTYSFDDMVKGNISFDSN-------------GIGDWVIVK-------KDG-----IPTYNFAVAIDDHYMQISDVIRGDD 217
Cdd:TIGR00463 215 NLERWEEMLEGKEEGGSVvvrvktdlkhknpAIRDWVIFRivktphpRTGdkyrvYPTMDFSVAIDDHLLGVTHVLRGKD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 218 HISNTPKQIMIYEAFGWEPPRFGHMSLI-VNE-------------ERKKLSKRDGQILQFIEQYRDLGYLPEALFNFIAL 283
Cdd:TIGR00463 295 HIDNRRKQEYIYRYFGWEPPEFIHWGRLkIDDvralstssarkgiLRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLS 374
|
..
gi 447206538 284 LG 285
Cdd:TIGR00463 375 IG 376
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
336-482 |
4.56e-31 |
|
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: 116.91 E-value: 4.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 336 TVFQLALPHLIKANLipEVPSEEDLswgRKLIALYQKEMSYAGEIVPLSEMFFKEM----PALGEEEQQVINGEQVPELM 411
Cdd:pfam19269 1 ELAELALPYLEEAGL--DGLDDEYL---KKVVPLLKERAETLSELAELADFFFELPleydEEAYAKKKMKTNKEESLEVL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447206538 412 THLFSKLEVLEPFEAAEIKKTIKEVQKETGIKGKQLFMPIRVAVTGQMHGPELPNTIEVLGKEKVLNRLKQ 482
Cdd:pfam19269 76 QELLPRLEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRK 146
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
4-71 |
7.01e-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: 7.01e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447206538 4 RIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWD 71
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY 68
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
4-329 |
9.44e-12 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 67.29 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 4 RIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDesvdkdngYGPY 83
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD--------VGPT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 84 RQSERQHIYQPLIDQLLAEDKAYkCymteeeleaereAQIARGEMP--RYGG-----QHAHLTEEQRQQFE-----AEGR 151
Cdd:PTZ00402 124 YSSDYMDLMYEKAEELIKKGLAY-C------------DKTPREEMQkcRFDGvptkyRDISVEETKRLWNEmkkgsAEGQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 152 QPSIRFRVP-QNQTYSFDDMVKGNISFDSNGIGDwviVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYE 230
Cdd:PTZ00402 191 ETCLRAKISvDNENKAMRDPVIYRVNLTPHARQG---TKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 231 AFGWEPPRFGHMSLIvNEERKKLSKRdgQILQFIEQYRDLGYLPEALFNFIALLgwspegeEEIFSKEEFIKIFDEKRLS 310
Cdd:PTZ00402 268 ALGIRKPIVEDFSRL-NMEYSVMSKR--KLTQLVDTHVVDGWDDPRFPTVRALV-------RRGLKMEALRQFVQEQGMS 337
|
330
....*....|....*....
gi 447206538 311 KSPAFFDKQKLAWVNNQYM 329
Cdd:PTZ00402 338 KTVNFMEWSKLWYFNTQIL 356
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
4-272 |
6.10e-11 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 64.65 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 4 RIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVDKDNGYGPY 83
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 84 RQSERQhiyqpLIDQLLAedkaykcYMTEEELEAEREAQIARGEmprygGQHAHLT-EEQRQQFE------AEGRQPSIR 156
Cdd:PLN03233 91 RCYAII-----LIEEGLA-------YMDDTPQEEMKKERADRAE-----SKHRNQSpEEALEMFKemcsgkEEGGAWCLR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 157 FRVpqnqtysfdDMvkgniSFDSNGIGDWVIVKKD------------GIPTYNFAVAIDDHYMQISDVIRGDDHISNTPK 224
Cdd:PLN03233 154 AKI---------DM-----QSDNGTLRDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQ 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447206538 225 QIMIYEAFGWEPPRFgHMSLIVNEERKKLSKRdgQILQFIEQYRDLGY 272
Cdd:PLN03233 220 FFWIQKALGLRRPRI-HAFARMNFMNTVLSKR--KLTWFVDNGHVTGW 264
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
3-106 |
1.77e-10 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 63.20 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 3 DRIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKrnLEDGE--TSQFDNLKWLGLDWDESVDKDNGY 80
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPE--TEDTEyvEAIKDDVRWLGFDWGEHLYYASDY 107
|
90 100
....*....|....*....|....*.
gi 447206538 81 GPyrqserqHIYQPLIdQLLAEDKAY 106
Cdd:PRK14703 108 FE-------RMYAYAE-QLIKMGLAY 125
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
4-72 |
2.53e-10 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 62.82 E-value: 2.53e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447206538 4 RIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDT--DKKRN------LEDGETsqfdnlkwLGLDWDE 72
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTnpSKESDefveniLKDIET--------LGIKYDA 281
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
3-74 |
3.39e-07 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 52.80 E-value: 3.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447206538 3 DRIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDT--DKkrnlEDGE--TSQFDNLKWLGLDWDESV 74
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTnpEK----EDQEyvDSIKEDVRWLGFDWSGEL 99
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
4-204 |
1.78e-05 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 47.45 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 4 RIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKkrnleDGETSQF-----DNLKWLGldWDesvdkdn 78
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNP-----EAEKKEYidhieEIVEWMG--WE------- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447206538 79 gygPYRQSERQHIYQPLID---QLLAEDKAYKCYMTEEELEAEREAQIARGEMPRYGGQHAHLTEEQRQQFEAEGrQPSI 155
Cdd:PLN02859 330 ---PFKITYTSDYFQELYElavELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEEG-KATL 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447206538 156 RFRVP-QNQTYSFDDMVKGNISFDSN-GIGD-WVIVkkdgiPTYNFAVAIDD 204
Cdd:PLN02859 406 RMKQDmQNDNFNMYDLIAYRIKFTPHpHAGDkWCIY-----PSYDYAHCIVD 452
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
8-70 |
5.43e-04 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 42.66 E-value: 5.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447206538 8 RYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTdkkrNLEDGETSQFDNL----KWLGL--DW 70
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDT----NPETEEQVYIDAImemvKWMGWkpDW 119
|
|
| |
