|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-455 |
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: 528.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 1 MIRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPdigggvgpY 80
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGP--------Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 81 RQSERLHIYQDIAQKLINEKLAYYAvYDGENEI----------HRSFEYPKKFKDKSI-------------VVKFKVvKE 137
Cdd:COG0008 76 YQSDRFDIYYEYAEKLIEKGKAYVC-FCTPEELealretqtapGKPPRYDGRCRDLSPeelermlaageppVLRFKI-PE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 138 DKTNFHDLLKGEMSFENKFFNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMHI 217
Cdd:COG0008 154 EGVVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 218 PLILGNDKTPLSKRHGGTSVDFFKESGILNNALLNYLAILGW-HVDE-EIFNVKKKIHTFDYRNISNKSVVFDYKKLEWL 295
Cdd:COG0008 234 PLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWsKSDDqEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 296 NGQHMRNLDIEELIIKFKEFLKLKNYnlnidetLEYTKDVIIICREKVNTLSQLFEISFSFFTEEynYEENYIKKFLKKK 375
Cdd:COG0008 314 NGPYIRALDDEELAELLAPELPEAGI-------REDLERLVPLVRERAKTLSELAELARFFFIER--EDEKAAKKRLAPE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 376 ETGDILRKAIESFEKLENYEISSIENTLRKIVEDMNLATKKVFQTIRGALLGKLVTPGLFESIEVLGKEKTLKRLKKTLD 455
Cdd:COG0008 385 EVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAID 464
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
2-452 |
1.42e-149 |
|
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: 434.09 E-value: 1.42e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 2 IRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPdigggvgpYR 81
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGP--------YY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 82 QSERLHIYQDIAQKLINEKLAYY---------------------AVYDGEneiHRSF--EYPKKFKDKSI--VVKFKVVK 136
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRcycskerlerlreeqkanketPRYDGR---CRNLheEEIENKLAKGIppVVRFKIPQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 137 EDKTNFHDLLKGEMSFENKFFNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMH 216
Cdd:TIGR00464 151 EAVVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 217 IPLILGNDKTPLSKRHGGTSVDFFKESGILNNALLNYLAILGWHV--DEEIFNVKKKIHTFDYRNISNKSVVFDYKKLEW 294
Cdd:TIGR00464 231 LPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPpdDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 295 LNGQHMRNLDIEELIikfkEFLKLKNYNLNIDETLEYT--KDVIIICREKVNTLSQLFEiSFSFFTEEYNYEENYIKKFL 372
Cdd:TIGR00464 311 LNAHYIKELPDEELF----ELLDPHLKSLVNTDTLNREqlAELLLLFKERLKTLKEIAE-LIRLFFEDKKEVDEDAFKKH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 373 KKKETGDILRKAIESFEKLENYEISSIENTLRKIVEDMNLATKKVFQTIRGALLGKLVTPGLFESIEVLGKEKTLKRLKK 452
Cdd:TIGR00464 386 LKKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA 465
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-446 |
6.48e-138 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 406.82 E-value: 6.48e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 2 IRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPDIGGGVGPYR 81
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 82 QSERLHIYQDIAQKLINEKLAYYA---------------------VYDG------ENEIHRSFEypkkfKDKSIVVKFKV 134
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCfctdeeleamkeeaelkklppRYTGkwatasDEEVQAELA-----KGTPYTYRFRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 135 VKEDKTNFHDLLKGEMSFENKFFNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTF 214
Cdd:PLN02627 201 PKEGSVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 215 MHIPLILGNDKTPLSKRHGGTSVDFFKESGILNNALLNYLAILGWH--VDEEIFNVKKKIHTFDYRNISNKSVVFDYKKL 292
Cdd:PLN02627 281 AHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNdgTENEIFTLEELVEKFSIDRINKSGAVFDSTKL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 293 EWLNGQHMRNLDIEELIIKFKEFLK----LKNYNLN-IDETLEYTKDVIIICREKVNTLSQLFeisfsffteEYNYEENY 367
Cdd:PLN02627 361 KWMNGQHLRLLPEEELVKLVGERWKsagiLKESDGSfVKEAVELLKDGIELVTDADKELLNLL---------SYPLAATL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 368 ----IKKFLKKK--ETGDILRKAIESFEKLENYEISSieNTLRKIV----EDMNLATKKVFQTIRGALLGKLVTPGLFES 437
Cdd:PLN02627 432 sspeAKTVVEDNfsEVADALIAAYDSGELAAALEEGH--DGWQKWVkafgKALKRKGKRLFMPLRVALTGKMHGPDVGES 509
|
....*....
gi 229470602 438 IEVLGKEKT 446
Cdd:PLN02627 510 LVLLHKAGT 518
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
1-302 |
2.82e-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: 371.15 E-value: 2.82e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 1 MIRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPDIGGGVGPY 80
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 81 RQSERLHIYQDIAQKLINEKlayyavydgeneihrsfeypkkfkdksivvkfkvvkedktnfhdllkgemsfenkffndf 160
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 161 iiiksNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMHIPLILGNDKTPLSKRHGGTSVDFF 240
Cdd:cd00808 101 -----DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLSKRKGDTSISDY 175
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229470602 241 KESGILNNALLNYLAILGW--HVDEEIFNVKKKIHTFDYRNISNKSVVFDYKKLEWLNGQHMRN 302
Cdd:cd00808 176 REEGYLPEALLNYLALLGWspPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
1-294 |
1.50e-103 |
|
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: 311.18 E-value: 1.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 1 MIRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPdigggvgpY 80
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGP--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 81 RQSERLHIYQDIAQKLINEKLAY-----------------------YAVYDGENeIHRSFEYPKKFKDKSI--VVKFKVV 135
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYvcfctpeeleeereeqealgspsRDRYDEEN-LHLFEEEMKKGSAEGGpaTVRAKIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 136 KEDKTNFHDLLKGEMSFENKFFNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFM 215
Cdd:pfam00749 152 MESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 216 HIPLILGNDKTPLSKRHGGTSVD--FFKESGILNNALLNYLAILGW--HVDEEIFNVKKKIHTFDYRNISNKSVVFDYKK 291
Cdd:pfam00749 232 HEYLRLNLDGTKLSKRKLSWSVDisQVKGWGDPREATLNGLRRRGWtpEGIREFFTREGVIKSFDVNRLSKSLEAFDRKK 311
|
...
gi 229470602 292 LEW 294
Cdd:pfam00749 312 LDW 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-455 |
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: 528.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 1 MIRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPdigggvgpY 80
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGP--------Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 81 RQSERLHIYQDIAQKLINEKLAYYAvYDGENEI----------HRSFEYPKKFKDKSI-------------VVKFKVvKE 137
Cdd:COG0008 76 YQSDRFDIYYEYAEKLIEKGKAYVC-FCTPEELealretqtapGKPPRYDGRCRDLSPeelermlaageppVLRFKI-PE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 138 DKTNFHDLLKGEMSFENKFFNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMHI 217
Cdd:COG0008 154 EGVVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 218 PLILGNDKTPLSKRHGGTSVDFFKESGILNNALLNYLAILGW-HVDE-EIFNVKKKIHTFDYRNISNKSVVFDYKKLEWL 295
Cdd:COG0008 234 PLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWsKSDDqEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 296 NGQHMRNLDIEELIIKFKEFLKLKNYnlnidetLEYTKDVIIICREKVNTLSQLFEISFSFFTEEynYEENYIKKFLKKK 375
Cdd:COG0008 314 NGPYIRALDDEELAELLAPELPEAGI-------REDLERLVPLVRERAKTLSELAELARFFFIER--EDEKAAKKRLAPE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 376 ETGDILRKAIESFEKLENYEISSIENTLRKIVEDMNLATKKVFQTIRGALLGKLVTPGLFESIEVLGKEKTLKRLKKTLD 455
Cdd:COG0008 385 EVRKVLKAALEVLEAVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAID 464
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
2-452 |
1.42e-149 |
|
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: 434.09 E-value: 1.42e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 2 IRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPdigggvgpYR 81
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGP--------YY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 82 QSERLHIYQDIAQKLINEKLAYY---------------------AVYDGEneiHRSF--EYPKKFKDKSI--VVKFKVVK 136
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRcycskerlerlreeqkanketPRYDGR---CRNLheEEIENKLAKGIppVVRFKIPQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 137 EDKTNFHDLLKGEMSFENKFFNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMH 216
Cdd:TIGR00464 151 EAVVSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 217 IPLILGNDKTPLSKRHGGTSVDFFKESGILNNALLNYLAILGWHV--DEEIFNVKKKIHTFDYRNISNKSVVFDYKKLEW 294
Cdd:TIGR00464 231 LPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPpdDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 295 LNGQHMRNLDIEELIikfkEFLKLKNYNLNIDETLEYT--KDVIIICREKVNTLSQLFEiSFSFFTEEYNYEENYIKKFL 372
Cdd:TIGR00464 311 LNAHYIKELPDEELF----ELLDPHLKSLVNTDTLNREqlAELLLLFKERLKTLKEIAE-LIRLFFEDKKEVDEDAFKKH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 373 KKKETGDILRKAIESFEKLENYEISSIENTLRKIVEDMNLATKKVFQTIRGALLGKLVTPGLFESIEVLGKEKTLKRLKK 452
Cdd:TIGR00464 386 LKKNVKEVLEALKKKLQALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKRLKA 465
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-446 |
6.48e-138 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 406.82 E-value: 6.48e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 2 IRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPDIGGGVGPYR 81
Cdd:PLN02627 46 VRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGPYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 82 QSERLHIYQDIAQKLINEKLAYYA---------------------VYDG------ENEIHRSFEypkkfKDKSIVVKFKV 134
Cdd:PLN02627 126 QSERNAIYKQYAEKLLESGHVYPCfctdeeleamkeeaelkklppRYTGkwatasDEEVQAELA-----KGTPYTYRFRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 135 VKEDKTNFHDLLKGEMSFENKFFNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTF 214
Cdd:PLN02627 201 PKEGSVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 215 MHIPLILGNDKTPLSKRHGGTSVDFFKESGILNNALLNYLAILGWH--VDEEIFNVKKKIHTFDYRNISNKSVVFDYKKL 292
Cdd:PLN02627 281 AHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNdgTENEIFTLEELVEKFSIDRINKSGAVFDSTKL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 293 EWLNGQHMRNLDIEELIIKFKEFLK----LKNYNLN-IDETLEYTKDVIIICREKVNTLSQLFeisfsffteEYNYEENY 367
Cdd:PLN02627 361 KWMNGQHLRLLPEEELVKLVGERWKsagiLKESDGSfVKEAVELLKDGIELVTDADKELLNLL---------SYPLAATL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 368 ----IKKFLKKK--ETGDILRKAIESFEKLENYEISSieNTLRKIV----EDMNLATKKVFQTIRGALLGKLVTPGLFES 437
Cdd:PLN02627 432 sspeAKTVVEDNfsEVADALIAAYDSGELAAALEEGH--DGWQKWVkafgKALKRKGKRLFMPLRVALTGKMHGPDVGES 509
|
....*....
gi 229470602 438 IEVLGKEKT 446
Cdd:PLN02627 510 LVLLHKAGT 518
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
1-302 |
2.82e-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: 371.15 E-value: 2.82e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 1 MIRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPDIGGGVGPY 80
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 81 RQSERLHIYQDIAQKLINEKlayyavydgeneihrsfeypkkfkdksivvkfkvvkedktnfhdllkgemsfenkffndf 160
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 161 iiiksNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMHIPLILGNDKTPLSKRHGGTSVDFF 240
Cdd:cd00808 101 -----DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLSKRKGDTSISDY 175
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229470602 241 KESGILNNALLNYLAILGW--HVDEEIFNVKKKIHTFDYRNISNKSVVFDYKKLEWLNGQHMRN 302
Cdd:cd00808 176 REEGYLPEALLNYLALLGWspPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLNGQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
1-294 |
1.50e-103 |
|
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: 311.18 E-value: 1.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 1 MIRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPdigggvgpY 80
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGP--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 81 RQSERLHIYQDIAQKLINEKLAY-----------------------YAVYDGENeIHRSFEYPKKFKDKSI--VVKFKVV 135
Cdd:pfam00749 73 YQSDRFDIYYKYAEELIKKGKAYvcfctpeeleeereeqealgspsRDRYDEEN-LHLFEEEMKKGSAEGGpaTVRAKIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 136 KEDKTNFHDLLKGEMSFENKFFNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFM 215
Cdd:pfam00749 152 MESPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 216 HIPLILGNDKTPLSKRHGGTSVD--FFKESGILNNALLNYLAILGW--HVDEEIFNVKKKIHTFDYRNISNKSVVFDYKK 291
Cdd:pfam00749 232 HEYLRLNLDGTKLSKRKLSWSVDisQVKGWGDPREATLNGLRRRGWtpEGIREFFTREGVIKSFDVNRLSKSLEAFDRKK 311
|
...
gi 229470602 292 LEW 294
Cdd:pfam00749 312 LDW 314
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
1-302 |
2.78e-85 |
|
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: 261.25 E-value: 2.78e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 1 MIRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPdigggvgpY 80
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGP--------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 81 RQSERLHIYQDIAQKLINEklayyavydgeneihrsfeypkkfkdksivvkfkvvkedktnfhdllkgemsfenkffndf 160
Cdd:cd00418 73 RQSDRFDLYRAYAEELIKK------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 161 iiiksNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMHIPLILGNDKTPLSKRHGGTSVDFF 240
Cdd:cd00418 92 -----GGYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLSKRKLNTTLRAL 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229470602 241 KESGILNNALLNYLAILGW--HVDEEIFNVKKKIHTFDYRNISNKSVVFDYKKLEWLNGQHMRN 302
Cdd:cd00418 167 RRRGYLPEALRNYLALIGWskPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEWLNREYIRE 230
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
5-264 |
2.69e-69 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 222.42 E-value: 2.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 5 RFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDeGPdigggvgPYRQSE 84
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWD-GP-------VLYQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 85 RLHIYQDIAQKLINEKLAYYA-------------------VYDGeneIHRSFEYPKKfKDKSIVVKfkvVKEDKTNFHDL 145
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCfcsrkeiaaaapappdgggIYPG---TCRDLLHGPR-NPPAWRLR---VPDAVIAFDDR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 146 LKGEMSFENKF-FNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMHIPLILGND 224
Cdd:PRK05710 154 LQGRQHQDLALaVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNAD 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 229470602 225 KTPLSKRHGGTSVDffkESGILnnALLNY-LAILGWHVDEE 264
Cdd:PRK05710 234 GQKLSKQNGAPALD---AAGPL--PVLAAaLRFLGQPPPAA 269
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
5-264 |
2.70e-65 |
|
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: 211.25 E-value: 2.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 5 RFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEGPDigggvgpyRQSE 84
Cdd:TIGR03838 4 RFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVV--------YQSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 85 RLHIYQDIAQKLINEKLAYY---------------AVYDGE--NEIHRsfeypKKFKDKSIVVKfkvVKEDKTNFHDLLK 147
Cdd:TIGR03838 76 RHALYQAALDRLLAAGLAYPcqctrkeiaaardggGIYPGTcrNGLPG-----RPGRPAAWRLR---VPDGVIAFDDRLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 148 GEMSFENKF-FNDFIIIKSNGFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMHIPLILGNDKT 226
Cdd:TIGR03838 148 GPQQQDLAAaVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGE 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 229470602 227 PLSKRHGGTSVDffkESGILnNALLNYLAILGWHVDEE 264
Cdd:TIGR03838 228 KLSKQNGAPALD---DSRPL-PALLAALRFLGLPPPPE 261
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
2-216 |
3.83e-46 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 168.11 E-value: 3.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 2 IRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTD--TERSTKE-YETkILSALEWLGLNWDEgpdigggvg 78
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEaYDM-ILEDLKWLGVKWDE--------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 79 PYRQSERLHIYQDIAQKLINEKLAYYAVYDGEneihrsfEYpKKFKDKSIVVK--FKVVKEDKTNFHDLLKGEM------ 150
Cdd:PRK04156 172 VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPE-------EF-KELRDAGKPCPhrDKSPEENLELWEKMLDGEYkegeav 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 151 -------SFENKFFNDFI---IIKSNG---------FPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKN 211
Cdd:PRK04156 244 vrvktdlEHPNPSVRDWVafrIVKTPHprvgdkyrvWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEY 323
|
....*
gi 229470602 212 PTFMH 216
Cdd:PRK04156 324 PETIH 328
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
2-216 |
7.67e-43 |
|
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: 151.35 E-value: 7.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 2 IRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYET--KILSALEWLGLNWDEgpdigggvgP 79
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEAydMIPEDLEWLGVKWDE---------V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 80 YRQSERLHIYQDIAQKLINEKLAYyavydgeneIHRsfeypkKFKDKSIVvkfkvvkedktnfhdllkgemsfenkffnd 159
Cdd:cd09287 73 VIASDRIELYYEYARKLIEMGGAY---------VHP------RTGSKYRV------------------------------ 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 229470602 160 fiiiksngFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMH 216
Cdd:cd09287 108 --------WPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIH 156
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
4-216 |
1.05e-33 |
|
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: 133.41 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 4 LRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEgpdigggvgPYRQS 83
Cdd:TIGR00463 96 MRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDE---------VVYQS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 84 ERLHIYQDIAQKLINEKLAYyaVYDGENEIHRSFE---YPKKFKDKSIVVKFKVVKEDKTNFHDL------LKGEMSFEN 154
Cdd:TIGR00463 167 DRIETYYDYTRKLIEMGKAY--VCDCRPEEFRELRnrgEACHCRDRSVEENLERWEEMLEGKEEGgsvvvrVKTDLKHKN 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229470602 155 KFFNDFIIIKSNG------------FPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPTFMH 216
Cdd:TIGR00463 245 PAIRDWVIFRIVKtphprtgdkyrvYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIH 318
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
307-454 |
4.64e-29 |
|
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: 111.13 E-value: 4.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 307 ELIIKFKEFLKLKNYNLNIDETLeytKDVIIICREKVNTLSQLFEISFSFFTEEYNYEENYIKKFLKKK---ETGDILRK 383
Cdd:pfam19269 1 ELAELALPYLEEAGLDGLDDEYL---KKVVPLLKERAETLSELAELADFFFELPLEYDEEAYAKKKMKTnkeESLEVLQE 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 229470602 384 AIESFEKLENYEISSIENTLRKIVEDMNLATKKVFQTIRGALLGKLVTPGLFESIEVLGKEKTLKRLKKTL 454
Cdd:pfam19269 78 LLPRLEALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
2-118 |
1.56e-18 |
|
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: 84.61 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 2 IRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEgpdigggvgPYR 81
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYK---------VTY 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 229470602 82 QSERLHIYQDIAQKLINEKLAY-----------YAVYDGENEIHRSFE 118
Cdd:cd00807 73 ASDYFDQLYEYAEQLIKKGKAYvhhrtgdkwciYPTYDFAHPIVDSIE 120
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
5-213 |
5.23e-18 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 86.55 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 5 RFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDegpdigggVGPYRQSE 84
Cdd:PTZ00402 56 RFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD--------VGPTYSSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 85 RLHIYQDIAQKLINEKLAYYAVYDGENEIHRSFE-YPKKFKDKSIVVKFKVVKEDKTNFHD----LLKGEMSF--ENKFF 157
Cdd:PTZ00402 128 YMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDgVPTKYRDISVEETKRLWNEMKKGSAEgqetCLRAKISVdnENKAM 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229470602 158 NDFIIIKSN------------GFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNPT 213
Cdd:PTZ00402 208 RDPVIYRVNltpharqgtkykAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPI 275
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
5-244 |
3.43e-15 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 77.74 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 5 RFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNwdegPDIGGGVGPYRQSE 84
Cdd:PLN03233 15 RFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK----PDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 85 RLHiyqdiAQKLINEKLAYYAVYDGEN-EIHRSFEYPKKFKDKSIVVKFKVVKEDKTNFHD------LLKGEMSFENKFF 157
Cdd:PLN03233 91 RCY-----AIILIEEGLAYMDDTPQEEmKKERADRAESKHRNQSPEEALEMFKEMCSGKEEggawclRAKIDMQSDNGTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 158 NDFIIIKSN------------GFPTYNFAVVVDDHFMKISHVFRGEDHLSNTPKQIMIYNALGWKNP---TFMHIPLIlg 222
Cdd:PLN03233 166 RDPVLFRQNttphhrsgtaykAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPrihAFARMNFM-- 243
|
250 260
....*....|....*....|..
gi 229470602 223 ndKTPLSKRhggtSVDFFKESG 244
Cdd:PLN03233 244 --NTVLSKR----KLTWFVDNG 259
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
2-103 |
4.67e-12 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 68.21 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 2 IRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDegpdigggVGPYr 81
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD--------AVTY- 284
|
90 100
....*....|....*....|..
gi 229470602 82 QSERLHIYQDIAQKLINEKLAY 103
Cdd:PLN02907 285 TSDYFPQLMEMAEKLIKEGKAY 306
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
5-128 |
2.38e-11 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 65.90 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 5 RFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEgpdigggvGPYRQSE 84
Cdd:PRK14703 35 RFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGE--------HLYYASD 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 229470602 85 RLHIYQDIAQKLINEKLAYYAVYDgENEIHR---SFEYP---KKFKDKSI 128
Cdd:PRK14703 107 YFERMYAYAEQLIKMGLAYVDSVS-EEEIRElrgTVTEPgtpSPYRDRSV 155
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
2-103 |
5.15e-09 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 58.19 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 2 IRLRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGLNWDEgpdigggvGPYR 81
Cdd:PRK05347 30 VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSG--------ELRY 101
|
90 100
....*....|....*....|....*
gi 229470602 82 QS---ERLHiyqDIAQKLINEKLAY 103
Cdd:PRK05347 102 ASdyfDQLY---EYAVELIKKGKAY 123
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
4-72 |
8.57e-08 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 54.60 E-value: 8.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229470602 4 LRFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGlnWDegPD 72
Cdd:PTZ00437 54 FRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMG--WK--PD 118
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
5-186 |
2.18e-07 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 53.22 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 5 RFAPSPTGLLHVGGARTALFNWLYAKKHNGKFIIRIEDTDTERSTKEYETKILSALEWLGlnWDegpdigggvgPYRQSE 84
Cdd:PLN02859 268 RFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WE----------PFKITY 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229470602 85 RLHIYQ---DIAQKLINEKLAYYAVYDGEnEI--HRSFEYPKKFKDKSIVVKFK--------VVKEDKTNFHdlLKGEMS 151
Cdd:PLN02859 336 TSDYFQelyELAVELIRRGHAYVDHQTPE-EIkeYREKKMNSPWRDRPIEESLKlfedmrrgLIEEGKATLR--MKQDMQ 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 229470602 152 FENKFFNDFII--IKSNG----------FPTYNFAVVVDDHFMKISH 186
Cdd:PLN02859 413 NDNFNMYDLIAyrIKFTPhphagdkwciYPSYDYAHCIVDSLENITH 459
|
|
| |
