|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-555 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 962.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 1 MNNKKYHNFICQIIDQDLNKNKNLSFHTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSI 80
Cdd:PRK05347 5 EAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 81 KYDISWLGYKWYGNVHYSSEYFFKLYQYAKQLIYQGLAYVDHLTKEQIREYRGTLNTPGRNSPYRDRTIQENIKLFKKMK 160
Cdd:PRK05347 85 KEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERMR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 161 KGEYNEGEACLRAKIDMNSSFIIMRDPVLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYN 240
Cdd:PRK05347 165 AGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 241 WILENTNVKHYPKQYEFSRLNLEFSILSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNL 320
Cdd:PRK05347 245 WVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 321 IEYSLLEHCIRKELNQTAIRSMAILEPIKIILYNLDKNHKEILIVPNHPNNPDMGTHEILFTNIIYIERSDFKEEYDKKY 400
Cdd:PRK05347 325 IDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 401 KRLRIGEEIRLRYAYIIKAEKIEKDKFNNIINIICYCDTNSL-GKKPKNKKNPAVIHWISIHNALPAEFRLYDQLFNIKN 479
Cdd:PRK05347 405 FRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLsGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPN 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345539328 480 PEQQTNFLSYINPKSLIKKYGFIEKKLEKMiykyimnyNDQLHFQFERIGYFCLDYiDSKKNYLVFNRTVHLRDVW 555
Cdd:PRK05347 485 PAAGKDFLDFLNPDSLVIKQGFVEPSLADA--------KPEDRFQFEREGYFCADK-DSTPGKLVFNRTVGLRDSW 551
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-555 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 722.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYFFKLY 106
Cdd:TIGR00440 2 HTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVDHLTKEQIREYRGTLNTPGRNSPYRDRTIQENIKLFKKMKKGEYNEGEACLRAKIDMNSSFIIMRD 186
Cdd:TIGR00440 82 RYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 187 PVLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHYPKQYEFSRLNLEFSI 266
Cdd:TIGR00440 162 PVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 267 LSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIRSMAILE 346
Cdd:TIGR00440 242 LSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVID 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 347 PIKIILYNLDKNHkEILIVPNHPNNPDMGTHEILFTNIIYIERSDFKEEYDKKYKRLRIGEEIRLRYAYIIKAEKIEKDK 426
Cdd:TIGR00440 322 PVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 427 FNNIINIICYCDTNSLGKKPKN-KKNPAVIHWISIHNALPAEFRLYDQLFNIKNPEQQTNFLSYINPKSLIKKYGFIEKK 505
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADgRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 345539328 506 LEKMIykyimnynDQLHFQFERIGYFCLDYIDSKKNYLVFNRTVHLRDVW 555
Cdd:TIGR00440 481 LGDAV--------ANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
27-335 |
6.28e-126 |
|
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: 371.65 E-value: 6.28e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYFFKLY 106
Cdd:pfam00749 3 RTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVDHLTKEQIREYRGTLntPGRNSPYRDRTIQENIKLF-KKMKKGEYNEGEACLRAKIDMNSSfIIMR 185
Cdd:pfam00749 83 KYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 186 DPVLYRILFA---HHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHYPKQYEFSRLNL 262
Cdd:pfam00749 160 DPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345539328 263 EFSILSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQ-NNLIEYSLLEHCIRKELN 335
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-340 |
8.98e-121 |
|
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: 355.41 E-value: 8.98e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYgNVHYSSEYFFKLY 106
Cdd:cd00807 3 VTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVdhltkeqireyrgtlntpgrnspyrdrtiqeniklfkkmkkgeynegeaclrakidmnssfiimrd 186
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 187 pvlyrilfahHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHyPKQYEFSRLNLEFSI 266
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYTV 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345539328 267 LSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIR 340
Cdd:cd00807 165 MSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
27-399 |
2.78e-96 |
|
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: 300.94 E-value: 2.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYFFKLY 106
Cdd:COG0008 6 RTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVDHLTKEQIREYRGTLNTPGRNSPY----RDRTIQEnikLFKKMKKGEynegEACLRAKI------- 175
Cdd:COG0008 86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE---LERMLAAGE----PPVLRFKIpeegvvf 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 176 -DMNSSFII-----MRDPVLYRilfahhhqtKDDwyiYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVK 249
Cdd:COG0008 159 dDLVRGEITfpnpnLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 250 HyPkqyEFSRLNL----EFSILSKRKlkiliddNIVegwndprisTISGLRRKGYTPSSIKHFCQKIGITKQNN--LIEY 323
Cdd:COG0008 227 P-P---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqeIFSL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 324 SLLEHCIrkELNQTAiRSMAILEPIKIILYNLDKNHK-------EILIvpnhPNNPDMGTHEIL---------------- 380
Cdd:COG0008 287 EELIEAF--DLDRVS-RSPAVFDPVKLVWLNGPYIRAlddeelaELLA----PELPEAGIREDLerlvplvreraktlse 359
|
410 420
....*....|....*....|..
gi 345539328 381 ---FTNIIYIERSDfkEEYDKK 399
Cdd:COG0008 360 laeLARFFFIERED--EKAAKK 379
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-555 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 962.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 1 MNNKKYHNFICQIIDQDLNKNKNLSFHTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSI 80
Cdd:PRK05347 5 EAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 81 KYDISWLGYKWYGNVHYSSEYFFKLYQYAKQLIYQGLAYVDHLTKEQIREYRGTLNTPGRNSPYRDRTIQENIKLFKKMK 160
Cdd:PRK05347 85 KEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERMR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 161 KGEYNEGEACLRAKIDMNSSFIIMRDPVLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYN 240
Cdd:PRK05347 165 AGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 241 WILENTNVKHYPKQYEFSRLNLEFSILSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNL 320
Cdd:PRK05347 245 WVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 321 IEYSLLEHCIRKELNQTAIRSMAILEPIKIILYNLDKNHKEILIVPNHPNNPDMGTHEILFTNIIYIERSDFKEEYDKKY 400
Cdd:PRK05347 325 IDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 401 KRLRIGEEIRLRYAYIIKAEKIEKDKFNNIINIICYCDTNSL-GKKPKNKKNPAVIHWISIHNALPAEFRLYDQLFNIKN 479
Cdd:PRK05347 405 FRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLsGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPN 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345539328 480 PEQQTNFLSYINPKSLIKKYGFIEKKLEKMiykyimnyNDQLHFQFERIGYFCLDYiDSKKNYLVFNRTVHLRDVW 555
Cdd:PRK05347 485 PAAGKDFLDFLNPDSLVIKQGFVEPSLADA--------KPEDRFQFEREGYFCADK-DSTPGKLVFNRTVGLRDSW 551
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-555 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 722.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYFFKLY 106
Cdd:TIGR00440 2 HTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVDHLTKEQIREYRGTLNTPGRNSPYRDRTIQENIKLFKKMKKGEYNEGEACLRAKIDMNSSFIIMRD 186
Cdd:TIGR00440 82 RYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 187 PVLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHYPKQYEFSRLNLEFSI 266
Cdd:TIGR00440 162 PVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 267 LSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIRSMAILE 346
Cdd:TIGR00440 242 LSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVID 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 347 PIKIILYNLDKNHkEILIVPNHPNNPDMGTHEILFTNIIYIERSDFKEEYDKKYKRLRIGEEIRLRYAYIIKAEKIEKDK 426
Cdd:TIGR00440 322 PVEVVIENLSDEY-ELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 427 FNNIINIICYCDTNSLGKKPKN-KKNPAVIHWISIHNALPAEFRLYDQLFNIKNPEQQTNFLSYINPKSLIKKYGFIEKK 505
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADgRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 345539328 506 LEKMIykyimnynDQLHFQFERIGYFCLDYIDSKKNYLVFNRTVHLRDVW 555
Cdd:TIGR00440 481 LGDAV--------ANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
8-555 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 702.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 8 NFICQIIDQDLNKNKNLSFHTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWL 87
Cdd:PRK14703 14 NFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 88 GYKWYGNVHYSSEYFFKLYQYAKQLIYQGLAYVDHLTKEQIREYRGTLNTPGRNSPYRDRTIQENIKLFKKMKKGEYNEG 167
Cdd:PRK14703 94 GFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 168 EACLRAKIDMNSSFIIMRDPVLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTN 247
Cdd:PRK14703 174 AHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 248 VKH-YPKQYEFSRLNLEFSILSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLL 326
Cdd:PRK14703 254 PWPpRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 327 EHCIRKELNQTAIRSMAILEPIKIILYNLDKNHKEILIVPNHPNN-PDMGTHEILFTNIIYIERSDFKEEYDKKYKRLRI 405
Cdd:PRK14703 334 EFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 406 GEEIRLRYAYIIKAEKIEKDKFNNIINIICYCDTNSLGKKPKNKKNPAVIHWISIHNALPAEFRLYDQLFNIKNPEQ-QT 484
Cdd:PRK14703 414 GREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEAaDE 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 345539328 485 NFLSYINPKSLIKKYGFIEKKLekmiykyIMNYNDQlHFQFERIGYFCLDYIDSKKNYLVFNRTVHLRDVW 555
Cdd:PRK14703 494 DFLEFLNPDSLRVAQGRVEPAV-------RDDPADT-RYQFERQGYFWADPVDSRPDALVFNRIITLKDTW 556
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
26-553 |
1.98e-165 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 489.66 E-value: 1.98e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 26 FHTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYgNVHYSSEYFFKL 105
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPF-KITYTSDYFQEL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 106 YQYAKQLIYQGLAYVDHLTKEQIREYRGTLntpgRNSPYRDRTIQENIKLFKKMKKGEYNEGEACLRAKIDMNSSFIIMR 185
Cdd:PLN02859 344 YELAVELIRRGHAYVDHQTPEEIKEYREKK----MNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMY 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 186 DPVLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVkHYPKQYEFSRLNLEFS 265
Cdd:PLN02859 420 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGL-YQPYVWEYSRLNVTNT 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 266 ILSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNN-LIEYSLLEHCIRKELNQTAIRSMAI 344
Cdd:PLN02859 499 VMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIRMDRLEHHIREELNKTAPRTMVV 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 345 LEPIKIILYNLDKNHKEIL---IVPNHPNNPDMGTHEILFTNIIYIERSDFKEEYDKKYKRLRIGEEIRLRYAYIIK-AE 420
Cdd:PLN02859 579 LHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKcTD 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 421 KIEKDKFNNIINIICYCDTnslgkkPKNKKNPAVIHWISI----HNALPAEFRLYDQLFNIKNPEQQTNFLSYINPKSLI 496
Cdd:PLN02859 659 VVLADDNETVVEIRAEYDP------EKKTKPKGVLHWVAEpspgVEPLKVEVRLFDKLFLSENPAELEDWLEDLNPQSKE 732
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 497 K---KYGFIEKKLEKMIYKyimnyndqlhFQFERIGYFCLDYiDSKKNYLVFNRTVHLRD 553
Cdd:PLN02859 733 VisgAYAVPSLKDAKVGDR----------FQFERLGYFAVDK-DSTPEKLVFNRTVTLKD 781
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
29-553 |
9.18e-154 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 452.51 E-value: 9.18e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 29 RFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYK--WygnVHYSSEYFFKLY 106
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKpdW---VTFSSDYFDQLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVDHLTKEQIREYRGTLntpgRNSPYRDRTIQENIKLFKKMKKGEYNEGEACLRAKIDMNSSFIIMRD 186
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQREQR----EDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 187 PVLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHyPKQYEFSRLNLEFSI 266
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWR-PHVWEFSRLNVTGSL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 267 LSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIRSMAILE 346
Cdd:PTZ00437 287 LSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVID 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 347 PIKIILYNLDKnhKEILIVPNHPNNPDMGTHEILFTNIIYIERSDFK-EEYDKKYKRLRIGEE-IRLRYAYIIKAEKIEK 424
Cdd:PTZ00437 367 PIKVVVDNWKG--EREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGPRvVGLKYSGNVVCKGFEV 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 425 DKFNNIINIICYCDtnslgkKPKNKKNPAVIHWISIHNALPAEFRLYDQLFNIKNPEQQTNFLSYINPKSLIKKYGFIEK 504
Cdd:PTZ00437 445 DAAGQPSVIHVDID------FERKDKPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEK 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 345539328 505 KLEKMiykyimnyndqLHF---QFERIGYFCLDyIDSKKNYLVFNRTVHLRD 553
Cdd:PTZ00437 519 GIENA-----------KHFesvQAERFGYFVVD-PDTRPDHLVMNRVLGLRE 558
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
27-335 |
6.28e-126 |
|
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: 371.65 E-value: 6.28e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYFFKLY 106
Cdd:pfam00749 3 RTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVDHLTKEQIREYRGTLntPGRNSPYRDRTIQENIKLF-KKMKKGEYNEGEACLRAKIDMNSSfIIMR 185
Cdd:pfam00749 83 KYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 186 DPVLYRILFA---HHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHYPKQYEFSRLNL 262
Cdd:pfam00749 160 DPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345539328 263 EFSILSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQ-NNLIEYSLLEHCIRKELN 335
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-340 |
8.98e-121 |
|
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: 355.41 E-value: 8.98e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYgNVHYSSEYFFKLY 106
Cdd:cd00807 3 VTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVdhltkeqireyrgtlntpgrnspyrdrtiqeniklfkkmkkgeynegeaclrakidmnssfiimrd 186
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 187 pvlyrilfahHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHyPKQYEFSRLNLEFSI 266
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYTV 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345539328 267 LSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIR 340
Cdd:cd00807 165 MSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
28-545 |
2.13e-104 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 329.76 E-value: 2.13e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 28 TRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKwYGNVHYSSEYFFKLYQ 107
Cdd:PLN02907 216 TRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIK-YDAVTYTSDYFPQLME 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 108 YAKQLIYQGLAYVDHLTKEQIREYRGTlntpGRNSPYRDRTIQENIKLFKKMKKGEYNEGEACLRAKIDMNSSFIIMRDP 187
Cdd:PLN02907 295 MAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 188 VLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHYpKQYEFSRLNLEFSIL 267
Cdd:PLN02907 371 VYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKV-HIWEFSRLNFVYTLL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 268 SKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIRSMAILEP 347
Cdd:PLN02907 450 SKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKE 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 348 IKIILYNLDKNHK-EILIVPNHPNNPDMGTHEILFTNIIYIERSDfkeeydkkYKRLRIGEEIRLRY--AYIIKaeKIEK 424
Cdd:PLN02907 530 GRVLLTLTDGPETpFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD--------AEAISEGEEVTLMDwgNAIIK--EITK 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 425 DKFNNIINIICycdtnSLGKKPKNKKNPAVIHWISIHNAL-PAEFRLYDQLFNIKNPEQQTNFLSYINPKSlikkygfie 503
Cdd:PLN02907 600 DEGGAVTALSG-----ELHLEGSVKTTKLKLTWLPDTNELvPLSLVEFDYLITKKKLEEDDNFLDVLNPCT--------- 665
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 345539328 504 kKLEKMIY--KYIMNYNDQLHFQFERIGYFCLD--YIDSKKNYLVF 545
Cdd:PLN02907 666 -KKETAALgdSNMRNLKRGEIIQLERKGYYRCDapFVRSSKPIVLF 710
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
27-399 |
2.78e-96 |
|
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: 300.94 E-value: 2.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYFFKLY 106
Cdd:COG0008 6 RTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVDHLTKEQIREYRGTLNTPGRNSPY----RDRTIQEnikLFKKMKKGEynegEACLRAKI------- 175
Cdd:COG0008 86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE---LERMLAAGE----PPVLRFKIpeegvvf 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 176 -DMNSSFII-----MRDPVLYRilfahhhqtKDDwyiYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVK 249
Cdd:COG0008 159 dDLVRGEITfpnpnLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 250 HyPkqyEFSRLNL----EFSILSKRKlkiliddNIVegwndprisTISGLRRKGYTPSSIKHFCQKIGITKQNN--LIEY 323
Cdd:COG0008 227 P-P---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqeIFSL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 324 SLLEHCIrkELNQTAiRSMAILEPIKIILYNLDKNHK-------EILIvpnhPNNPDMGTHEIL---------------- 380
Cdd:COG0008 287 EELIEAF--DLDRVS-RSPAVFDPVKLVWLNGPYIRAlddeelaELLA----PELPEAGIREDLerlvplvreraktlse 359
|
410 420
....*....|....*....|..
gi 345539328 381 ---FTNIIYIERSDfkEEYDKK 399
Cdd:COG0008 360 laeLARFFFIERED--EKAAKK 379
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
28-540 |
2.05e-90 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 289.94 E-value: 2.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 28 TRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYFFKLYQ 107
Cdd:PTZ00402 55 TRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDLMYE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 108 YAKQLIYQGLAYVDHLTKEQIREYRgtlnTPGRNSPYRDRTIQENIKLFKKMKKGEYNEGEACLRAKIDMNSSFIIMRDP 187
Cdd:PTZ00402 135 KAEELIKKGLAYCDKTPREEMQKCR----FDGVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNENKAMRDP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 188 VLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHyPKQYEFSRLNLEFSIL 267
Cdd:PTZ00402 211 VIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRK-PIVEDFSRLNMEYSVM 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 268 SKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIRSMAILEP 347
Cdd:PTZ00402 290 SKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSNT 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 348 IKIILYNLDKNHKEILIVPNHPNNPDMGTHEILFTNIIYIERSDFkeeydkkyKRLRIGEEIRLR---YAYIIKAEKIEK 424
Cdd:PTZ00402 370 LKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDV--------ALLKEGDEVTLMdwgNAYIKNIRRSGE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 425 DKFNNIINIICYCDTNslgkkpkNKKNPAVIHWISIH-NALPAEFRLYDQLFNIKNPEQQTNFLSYINPKSLIKKYGFIE 503
Cdd:PTZ00402 442 DALITDADIVLHLEGD-------VKKTKFKLTWVPESpKAEVMELNEYDHLLTKKKPDPEESIDDIIAPVTKYTQEVYGE 514
|
490 500 510
....*....|....*....|....*....|....*..
gi 345539328 504 KKLEKMIYKYIMnyndqlhfQFERIGYFCLDYIDSKK 540
Cdd:PTZ00402 515 EALSVLKKGDII--------QLERRGYYIVDDVTPKK 543
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
28-537 |
3.08e-90 |
|
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: 288.26 E-value: 3.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 28 TRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWyGNVHYSSEYFFKLYQ 107
Cdd:TIGR00463 96 MRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKW-DEVVYQSDRIETYYD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 108 YAKQLIYQGLAYVDHLTKEQIREYRGTlntpGRNSPYRDRTIQENIKLFKKMKKGEYNEGEACLRAKIDMNSSFIIMRDP 187
Cdd:TIGR00463 175 YTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDW 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 188 VLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKR-------LYNWILENTnvkhypKQYEFSRL 260
Cdd:TIGR00463 251 VIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqeyiyrYFGWEPPEF------IHWGRLKI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 261 NLEFSILSKRKLKiLIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIR 340
Cdd:TIGR00463 325 DDVRALSTSSARK-GILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARR 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 341 SMAILEPIKIILYNLDKnhKEILIVPNHPNNPDMGTHEILFTNIIYIERSDFKEEYdkkykrlrigEEIRLryayiikae 420
Cdd:TIGR00463 404 YFFIWNPVKIEIVGLPE--PKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRL--------- 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 421 kieKDKFNNIINIIcYCDTNSLGKKPKNKKNPAVIHWISIHNALPAEFrlydqlfniknpeqqtnflsyINPKSLIKKyG 500
Cdd:TIGR00463 463 ---MDAVNVIYSKK-ELRYHSEGLEGARKLGKSIIHWLPAKDAVKVKV---------------------IMPDASIVE-G 516
|
490 500 510
....*....|....*....|....*....|....*..
gi 345539328 501 FIEKKLEKMIYKYIMnyndqlhfQFERIGYFCLDYID 537
Cdd:TIGR00463 517 VIEADASELEVGDVV--------QFERFGFARLDSAD 545
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
28-545 |
1.74e-88 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 282.67 E-value: 1.74e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 28 TRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKwYGNVHYSSEYFFKLYQ 107
Cdd:PLN03233 14 TRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSFTSDYFEPIRC 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 108 YAKQLIYQGLAYVDHLTKEQIREYRgtlnTPGRNSPYRDRTIQENIKLFKKMKKGEYNEGEACLRAKIDMNSSFIIMRDP 187
Cdd:PLN03233 93 YAIILIEEGLAYMDDTPQEEMKKER----ADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLRDP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 188 VLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHyPKQYEFSRLNLEFSIL 267
Cdd:PLN03233 169 VLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRR-PRIHAFARMNFMNTVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 268 SKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIRSMAI--L 345
Cdd:PLN03233 248 SKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 346 EPIKIILYNLDKN-HKEILIVPNHPNNPDMGTHEILFTNIIYIERSDFKEeydkkykrLRIGEEIRLRYAYIIKAEKIEK 424
Cdd:PLN03233 328 DHTALTVTNADEEaDFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLLRWGVIEISKIDG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 425 DKFNNIIniicycdtnslgKKPKNKKNPAVIHWIS-IHNALPAEFRLYDQLFNIKNPEQQTNFLSYINPKSLIKKYGFIE 503
Cdd:PLN03233 400 DLEGHFI------------PDGDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDVIGD 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 345539328 504 KKLEKMiykyimnyndQLH--FQFERIGYFCLD--YIDSKKNYLVF 545
Cdd:PLN03233 468 AGLKTL----------KEHdiIQLERRGFYRVDrpYMGEEKPLILF 503
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
28-541 |
1.03e-76 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 252.85 E-value: 1.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 28 TRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENI---KYiNSIKYDISWLGYKWyGNVHYSSEYFFK 104
Cdd:PRK04156 104 MRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPdpeAY-DMILEDLKWLGVKW-DEVVIQSDRLEI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 105 LYQYAKQLIYQGLAYVDHLTKEQIREYRGTlntpGRNSPYRDRTIQENIKLFKKMKKGEYNEGEACLRAKIDMNSSFIIM 184
Cdd:PRK04156 182 YYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 185 RDPVLYRILFAHHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKhYPKQYEFSRLNLEF 264
Cdd:PRK04156 258 RDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWE-YPETIHYGRLKIEG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 265 SILSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIRSMAI 344
Cdd:PRK04156 337 FVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYFFV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 345 LEPIKIILYNLDKNHKEIlivPNHPNNPDMGTHEILFTNIIYIERSDFKEeydkkykrlrIGEEIRLRYAYIIKAEKIEK 424
Cdd:PRK04156 417 RDPVELEIEGAEPLEAKI---PLHPDRPERGEREIPVGGKVYVSSDDLEA----------EGKMVRLMDLFNVEITGVSV 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 425 DKFnniiniicycDTNSLGKKPKNKKNPAVIHWISIHNALPAEFRLYDQlfniknpeqqtnflsyinpkslIKKYGFIEK 504
Cdd:PRK04156 484 DKA----------RYHSDDLEEARKNKAPIIQWVPEDESVPVRVLKPDG----------------------GDIEGLAEP 531
|
490 500 510
....*....|....*....|....*....|....*..
gi 345539328 505 KLEKMIYKYIMnyndqlhfQFERIGyFCldYIDSKKN 541
Cdd:PRK04156 532 DVADLEVDDIV--------QFERFG-FV--RIDSVED 557
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
27-327 |
1.07e-54 |
|
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: 184.60 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYFFKLY 106
Cdd:cd00418 3 VTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGlayvdhltkeqireyrgtlntpgrnspyrdrtiqeniklfkkmkkgeynegeaclrakidmnssfiimrd 186
Cdd:cd00418 83 AYAEELIKKG---------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 187 pvlyrilfahhhqtkddwyIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKHyPKQYEFSRLNLEFS- 265
Cdd:cd00418 93 -------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEP-PRFYHFPRLLLEDGt 152
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 345539328 266 ILSKRKLKiliddnivegwndpriSTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLE 327
Cdd:cd00418 153 KLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEE 198
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
338-534 |
4.73e-54 |
|
tRNA synthetases class I (E and Q), anti-codon binding 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: 427609 [Multi-domain] Cd Length: 175 Bit Score: 180.93 E-value: 4.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 338 AIRSMAILEPIKIILYNLDKNHKEILIVPNHPNNPDMGTHEILFTNIIYIERSDFkeeydkkyKRLRIGEEIRLRYAYII 417
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 418 KAEKIEKDKFNNIINIICYCDTNSLGKKPKNKKNpaVIHWISIHNALPAEFRLYDQLFNIKNPEqqtNFLsyINPKSL-I 496
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGARKVKGK--IIHWVSASDAVPAEVRLYDRLFKDEDDA---DFL--LNPDSLkV 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 345539328 497 KKYGFIEkklekmiyKYIMNYNDQLHFQFERIGYFCLD 534
Cdd:pfam03950 146 LTEGLAE--------PALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
28-340 |
2.39e-36 |
|
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: 135.56 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 28 TRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNP--LKENIKYINSIKYDISWLGYKWyGNVHYSSEYFFKL 105
Cdd:cd09287 4 MRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKW-DEVVIASDRIELY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 106 YQYAKQLIYQGLAYVdhltkeqireyrgtlntpgrnspyrdrtiqeniklfkkmkkgeynegeaclrakidmnssfiimr 185
Cdd:cd09287 83 YEYARKLIEMGGAYV----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 186 dpvlyrilfahHHQTKDDWYIYPTYDFAHCLSDSIEKITHSLCTLEFQDNKRLYNWILENTNVKhYPKQYEFSRLNLEFS 265
Cdd:cd09287 98 -----------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWE-YPETIHWGRLKIEGG 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345539328 266 ILSKRKLKILIDDNIVEGWNDPRISTISGLRRKGYTPSSIKHFCQKIGITKQNNLIEYSLLEHCIRKELNQTAIR 340
Cdd:cd09287 166 KLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
28-227 |
4.09e-15 |
|
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: 77.78 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 28 TRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNpLKENIK-YINSIKYDISWLGYKWYGNVHYSSEYFFKLY 106
Cdd:TIGR00464 4 TRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTD-LERNIEeAEEAILEGLKWLGISWDEGPYYQSQRLDIYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 107 QYAKQLIYQGLAYVDHLTKEQIREYRGTLNTPGRNSPYRDRTIQenikLFKKMKKGEYNEGEAC-LRAKIDMNSSfIIMR 185
Cdd:TIGR00464 83 KYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRN----LHEEEIENKLAKGIPPvVRFKIPQEAV-VSFN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 345539328 186 DPVLYRILFAHhhQTKDDWYIY-----PTYDFAHCLSDSIEKITHSL 227
Cdd:TIGR00464 158 DQVRGEITFQN--SELDDFVILrsdgsPTYNFAVVVDDYLMKITHVI 202
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
27-72 |
2.93e-09 |
|
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: 55.56 E-value: 2.93e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 345539328 27 HTRFPPEPNGHLHIGHAKSICLNFELAYL-----YKGRCNLRFDDTNPLKE 72
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIG 51
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
28-123 |
3.14e-09 |
|
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: 57.60 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 28 TRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYF----- 102
Cdd:cd00808 4 TRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGpyrqs 83
|
90 100 110
....*....|....*....|....*....|...
gi 345539328 103 --FKLYQ-YAKQLIYQG-------LAYV--DHL 123
Cdd:cd00808 84 erLEIYRkYAEKLLEKGdgfptyhLANVvdDHL 116
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
27-97 |
4.01e-09 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 54.08 E-value: 4.01e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345539328 27 HTRFPPEPnGHLHIGHAKSICLNFELAYlykgRCNLRFDDTNPLK------ENIKYINSIKYDISWLGYKWYGNVHY 97
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIAD----QCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNREL 72
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
28-133 |
4.97e-09 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 57.94 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 28 TRFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKWYGNVHYSSEYfFKLYQ 107
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQR-HDAYR 86
|
90 100
....*....|....*....|....*..
gi 345539328 108 YA-KQLIYQGLAYVDHLTKEQIREYRG 133
Cdd:PRK05710 87 AAlDRLRAQGLVYPCFCSRKEIAAAAP 113
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
29-119 |
1.46e-06 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 50.90 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345539328 29 RFPPEPNGHLHIGHAKSICLNFELAYLYKGRCNLRFDDTNPLKENIKYINSIKYDISWLGYKW---------YGNvHYSS 99
Cdd:PLN02627 49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWdegpdvggeYGP-YRQS 127
|
90 100
....*....|....*....|
gi 345539328 100 EYFFKLYQYAKQLIYQGLAY 119
Cdd:PLN02627 128 ERNAIYKQYAEKLLESGHVY 147
|
|
| |
