|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-550 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1203.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 1 MAEIENRPSNFIRTRIDQDLASGKHASTHTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVN 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 81 SIKEDVQWLGFNWDGEIKYSSNYFDILYDYAVELINKGLAYVCFLTADQAREYRGTLKEPGKNSPYRDTASDENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 161 MRNGEFKEGECVLRAKIDMASSFMVLRDPIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 241 YDWVLDNISLECHPQQIEFSRLNLEYTIMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQE 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 321 NMVEMGMLEACIREDLNENAPRAMAVLDPVKIVIENYDADKVETLSVANHPNKEEMGRRDVPFTREIYIEREDFKEEANN 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 401 KFKRLVLDKEVRLRGAYVIKAQRVEKDENGEITTIYCTYDPETLGKNPSDGRKVKGVIHWVSASEAITAEVRLYDRLFSV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76875494 481 PNPAAADEFESTLNPDSLVIlTNAKLEPSLANSAAEQGFQFERTGYFS--RDSKAKNIVFNQTVGLRDSWSK 550
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVI-KQGFVEPSLADAKPEDRFQFEREGYFCadKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
29-548 |
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: 876.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNYFDILY 108
Cdd:TIGR00440 2 HTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 109 DYAVELINKGLAYVCFLTADQAREYRGTLKEPGKNSPYRDTASDENLALFEKMRNGEFKEGECVLRAKIDMASSFMVLRD 188
Cdd:TIGR00440 82 RYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 189 PIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLECHPQQIEFSRLNLEYTI 268
Cdd:TIGR00440 162 PVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 269 MSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNENAPRAMAVLD 348
Cdd:TIGR00440 242 LSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVID 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 349 PVKIVIENYDADkVETLSVANHPNKEEMGRRDVPFTREIYIEREDFKEEANNKFKRLVLDKEVRLRGAYVIKAQRVEKDE 428
Cdd:TIGR00440 322 PVEVVIENLSDE-YELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 429 NGEITTIYCTYDPETLGKNPSDGRKVKGVIHWVSASEAITAEVRLYDRLFSVPNPAAADEFESTLNPDSLVIlTNAKLEP 508
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVI-KQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 76875494 509 SLANSAAEQGFQFERTGYF---SRDSKAKNIVFNQTVGLRDSW 548
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFcldSKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
29-338 |
1.55e-153 |
|
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: 441.76 E-value: 1.55e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNYFDILY 108
Cdd:pfam00749 3 RTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 109 DYAVELINKGLAYVCFLTADQAREYRGTLkePGKNSPYRDTASDENLALF-EKMRNGEFKEGECVLRAKIDMASSfMVLR 187
Cdd:pfam00749 83 KYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 188 DPIIYRVRFA---HHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLECHPQQIEFSRLNL 264
Cdd:pfam00749 160 DPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76875494 265 EYTIMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQ-ENMVEMGMLEACIREDLNE 338
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
29-342 |
7.57e-148 |
|
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: 424.36 E-value: 7.57e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDgEIKYSSNYFDILY 108
Cdd:cd00807 3 VTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 109 DYAVELINKGLAYVcfltadqareyrgtlkepgknspyrdtasdenlalfekmrngefkegecvlrakidmassfmvlrd 188
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 189 piiyrvrfahHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLEChPQQIEFSRLNLEYTI 268
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYTV 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 76875494 269 MSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNENAPR 342
Cdd:cd00807 165 MSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
29-527 |
9.41e-142 |
|
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: 417.66 E-value: 9.41e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNYFDILY 108
Cdd:COG0008 6 RTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 109 DYAVELINKGLAYVCFLTADQAREYRGTLKEPGKNSPYRDTA---SDENLalfEKMR-NGEfkegECVLRAKI------- 177
Cdd:COG0008 86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCrdlSPEEL---ERMLaAGE----PPVLRFKIpeegvvf 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 178 -DMAS-----SFMVLRDPIIYRvrfahhhqtADKwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLE 251
Cdd:COG0008 159 dDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 252 cHPqqiEFSRLNLEY----TIMSKRKlsdlvvnNHVegwddprmpTIAGLRRRGYTPASIREFCLRIGVTKQENMV--EM 325
Cdd:COG0008 227 -PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEifSL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 326 GMLEACIreDLNENaPRAMAVLDPVKIVIENY------DADKVETLSVANHPNK--EEMGRRDVPFTRE----------- 386
Cdd:COG0008 287 EELIEAF--DLDRV-SRSPAVFDPVKLVWLNGpyiralDDEELAELLAPELPEAgiREDLERLVPLVREraktlselael 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 387 ---IYIEREDfkEEANNkfKRLVlDKEVRLrgayVIKAQRvEKDENGEittiycTYDPETlgknpsdgrkVKGVIHWVSA 463
Cdd:COG0008 364 arfFFIERED--EKAAK--KRLA-PEEVRK----VLKAAL-EVLEAVE------TWDPET----------VKGTIHWVSA 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76875494 464 SeaitAEVRlyDRLFSVPnpaaadefestlnpdsL-VILTNAKLEPSLANSAAEQGFQ--FERTGYF 527
Cdd:COG0008 418 E----AGVK--DGLLFMP----------------LrVALTGRTVEPSLFDVLELLGKErvFERLGYA 462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-550 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1203.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 1 MAEIENRPSNFIRTRIDQDLASGKHASTHTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVN 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 81 SIKEDVQWLGFNWDGEIKYSSNYFDILYDYAVELINKGLAYVCFLTADQAREYRGTLKEPGKNSPYRDTASDENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 161 MRNGEFKEGECVLRAKIDMASSFMVLRDPIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 241 YDWVLDNISLECHPQQIEFSRLNLEYTIMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQE 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 321 NMVEMGMLEACIREDLNENAPRAMAVLDPVKIVIENYDADKVETLSVANHPNKEEMGRRDVPFTREIYIEREDFKEEANN 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 401 KFKRLVLDKEVRLRGAYVIKAQRVEKDENGEITTIYCTYDPETLGKNPSDGRKVKGVIHWVSASEAITAEVRLYDRLFSV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76875494 481 PNPAAADEFESTLNPDSLVIlTNAKLEPSLANSAAEQGFQFERTGYFS--RDSKAKNIVFNQTVGLRDSWSK 550
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVI-KQGFVEPSLADAKPEDRFQFEREGYFCadKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
29-548 |
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: 876.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNYFDILY 108
Cdd:TIGR00440 2 HTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 109 DYAVELINKGLAYVCFLTADQAREYRGTLKEPGKNSPYRDTASDENLALFEKMRNGEFKEGECVLRAKIDMASSFMVLRD 188
Cdd:TIGR00440 82 RYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 189 PIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLECHPQQIEFSRLNLEYTI 268
Cdd:TIGR00440 162 PVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 269 MSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNENAPRAMAVLD 348
Cdd:TIGR00440 242 LSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVID 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 349 PVKIVIENYDADkVETLSVANHPNKEEMGRRDVPFTREIYIEREDFKEEANNKFKRLVLDKEVRLRGAYVIKAQRVEKDE 428
Cdd:TIGR00440 322 PVEVVIENLSDE-YELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 429 NGEITTIYCTYDPETLGKNPSDGRKVKGVIHWVSASEAITAEVRLYDRLFSVPNPAAADEFESTLNPDSLVIlTNAKLEP 508
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVI-KQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 76875494 509 SLANSAAEQGFQFERTGYF---SRDSKAKNIVFNQTVGLRDSW 548
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFcldSKESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
10-551 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 833.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 10 NFIRTRIDQDLASGKHASTHTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWL 89
Cdd:PRK14703 14 NFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 90 GFNWDGEIKYSSNYFDILYDYAVELINKGLAYVCFLTADQAREYRGTLKEPGKNSPYRDTASDENLALFEKMRNGEFKEG 169
Cdd:PRK14703 94 GFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 170 ECVLRAKIDMASSFMVLRDPIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNIS 249
Cdd:PRK14703 174 AHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 250 L-ECHPQQIEFSRLNLEYTIMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGML 328
Cdd:PRK14703 254 PwPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 329 EACIREDLNENAPRAMAVLDPVKIVIENYDADKVETLSVANHPNK-EEMGRRDVPFTREIYIEREDFKEEANNKFKRLVL 407
Cdd:PRK14703 334 EFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 408 DKEVRLRGAYVIKAQRVEKDENGEITTIYCTYDPETLGKNPSdGRKVKGVIHWVSASEAITAEVRLYDRLFSVPNPAAAD 487
Cdd:PRK14703 414 GREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEAAD 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76875494 488 E-FESTLNPDSLVILTNaKLEPSLANSAAEQGFQFERTGYFSRD---SKAKNIVFNQTVGLRDSWSKT 551
Cdd:PRK14703 493 EdFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADpvdSRPDALVFNRIITLKDTWGAR 559
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
7-550 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 576.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 7 RPSNfIRTRIDQDL--ASGKhasTHTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKE 84
Cdd:PLN02859 246 RPSN-TKEILEKHLkaTGGK---VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 85 DVQWLGfnWDG-EIKYSSNYFDILYDYAVELINKGLAYVCFLTADQAREYRgtlkEPGKNSPYRDTASDENLALFEKMRN 163
Cdd:PLN02859 322 IVEWMG--WEPfKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 164 GEFKEGECVLRAKIDMASSFMVLRDPIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDW 243
Cdd:PLN02859 396 GLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYW 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 244 VLDNISLEcHPQQIEFSRLNLEYTIMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQEN-M 322
Cdd:PLN02859 476 LLDSLGLY-QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 323 VEMGMLEACIREDLNENAPRAMAVLDPVKIVIENYDADKVETLSVANHPNKEEM---GRRDVPFTREIYIEREDFKEEAN 399
Cdd:PLN02859 555 IRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDdpsAFYKVPFSRVVYIERSDFRLKDS 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 400 NKFKRLVLDKEVRLRGAYVIKAQRV-EKDENGEITTIYCTYDPEtlgknpsDGRKVKGVIHWVSAS----EAITAEVRLY 474
Cdd:PLN02859 635 KDYYGLAPGKSVLLRYAFPIKCTDVvLADDNETVVEIRAEYDPE-------KKTKPKGVLHWVAEPspgvEPLKVEVRLF 707
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76875494 475 DRLFSVPNPAAADEFESTLNPDSLVILTNAKLEPSLANSAAEQGFQFERTGYFS--RDSKAKNIVFNQTVGLRDSWSK 550
Cdd:PLN02859 708 DKLFLSENPAELEDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAvdKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
31-551 |
8.28e-163 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 475.24 E-value: 8.28e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 31 RFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGeIKYSSNYFDILYDY 110
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDW-VTFSSDYFDQLHEF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 111 AVELINKGLAYVCFLTADQAREYRgtlkEPGKNSPYRDTASDENLALFEKMRNGEFKEGECVLRAKIDMASSFMVLRDPI 190
Cdd:PTZ00437 134 AVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 191 IYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLeCHPQQIEFSRLNLEYTIMS 270
Cdd:PTZ00437 210 AYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSLLS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 271 KRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNENAPRAMAVLDPV 350
Cdd:PTZ00437 289 KRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 351 KIVIENYDADKveTLSVANHPNKEEMGRRDVPFTREIYIEREDFKEEANN-KFKRLVLD-KEVRLRGAYVIKAQRVEKDE 428
Cdd:PTZ00437 369 KVVVDNWKGER--EFECPNHPRKPELGSRKVMFTDTFYVDRSDFRTEDNNsKFYGLAPGpRVVGLKYSGNVVCKGFEVDA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 429 NGEITTIYCTYDPETLGKNPSDgrkvkgvIHWVSASEAITAEVRLYDRLFSVPNPAAADEFESTLNPDSLVIlTNAKLEP 508
Cdd:PTZ00437 447 AGQPSVIHVDIDFERKDKPKTN-------ISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVV-SHGYAEK 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 76875494 509 SLANSAAEQGFQFERTGYF--SRDSKAKNIVFNQTVGLRDSWSKT 551
Cdd:PTZ00437 519 GIENAKHFESVQAERFGYFvvDPDTRPDHLVMNRVLGLREDKEKA 563
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
29-338 |
1.55e-153 |
|
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: 441.76 E-value: 1.55e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNYFDILY 108
Cdd:pfam00749 3 RTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 109 DYAVELINKGLAYVCFLTADQAREYRGTLkePGKNSPYRDTASDENLALF-EKMRNGEFKEGECVLRAKIDMASSfMVLR 187
Cdd:pfam00749 83 KYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 188 DPIIYRVRFA---HHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLECHPQQIEFSRLNL 264
Cdd:pfam00749 160 DPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76875494 265 EYTIMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQ-ENMVEMGMLEACIREDLNE 338
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
29-342 |
7.57e-148 |
|
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: 424.36 E-value: 7.57e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDgEIKYSSNYFDILY 108
Cdd:cd00807 3 VTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 109 DYAVELINKGLAYVcfltadqareyrgtlkepgknspyrdtasdenlalfekmrngefkegecvlrakidmassfmvlrd 188
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 189 piiyrvrfahHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLEChPQQIEFSRLNLEYTI 268
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYTV 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 76875494 269 MSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNENAPR 342
Cdd:cd00807 165 MSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
29-527 |
9.41e-142 |
|
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: 417.66 E-value: 9.41e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNYFDILY 108
Cdd:COG0008 6 RTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 109 DYAVELINKGLAYVCFLTADQAREYRGTLKEPGKNSPYRDTA---SDENLalfEKMR-NGEfkegECVLRAKI------- 177
Cdd:COG0008 86 EYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCrdlSPEEL---ERMLaAGE----PPVLRFKIpeegvvf 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 178 -DMAS-----SFMVLRDPIIYRvrfahhhqtADKwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLE 251
Cdd:COG0008 159 dDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 252 cHPqqiEFSRLNLEY----TIMSKRKlsdlvvnNHVegwddprmpTIAGLRRRGYTPASIREFCLRIGVTKQENMV--EM 325
Cdd:COG0008 227 -PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEifSL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 326 GMLEACIreDLNENaPRAMAVLDPVKIVIENY------DADKVETLSVANHPNK--EEMGRRDVPFTRE----------- 386
Cdd:COG0008 287 EELIEAF--DLDRV-SRSPAVFDPVKLVWLNGpyiralDDEELAELLAPELPEAgiREDLERLVPLVREraktlselael 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 387 ---IYIEREDfkEEANNkfKRLVlDKEVRLrgayVIKAQRvEKDENGEittiycTYDPETlgknpsdgrkVKGVIHWVSA 463
Cdd:COG0008 364 arfFFIERED--EKAAK--KRLA-PEEVRK----VLKAAL-EVLEAVE------TWDPET----------VKGTIHWVSA 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76875494 464 SeaitAEVRlyDRLFSVPnpaaadefestlnpdsL-VILTNAKLEPSLANSAAEQGFQ--FERTGYF 527
Cdd:COG0008 418 E----AGVK--DGLLFMP----------------LrVALTGRTVEPSLFDVLELLGKErvFERLGYA 462
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
30-537 |
2.78e-108 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 334.90 E-value: 2.78e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 30 TRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPE--KEDINYVNSIKEDVQWLGFNWDgEIKYSSNYFDIL 107
Cdd:PRK04156 104 MRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLEIY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 108 YDYAVELINKGLAYVCFLTADQAREyrgtLKEPGKNSPYRDTASDENLALFEKMRNGEFKEGECVLRAKIDMASSFMVLR 187
Cdd:PRK04156 183 YEYARKLIEMGGAYVCTCDPEEFKE----LRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 188 DPIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLEcHPQQIEFSRLNLEYT 267
Cdd:PRK04156 259 DWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWE-YPETIHYGRLKIEGF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 268 IMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNENAPRAMAVL 347
Cdd:PRK04156 338 VLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYFFVR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 348 DPVKIVIENYDADKVEtlsVANHPNKEEMGRRDVPFTREIYIEREDFKEeannkfkrlvLDKEVRLRGAYVIKAQRVEkd 427
Cdd:PRK04156 418 DPVELEIEGAEPLEAK---IPLHPDRPERGEREIPVGGKVYVSSDDLEA----------EGKMVRLMDLFNVEITGVS-- 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 428 engeitTIYCTYDPETLgknpSDGRKVKG-VIHWVSASEAITAEVrlydrlfsvpnpaaadefestLNPDSLVIltNAKL 506
Cdd:PRK04156 483 ------VDKARYHSDDL----EEARKNKApIIQWVPEDESVPVRV---------------------LKPDGGDI--EGLA 529
|
490 500 510
....*....|....*....|....*....|.
gi 76875494 507 EPSLANSAAEQGFQFERTGYFSRDSKAKNIV 537
Cdd:PRK04156 530 EPDVADLEVDDIVQFERFGFVRIDSVEDDEV 560
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
19-534 |
1.66e-107 |
|
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: 332.94 E-value: 1.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 19 DLASGKHASTHTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDgEIK 98
Cdd:TIGR00463 85 ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 99 YSSNYFDILYDYAVELINKGLAYVCFLTADQAREyrgtLKEPGKNSPYRDTASDENLALFEKMRNGEFKEGECVLRAKID 178
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRE----LRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 179 MASSFMVLRDPIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR--LYDWVLDNISLechPQQ 256
Cdd:TIGR00463 240 LKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqEYIYRYFGWEP---PEF 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 257 IEFSRLNLEY--TIMSKRKLSDlVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIRE 334
Cdd:TIGR00463 317 IHWGRLKIDDvrALSTSSARKG-ILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRK 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 335 DLNENAPRAMAVLDPVKIVIENYDADKVETLSVanHPNKEEMGRRDVPFTREIYIEREDFKEeannkfkrlvLDKEVRLR 414
Cdd:TIGR00463 396 IIDEEARRYFFIWNPVKIEIVGLPEPKRVERPL--HPDHPEIGERVLILRGEIYVPKDDLEE----------GVEPVRLM 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 415 GAYVIkaqrvekdengeittIYCTYDPETLGKNPSDGRKV-KGVIHWVSASEAITAEVrlydrlfsvpnpaaadefestL 493
Cdd:TIGR00463 464 DAVNV---------------IYSKKELRYHSEGLEGARKLgKSIIHWLPAKDAVKVKV---------------------I 507
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 76875494 494 NPDSLVilTNAKLEPSLANSAAEQGFQFERTGYFSRDSKAK 534
Cdd:TIGR00463 508 MPDASI--VEGVIEADASELEVGDVVQFERFGFARLDSADK 546
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
19-530 |
1.32e-100 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 319.75 E-value: 1.32e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 19 DLASGKHASTHTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDgEIK 98
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 99 YSSNYFDILYDYAVELINKGLAYVCFLTADQAREYRGTlkepGKNSPYRDTASDENLALFEKMRNGEFKEGECVLRAKID 178
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 179 MASSFMVLRDPIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLEcHPQQIE 258
Cdd:PLN02907 360 MQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHIWE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 259 FSRLNLEYTIMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNE 338
Cdd:PLN02907 439 FSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDP 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 339 NAPRAMAVLDPVKIVIENYDA-DKVETLSVANHPNKEEMGRRDVPFTREIYIEREDfkEEANNKfkrlvlDKEVRLR--G 415
Cdd:PLN02907 519 VCPRHTAVLKEGRVLLTLTDGpETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD--AEAISE------GEEVTLMdwG 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 416 AYVIKAqrVEKDENGEITTIYCTYDPEtlgknpSDGRKVKGVIHWVSA-SEAITAEVRLYDRLFSVPNPAAADEFESTLN 494
Cdd:PLN02907 591 NAIIKE--ITKDEGGAVTALSGELHLE------GSVKTTKLKLTWLPDtNELVPLSLVEFDYLITKKKLEEDDNFLDVLN 662
|
490 500 510
....*....|....*....|....*....|....*.
gi 76875494 495 PDSLVIlTNAKLEPSLANSAAEQGFQFERTGYFSRD 530
Cdd:PLN02907 663 PCTKKE-TAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
20-531 |
2.48e-89 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 286.86 E-value: 2.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 20 LASGKHASTHTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKY 99
Cdd:PTZ00402 45 LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 100 SSNYFDILYDYAVELINKGLAYvCFLTadqAREYRGTLKEPGKNSPYRDTASDENLALFEKMRNGEFKEGECVLRAKIDM 179
Cdd:PTZ00402 125 SSDYMDLMYEKAEELIKKGLAY-CDKT---PREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 180 ASSFMVLRDPIIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLEcHPQQIEF 259
Cdd:PTZ00402 201 DNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIR-KPIVEDF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 260 SRLNLEYTIMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNEN 339
Cdd:PTZ00402 280 SRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 340 APRAMAVLDPVKIVIENYDADKVETLSVANHPNKEEMGRRDVPFTREIYIEREDFKeeannkfkrLVLD-KEVRLR---G 415
Cdd:PTZ00402 360 VPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVA---------LLKEgDEVTLMdwgN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 416 AYVIKAQRveKDENGEITTIYCTYDPEtlgknpSDGRKVKGVIHWVSAS-EAITAEVRLYDRLFSVPNPAAADEFESTLN 494
Cdd:PTZ00402 431 AYIKNIRR--SGEDALITDADIVLHLE------GDVKKTKFKLTWVPESpKAEVMELNEYDHLLTKKKPDPEESIDDIIA 502
|
490 500 510
....*....|....*....|....*....|....*....
gi 76875494 495 PdslVILTNAKLEPSLANSAAEQG--FQFERTGYFSRDS 531
Cdd:PTZ00402 503 P---VTKYTQEVYGEEALSVLKKGdiIQLERRGYYIVDD 538
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
30-530 |
9.51e-88 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 280.36 E-value: 9.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 30 TRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDgEIKYSSNYFDILYD 109
Cdd:PLN03233 14 TRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPD-SVSFTSDYFEPIRC 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 110 YAVELINKGLAYVcfltADQAREYRGTLKEPGKNSPYRDTASDENLALFEKMRNGEFKEGECVLRAKIDMASSFMVLRDP 189
Cdd:PLN03233 93 YAIILIEEGLAYM----DDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLRDP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 190 IIYRVRFAHHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLEcHPQQIEFSRLNLEYTIM 269
Cdd:PLN03233 169 VLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAFARMNFMNTVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 270 SKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNENAPRAMAV--L 347
Cdd:PLN03233 248 SKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 348 DPVKIVIENYDAD-KVETLSVANHPNKEEMGRRDVPFTREIYIEREDFKEeannkfkrLVLDKEVRLRGAYVIKAQRVEK 426
Cdd:PLN03233 328 DHTALTVTNADEEaDFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLLRWGVIEISKIDG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 427 DENGEittiyctYDPEtlgknpSDGRKVKGVIHWVS-ASEAITAEVRLYDRLFSVPNPAAADEFESTLNPDSLViLTNAK 505
Cdd:PLN03233 400 DLEGH-------FIPD------GDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLA-ETDVI 465
|
490 500
....*....|....*....|....*
gi 76875494 506 LEPSLANSAAEQGFQFERTGYFSRD 530
Cdd:PLN03233 466 GDAGLKTLKEHDIIQLERRGFYRVD 490
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
340-530 |
2.78e-82 |
|
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: 254.12 E-value: 2.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 340 APRAMAVLDPVKIVIENYDADKVETLSVANHPNKEEMGRRDVPFTREIYIEREDfkeeannkFKRLVLDKEVRLRGAYVI 419
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIERED--------FKRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 420 KAQRVEKDENGEITTIYCTYDPETLGKNpsdgRKVKG-VIHWVSASEAITAEVRLYDRLFSVPNpaaadEFESTLNPDSL 498
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED-----DADFLLNPDSL 143
|
170 180 190
....*....|....*....|....*....|..
gi 76875494 499 VILTNAKLEPSLANSAAEQGFQFERTGYFSRD 530
Cdd:pfam03950 144 KVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
29-338 |
1.14e-72 |
|
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: 231.59 E-value: 1.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNYFDILY 108
Cdd:cd00418 3 VTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 109 DYAVELINKGlayvcfltadqareyrgtlkepgknspyrdtasdenlalfekmrngefkegecvlrakidmassfmvlrd 188
Cdd:cd00418 83 AYAEELIKKG---------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 189 piiyrvrfahhhqtadkwcIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLEcHPQQIEFSRLNLEY-T 267
Cdd:cd00418 93 -------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLEDgT 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 268 IMSKRKLSdlvvnnhvegwddprmPTIAGLRRRGYTPASIREFCLRIGVTKQE-----------------------NMVE 324
Cdd:cd00418 153 KLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDghelftleemiaafsvervnsadATFD 216
|
330
....*....|....
gi 76875494 325 MGMLEACIREDLNE 338
Cdd:cd00418 217 WAKLEWLNREYIRE 230
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
30-342 |
7.44e-54 |
|
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: 182.55 E-value: 7.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 30 TRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPE--KEDINYVNSIKEDVQWLGFNWDgEIKYSSNYFDIL 107
Cdd:cd09287 4 MRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIELY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 108 YDYAVELINKGLAYVcfltadqareyrgtlkepgknspyrdtasdenlalfekmrngefkegecvlrakidmassfmvlr 187
Cdd:cd09287 83 YEYARKLIEMGGAYV----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 188 dpiiyrvrfahHHQTADKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISLEcHPQQIEFSRLNLEYT 267
Cdd:cd09287 98 -----------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWE-YPETIHWGRLKIEGG 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76875494 268 IMSKRKLSDLVVNNHVEGWDDPRMPTIAGLRRRGYTPASIREFCLRIGVTKQENMVEMGMLEACIREDLNENAPR 342
Cdd:cd09287 166 KLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
27-229 |
8.84e-25 |
|
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: 107.44 E-value: 8.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 27 STHTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNYFDI 106
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 107 LYDYAVELINKGLAYVCFLTADQAREYRGTLKEPGKNSPY----RDTASDENLALFEKMRngefkegECVLRAKIDMASS 182
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYdgrcRNLHEEEIENKLAKGI-------PPVVRFKIPQEAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76875494 183 FM--------------VLRDPIIYRvrfahhhqtADKwciYPMYDFTHCISDALEGITHSL 229
Cdd:TIGR00464 154 VSfndqvrgeitfqnsELDDFVILR---------SDG---SPTYNFAVVVDDYLMKITHVI 202
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
30-126 |
7.74e-17 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 81.05 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 30 TRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNYFDIlYD 109
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHDA-YR 86
|
90
....*....|....*...
gi 76875494 110 YAVE-LINKGLAYVCFLT 126
Cdd:PRK05710 87 AALDrLRAQGLVYPCFCS 104
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
30-118 |
7.66e-15 |
|
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: 74.16 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 30 TRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWDGEIKYSSNY------ 103
Cdd:cd00808 4 TRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYgpyrqs 83
|
90
....*....|....*..
gi 76875494 104 --FDILYDYAVELINKG 118
Cdd:cd00808 84 erLEIYRKYAEKLLEKG 100
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
29-273 |
9.35e-13 |
|
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: 65.58 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 29 HTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGL-----CNLRFDDTNPEKEDINYVNsikedvqwlGFNWDGEIKYSSNY 103
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLgykvrCIALIDDAGGLIGDPANKK---------GENAKAFVERWIER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 104 FDILYDYavelinkglayvcfltadqareyrgtlkepgknspyrdtasdenlalfekmrngefkegecvlrakidmassf 183
Cdd:cd00802 72 IKEDVEY------------------------------------------------------------------------- 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 184 mvlrdpiiyrvrfahhhqtadkwciypmyDFTHCISDALEGITH---SLCTLEFQDNRRLYDWVLDNISLECHPQQIEFS 260
Cdd:cd00802 79 -----------------------------MFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLTFG 129
|
250
....*....|....
gi 76875494 261 RLNLEY-TIMSKRK 273
Cdd:cd00802 130 RVMGADgTKMSKSK 143
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
21-229 |
1.73e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 69.77 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 21 ASGKHASTHTRFPPEPNGFLHIGHAKSICLNFGIAKDYNGLCNLRFDDTNPEKEDINYVNSIKEDVQWLGFNWD------ 94
Cdd:PLN02627 39 GESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76875494 95 GEI-KY-SSNYFDILYDYAVELINKGLAYVCFLTADQAREYRGTLKEPGKNSPYRD---TASDENLAlfEKMRNGE---- 165
Cdd:PLN02627 119 GEYgPYrQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGkwaTASDEEVQ--AELAKGTpyty 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76875494 166 -F---KEGECVL----RAKI----DMASSFMVLRDPIIyrvrfahhhqtadkwciyPMYDFTHCISDALEGITHSL 229
Cdd:PLN02627 197 rFrvpKEGSVKIddliRGEVswntDTLGDFVLLRSNGQ------------------PVYNFCVAVDDATMGITHVI 254
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
227-273 |
1.78e-10 |
|
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: 57.93 E-value: 1.78e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 76875494 227 HSLCTLEFQDNRRLYDWVLDNISLECHPQQIEFSRLNLEYTIMSKRK 273
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
29-99 |
1.88e-10 |
|
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: 57.93 E-value: 1.88e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76875494 29 HTRFPPEPnGFLHIGHAKSICLNFGIAkdynGLCNLRFDDTNPEK------EDINYVNSIKEDVQWLGFNWDGEIKY 99
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNREL 72
|
|
| |
