|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-553 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1284.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 1 MSEAEARPSNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVE 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 81 SIKNDVQWLGFNWSGDICYSSDYFDQLYAYAVELINKGLAYVDELSADEIREYRGTLTQPGKNSPFRDRSVEENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 161 MRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 241 YDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 321 NTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYPQGGSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFREEANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 401 QYKRLVLGKEVRLRNAYVIKAERVEKDAEGNITTIFCTYDAETLSKDPADGRKVKGVIHWVSAQHALPVEIRLYDRLFSV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505384025 481 PNPGAAEDFLAVINPESLIIKQGYAEPSLKAAEAGKAFQFEREGYFCLDsRYSTAEKPVFNRTVGLRDTWTKI 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-550 |
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: 1025.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDICYSSDYFDQL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 108 YAYAVELINKGLAYVDELSADEIREYRGTLTQPGKNSPFRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 188 DPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYT 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 268 VMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVI 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 348 DPVKLVIENYpQGGSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 427
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 428 AEGNITTIFCTYDAETLSKDPADGRKVKGVIHWVSAQHALPVEIRLYDRLFSVPNPGAAEDFLAVINPESLIIKQGYAEP 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 505384025 508 SLKAAEAGKAFQFEREGYFCLDSRYSTAEKPVFNRTVGLRDTW 550
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
6.00e-168 |
|
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: 478.74 E-value: 6.00e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDICYSSDYFDQL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 108 YAYAVELINKGLAYVDELSADEIREYRGTltQPGKNSPFRDRSVEENLALF-EKMRAGGFEEGKACLRAKIDMASPfIVM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREE--QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 187 RDPVLYRIKFAE---HHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505384025 264 LEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQ-DNTIEMASLESCIREDLNE 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-342 |
5.36e-156 |
|
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: 445.16 E-value: 5.36e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWsGDICYSSDYFDQ 106
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 107 LYAYAVELINKGLAYVdelsadeireyrgtltqpgknspfrdrsveenlalfekmraggfeegkaclrakidmaspfivm 186
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 187 rdpvlyrikfaeHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEY 266
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505384025 267 TVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPR 342
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-526 |
3.37e-137 |
|
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: 406.10 E-value: 3.37e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 26 TTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDICYSSDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 106 QLYAYAVELINKGLAYVDELSADEIREYRGTLTQPGKN----SPFRDRSVEENlalfEKMRAGGFEegkACLRAKI---- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEEL----ERMLAAGEP---PVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 178 ----DMAS-----PFIVMRDPVLYRikfaehhQTGnkwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNI 248
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 249 TIPVhPrqyEFSRLNLEY----TVMSKRKlnllvtdKHVegwddprmpTISGLRRRGYTSASIREFCKRIGVTKQDNT-- 322
Cdd:COG0008 224 GWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQei 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 323 IEMASLESCIreDLNENaPRAMAVIDPVKLVIENYPQggseLVSMPN-------HPNKPEMG-----TRDVPFSGE---- 386
Cdd:COG0008 284 FSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPY----IRALDDeelaellAPELPEAGiredlERLVPLVRErakt 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 387 ----------IWIDRADfrEEANKqyKRLVLgKEVRLrnayVIKAERvekDAEGNITtifcTYDAETlskdpadgrkVKG 456
Cdd:COG0008 357 lselaelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL---EVLEAVE----TWDPET----------VKG 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505384025 457 VIHWVSAQHalpvEIRlyDRLFSVPnpgaaedfLAVinpeslIIKQGYAEPSLKAAEA--GKAFQFEREGYF 526
Cdd:COG0008 411 TIHWVSAEA----GVK--DGLLFMP--------LRV------ALTGRTVEPSLFDVLEllGKERVFERLGYA 462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-553 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1284.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 1 MSEAEARPSNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVE 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 81 SIKNDVQWLGFNWSGDICYSSDYFDQLYAYAVELINKGLAYVDELSADEIREYRGTLTQPGKNSPFRDRSVEENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 161 MRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 241 YDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 321 NTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYPQGGSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFREEANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 401 QYKRLVLGKEVRLRNAYVIKAERVEKDAEGNITTIFCTYDAETLSKDPADGRKVKGVIHWVSAQHALPVEIRLYDRLFSV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505384025 481 PNPGAAEDFLAVINPESLIIKQGYAEPSLKAAEAGKAFQFEREGYFCLDsRYSTAEKPVFNRTVGLRDTWTKI 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-550 |
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: 1025.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDICYSSDYFDQL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 108 YAYAVELINKGLAYVDELSADEIREYRGTLTQPGKNSPFRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 188 DPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYT 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 268 VMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVI 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 348 DPVKLVIENYpQGGSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 427
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 428 AEGNITTIFCTYDAETLSKDPADGRKVKGVIHWVSAQHALPVEIRLYDRLFSVPNPGAAEDFLAVINPESLIIKQGYAEP 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 505384025 508 SLKAAEAGKAFQFEREGYFCLDSRYSTAEKPVFNRTVGLRDTW 550
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
1-552 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 877.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 1 MSEAEaRPS-----NFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKED 75
Cdd:PRK14703 1 MSDAP-RPRmlvspNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 76 IEYVESIKNDVQWLGFNWSGDICYSSDYFDQLYAYAVELINKGLAYVDELSADEIREYRGTLTQPGKNSPFRDRSVEENL 155
Cdd:PRK14703 80 TEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 156 ALFEKMRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQ 235
Cdd:PRK14703 160 DLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 236 DNRRLYDWVLDNIT-IPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRI 314
Cdd:PRK14703 240 NNRAIYDWVLDHLGpWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 315 GVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYPQGGSELVSMPNHPNK-PEMGTRDVPFSGEIWIDRAD 393
Cdd:PRK14703 320 GVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 394 FREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAEGNITTIFCTYDAETLSKDPAdGRKVKGVIHWVSAQHALPVEIRL 473
Cdd:PRK14703 400 FSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 474 YDRLFSVPNP-GAAEDFLAVINPESLIIKQGYAEPSLKAAEAGKAFQFEREGYFCLDSRYSTAEKPVFNRTVGLRDTWTK 552
Cdd:PRK14703 479 YDRLFKVPQPeAADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGA 558
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
7-554 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 618.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 7 RPSNfIRQIIDEDL--ASGKhttVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKN 84
Cdd:PLN02859 246 RPSN-TKEILEKHLkaTGGK---VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 85 DVQWLGfnWSG-DICYSSDYFDQLYAYAVELINKGLAYVDELSADEIREYRgtltQPGKNSPFRDRSVEENLALFEKMRA 163
Cdd:PLN02859 322 IVEWMG--WEPfKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 164 GGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDW 243
Cdd:PLN02859 396 GLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYW 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 244 VLDNITIpVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNT- 322
Cdd:PLN02859 476 LLDSLGL-YQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSl 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 323 IEMASLESCIREDLNENAPRAMAVIDPVKLVIENYPQGGSELVS---MPNHPNKPEMGTRDVPFSGEIWIDRADFREEAN 399
Cdd:PLN02859 555 IRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDakrWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDS 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 400 KQYKRLVLGKEVRLRNAYVIK-AERVEKDAEGNITTIFCTYDAETLSKDpadgrkvKGVIHWVSA----QHALPVEIRLY 474
Cdd:PLN02859 635 KDYYGLAPGKSVLLRYAFPIKcTDVVLADDNETVVEIRAEYDPEKKTKP-------KGVLHWVAEpspgVEPLKVEVRLF 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 475 DRLFSVPNPGAAEDFLAVINPES-LIIKQGYAEPSLKAAEAGKAFQFEREGYFCLDsRYSTAEKPVFNRTVGLRDTWTKI 553
Cdd:PLN02859 708 DKLFLSENPAELEDWLEDLNPQSkEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYGKG 786
|
.
gi 505384025 554 G 554
Cdd:PLN02859 787 G 787
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
31-552 |
1.32e-177 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 513.38 E-value: 1.32e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 31 RFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGfnWSGD-ICYSSDYFDQLYA 109
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMG--WKPDwVTFSSDYFDQLHE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 110 YAVELINKGLAYVDELSADEIREYRgtltQPGKNSPFRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMRDP 189
Cdd:PTZ00437 133 FAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 190 VLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIpVHPRQYEFSRLNLEYTVM 269
Cdd:PTZ00437 209 IAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSLL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 270 SKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDP 349
Cdd:PTZ00437 288 SKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 350 VKLVIENYPqgGSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFR-EEANKQYKRLVLG-KEVRLRNAYVIKAERVEKD 427
Cdd:PTZ00437 368 IKVVVDNWK--GEREFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKYSGNVVCKGFEVD 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 428 AEGNITTIFCTYDAETLSKDpadgrkvKGVIHWVSAQHALPVEIRLYDRLFSVPNPGAAEDFLAVINPESLIIKQGYAEP 507
Cdd:PTZ00437 446 AAGQPSVIHVDIDFERKDKP-------KTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEK 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 505384025 508 SLKAAEAGKAFQFEREGYFCLDSRySTAEKPVFNRTVGLRDTWTK 552
Cdd:PTZ00437 519 GIENAKHFESVQAERFGYFVVDPD-TRPDHLVMNRVLGLREDKEK 562
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
6.00e-168 |
|
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: 478.74 E-value: 6.00e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDICYSSDYFDQL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 108 YAYAVELINKGLAYVDELSADEIREYRGTltQPGKNSPFRDRSVEENLALF-EKMRAGGFEEGKACLRAKIDMASPfIVM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREE--QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 187 RDPVLYRIKFAE---HHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505384025 264 LEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQ-DNTIEMASLESCIREDLNE 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-342 |
5.36e-156 |
|
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: 445.16 E-value: 5.36e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWsGDICYSSDYFDQ 106
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 107 LYAYAVELINKGLAYVdelsadeireyrgtltqpgknspfrdrsveenlalfekmraggfeegkaclrakidmaspfivm 186
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 187 rdpvlyrikfaeHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEY 266
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505384025 267 TVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPR 342
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-526 |
3.37e-137 |
|
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: 406.10 E-value: 3.37e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 26 TTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDICYSSDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 106 QLYAYAVELINKGLAYVDELSADEIREYRGTLTQPGKN----SPFRDRSVEENlalfEKMRAGGFEegkACLRAKI---- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEEL----ERMLAAGEP---PVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 178 ----DMAS-----PFIVMRDPVLYRikfaehhQTGnkwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNI 248
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 249 TIPVhPrqyEFSRLNLEY----TVMSKRKlnllvtdKHVegwddprmpTISGLRRRGYTSASIREFCKRIGVTKQDNT-- 322
Cdd:COG0008 224 GWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQei 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 323 IEMASLESCIreDLNENaPRAMAVIDPVKLVIENYPQggseLVSMPN-------HPNKPEMG-----TRDVPFSGE---- 386
Cdd:COG0008 284 FSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPY----IRALDDeelaellAPELPEAGiredlERLVPLVRErakt 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 387 ----------IWIDRADfrEEANKqyKRLVLgKEVRLrnayVIKAERvekDAEGNITtifcTYDAETlskdpadgrkVKG 456
Cdd:COG0008 357 lselaelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL---EVLEAVE----TWDPET----------VKG 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505384025 457 VIHWVSAQHalpvEIRlyDRLFSVPnpgaaedfLAVinpeslIIKQGYAEPSLKAAEA--GKAFQFEREGYF 526
Cdd:COG0008 411 TIHWVSAEA----GVK--DGLLFMP--------LRV------ALTGRTVEPSLFDVLEllGKERVFERLGYA 462
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
19-539 |
1.09e-124 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 382.54 E-value: 1.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 19 DLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSgDIC 98
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 99 YSSDYFDQLYAYAVELINKGLAYVDELSADEIREYRGTltqpGKNSPFRDRSVEENLALFEKMRAGGfEEGKAC-LRAKI 177
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGS-ERGLQCcVRGKL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 178 DMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIP-VHprQ 256
Cdd:PLN02907 359 DMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRkVH--I 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 257 YEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDL 336
Cdd:PLN02907 437 WEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKII 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 337 NENAPRAMAVIDP--VKLVIENYPQgGSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFREeankqykrLVLGKEVRLR 414
Cdd:PLN02907 517 DPVCPRHTAVLKEgrVLLTLTDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLM 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 415 ---NAYVikaERVEKDAEGNITTIFCTYDAEtlskdpADGRKVKGVIHWVSAQHAL-PVEIRLYDRLFSVPNPGAAEDFL 490
Cdd:PLN02907 588 dwgNAII---KEITKDEGGAVTALSGELHLE------GSVKTTKLKLTWLPDTNELvPLSLVEFDYLITKKKLEEDDNFL 658
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 505384025 491 AVINPESLIIKQGYAEPSLKAAEAGKAFQFEREGYFCLDSRYSTAEKPV 539
Cdd:PLN02907 659 DVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSSKPI 707
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
19-530 |
1.69e-118 |
|
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: 361.06 E-value: 1.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 19 DLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSgDIC 98
Cdd:TIGR00463 85 ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 99 YSSDYFDQLYAYAVELINKGLAYVDELSADEIREYRGTltqpGKNSPFRDRSVEENLALFEKMRAGGFEEGKACLRAKID 178
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 179 MASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR--LYDWVLDNITIPVHpRQ 256
Cdd:TIGR00463 240 LKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqEYIYRYFGWEPPEF-IH 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 257 YEFSRLNLEYTVMSKRKLNLLVtDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDL 336
Cdd:TIGR00463 319 WGRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKII 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 337 NENAPRAMAVIDPVKLVIENYPqgGSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFREeankqykrlvLGKEVRLRNA 416
Cdd:TIGR00463 398 DEEARRYFFIWNPVKIEIVGLP--EPKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEE----------GVEPVRLMDA 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 417 YVIKAErvEKDAEgnittiFCTYDAEtlskdpADGRKVKGVIHWVSAQHALPVEirlydrlfsvpnpgaaedflaVINPE 496
Cdd:TIGR00463 466 VNVIYS--KKELR------YHSEGLE------GARKLGKSIIHWLPAKDAVKVK---------------------VIMPD 510
|
490 500 510
....*....|....*....|....*....|....
gi 505384025 497 SLiIKQGYAEPSLKAAEAGKAFQFEREGYFCLDS 530
Cdd:TIGR00463 511 AS-IVEGVIEADASELEVGDVVQFERFGFARLDS 543
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
28-530 |
1.69e-115 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 353.77 E-value: 1.69e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPV--KEDIEYVESIKNDVQWLGFNWSgDICYSSDYFD 105
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 106 QLYAYAVELINKGLAYVDELSADEIREYRGTltqpGKNSPFRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIV 185
Cdd:PRK04156 181 IYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 186 MRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDN----RRLYD---WVLdnitipvhPRQYE 258
Cdd:PRK04156 257 VRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNtekqRYIYDyfgWEY--------PETIH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 259 FSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDLNE 338
Cdd:PRK04156 329 YGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 339 NAPRAMAVIDPVKLVIENYPqggSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFREeankqykrlvLGKEVRLRNAYV 418
Cdd:PRK04156 409 IANRYFFVRDPVELEIEGAE---PLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEA----------EGKMVRLMDLFN 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 419 IKAERVEKDAegnittifctydAETLSKDPADGRKVKG-VIHWVSAQHALPVEirlydrlfsvpnpgaaedflaVINPES 497
Cdd:PRK04156 476 VEITGVSVDK------------ARYHSDDLEEARKNKApIIQWVPEDESVPVR---------------------VLKPDG 522
|
490 500 510
....*....|....*....|....*....|...
gi 505384025 498 lIIKQGYAEPSLKAAEAGKAFQFEREGYFCLDS 530
Cdd:PRK04156 523 -GDIEGLAEPDVADLEVDDIVQFERFGFVRIDS 554
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
1-530 |
6.41e-111 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 343.10 E-value: 6.41e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 1 MSEAEARPSNFIRQiidedLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVE 80
Cdd:PTZ00402 31 FTAANANEENDKLQ-----LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 81 SIKNDVQWLGFNWSGDICYSSDYFDQLYAYAVELINKGLAYVDELSADEIREYRGTltqpGKNSPFRDRSVEENLALFEK 160
Cdd:PTZ00402 106 AILDDLATLGVSWDVGPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 161 MRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PTZ00402 182 MKKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 241 YDWVLDNITIPvHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQD 320
Cdd:PTZ00402 262 YYWFCDALGIR-KPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 321 NTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYPQGGSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFreeank 400
Cdd:PTZ00402 341 NFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDV------ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 401 qyKRLVLGKEVRLR---NAYVIKAERveKDAEGNITtifctyDAETLSKDPADGRKVKGVIHWV-SAQHALPVEIRLYDR 476
Cdd:PTZ00402 415 --ALLKEGDEVTLMdwgNAYIKNIRR--SGEDALIT------DADIVLHLEGDVKKTKFKLTWVpESPKAEVMELNEYDH 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 505384025 477 LFSVPNPGAAEDFLAVINPESLIIKQGYAEPSLKAAEAGKAFQFEREGYFCLDS 530
Cdd:PTZ00402 485 LLTKKKPDPEESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDD 538
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
28-539 |
3.80e-106 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 328.51 E-value: 3.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNwSGDICYSSDYFDQL 107
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 108 YAYAVELINKGLAYVDELSADEIREYRGTLTQpgknSPFRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMR 187
Cdd:PLN03233 91 RCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 188 DPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEYT 267
Cdd:PLN03233 167 DPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAFARMNFMNT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 268 VMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAV- 346
Cdd:PLN03233 246 VLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAId 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 347 -IDPVKLVIENYPQGGSELVSMPN-HPNKPEMGTRDVPFSGEIWIDRADfreeankqYKRLVLGKEVRLRNAYVIKAERV 424
Cdd:PLN03233 326 kADHTALTVTNADEEADFAFSETDcHPKDPGFGKRAMRICDEVLLEKAD--------TEDIQLGEDIVLLRWGVIEISKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 425 EKDAEGNITTifctydaetlskdPADGRKVKGVIHWVS-AQHALPVEIRLYDRLFSVPNPGAAEDFLAVINPESLIIKQG 503
Cdd:PLN03233 398 DGDLEGHFIP-------------DGDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDV 464
|
490 500 510
....*....|....*....|....*....|....*.
gi 505384025 504 YAEPSLKAAEAGKAFQFEREGYFCLDSRYSTAEKPV 539
Cdd:PLN03233 465 IGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPL 500
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
340-529 |
5.58e-84 |
|
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: 258.74 E-value: 5.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 340 APRAMAVIDPVKLVIENYPQGGSELVSMPNHPNKPEMGTRDVPFSGEIWIDRADFreeankqyKRLVLGKEVRLRNAYVI 419
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 420 KAERVEKDAEGNITTIFCTYDAETLSKDpadgRKVKG-VIHWVSAQHALPVEIRLYDRLFSVPNpgaAEDFlaVINPESL 498
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED---DADF--LLNPDSL 143
|
170 180 190
....*....|....*....|....*....|..
gi 505384025 499 -IIKQGYAEPSLKAAEAGKAFQFEREGYFCLD 529
Cdd:pfam03950 144 kVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
27-338 |
1.86e-82 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 257.02 E-value: 1.86e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDICYSSDYFDQ 106
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 107 LYAYAVELINKGlayvdelsadeireyrgtltqpgknspfrdrsveenlalfekmraggfeegkaclrakidmaspfivm 186
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 187 rdpvlyrikfaehhqtgnkwcIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEY 266
Cdd:cd00418 93 ---------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLED 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 267 -TVMSKRKLNllvtdkhvegwddprmPTISGLRRRGYTSASIREFCKRIGVTK-----------------------QDNT 322
Cdd:cd00418 151 gTKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKpdghelftleemiaafsvervnsADAT 214
|
330
....*....|....*.
gi 505384025 323 IEMASLESCIREDLNE 338
Cdd:cd00418 215 FDWAKLEWLNREYIRE 230
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
28-342 |
1.33e-49 |
|
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: 171.38 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNP--VKEDIEYVESIKNDVQWLGFNWSgDICYSSDYFD 105
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 106 QLYAYAVELINKGLAYVdelsadeireyrgtltqpgknspfrdrsveenlalfekmraggfeegkaclrakidmaspfiv 185
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 186 mrdpvlyrikfaeHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR----LYD---WVldnitipvHPRQYE 258
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEkqryIYEyfgWE--------YPETIH 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 259 FSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTSASIREFCKRIGVTKQDNTIEMASLESCIREDLNE 338
Cdd:cd09287 157 WGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDP 236
|
....
gi 505384025 339 NAPR 342
Cdd:cd09287 237 RANR 240
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
29-273 |
2.57e-19 |
|
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: 84.45 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 29 HTRFPPEPNGYLHIGHAKSICLNFGIAQD-----YQGQCNLRFDDTNPVKEDIEYVesikndvqwlgfnwsgdicyssdy 103
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDPANK------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 104 fdqlyayavelinkglayvdelsadeireyrgtltqPGKNSP-FRDRSVEENLALFEkmraggfeegkaclrakidmasp 182
Cdd:cd00802 57 ------------------------------------KGENAKaFVERWIERIKEDVE----------------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 183 fivmrdpvlyrikfaehhqtgnkwciypmYDFTHCISDALEGITH---SLCTLEFQDNRRLYDWVLDNITIPVHPRQYEF 259
Cdd:cd00802 78 -----------------------------YMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLTF 128
|
250
....*....|....*
gi 505384025 260 SRLNLEY-TVMSKRK 273
Cdd:cd00802 129 GRVMGADgTKMSKSK 143
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
30-121 |
4.68e-14 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 72.96 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDICYSSDYFDqLYA 109
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD-AYR 86
|
90
....*....|...
gi 505384025 110 YAVE-LINKGLAY 121
Cdd:PRK05710 87 AALDrLRAQGLVY 99
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
29-111 |
9.05e-14 |
|
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: 67.56 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 29 HTRFPPEPnGYLHIGHAKSICLNFGIAqdyqGQCNLRFDDTNPVK------EDIEYVESIKNDVQWLGFNWSGDIcyssD 102
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNR----E 71
|
....*....
gi 505384025 103 YFDQLYAYA 111
Cdd:cd02156 72 LYRWVKDNI 80
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
227-273 |
1.70e-13 |
|
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: 66.79 E-value: 1.70e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 505384025 227 HSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRK 273
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
27-118 |
1.52e-12 |
|
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: 67.61 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDIC-------- 98
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDvggpygpy 80
|
90 100
....*....|....*....|
gi 505384025 99 YSSDYFDQLYAYAVELINKG 118
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG 100
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| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
21-229 |
1.64e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 53.98 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 21 ASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPVKEDIEYVESIKNDVQWLGFNWSGDICYS 100
Cdd:PLN02627 39 GESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384025 101 SDY--FDQ-----LY-AYAVELINKGLAY-----VDELSA-DEIREYRGtlTQPGKNSPFRDRSVEENLALFEK------ 160
Cdd:PLN02627 119 GEYgpYRQsernaIYkQYAEKLLESGHVYpcfctDEELEAmKEEAELKK--LPPRYTGKWATASDEEVQAELAKgtpyty 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505384025 161 ---MRAGGFEEGKACLRAKI----DMASPFIVMRdpvlyrikfaehhQTGNkwciyPMYDFTHCISDALEGITHSL 229
Cdd:PLN02627 197 rfrVPKEGSVKIDDLIRGEVswntDTLGDFVLLR-------------SNGQ-----PVYNFCVAVDDATMGITHVI 254
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