|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
23-572 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1086.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 23 DAAQQEQQPGLDFVRQVITDDLAAGRTEKVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEY 102
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 103 VDGIANDVKWLGFNWNGEPRYASSYFDQLYSWAVQLIEQGDAYVDLQTPEEIKLNRGSFVEPGKNSPYRDASVEDNLARF 182
Cdd:PRK05347 81 VDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 183 EQMRNGALGEGQAVLRAKIDMASPNVHMRDPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHR 262
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 263 PFYDWVVEKVKSAAVPRQYESSRLNVDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSK 342
Cdd:PRK05347 241 PLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 343 SDGIVDVAMLEYCIRQSLENTAARGMAVLNPLKVTLTNLPAEM--DLTHSRHP-NVDMGERVIPLTSEIYIDRKDFEEEP 419
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQveELEAPNHPeDPEMGTREVPFSRELYIEREDFMEEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 420 PKGFKRLIPGGEVRLRHAYVIKCDEIIKDDKGEIIELKCSIDPETLGKNP-EGRKVKGVIHWVSATKGVKAEVRIYDRLF 498
Cdd:PRK05347 401 PKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPaDGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514970759 499 TESDPEVGDDFLANLNPDSLKVVQAVIEPALAQAQAEDRFQFEREGYFVADQyDHSSETPVFNRILDLKDSFKP 572
Cdd:PRK05347 481 TVPNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADK-DSTPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
52-570 |
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: 718.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 52 VITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSYFDQL 131
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 132 YSWAVQLIEQGDAYVDLQTPEEIKLNRGSFVEPGKNSPYRDASVEDNLARFEQMRNGALGEGQAVLRAKIDMASPNVHMR 211
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 212 DPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVKSAAVPRQYESSRLNVDYT 291
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 292 ITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQSLENTAARGMAVL 371
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 372 NPLKVTLTNLPAEMDL-THSRHPNV-DMGERVIPLTSEIYIDRKDFEEEPPKGFKRLIPGGEVRLRHAYVIKCDEIIKDD 449
Cdd:TIGR00440 321 DPVEVVIENLSDEYELaTIPNHPNTpEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 450 KGEIIELKCSIDPETLGKNP-EGRKVKGVIHWVSATKGVKAEVRIYDRLFTESDPEVGDDFLANLNPDSLKVVQAVIEPA 528
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPaDGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 514970759 529 LAQAQAEDRFQFEREGYFVADQYDHSSETPVFNRILDLKDSF 570
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
51-366 |
1.01e-138 |
|
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: 402.02 E-value: 1.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWnGEPRYASSYFDQ 130
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 131 LYSWAVQLIEQGDAYVdlqtpeeiklnrgsfvepgknspyrdasvednlarfeqmrngalgegqavlrakidmaspnvhm 210
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 211 rdpilyrvlhseHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVkSAAVPRQYESSRLNVDY 290
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL-RLYRPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514970759 291 TITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQSLENTAAR 366
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
51-361 |
5.59e-136 |
|
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: 397.85 E-value: 5.59e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSYFDQ 130
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 131 LYSWAVQLIEQGDAYVDLQTPEEIKLNRGSfvEPGKNSPYRDASVEDNLARF-EQMRNGALGEGQAVLRAKIDMASPNVh 209
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREE--QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESPYV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 210 MRDPILYRVLHSE---HHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVKSAAVPRQYESSRL 286
Cdd:pfam00749 158 FRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514970759 287 NVDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGI-VDVAMLEYCIRQSLE 361
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
51-548 |
6.88e-125 |
|
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: 375.29 E-value: 6.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSYFDQ 130
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 131 LYSWAVQLIEQGDAYVDLQTPEEIKLNRGSFVEPGKNSPY----RDASVEDnLARFEqmrngALGEgQAVLRAKI----- 201
Cdd:COG0008 84 YYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE-LERML-----AAGE-PPVLRFKIpeegv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 202 ---DMAS-----PNVHMRDPILYRVlhsehhqTGdkwkmYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVK 273
Cdd:COG0008 157 vfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 274 sAAVPrQYesSRLNVDY----TITSKRKlrrlvegGFVkgwddprmpTVVGMRRRGFTPEGLRDFCKRVGVSKSDG--IV 347
Cdd:COG0008 225 -WEPP-EF--AHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqeIF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 348 DVAMLEYCIrqSLENTaARGMAVLNPLKVTLTN------LPAEMDLTHSRHPNVDMG-----ERVIPLTSE--------- 407
Cdd:COG0008 285 SLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAGiredlERLVPLVREraktlsela 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 408 -----IYIDRKDfeEEPPKgfKRLIPgGEVRlrhayvikcdEIIKDDKGEIIELKcSIDPETlgknpegrkVKGVIHWVS 482
Cdd:COG0008 362 elarfFFIERED--EKAAK--KRLAP-EEVR----------KVLKAALEVLEAVE-TWDPET---------VKGTIHWVS 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514970759 483 ATKGVKaevriyDRLFTesdpevgddflanlNPDSLKVVQAVIEPALAQAQA---EDRFqFEREGYFVA 548
Cdd:COG0008 417 AEAGVK------DGLLF--------------MPLRVALTGRTVEPSLFDVLEllgKERV-FERLGYAID 464
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
23-572 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1086.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 23 DAAQQEQQPGLDFVRQVITDDLAAGRTEKVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEY 102
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 103 VDGIANDVKWLGFNWNGEPRYASSYFDQLYSWAVQLIEQGDAYVDLQTPEEIKLNRGSFVEPGKNSPYRDASVEDNLARF 182
Cdd:PRK05347 81 VDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 183 EQMRNGALGEGQAVLRAKIDMASPNVHMRDPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHR 262
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 263 PFYDWVVEKVKSAAVPRQYESSRLNVDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSK 342
Cdd:PRK05347 241 PLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 343 SDGIVDVAMLEYCIRQSLENTAARGMAVLNPLKVTLTNLPAEM--DLTHSRHP-NVDMGERVIPLTSEIYIDRKDFEEEP 419
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQveELEAPNHPeDPEMGTREVPFSRELYIEREDFMEEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 420 PKGFKRLIPGGEVRLRHAYVIKCDEIIKDDKGEIIELKCSIDPETLGKNP-EGRKVKGVIHWVSATKGVKAEVRIYDRLF 498
Cdd:PRK05347 401 PKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPaDGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514970759 499 TESDPEVGDDFLANLNPDSLKVVQAVIEPALAQAQAEDRFQFEREGYFVADQyDHSSETPVFNRILDLKDSFKP 572
Cdd:PRK05347 481 TVPNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADK-DSTPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
23-574 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 833.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 23 DAAQQEQQPGLDFVRQVITDDLAAGRTEKVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEY 102
Cdd:PRK14703 3 DAPRPRMLVSPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 103 VDGIANDVKWLGFNWNGEPRYASSYFDQLYSWAVQLIEQGDAYVDLQTPEEIKLNRGSFVEPGKNSPYRDASVEDNLARF 182
Cdd:PRK14703 83 VEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 183 EQMRNGALGEGQAVLRAKIDMASPNVHMRDPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHR 262
Cdd:PRK14703 163 RRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 263 PFYDWVVEKVKSAAV-PRQYESSRLNVDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVS 341
Cdd:PRK14703 243 AIYDWVLDHLGPWPPrPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 342 KSDGIVDVAMLEYCIRQSLENTAARGMAVLNPLKVTLTNLPA----EMDLTHSRHPNVDMGERVIPLTSEIYIDRKDFEE 417
Cdd:PRK14703 323 KTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAgkveELDLPYWPHDVPKEGSRKVPFTRELYIERDDFSE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 418 EPPKGFKRLIPGGEVRLRHAYVIKCDEIIKDDKGEIIELKCSIDPETLGKNPEGRKVKGVIHWVSATKGVKAEVRIYDRL 497
Cdd:PRK14703 403 DPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRKAAGVIHWVSAKHALPAEVRLYDRL 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514970759 498 FTESDPEVGD-DFLANLNPDSLKVVQAVIEPALAQAQAEDRFQFEREGYFVADQYDHSSETPVFNRILDLKDSFKPGK 574
Cdd:PRK14703 483 FKVPQPEAADeDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
52-570 |
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: 718.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 52 VITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSYFDQL 131
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 132 YSWAVQLIEQGDAYVDLQTPEEIKLNRGSFVEPGKNSPYRDASVEDNLARFEQMRNGALGEGQAVLRAKIDMASPNVHMR 211
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 212 DPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVKSAAVPRQYESSRLNVDYT 291
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 292 ITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQSLENTAARGMAVL 371
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 372 NPLKVTLTNLPAEMDL-THSRHPNV-DMGERVIPLTSEIYIDRKDFEEEPPKGFKRLIPGGEVRLRHAYVIKCDEIIKDD 449
Cdd:TIGR00440 321 DPVEVVIENLSDEYELaTIPNHPNTpEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 450 KGEIIELKCSIDPETLGKNP-EGRKVKGVIHWVSATKGVKAEVRIYDRLFTESDPEVGDDFLANLNPDSLKVVQAVIEPA 528
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPaDGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 514970759 529 LAQAQAEDRFQFEREGYFVADQYDHSSETPVFNRILDLKDSF 570
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
51-574 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 564.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGfnWngEP---RYASSY 127
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--W--EPfkiTYTSDY 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 128 FDQLYSWAVQLIEQGDAYVDLQTPEEIKLNRgsfvEPGKNSPYRDASVEDNLARFEQMRNGALGEGQAVLRAKIDMASPN 207
Cdd:PLN02859 340 FQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDN 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 208 VHMRDPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVkSAAVPRQYESSRLN 287
Cdd:PLN02859 416 FNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL-GLYQPYVWEYSRLN 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 288 VDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDG-IVDVAMLEYCIRQSLENTAAR 366
Cdd:PLN02859 495 VTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIRMDRLEHHIREELNKTAPR 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 367 GMAVLNPLKVTLTNLPAE--MDLTHSRHPNVDMGERV----IPLTSEIYIDRKDFEEEPPKGFKRLIPGGEVRLRHAYVI 440
Cdd:PLN02859 575 TMVVLHPLKVVITNLESGevIELDAKRWPDAQNDDPSafykVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPI 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 441 KCDEII-KDDKGEIIELKCSIDPEtlgknpEGRKVKGVIHWVSA----TKGVKAEVRIYDRLFTESDPEVGDDFLANLNP 515
Cdd:PLN02859 655 KCTDVVlADDNETVVEIRAEYDPE------KKTKPKGVLHWVAEpspgVEPLKVEVRLFDKLFLSENPAELEDWLEDLNP 728
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 516 DSLKVVQ-AVIEPALAQAQAEDRFQFEREGYFVADQyDHSSETPVFNRILDLKDSFKPGK 574
Cdd:PLN02859 729 QSKEVISgAYAVPSLKDAKVGDRFQFERLGYFAVDK-DSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
55-568 |
7.26e-153 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 450.97 E-value: 7.26e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 55 RFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGF--NWngePRYASSYFDQLY 132
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDW---VTFSSDYFDQLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 133 SWAVQLIEQGDAYVDLQTPEEIKLNRgsfvEPGKNSPYRDASVEDNLARFEQMRNGALGEGQAVLRAKIDMASPNVHMRD 212
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 213 PILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVkSAAVPRQYESSRLNVDYTI 292
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEEL-NLWRPHVWEFSRLNVTGSL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 293 TSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQSLENTAARGMAVLN 372
Cdd:PTZ00437 287 LSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVID 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 373 PLKVTLTNLPAEMD---LTHSRHPnvDMGERVIPLTSEIYIDRKDFE-EEPPKGFKRLIPGGE-VRLRHAYVIKCDEIIK 447
Cdd:PTZ00437 367 PIKVVVDNWKGEREfecPNHPRKP--ELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGPRvVGLKYSGNVVCKGFEV 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 448 DDKGEIIELKCSIDPEtlgknpEGRKVKGVIHWVSATKGVKAEVRIYDRLFTESDPEVGDDFLANLNPDSLKVVQAVIEP 527
Cdd:PTZ00437 445 DAAGQPSVIHVDIDFE------RKDKPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEK 518
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 514970759 528 ALAQAQAEDRFQFEREGYFVADQyDHSSETPVFNRILDLKD 568
Cdd:PTZ00437 519 GIENAKHFESVQAERFGYFVVDP-DTRPDHLVMNRVLGLRE 558
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
51-366 |
1.01e-138 |
|
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: 402.02 E-value: 1.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWnGEPRYASSYFDQ 130
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 131 LYSWAVQLIEQGDAYVdlqtpeeiklnrgsfvepgknspyrdasvednlarfeqmrngalgegqavlrakidmaspnvhm 210
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 211 rdpilyrvlhseHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVkSAAVPRQYESSRLNVDY 290
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL-RLYRPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514970759 291 TITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQSLENTAAR 366
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
51-361 |
5.59e-136 |
|
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: 397.85 E-value: 5.59e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSYFDQ 130
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 131 LYSWAVQLIEQGDAYVDLQTPEEIKLNRGSfvEPGKNSPYRDASVEDNLARF-EQMRNGALGEGQAVLRAKIDMASPNVh 209
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREE--QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESPYV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 210 MRDPILYRVLHSE---HHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVKSAAVPRQYESSRL 286
Cdd:pfam00749 158 FRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514970759 287 NVDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGI-VDVAMLEYCIRQSLE 361
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
51-548 |
6.88e-125 |
|
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: 375.29 E-value: 6.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSYFDQ 130
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 131 LYSWAVQLIEQGDAYVDLQTPEEIKLNRGSFVEPGKNSPY----RDASVEDnLARFEqmrngALGEgQAVLRAKI----- 201
Cdd:COG0008 84 YYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE-LERML-----AAGE-PPVLRFKIpeegv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 202 ---DMAS-----PNVHMRDPILYRVlhsehhqTGdkwkmYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVK 273
Cdd:COG0008 157 vfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 274 sAAVPrQYesSRLNVDY----TITSKRKlrrlvegGFVkgwddprmpTVVGMRRRGFTPEGLRDFCKRVGVSKSDG--IV 347
Cdd:COG0008 225 -WEPP-EF--AHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqeIF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 348 DVAMLEYCIrqSLENTaARGMAVLNPLKVTLTN------LPAEMDLTHSRHPNVDMG-----ERVIPLTSE--------- 407
Cdd:COG0008 285 SLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAGiredlERLVPLVREraktlsela 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 408 -----IYIDRKDfeEEPPKgfKRLIPgGEVRlrhayvikcdEIIKDDKGEIIELKcSIDPETlgknpegrkVKGVIHWVS 482
Cdd:COG0008 362 elarfFFIERED--EKAAK--KRLAP-EEVR----------KVLKAALEVLEAVE-TWDPET---------VKGTIHWVS 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514970759 483 ATKGVKaevriyDRLFTesdpevgddflanlNPDSLKVVQAVIEPALAQAQA---EDRFqFEREGYFVA 548
Cdd:COG0008 417 AEAGVK------DGLLF--------------MPLRVALTGRTVEPSLFDVLEllgKERV-FERLGYAID 464
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
43-559 |
2.31e-112 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 350.95 E-value: 2.31e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 43 DLAAGRTEKVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNgEPR 122
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 123 YASSYFDQLYSWAVQLIEQGDAYVDlQTP-EEIKLNRGSFVEpgknSPYRDASVEDNLARFEQMRNGALGEGQAVLRAKI 201
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVD-DTPrEQMRKERMDGIE----SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 202 DMASPNVHMRDPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEkvkSAAVPRQ- 280
Cdd:PLN02907 359 DMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILE---DMGLRKVh 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 281 -YESSRLNVDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQS 359
Cdd:PLN02907 436 iWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKI 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 360 LENTAARGMAVLNPLKV--TLTNLPAE----MDLTHSRHPnvDMGERVIPLTSEIYIDRKDFEEeppkgfkrLIPGGEVR 433
Cdd:PLN02907 516 IDPVCPRHTAVLKEGRVllTLTDGPETpfvrIIPRHKKYE--GAGKKATTFTNRIWLDYADAEA--------ISEGEEVT 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 434 LR---HAyVIKcdEIIKDDKGEIIELKCSIdpetlgkNPEG--RKVKGVIHWVSATKG-VKAEVRIYDRLFTESDPEVGD 507
Cdd:PLN02907 586 LMdwgNA-IIK--EITKDEGGAVTALSGEL-------HLEGsvKTTKLKLTWLPDTNElVPLSLVEFDYLITKKKLEEDD 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 514970759 508 DFLANLNPDSLKVVQAVIEPALAQAQAEDRFQFEREGYFVADQYDHSSETPV 559
Cdd:PLN02907 656 NFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSSKPI 707
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
51-549 |
9.80e-104 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 324.99 E-value: 9.80e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSYFDQ 130
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 131 LYSWAVQLIEQGDAYVDLQTPEEIKLNRGSfvepGKNSPYRDASVEDNLARFEQMRNGAlGEGQ-AVLRAKIDMASPNVH 209
Cdd:PTZ00402 132 MYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGS-AEGQeTCLRAKISVDNENKA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 210 MRDPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVkSAAVPRQYESSRLNVD 289
Cdd:PTZ00402 207 MRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDAL-GIRKPIVEDFSRLNME 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 290 YTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQSLENTAARGMA 369
Cdd:PTZ00402 286 YSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTV 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 370 VLNPLKVTLT-----NLPAEMDLTHSRHPnvDMGERVIPLTSEIYIDRKDfeeeppkgFKRLIPGGEVRLR---HAYvik 441
Cdd:PTZ00402 366 VSNTLKVRCTvegqiHLEACEKLLHKKVP--DMGEKTYYKSDVIFLDAED--------VALLKEGDEVTLMdwgNAY--- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 442 cdeiIKDDK--GEiielKCSIDPETLGKNPEG--RKVKGVIHWVSAT-KGVKAEVRIYDRLFTESDP---EVGDDFLANL 513
Cdd:PTZ00402 433 ----IKNIRrsGE----DALITDADIVLHLEGdvKKTKFKLTWVPESpKAEVMELNEYDHLLTKKKPdpeESIDDIIAPV 504
|
490 500 510
....*....|....*....|....*....|....*..
gi 514970759 514 NpdslKVVQAVI-EPALAQAQAEDRFQFEREGYFVAD 549
Cdd:PTZ00402 505 T----KYTQEVYgEEALSVLKKGDIIQLERRGYYIVD 537
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
43-560 |
4.87e-101 |
|
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: 316.76 E-value: 4.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 43 DLAAGRTEKVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNgEPR 122
Cdd:TIGR00463 85 ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 123 YASSYFDQLYSWAVQLIEQGDAYVDLQTPEEIKLNRGSfvepGKNSPYRDASVEDNLARFEQMRNGALGEGQAVLRAKID 202
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 203 MASPNVHMRDPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRP-------FYDWVVEKVKsa 275
Cdd:TIGR00463 240 LKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqeyiyrYFGWEPPEFI-- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 276 avprQYESSRLNVDYTITSKRKLRRLVEGGFVkGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYC 355
Cdd:TIGR00463 318 ----HWGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYAL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 356 IRQSLENTAARGMAVLNPLKVTLTNLPA---EMDLTHSRHPNVdmGERVIPLTSEIYIDRKDFEEEPPkgfkrlipggEV 432
Cdd:TIGR00463 393 NRKIIDEEARRYFFIWNPVKIEIVGLPEpkrVERPLHPDHPEI--GERVLILRGEIYVPKDDLEEGVE----------PV 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 433 RLRHAYVIkcdeiikddkgeIIELKcsiDPETLGKNPEGRKVKG--VIHWVSATKGVKAEVRIYDRLFTEsdpevgddfl 510
Cdd:TIGR00463 461 RLMDAVNV------------IYSKK---ELRYHSEGLEGARKLGksIIHWLPAKDAVKVKVIMPDASIVE---------- 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 514970759 511 anlnpdslkvvqAVIEPALAQAQAEDRFQFEREGYFVADQYDHSSETPVF 560
Cdd:TIGR00463 516 ------------GVIEADASELEVGDVVQFERFGFARLDSADKDGMVFVY 553
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
50-545 |
6.17e-95 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 301.00 E-value: 6.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 50 EKVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAE--EQEYVDGIANDVKWLGFNWNgEPRYASSY 127
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKrpDPEAYDMILEDLKWLGVKWD-EVVIQSDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 128 FDQLYSWAVQLIEQGDAYVDLQTPEEIKLNRGSfvepGKNSPYRDASVEDNLARFEQMRNGALGEGQAVLRAKIDMASPN 207
Cdd:PRK04156 179 LEIYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 208 VHMRDPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHslcTLEFQDH-------RPFYD---WVvekvksaaV 277
Cdd:PRK04156 255 PSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTH---VLRGKDHidntekqRYIYDyfgWE--------Y 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 278 PRQYESSRLNVDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDgiVDVAM--LEYC 355
Cdd:PRK04156 324 PETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETD--ATISWenLYAI 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 356 IRQSLENTAARGMAVLNPLKVTLTNLPaEMDLTHSRHPNV-DMGERVIPLTSEIYIDRKDFEEEppkgfkrlipGGEVRL 434
Cdd:PRK04156 402 NRKLIDPIANRYFFVRDPVELEIEGAE-PLEAKIPLHPDRpERGEREIPVGGKVYVSSDDLEAE----------GKMVRL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 435 RHAYVIKCDEIikddkgEIIELKC-SIDPEtlgknpEGRKVKG-VIHWVSATKGVKAEVRIydrlftesdPEVGDdflan 512
Cdd:PRK04156 471 MDLFNVEITGV------SVDKARYhSDDLE------EARKNKApIIQWVPEDESVPVRVLK---------PDGGD----- 524
|
490 500 510
....*....|....*....|....*....|...
gi 514970759 513 lnpdslkvVQAVIEPALAQAQAEDRFQFEREGY 545
Cdd:PRK04156 525 --------IEGLAEPDVADLEVDDIVQFERFGF 549
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
44-559 |
1.13e-92 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 293.84 E-value: 1.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 44 LAAGRTEKVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNgEPRY 123
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPD-SVSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 124 ASSYFDQLYSWAVQLIEQGDAYVDLQTPEEIKLNRGSFVEpgknSPYRDASVEDNLARFEQMRNGALGEGQAVLRAKIDM 203
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 204 ASPNVHMRDPILYRVLHSEHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVKSAAvPRQYES 283
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRR-PRIHAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 284 SRLNVDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQSLENT 363
Cdd:PLN03233 238 ARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 364 AARGMAV--LNPLKVTLTNLPAEMDLTHSR---HP-NVDMGERVIPLTSEIYIDRKDFEEeppkgfkrLIPGGEVRLRHA 437
Cdd:PLN03233 318 AKRFMAIdkADHTALTVTNADEEADFAFSEtdcHPkDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLLRW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 438 YVIKCDEIIKDDKGEIIelkcsidpetlgknPEG--RKVKGVIHWVS-ATKGVKAEVRIYDRLFTESDPEVGDDFLANLN 514
Cdd:PLN03233 390 GVIEISKIDGDLEGHFI--------------PDGdfKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFIN 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 514970759 515 PDSLKVVQAVIEPALAQAQAEDRFQFEREGYFVADQYDHSSETPV 559
Cdd:PLN03233 456 PDTLAETDVIGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPL 500
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
364-549 |
1.05e-69 |
|
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: 222.15 E-value: 1.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 364 AARGMAVLNPLKVTLTNLPA--EMDLTHSRHPNV-DMGERVIPLTSEIYIDRKDFeeeppkgfKRLIPGGEVRLRHAYVI 440
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEgqEETAEVPNHPKNpELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 441 KCDEIIKDDKGEIIELKCSIDPETLGKNpegRKVKG-VIHWVSATKGVKAEVRIYDRLFTESDpevGDDFLanLNPDSLK 519
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA---RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED---DADFL--LNPDSLK 144
|
170 180 190
....*....|....*....|....*....|.
gi 514970759 520 VV-QAVIEPALAQAQAEDRFQFEREGYFVAD 549
Cdd:pfam03950 145 VLtEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
51-361 |
8.37e-63 |
|
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: 206.17 E-value: 8.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSYFDQ 130
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 131 LYSWAVQLIEQGdayvdlqtpeeiklnrgsfvepgknspyrdasvednlarfeqmrngalgegqavlrakidmaspnvhm 210
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 211 rdpilyrvlhsehhqtgdkwkMYPMYDYAHPLSDAIEGITHSLCTLEFQDHRPFYDWVVEKVkSAAVPRQYESSRLNVDY 290
Cdd:cd00418 93 ---------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEAL-GWEPPRFYHFPRLLLED 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514970759 291 -TITSKRKLRrlveggfvkgwddprmPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQSLE 361
Cdd:cd00418 151 gTKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVE 206
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
51-366 |
1.12e-40 |
|
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: 147.50 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPD--AEEQEYVDGIANDVKWLGFNWNgEPRYASSYF 128
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 129 DQLYSWAVQLIEQGDAYVdlqtpeeiklnrgsfvepgknspyrdasvednlarfeqmrngalgegqavlrakidmaspnv 208
Cdd:cd09287 80 ELYYEYARKLIEMGGAYV-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 209 hmrdpilyrvlhseHHQTGDKWKMYPMYDYAHPLSDAIEGITHSLCTLEFQD----HRPFYD---WvvekvksaAVPRQY 281
Cdd:cd09287 98 --------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEyfgW--------EYPETI 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 282 ESSRLNVDYTITSKRKLRRLVEGGFVKGWDDPRMPTVVGMRRRGFTPEGLRDFCKRVGVSKSDGIVDVAMLEYCIRQSLE 361
Cdd:cd09287 156 HWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLID 235
|
....*
gi 514970759 362 NTAAR 366
Cdd:cd09287 236 PRANR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
48-145 |
3.29e-14 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 73.35 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 48 RTEKVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSY 127
Cdd:PRK05710 2 TMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQR 81
|
90
....*....|....*....
gi 514970759 128 FDqLYSWAV-QLIEQGDAY 145
Cdd:PRK05710 82 HD-AYRAALdRLRAQGLVY 99
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
51-145 |
4.34e-14 |
|
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: 71.85 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 51 KVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPRYASSY--F 128
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYgpY 80
|
90 100
....*....|....*....|...
gi 514970759 129 DQ-----LYSWAVQ-LIEQGDAY 145
Cdd:cd00808 81 RQserleIYRKYAEkLLEKGDGF 103
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
45-154 |
1.37e-08 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 57.44 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 45 AAGRTEKVITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGLCNLRFDDTNPDAEEQEYVDGIANDVKWLGFNWNGEPR-- 122
Cdd:PLN02627 39 GESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDvg 118
|
90 100 110
....*....|....*....|....*....|....*...
gi 514970759 123 -----YASSYFDQLYS-WAVQLIEQGDAYVDLQTPEEI 154
Cdd:PLN02627 119 geygpYRQSERNAIYKqYAEKLLESGHVYPCFCTDEEL 156
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
53-146 |
1.73e-08 |
|
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: 53.64 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514970759 53 ITRFPPEPNGYLHIGHVKAICLNFGIAEEFNGL-----CNLRFDDTN-------------PDAEEQEYVDGIANDVKWLg 114
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLgykvrCIALIDDAGgligdpankkgenAKAFVERWIERIKEDVEYM- 79
|
90 100 110
....*....|....*....|....*....|..
gi 514970759 115 fnwngepryassyFDQLYSWAVQLIEQGDAYV 146
Cdd:cd00802 80 -------------FLQAADFLLLYETECDIHL 98
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
54-123 |
3.01e-08 |
|
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: 51.77 E-value: 3.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514970759 54 TRFPPEPnGYLHIGHVKAICLNFGIAEEfnglCNLRFDDTNPD------AEEQEYVDGIANDVKWLGFNWNGEPRY 123
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIADQ----CVVRIDDNPPVkvwqdpHELEERKESIEEDISVCGEDFQQNREL 72
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
251-297 |
3.29e-04 |
|
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: 40.21 E-value: 3.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 514970759 251 HSLCTLEFQDHRPFYDWVVEKVKSAAVPRQYESSRLNVDYTITSKRK 297
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| |
