|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
12-566 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1213.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 12 AAAKGAPAVPANFLRPIIQADLDSGKHSSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEY 91
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 92 IDAIQSDVKWLGFDWAGDVRYASDYFDQLHDWAVELIKRGKAYVCDLTPEQAKEYRGNLKEPGKNSPFRERSVDENLDLF 171
Cdd:PRK05347 81 VDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 172 ARMKAGEFKDGERVLRAKIDMASPNMNLRDPILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHR 251
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 252 PLYDWFLDNLPVPAHPRQYEFSRLNLNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNR 331
Cdd:PRK05347 241 PLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 332 SDGVVDMSMLEFSIRDDLDRTAPRAMCVLRPLKVVITNYPEGQVEQLELPRHP-KEDMGVRVLPFSRELYIDRDDFMEEP 410
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPeDPEMGTREVPFSRELYIEREDFMEEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 411 PKGYKRLEPAGEVRLRGSYVIRADEAIKDADGNIVELRCSYDPDTLGKNP-EGRKVKGVIHWVPAEGSVECEVRLYDRLF 489
Cdd:PRK05347 401 PKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPaDGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2447139321 490 RSPNPektEEGGSFLDNINPGSLqVLSGCRAEPSLAQAQPEDRFQFEREGYFCADlKDSQPGRPVFNRTVTLRDSWG 566
Cdd:PRK05347 481 TVPNP---AAGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWA 552
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
43-565 |
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: 757.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 43 TRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVRYASDYFDQLHD 122
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 123 WAVELIKRGKAYVCDLTPEQAKEYRGNLKEPGKNSPFRERSVDENLDLFARMKAGEFKDGERVLRAKIDMASPNMNLRDP 202
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 203 ILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVPAHPRQYEFSRLNLNYTIT 282
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 283 SKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVDMSMLEFSIRDDLDRTAPRAMCVLRP 362
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 363 LKVVITNYpEGQVEQLELPRHP-KEDMGVRVLPFSRELYIDRDDFMEEPPKGYKRLEPAGEVRLRGSYVIRADEAIKDAD 441
Cdd:TIGR00440 323 VEVVIENL-SDEYELATIPNHPnTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 442 GNIVELRCSYDPDTLGKNP-EGRKVKGVIHWVPAEGSVECEVRLYDRLFRSPNPEKTEEggsFLDNINPGSLQVLSGCrA 520
Cdd:TIGR00440 402 GKITTIFCTYDNKTLGKEPaDGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDD---FLSVINPESLVIKQGF-M 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2447139321 521 EPSLAQAQPEDRFQFEREGYFCADLKDSQPGRPVFNRTVTLRDSW 565
Cdd:TIGR00440 478 EHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
41-355 |
3.04e-149 |
|
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: 428.59 E-value: 3.04e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 41 IVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWaGDVRYASDYFDQL 120
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 121 HDWAVELIKRGKAYVcdltpeqakeyrgnlkepgknspfrersvdenldlfarmkagefkdgervlrakidmaspnmnlr 200
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 201 dpilyrirhahHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVPaHPRQYEFSRLNLNYT 280
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447139321 281 ITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVDMSMLEFSIRDDLDRTAPR 355
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
39-546 |
3.23e-144 |
|
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: 424.59 E-value: 3.23e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 39 SSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVRYASDYFD 118
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 119 QLHDWAVELIKRGKAYVCDLTPEQAKEYRGNLKEPGKN----SPFRERSVDEnldLFARMKAGEfkdgERVLRAKI---- 190
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEE---LERMLAAGE----PPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 191 ----DMAS-----PNMNLRDPILYRirhahhhqtGDKwciYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNL 261
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 262 PVPaHPrqyEFSRLNLNY----TITSKRKlkqlvdeKHVegwddprmsTLSGFRRRGYTPASIRNFCEMIGTNRSDG--V 335
Cdd:COG0008 224 GWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqeI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 336 VDMSMLEFSIrdDLDRTaPRAMCVLRPLKVVITNY------PEGQVEQLELPRHPKEDMGV---RVLPFSRE-------- 398
Cdd:COG0008 284 FSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGpyiralDDEELAELLAPELPEAGIREdleRLVPLVREraktlsel 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 399 ------LYIDRDDfmEEPPKgyKRLEPaGEVRlrgsyviradEAIKdADGNIVELRCSYDPDTlgknpegrkVKGVIHWV 472
Cdd:COG0008 361 aelarfFFIERED--EKAAK--KRLAP-EEVR----------KVLK-AALEVLEAVETWDPET---------VKGTIHWV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2447139321 473 PAegsvECEVRlyDRLFRSPnpekteeggsfldninpgsLQV-LSGCRAEPSLAQAQP---EDRFqFEREGYFCADLK 546
Cdd:COG0008 416 SA----EAGVK--DGLLFMP-------------------LRVaLTGRTVEPSLFDVLEllgKERV-FERLGYAIDKLA 467
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
41-350 |
8.15e-140 |
|
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: 407.48 E-value: 8.15e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 41 IVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVRYASDYFDQL 120
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 121 HDWAVELIKRGKAYVCDLTPEQAKEYRGnlKEPGKNSPFRERSVDENLDLFAR-MKAGEFKDGERVLRAKIDMASPnMNL 199
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 200 RDPILYRIR---HAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVPAHPRQYEFSRLN 276
Cdd:pfam00749 159 RDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447139321 277 LNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGV-VDMSMLEFSIRDDLD 350
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
12-566 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1213.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 12 AAAKGAPAVPANFLRPIIQADLDSGKHSSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEY 91
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 92 IDAIQSDVKWLGFDWAGDVRYASDYFDQLHDWAVELIKRGKAYVCDLTPEQAKEYRGNLKEPGKNSPFRERSVDENLDLF 171
Cdd:PRK05347 81 VDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 172 ARMKAGEFKDGERVLRAKIDMASPNMNLRDPILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHR 251
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 252 PLYDWFLDNLPVPAHPRQYEFSRLNLNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNR 331
Cdd:PRK05347 241 PLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 332 SDGVVDMSMLEFSIRDDLDRTAPRAMCVLRPLKVVITNYPEGQVEQLELPRHP-KEDMGVRVLPFSRELYIDRDDFMEEP 410
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPeDPEMGTREVPFSRELYIEREDFMEEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 411 PKGYKRLEPAGEVRLRGSYVIRADEAIKDADGNIVELRCSYDPDTLGKNP-EGRKVKGVIHWVPAEGSVECEVRLYDRLF 489
Cdd:PRK05347 401 PKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPaDGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2447139321 490 RSPNPektEEGGSFLDNINPGSLqVLSGCRAEPSLAQAQPEDRFQFEREGYFCADlKDSQPGRPVFNRTVTLRDSWG 566
Cdd:PRK05347 481 TVPNP---AAGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWA 552
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
9-566 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 893.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 9 APNAAAKGAPavpaNFLRPIIQADLDSGKHSSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKED 88
Cdd:PRK14703 4 APRPRMLVSP----NFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 89 QEYIDAIQSDVKWLGFDWAGDVRYASDYFDQLHDWAVELIKRGKAYVCDLTPEQAKEYRGNLKEPGKNSPFRERSVDENL 168
Cdd:PRK14703 80 TEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 169 DLFARMKAGEFKDGERVLRAKIDMASPNMNLRDPILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFE 248
Cdd:PRK14703 160 DLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 249 GHRPLYDWFLDNL-PVPAHPRQYEFSRLNLNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMI 327
Cdd:PRK14703 240 NNRAIYDWVLDHLgPWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 328 GTNRSDGVVDMSMLEFSIRDDLDRTAPRAMCVLRPLKVVITNYPEGQVEQLELPRHPKE--DMGVRVLPFSRELYIDRDD 405
Cdd:PRK14703 320 GVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvpKEGSRKVPFTRELYIERDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 406 FMEEPPKGYKRLEPAGEVRLRGSYVIRADEAIKDADGNIVELRCSYDPDTLGKNPEGRKVKGVIHWVPAEGSVECEVRLY 485
Cdd:PRK14703 400 FSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTGRKAAGVIHWVSAKHALPAEVRLY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 486 DRLFRSPNPEKTEEGgsFLDNINPGSLQVLSGcRAEPSLAQAQPEDRFQFEREGYFCADLKDSQPGRPVFNRTVTLRDSW 565
Cdd:PRK14703 480 DRLFKVPQPEAADED--FLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTW 556
|
.
gi 2447139321 566 G 566
Cdd:PRK14703 557 G 557
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
43-565 |
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: 757.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 43 TRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVRYASDYFDQLHD 122
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 123 WAVELIKRGKAYVCDLTPEQAKEYRGNLKEPGKNSPFRERSVDENLDLFARMKAGEFKDGERVLRAKIDMASPNMNLRDP 202
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 203 ILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVPAHPRQYEFSRLNLNYTIT 282
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 283 SKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVDMSMLEFSIRDDLDRTAPRAMCVLRP 362
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 363 LKVVITNYpEGQVEQLELPRHP-KEDMGVRVLPFSRELYIDRDDFMEEPPKGYKRLEPAGEVRLRGSYVIRADEAIKDAD 441
Cdd:TIGR00440 323 VEVVIENL-SDEYELATIPNHPnTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 442 GNIVELRCSYDPDTLGKNP-EGRKVKGVIHWVPAEGSVECEVRLYDRLFRSPNPEKTEEggsFLDNINPGSLQVLSGCrA 520
Cdd:TIGR00440 402 GKITTIFCTYDNKTLGKEPaDGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDD---FLSVINPESLVIKQGF-M 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2447139321 521 EPSLAQAQPEDRFQFEREGYFCADLKDSQPGRPVFNRTVTLRDSW 565
Cdd:TIGR00440 478 EHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
41-566 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 623.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 41 IVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGfdWAG-DVRYASDYFDQ 119
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WEPfKITYTSDYFQE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 120 LHDWAVELIKRGKAYVCDLTPEQAKEYRgnlkEPGKNSPFRERSVDENLDLFARMKAGEFKDGERVLRAKIDMASPNMNL 199
Cdd:PLN02859 343 LYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNM 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 200 RDPILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVpAHPRQYEFSRLNLNY 279
Cdd:PLN02859 419 YDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGL-YQPYVWEYSRLNVTN 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 280 TITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDG-VVDMSMLEFSIRDDLDRTAPRAMC 358
Cdd:PLN02859 498 TVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIRMDRLEHHIREELNKTAPRTMV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 359 VLRPLKVVITNYPEGQVEQLE---LPRHPKEDM-GVRVLPFSRELYIDRDDFMEEPPKGYKRLEPAGEVRLRGSYVIRAD 434
Cdd:PLN02859 578 VLHPLKVVITNLESGEVIELDakrWPDAQNDDPsAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKCT 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 435 EAI-KDADGNIVELRCSYDPDtlgknpEGRKVKGVIHWV--PAEGS--VECEVRLYDRLFRSPNPEKTEEggsFLDNINP 509
Cdd:PLN02859 658 DVVlADDNETVVEIRAEYDPE------KKTKPKGVLHWVaePSPGVepLKVEVRLFDKLFLSENPAELED---WLEDLNP 728
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2447139321 510 GSLQVLSGCRAEPSLAQAQPEDRFQFEREGYFCADlKDSQPGRPVFNRTVTLRDSWG 566
Cdd:PLN02859 729 QSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYG 784
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
44-563 |
4.21e-159 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 466.38 E-value: 4.21e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 44 RFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGF--DWagdVRYASDYFDQLH 121
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDW---VTFSSDYFDQLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 122 DWAVELIKRGKAYVCDLTPEQAKEYRGNLKEpgknSPFRERSVDENLDLFARMKAGEFKDGERVLRAKIDMASPNMNLRD 201
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQREQRED----SPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 202 PILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVpAHPRQYEFSRLNLNYTI 281
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 282 TSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVDMSMLEFSIRDDLDRTAPRAMCVLR 361
Cdd:PTZ00437 287 LSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVID 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 362 PLKVVITNYpEGQVEqLELPRHP-KEDMGVRVLPFSRELYIDRDDF-MEEPPKGYKRLEPAGEV---RLRGSYVIRADEA 436
Cdd:PTZ00437 367 PIKVVVDNW-KGERE-FECPNHPrKPELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPGPRVvglKYSGNVVCKGFEV 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 437 IKDADGNIVELRCSYDPDTlgknpegrKVKGVIHWVPAEGSVECEVRLYDRLFRSpnpEKTEEGGSFLDNINPGSLQVLS 516
Cdd:PTZ00437 445 DAAGQPSVIHVDIDFERKD--------KPKTNISWVSATACTPVEVRLYNALLKD---DRAAIDPEFLKFIDEDSEVVSH 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2447139321 517 GcRAEPSLAQAQPEDRFQFEREGYFCADlKDSQPGRPVFNRTVTLRD 563
Cdd:PTZ00437 514 G-YAEKGIENAKHFESVQAERFGYFVVD-PDTRPDHLVMNRVLGLRE 558
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
41-355 |
3.04e-149 |
|
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: 428.59 E-value: 3.04e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 41 IVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWaGDVRYASDYFDQL 120
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 121 HDWAVELIKRGKAYVcdltpeqakeyrgnlkepgknspfrersvdenldlfarmkagefkdgervlrakidmaspnmnlr 200
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 201 dpilyrirhahHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVPaHPRQYEFSRLNLNYT 280
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447139321 281 ITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVDMSMLEFSIRDDLDRTAPR 355
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
39-546 |
3.23e-144 |
|
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: 424.59 E-value: 3.23e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 39 SSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVRYASDYFD 118
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 119 QLHDWAVELIKRGKAYVCDLTPEQAKEYRGNLKEPGKN----SPFRERSVDEnldLFARMKAGEfkdgERVLRAKI---- 190
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEE---LERMLAAGE----PPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 191 ----DMAS-----PNMNLRDPILYRirhahhhqtGDKwciYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNL 261
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 262 PVPaHPrqyEFSRLNLNY----TITSKRKlkqlvdeKHVegwddprmsTLSGFRRRGYTPASIRNFCEMIGTNRSDG--V 335
Cdd:COG0008 224 GWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqeI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 336 VDMSMLEFSIrdDLDRTaPRAMCVLRPLKVVITNY------PEGQVEQLELPRHPKEDMGV---RVLPFSRE-------- 398
Cdd:COG0008 284 FSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGpyiralDDEELAELLAPELPEAGIREdleRLVPLVREraktlsel 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 399 ------LYIDRDDfmEEPPKgyKRLEPaGEVRlrgsyviradEAIKdADGNIVELRCSYDPDTlgknpegrkVKGVIHWV 472
Cdd:COG0008 361 aelarfFFIERED--EKAAK--KRLAP-EEVR----------KVLK-AALEVLEAVETWDPET---------VKGTIHWV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2447139321 473 PAegsvECEVRlyDRLFRSPnpekteeggsfldninpgsLQV-LSGCRAEPSLAQAQP---EDRFqFEREGYFCADLK 546
Cdd:COG0008 416 SA----EAGVK--DGLLFMP-------------------LRVaLTGRTVEPSLFDVLEllgKERV-FERLGYAIDKLA 467
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
41-350 |
8.15e-140 |
|
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: 407.48 E-value: 8.15e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 41 IVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVRYASDYFDQL 120
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 121 HDWAVELIKRGKAYVCDLTPEQAKEYRGnlKEPGKNSPFRERSVDENLDLFAR-MKAGEFKDGERVLRAKIDMASPnMNL 199
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 200 RDPILYRIR---HAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVPAHPRQYEFSRLN 276
Cdd:pfam00749 159 RDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447139321 277 LNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGV-VDMSMLEFSIRDDLD 350
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
6-554 |
9.48e-111 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 346.71 E-value: 9.48e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 6 ADNAPNAAAKGAPAVpanflrpiiqaDLDSGKHSSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPA 85
Cdd:PLN02907 190 AGKADGAKDKGSFEV-----------DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 86 KEDQEYIDAIQSDVKWLGFDwaGD-VRYASDYFDQLHDWAVELIKRGKAYVCDLTPEQAKEYRGNlkepGKNSPFRERSV 164
Cdd:PLN02907 259 KESDEFVENILKDIETLGIK--YDaVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSV 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 165 DENLDLFARMKAGEFKDGERVLRAKIDMASPNMNLRDPILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICT 244
Cdd:PLN02907 333 EENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRS 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 245 LEFEGHRPLYDWFLDNLPVPaHPRQYEFSRLNLNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFC 324
Cdd:PLN02907 413 SEYHDRNAQYYRILEDMGLR-KVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFI 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 325 EMIGTNRSDGVVDMSMLEFSIRDDLDRTAPRAMCVLRPLKVVIT--NYPEGQvEQLELPRHPK-EDMGVRVLPFSRELYI 401
Cdd:PLN02907 492 LSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLTltDGPETP-FVRIIPRHKKyEGAGKKATTFTNRIWL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 402 DRDDfmeeppkgYKRLEPAGEVRLR--GSYVIRadEAIKDADGNIVELRCSYdpdtlgkNPEG--RKVKGVIHWVPA-EG 476
Cdd:PLN02907 571 DYAD--------AEAISEGEEVTLMdwGNAIIK--EITKDEGGAVTALSGEL-------HLEGsvKTTKLKLTWLPDtNE 633
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2447139321 477 SVECEVRLYDRLFRSpnpEKTEEGGSFLDNINPGSlQVLSGCRAEPSLAQAQPEDRFQFEREGYFCADLKDSQPGRPV 554
Cdd:PLN02907 634 LVPLSLVEFDYLITK---KKLEEDDNFLDVLNPCT-KKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSSKPI 707
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
22-553 |
3.06e-105 |
|
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: 327.55 E-value: 3.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 22 ANFLRpiiqaDLDSGKHSSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKW 101
Cdd:TIGR00463 80 RKGLR-----ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEW 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 102 LGFDWaGDVRYASDYFDQLHDWAVELIKRGKAYVCDLTPEQAKEYRGNlkepGKNSPFRERSVDENLDLFARMKAGEFKD 181
Cdd:TIGR00463 155 LGVKW-DEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 182 GERVLRAKIDMASPNMNLRDPILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEF----EGHRPLYDWF 257
Cdd:TIGR00463 230 GSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidnrRKQEYIYRYF 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 258 LDNLPVPAHprqYEFSRLNLNYTITSKRKLKQLVDEKHvEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVD 337
Cdd:TIGR00463 310 GWEPPEFIH---WGRLKIDDVRALSTSSARKGILRGEY-SGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMS 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 338 MSMLEFSIRDDLDRTAPRAMCVLRPLKVVITNYPEGQVEqlELPRHPKE-DMGVRVLPFSRELYIDRDDFMEEppKGYKR 416
Cdd:TIGR00463 386 WKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRV--ERPLHPDHpEIGERVLILRGEIYVPKDDLEEG--VEPVR 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 417 LEPAGEVRLRGSYVIRADEAIKDADgnivelrcsydpdtlgknpegRKVKGVIHWVPAEGSVECEVRLYDRLFRspnpek 496
Cdd:TIGR00463 462 LMDAVNVIYSKKELRYHSEGLEGAR---------------------KLGKSIIHWLPAKDAVKVKVIMPDASIV------ 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2447139321 497 teEGgsfldninpgslqvlsgcRAEPSLAQAQPEDRFQFEREGYFCADLKDsQPGRP 553
Cdd:TIGR00463 515 --EG------------------VIEADASELEVGDVVQFERFGFARLDSAD-KDGMV 550
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
32-540 |
4.18e-103 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 322.19 E-value: 4.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 32 DLDSGKHSSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPA--KEDQEYIDAIQSDVKWLGFDWAgD 109
Cdd:PRK04156 93 PLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-E 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 110 VRYASDYFDQLHDWAVELIKRGKAYVCDLTPEQAKEYRGNlkepGKNSPFRERSVDENLDLFARMKAGEFKDGERVLRAK 189
Cdd:PRK04156 172 VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVK 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 190 IDMASPNMNLRDPILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEF----EGHRPLYDWFLDNLPVPA 265
Cdd:PRK04156 248 TDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHidntEKQRYIYDYFGWEYPETI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 266 HprqyeFSRLNLNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVDMSMLeFSI 345
Cdd:PRK04156 328 H-----YGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENL-YAI 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 346 -RDDLDRTAPRAMCVLRPLKVVITNYPEgqvEQLELPRHP-KEDMGVRVLPFSRELYIDRDDfmeeppkgykrLEPAGE- 422
Cdd:PRK04156 402 nRKLIDPIANRYFFVRDPVELEIEGAEP---LEAKIPLHPdRPERGEREIPVGGKVYVSSDD-----------LEAEGKm 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 423 VRLRGSYVIRADEaikdadgnIVELRCSYDPDTLgknPEGRKVKG-VIHWVPAEGSVECEVRlydrlfrspNPEKTEEGG 501
Cdd:PRK04156 468 VRLMDLFNVEITG--------VSVDKARYHSDDL---EEARKNKApIIQWVPEDESVPVRVL---------KPDGGDIEG 527
|
490 500 510
....*....|....*....|....*....|....*....
gi 2447139321 502 sfldninpgslqvlsgcRAEPSLAQAQPEDRFQFEREGY 540
Cdd:PRK04156 528 -----------------LAEPDVADLEVDDIVQFERFGF 549
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
33-552 |
1.55e-97 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 308.81 E-value: 1.55e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 33 LDSGKHSSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVRY 112
Cdd:PTZ00402 45 LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 113 ASDYFDQLHDWAVELIKRGKAYvCDLTP-EQAKEYRGNlkepGKNSPFRERSVDENLDLFARMKAGEFKDGERVLRAKID 191
Cdd:PTZ00402 125 SSDYMDLMYEKAEELIKKGLAY-CDKTPrEEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKIS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 192 MASPNMNLRDPILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVpAHPRQYE 271
Cdd:PTZ00402 200 VDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGI-RKPIVED 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 272 FSRLNLNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVDMSMLEFSIRDDLDR 351
Cdd:PTZ00402 279 FSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 352 TAPRAMCVLRPLKVVITNYPEGQVEQLELPRHPKE-DMGVRVLPFSRELYIDRDDFMeeppkgykRLEPAGEVRLR---G 427
Cdd:PTZ00402 359 SVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVpDMGEKTYYKSDVIFLDAEDVA--------LLKEGDEVTLMdwgN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 428 SYV--IR---ADEAIKDADgnIVelrcsydpdtlgKNPEG--RKVKGVIHWVPAEGSVEC-EVRLYDRLFRSPNPEKTEE 499
Cdd:PTZ00402 431 AYIknIRrsgEDALITDAD--IV------------LHLEGdvKKTKFKLTWVPESPKAEVmELNEYDHLLTKKKPDPEES 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2447139321 500 GGSFLDNINPGSLQVLsgcrAEPSLAQAQPEDRFQFEREGYFCADlkDSQPGR 552
Cdd:PTZ00402 497 IDDIIAPVTKYTQEVY----GEEALSVLKKGDIIQLERRGYYIVD--DVTPKK 543
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
33-554 |
9.30e-87 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 278.43 E-value: 9.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 33 LDSGKHSSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDwAGDVRY 112
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 113 ASDYFDQLHDWAVELIKRGKAYVCDLTPEQAKEYRGNLKEpgknSPFRERSVDENLDLFARMKAGEFKDGERVLRAKIDM 192
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 193 ASPNMNLRDPILYRIRHAHHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVpAHPRQYEF 272
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGL-RRPRIHAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 273 SRLNLNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFceMIGTNRSDGVVDMSMLEF--SIRDDLD 350
Cdd:PLN03233 238 ARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMF--MCSQGASRRVVNLDWAKFwaENKKEID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 351 RTAPRAMCVLRP--LKVVITNYPEG-QVEQLELPRHPKE-DMGVRVLPFSRELYIDRDDfmeeppkgYKRLEPAGEVRLR 426
Cdd:PLN03233 316 KRAKRFMAIDKAdhTALTVTNADEEaDFAFSETDCHPKDpGFGKRAMRICDEVLLEKAD--------TEDIQLGEDIVLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 427 GSYVIRADEAIKDADGNIVelrcsydpdtlgknPEG--RKVKGVIHWVpAEGSVECEVRLY--DRLFrspNPEKTEEGGS 502
Cdd:PLN03233 388 RWGVIEISKIDGDLEGHFI--------------PDGdfKAAKKKISWI-ADVSDNIPVVLSefDNLI---IKEKLEEDDK 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2447139321 503 FLDNINPGSlQVLSGCRAEPSLAQAQPEDRFQFEREGYFCADLKDSQPGRPV 554
Cdd:PLN03233 450 FEDFINPDT-LAETDVIGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPL 500
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
353-544 |
4.18e-82 |
|
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 427609 [Multi-domain] Cd Length: 175 Bit Score: 254.12 E-value: 4.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 353 APRAMCVLRPLKVVITNYPEGQVEQLELPRHPK-EDMGVRVLPFSRELYIDRDDFmeeppkgyKRLEPAGEVRLRGSYVI 431
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKnPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 432 RADEAIKDADGNIVELRCSYDPDTLGKNpegRKVKG-VIHWVPAEGSVECEVRLYDRLFrspnpeKTEEGGSFLdnINPG 510
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA---RKVKGkIIHWVSASDAVPAEVRLYDRLF------KDEDDADFL--LNPD 141
|
170 180 190
....*....|....*....|....*....|....
gi 2447139321 511 SLQVLSGCRAEPSLAQAQPEDRFQFEREGYFCAD 544
Cdd:pfam03950 142 SLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
41-354 |
1.24e-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: 208.10 E-value: 1.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 41 IVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVRYASDYFDQL 120
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 121 HDWAVELIKRGkayvcdltpeqakeyrgnlkepgknspfrersvdenldlfarmkagefkdgervlrakidmaspnmnlr 200
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 201 dpilyrirhahhhqtgdkwcIYPNYDFTHGQSDAIEGITHSICTLEFEGHRPLYDWFLDNLPVPaHPRQYEFSRLNLNY- 279
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLEDg 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447139321 280 TITSKRKLKqlvdekhvegwddprmSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVDMSMLEFSIRDDLDRTAP 354
Cdd:cd00418 152 TKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNS 210
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
41-355 |
3.29e-43 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 154.43 E-value: 3.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 41 IVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNP--AKEDQEYIDAIQSDVKWLGFDWAgDVRYASDYFD 118
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 119 QLHDWAVELIKRGKAYVcdltpeqakeyrgnlkepgknspfrersvdenldlfarmkagefkdgervlrakidmaspnmn 198
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 199 lrdpilyrirhahHHQTGDKWCIYPNYDFTHGQSDAIEGITHSICTLEF----EGHRPLYDWFLDNLPVPAHprqyeFSR 274
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHidntEKQRYIYEYFGWEYPETIH-----WGR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 275 LNLNYTITSKRKLKQLVDEKHVEGWDDPRMSTLSGFRRRGYTPASIRNFCEMIGTNRSDGVVDMSMLEFSIRDDLDRTAP 354
Cdd:cd09287 160 LKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRAN 239
|
.
gi 2447139321 355 R 355
Cdd:cd09287 240 R 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
39-136 |
1.14e-18 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 86.83 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 39 SSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVRYASDYFD 118
Cdd:PRK05710 4 TPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD 83
|
90
....*....|....*...
gi 2447139321 119 QLHDWAVELIKRGKAYVC 136
Cdd:PRK05710 84 AYRAALDRLRAQGLVYPC 101
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
40-131 |
2.71e-15 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 75.70 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 40 SIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDWAGDVR-------- 111
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDvggpygpy 80
|
90 100
....*....|....*....|
gi 2447139321 112 YASDYFDQLHDWAVELIKRG 131
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
34-349 |
8.94e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 67.46 E-value: 8.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 34 DSGKHSSIVTRFPPEPNGYLHIGHAKSICVNFGLAKEFGGVCHLRFDDTNPAKEDQEYIDAIQSDVKWLGFDW------- 106
Cdd:PLN02627 39 GESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWdegpdvg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 107 --AGDVRYA--SDYFDQLhdwAVELIKRGKAYVCDLTPEQAKEYRGNLKEpgKNSP------FRERSVDEnldLFARMKA 176
Cdd:PLN02627 119 geYGPYRQSerNAIYKQY---AEKLLESGHVYPCFCTDEELEAMKEEAEL--KKLPprytgkWATASDEE---VQAELAK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 177 GE-----FK--DGERVlraKID-----MASPNMN-LRDPILYRirhahhhQTGdkwciYPNYDFTHGQSDAIEGITHSIc 243
Cdd:PLN02627 191 GTpytyrFRvpKEGSV---KIDdlirgEVSWNTDtLGDFVLLR-------SNG-----QPVYNFCVAVDDATMGITHVI- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 244 tlEFEGHRP-------LYDWFldNLPVPahprqyEFSRLNL----NYTITSKRKLKQLVDEkhvegwddprmstlsgFRR 312
Cdd:PLN02627 255 --RAEEHLPntlrqalIYKAL--GFPMP------RFAHVSLilapDRSKLSKRHGATSVGQ----------------FRE 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 2447139321 313 RGYTPASIRNFCEMIGTNrsDGVVDmsmlEFSIRDDL 349
Cdd:PLN02627 309 MGYLPDAMVNYLALLGWN--DGTEN----EIFTLEEL 339
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
42-123 |
9.61e-12 |
|
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: 62.88 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 42 VTRFPPEPNGYLHIGHAKSICVNFGLAKE-----FGGVCHLRFDDTNPAKEDQ-------------EYIDAIQSDVKWLg 103
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM- 79
|
90 100
....*....|....*....|
gi 2447139321 104 FDWAGDvryASDYFDQLHDW 123
Cdd:cd00802 80 FLQAAD---FLLLYETECDI 96
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
42-118 |
4.27e-10 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 57.16 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447139321 42 VTRFPPEPnGYLHIGHAKSICVNFGLAkefgGVCHLRFDDTNPAK------EDQEYIDAIQSDVKWLGFDWAGDVRYASD 115
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNRELYRW 75
|
...
gi 2447139321 116 YFD 118
Cdd:cd02156 76 VKD 78
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
240-286 |
5.12e-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: 51.00 E-value: 5.12e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2447139321 240 HSICTLEFEGHRPLYDWFLDNLPVPAHPRQYEFSRLNLNYTITSKRK 286
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| |
