|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-557 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1144.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 1 MEKPITPPNFIKNVIEEDLRTGKVKEVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNS 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 81 IQEDVKWLGYEWEEK-HFASNYFEEMYKRAILLIQKGKAYVDDQSADQIRETRGTLTEPGQNSPYRDRSVEDNLKLFEEM 159
Cdd:PRK05347 84 IKEDVRWLGFDWSGElRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 160 RAGKYQNGEKVLRAKIDMASPNINLRDPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLY 239
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 240 DWVVAECEMENVPHQYEFGRLNLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYG 319
Cdd:PRK05347 244 DWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 320 VIDLQVLEHFAREDLKLKAPRTMAVIDPLKVVITNYPEGQVEMLEAENNTENPELGTRQIPFSREIYIEREDFMENPPSK 399
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 400 YFRLFPGNEVRLKHAYFIKCNDVIKDAEGNVTEIHCTYDIETKSGSGFTGRKVKGTIHWVEATQAVPAEFRLYEPLINAE 479
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309249370 480 EPevleedGSEKTFLDQLNPNSLEIAHGYVERNMKEAQSQDKFQFFRHGYFSVDPKlSKPGEPVFNRVVSLKSSFQLP 557
Cdd:PRK05347 484 NP------AAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKD-STPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-554 |
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: 678.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 27 VVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWE-EKHFASNYFEEM 105
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 106 YKRAILLIQKGKAYVDDQSADQIRETRGTLTEPGQNSPYRDRSVEDNLKLFEEMRAGKYQNGEKVLRAKIDMASPNINLR 185
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 186 DPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMENVPHQYEFGRLNLAQT 265
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 266 VTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFAREDLKLKAPRTMAVI 345
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 346 DPLKVVITNYpEGQVEMLEAENNTENPELGTRQIPFSREIYIEREDFMENPPSKYFRLFPGNEVRLKHAYFIKCNDVIKD 425
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 426 AEGNVTEIHCTYDIETKSGSGFTGRKVKGTIHWVEATQAVPAEFRLYEPLINAEEPevleedGSEKTFLDQLNPNSLEIA 505
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNP------GAPDDFLSVINPESLVIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 309249370 506 HGYVERNMKEAQSQDKFQFFRHGYFSVDPKLSKPGEPVFNRVVSLKSSF 554
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
26-340 |
8.98e-135 |
|
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: 391.23 E-value: 8.98e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 26 EVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEEKHFASNYFEEM 105
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 106 YKRAILLIQKGKAYVddqsadqiretrgtltepgqnspyrdrsvednlklfeemragkyqngekvlrakidmaspninlr 185
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 186 dpviyrishtaHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMeNVPHQYEFGRLNLAQT 265
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRL-YRPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309249370 266 VTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFAREDLKLKAPR 340
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
26-335 |
8.24e-126 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 371.27 E-value: 8.24e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 26 EVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEEK-HFASNYFEE 104
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGpYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 105 MYKRAILLIQKGKAYVDDQSADQIRETRGTLtePGQNSPYRDRSVEDNLKLF-EEMRAGKYQNGEKVLRAKIDMASPnIN 183
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 184 LRDPVIYRI---SHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMENVPHQYEFGRL 260
Cdd:pfam00749 158 FRDPVRGRIkftPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309249370 261 NLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGV-IDLQVLEHFAREDLK 335
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-493 |
1.63e-116 |
|
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: 353.33 E-value: 1.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 25 KEVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEW-EEKHFASNYFE 103
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 104 EMYKRAILLIQKGKAYVDDQSADQIRETRGTLTEPGQNSPY----RDRSVEDNlklfEEMRAgkyqNGEK-VLRAKI--- 175
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERMLA----AGEPpVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 176 -----DMAS-----PNINLRDPVIYRiSHtahhntGdtwciYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAE 245
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-AD------G-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 246 CEMEnVPhqyEFGRLNL----AQTVTSKRKlkllvdeKHVdgwddprmpTISGLRRRGYTPEAIRSFVYETGISKAYG-- 319
Cdd:COG0008 223 LGWE-PP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqe 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 320 VIDLQVLEH-FareDLKlKAPRTMAVIDPLKVVITNY------PEGQV-EMLEAEN-NTENPELGTRQIPFSRE------ 384
Cdd:COG0008 283 IFSLEELIEaF---DLD-RVSRSPAVFDPVKLVWLNGpyiralDDEELaELLAPELpEAGIREDLERLVPLVREraktls 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 385 --------IYIEREDfmENPPSKyfRLFPgNEVRLkhayFIKCndvIKDAEGNVTeihcTYDIETksgsgftgrkVKGTI 456
Cdd:COG0008 359 elaelarfFFIERED--EKAAKK--RLAP-EEVRK----VLKA---ALEVLEAVE----TWDPET----------VKGTI 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 309249370 457 HWVeatqAVPAEFR---LYEPLINAE-----EP---EVLEEDGSEKTF 493
Cdd:COG0008 413 HWV----SAEAGVKdglLFMPLRVALtgrtvEPslfDVLELLGKERVF 456
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-557 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1144.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 1 MEKPITPPNFIKNVIEEDLRTGKVKEVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNS 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 81 IQEDVKWLGYEWEEK-HFASNYFEEMYKRAILLIQKGKAYVDDQSADQIRETRGTLTEPGQNSPYRDRSVEDNLKLFEEM 159
Cdd:PRK05347 84 IKEDVRWLGFDWSGElRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 160 RAGKYQNGEKVLRAKIDMASPNINLRDPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLY 239
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 240 DWVVAECEMENVPHQYEFGRLNLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYG 319
Cdd:PRK05347 244 DWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 320 VIDLQVLEHFAREDLKLKAPRTMAVIDPLKVVITNYPEGQVEMLEAENNTENPELGTRQIPFSREIYIEREDFMENPPSK 399
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 400 YFRLFPGNEVRLKHAYFIKCNDVIKDAEGNVTEIHCTYDIETKSGSGFTGRKVKGTIHWVEATQAVPAEFRLYEPLINAE 479
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309249370 480 EPevleedGSEKTFLDQLNPNSLEIAHGYVERNMKEAQSQDKFQFFRHGYFSVDPKlSKPGEPVFNRVVSLKSSFQLP 557
Cdd:PRK05347 484 NP------AAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKD-STPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
8-553 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 838.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 8 PNFIKNVIEEDLRTGKVKEVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKW 87
Cdd:PRK14703 13 PNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 88 LGYEWEEK-HFASNYFEEMYKRAILLIQKGKAYVDDQSADQIRETRGTLTEPGQNSPYRDRSVEDNLKLFEEMRAGKYQN 166
Cdd:PRK14703 93 LGFDWGEHlYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 167 GEKVLRAKIDMASPNINLRDPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAEC 246
Cdd:PRK14703 173 GAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 247 -EMENVPHQYEFGRLNLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQV 325
Cdd:PRK14703 253 gPWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 326 LEHFAREDLKLKAPRTMAVIDPLKVVITNYPEGQVEMLEAEN-NTENPELGTRQIPFSREIYIEREDFMENPPSKYFRLF 404
Cdd:PRK14703 333 LEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYwPHDVPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 405 PGNEVRLKHAYFIKCNDVIKDAEGNVTEIHCTYDIETKSGSGfTGRKVKGTIHWVEATQAVPAEFRLYEPLINAEEPEVL 484
Cdd:PRK14703 413 PGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGED-TGRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEAA 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309249370 485 EEDgsektFLDQLNPNSLEIAHGYVERNMKEAQSQDKFQFFRHGYFSVDPKLSKPGEPVFNRVVSLKSS 553
Cdd:PRK14703 492 DED-----FLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDT 555
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-554 |
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: 678.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 27 VVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWE-EKHFASNYFEEM 105
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 106 YKRAILLIQKGKAYVDDQSADQIRETRGTLTEPGQNSPYRDRSVEDNLKLFEEMRAGKYQNGEKVLRAKIDMASPNINLR 185
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 186 DPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMENVPHQYEFGRLNLAQT 265
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 266 VTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFAREDLKLKAPRTMAVI 345
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 346 DPLKVVITNYpEGQVEMLEAENNTENPELGTRQIPFSREIYIEREDFMENPPSKYFRLFPGNEVRLKHAYFIKCNDVIKD 425
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 426 AEGNVTEIHCTYDIETKSGSGFTGRKVKGTIHWVEATQAVPAEFRLYEPLINAEEPevleedGSEKTFLDQLNPNSLEIA 505
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNP------GAPDDFLSVINPESLVIK 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 309249370 506 HGYVERNMKEAQSQDKFQFFRHGYFSVDPKLSKPGEPVFNRVVSLKSSF 554
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
12-554 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 565.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 12 KNVIEEDL-RTGKvkEVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGY 90
Cdd:PLN02859 251 KEILEKHLkATGG--KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGW 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 91 EWEEKHFASNYFEEMYKRAILLIQKGKAYVDDQSADQIRETRgtltEPGQNSPYRDRSVEDNLKLFEEMRAGKYQNGEKV 170
Cdd:PLN02859 329 EPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKAT 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 171 LRAKIDMASPNINLRDPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMEn 250
Cdd:PLN02859 405 LRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 251 VPHQYEFGRLNLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYG-VIDLQVLEHF 329
Cdd:PLN02859 484 QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIRMDRLEHH 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 330 AREDLKLKAPRTMAVIDPLKVVITNYPEGQVEMLEA----ENNTENPElGTRQIPFSREIYIEREDFMENPPSKYFRLFP 405
Cdd:PLN02859 564 IREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwpDAQNDDPS-AFYKVPFSRVVYIERSDFRLKDSKDYYGLAP 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 406 GNEVRLKHAYFIKCNDVI-KDAEGNVTEIHCTYDIETKSgsgftgrKVKGTIHWV----EATQAVPAEFRLYEPLINAEE 480
Cdd:PLN02859 643 GKSVLLRYAFPIKCTDVVlADDNETVVEIRAEYDPEKKT-------KPKGVLHWVaepsPGVEPLKVEVRLFDKLFLSEN 715
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309249370 481 PEVLEedgsekTFLDQLNPNSLEIAHG-YVERNMKEAQSQDKFQFFRHGYFSVDPKlSKPGEPVFNRVVSLKSSF 554
Cdd:PLN02859 716 PAELE------DWLEDLNPQSKEVISGaYAVPSLKDAKVGDRFQFERLGYFAVDKD-STPEKLVFNRTVTLKDSY 783
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
30-551 |
2.41e-163 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 477.17 E-value: 2.41e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 30 RFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEEKHFASNYFEEMYKRA 109
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHEFA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 110 ILLIQKGKAYVDDQSADQIRETRgtltEPGQNSPYRDRSVEDNLKLFEEMRAGKYQNGEKVLRAKIDMASPNINLRDPVI 189
Cdd:PTZ00437 135 VQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 190 YRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMENvPHQYEFGRLNLAQTVTSK 269
Cdd:PTZ00437 211 YRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWR-PHVWEFSRLNVTGSLLSK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 270 RKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFAREDLKLKAPRTMAVIDPLK 349
Cdd:PTZ00437 290 RKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPIK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 350 VVITNYpEGQVEmLEAENNTENPELGTRQIPFSREIYIEREDF-MENPPSKYFRLFPGNE-VRLKHAYFIKCNDVIKDAE 427
Cdd:PTZ00437 370 VVVDNW-KGERE-FECPNHPRKPELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPGPRvVGLKYSGNVVCKGFEVDAA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 428 GNVTEIHCTYDIETKSgsgftgrKVKGTIHWVEATQAVPAEFRLYEPLINAEEPEVleedgsEKTFLDQLNPNSLEIAHG 507
Cdd:PTZ00437 448 GQPSVIHVDIDFERKD-------KPKTNISWVSATACTPVEVRLYNALLKDDRAAI------DPEFLKFIDEDSEVVSHG 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 309249370 508 YVERNMKEAQSQDKFQFFRHGYFSVDPKlSKPGEPVFNRVVSLK 551
Cdd:PTZ00437 515 YAEKGIENAKHFESVQAERFGYFVVDPD-TRPDHLVMNRVLGLR 557
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
26-340 |
8.98e-135 |
|
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: 391.23 E-value: 8.98e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 26 EVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEEKHFASNYFEEM 105
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 106 YKRAILLIQKGKAYVddqsadqiretrgtltepgqnspyrdrsvednlklfeemragkyqngekvlrakidmaspninlr 185
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 186 dpviyrishtaHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMeNVPHQYEFGRLNLAQT 265
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRL-YRPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309249370 266 VTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFAREDLKLKAPR 340
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
26-335 |
8.24e-126 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 371.27 E-value: 8.24e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 26 EVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEEK-HFASNYFEE 104
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGpYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 105 MYKRAILLIQKGKAYVDDQSADQIRETRGTLtePGQNSPYRDRSVEDNLKLF-EEMRAGKYQNGEKVLRAKIDMASPnIN 183
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 184 LRDPVIYRI---SHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMENVPHQYEFGRL 260
Cdd:pfam00749 158 FRDPVRGRIkftPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309249370 261 NLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGV-IDLQVLEHFAREDLK 335
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
16-543 |
8.03e-122 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 375.22 E-value: 8.03e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 16 EEDLRTGKVKEVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEEK 95
Cdd:PLN02907 203 EVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 96 HFASNYFEEMYKRAILLIQKGKAYVDDQSADQIRETRGTLTEpgqnSPYRDRSVEDNLKLFEEMRAGKYQNGEKVLRAKI 175
Cdd:PLN02907 283 TYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIE----SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 176 DMASPNINLRDPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMENVpHQY 255
Cdd:PLN02907 359 DMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKV-HIW 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 256 EFGRLNLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFAREDLK 335
Cdd:PLN02907 438 EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIID 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 336 LKAPRTMAVIDPLKVVIT--NYPEGQvEMLEAENNTENPELGTRQIPFSREIYIEREDfmENPPSKyfrlfpGNEVRLK- 412
Cdd:PLN02907 518 PVCPRHTAVLKEGRVLLTltDGPETP-FVRIIPRHKKYEGAGKKATTFTNRIWLDYAD--AEAISE------GEEVTLMd 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 413 --HAyFIKcnDVIKDAEGNVTEIHCTYDIEtksGSgftgrkVKGT---IHWVEAT-QAVPAEFRLYEPLINAEEPEvlEE 486
Cdd:PLN02907 589 wgNA-IIK--EITKDEGGAVTALSGELHLE---GS------VKTTklkLTWLPDTnELVPLSLVEFDYLITKKKLE--ED 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 309249370 487 DgsekTFLDQLNPNS-LEI-AHGyvERNMKEAQSQDKFQFFRHGYFSVDPKLSKPGEPV 543
Cdd:PLN02907 655 D----NFLDVLNPCTkKETaALG--DSNMRNLKRGEIIQLERKGYYRCDAPFVRSSKPI 707
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
16-542 |
1.04e-118 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 361.83 E-value: 1.04e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 16 EEDLRTGKVKEVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEEK 95
Cdd:TIGR00463 83 LRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 96 HFASNYFEEMYKRAILLIQKGKAYVDDQSADQIRETRGTltepGQNSPYRDRSVEDNLKLFEEMRAGKYQNGEKVLRAKI 175
Cdd:TIGR00463 163 VYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 176 DMASPNINLRDPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFED--QRPLYDWVVAECEMENVPH 253
Cdd:TIGR00463 239 DLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEPPEFIH 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 254 qYEFGRLNLAQTVTSKRKLKLLVDEKHVdGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFARED 333
Cdd:TIGR00463 319 -WGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 334 LKLKAPRTMAVIDPLKVVITNYPEGQVEMLEAenNTENPELGTRQIPFSREIYIEREDFMENPpskyfrlfpgNEVRLKH 413
Cdd:TIGR00463 397 IDEEARRYFFIWNPVKIEIVGLPEPKRVERPL--HPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRLMD 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 414 AyfikCNDVIkdaEGNVTEIHctydietksGSGFTGRKVKGT--IHWVEATQAVPAefrlyeplinaeepEVLEEDGsek 491
Cdd:TIGR00463 465 A----VNVIY---SKKELRYH---------SEGLEGARKLGKsiIHWLPAKDAVKV--------------KVIMPDA--- 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 309249370 492 tfldqlnpnslEIAHGYVERNMKEAQSQDKFQFFRHGYFSVDpKLSKPGEP 542
Cdd:TIGR00463 512 -----------SIVEGVIEADASELEVGDVVQFERFGFARLD-SADKDGMV 550
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-493 |
1.63e-116 |
|
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: 353.33 E-value: 1.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 25 KEVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEW-EEKHFASNYFE 103
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 104 EMYKRAILLIQKGKAYVDDQSADQIRETRGTLTEPGQNSPY----RDRSVEDNlklfEEMRAgkyqNGEK-VLRAKI--- 175
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERMLA----AGEPpVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 176 -----DMAS-----PNINLRDPVIYRiSHtahhntGdtwciYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAE 245
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-AD------G-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 246 CEMEnVPhqyEFGRLNL----AQTVTSKRKlkllvdeKHVdgwddprmpTISGLRRRGYTPEAIRSFVYETGISKAYG-- 319
Cdd:COG0008 223 LGWE-PP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqe 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 320 VIDLQVLEH-FareDLKlKAPRTMAVIDPLKVVITNY------PEGQV-EMLEAEN-NTENPELGTRQIPFSRE------ 384
Cdd:COG0008 283 IFSLEELIEaF---DLD-RVSRSPAVFDPVKLVWLNGpyiralDDEELaELLAPELpEAGIREDLERLVPLVREraktls 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 385 --------IYIEREDfmENPPSKyfRLFPgNEVRLkhayFIKCndvIKDAEGNVTeihcTYDIETksgsgftgrkVKGTI 456
Cdd:COG0008 359 elaelarfFFIERED--EKAAKK--RLAP-EEVRK----VLKA---ALEVLEAVE----TWDPET----------VKGTI 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 309249370 457 HWVeatqAVPAEFR---LYEPLINAE-----EP---EVLEEDGSEKTF 493
Cdd:COG0008 413 HWV----SAEAGVKdglLFMPLRVALtgrtvEPslfDVLELLGKERVF 456
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
19-543 |
2.29e-103 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 321.19 E-value: 2.29e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 19 LRTGKVKEVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEEKHFA 98
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 99 SNYFEEMYKRAILLIQKGKAYVDDQSADQIRETRGTLtepgQNSPYRDRSVEDNLKLFEEMRAGKYQNGEKVLRAKIDMA 178
Cdd:PLN03233 84 SDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADR----AESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 179 SPNINLRDPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMENvPHQYEFG 258
Cdd:PLN03233 160 SDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRR-PRIHAFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 259 RLNLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAygVIDLQVLEHFA--REDLKL 336
Cdd:PLN03233 239 RMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRR--VVNLDWAKFWAenKKEIDK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 337 KAPRTMAV--IDPLKVVITNYPEG-QVEMLEAENNTENPELGTRQIPFSREIYIEREDFMEnppskyfrLFPGNEVRLKH 413
Cdd:PLN03233 317 RAKRFMAIdkADHTALTVTNADEEaDFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 414 AYFIKCNDVIKDAEGnvteiHCTYDIETKSGsgftgrkvKGTIHWV-EATQAVPAEFRLYEPLINAEEpevLEEDgseKT 492
Cdd:PLN03233 389 WGVIEISKIDGDLEG-----HFIPDGDFKAA--------KKKISWIaDVSDNIPVVLSEFDNLIIKEK---LEED---DK 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 309249370 493 FLDQLNPNSLEIAHGYVERNMKEAQSQDKFQFFRHGYFSVDPKLSKPGEPV 543
Cdd:PLN03233 450 FEDFINPDTLAETDVIGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPL 500
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
26-533 |
1.81e-99 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 313.44 E-value: 1.81e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 26 EVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEE-KHFASNYFEE 104
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVgPTYSSDYMDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 105 MYKRAILLIQKGKAYVDDQSADQIRETRGTltepGQNSPYRDRSVEDNLKLFEEMRAGKYQNGEKVLRAKIDMASPNINL 184
Cdd:PTZ00402 132 MYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNENKAM 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 185 RDPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVvaeCEMENV--PHQYEFGRLNL 262
Cdd:PTZ00402 208 RDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWF---CDALGIrkPIVEDFSRLNM 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 263 AQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFAREDLKLKAPRTM 342
Cdd:PTZ00402 285 EYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 343 AVIDPLKVVITnyPEGQVEMLEAEN--NTENPELGTRQIPFSREIYIEREDFMenppskyfRLFPGNEVRLK---HAYfi 417
Cdd:PTZ00402 365 VVSNTLKVRCT--VEGQIHLEACEKllHKKVPDMGEKTYYKSDVIFLDAEDVA--------LLKEGDEVTLMdwgNAY-- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 418 kcndvIKD-----AEGNVTE----IHCTYDIetksgsgftgRKVKGTIHWV-EATQAVPAEFRLYEPLINAEEPEvLEED 487
Cdd:PTZ00402 433 -----IKNirrsgEDALITDadivLHLEGDV----------KKTKFKLTWVpESPKAEVMELNEYDHLLTKKKPD-PEES 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 309249370 488 gsektFLDQLNPNSLEIAHGYVERNMKEAQSQDKFQFFRHGYFSVD 533
Cdd:PTZ00402 497 -----IDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVD 537
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
26-543 |
2.55e-99 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 312.17 E-value: 2.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 26 EVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPA--KEDTEYVNSIQEDVKWLGYEWEEKHFASNYFE 103
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDEVVIQSDRLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 104 EMYKRAILLIQKGKAYVDDQSADQIRETRgtltEPGQNSPYRDRSVEDNLKLFEEMRAGKYQNGEKVLRAKIDMASPNIN 183
Cdd:PRK04156 181 IYYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 184 LRDPVIYRISHTAHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFED----QRPLYD---WvvaecemeNVPHQYE 256
Cdd:PRK04156 257 VRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYDyfgW--------EYPETIH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 257 FGRLNLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFAREDLKL 336
Cdd:PRK04156 329 YGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 337 KAPRTMAVIDPLKVVITNYPEgqvemLEAEN--NTENPELGTRQIPFSREIYIEREDFMENppskyfrlfpGNEVRLKHA 414
Cdd:PRK04156 409 IANRYFFVRDPVELEIEGAEP-----LEAKIplHPDRPERGEREIPVGGKVYVSSDDLEAE----------GKMVRLMDL 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 415 yfikCNDVIKDAEGNVTEIHcTYDIEtksgsgfTGRKVKGTI-HWVEATQAVPAefrlyeplinaeepEVLEEDGSEKTf 493
Cdd:PRK04156 474 ----FNVEITGVSVDKARYH-SDDLE-------EARKNKAPIiQWVPEDESVPV--------------RVLKPDGGDIE- 526
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 309249370 494 ldqlnpnsleiahGYVERNMKEAQSQDKFQFFRHGYFSVDpklSKPGEPV 543
Cdd:PRK04156 527 -------------GLAEPDVADLEVDDIVQFERFGFVRID---SVEDDEV 560
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
338-533 |
1.88e-72 |
|
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: 229.08 E-value: 1.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 338 APRTMAVIDPLKVVITNYPEGQVEMLEAENNTENPELGTRQIPFSREIYIEREDFmenppskyFRLFPGNEVRLKHAYFI 417
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 418 KCNDVIKDAEGNVTEIHCTYDIETKSGSgftgRKVKG-TIHWVEATQAVPAEFRLYEPLINAEEpevleedgsEKTFLdq 496
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED---------DADFL-- 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 309249370 497 LNPNSLE-IAHGYVERNMKEAQSQDKFQFFRHGYFSVD 533
Cdd:pfam03950 138 LNPDSLKvLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
27-340 |
7.48e-53 |
|
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: 179.59 E-value: 7.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 27 VVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEEK-HFASNYFEEM 105
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGpYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 106 YKRAILLIQKGkayvddqsadqiretrgtltepgqnspyrdrsvednlklfeemragkyqngekvlrakidmaspninlr 185
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 186 dpviyrishtahhntgdtwcIYPMYSYAHPLEDAIEGVTHSLCSLEFEDQRPLYDWVVAECEMEnVPHQYEFGRLNLA-Q 264
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLEdG 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309249370 265 TVTSKRKLKllvdekhvdgwddprmPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLE---HFAREDLKLKAPR 340
Cdd:cd00418 152 TKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEmiaAFSVERVNSADAT 214
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
26-340 |
3.83e-48 |
|
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: 167.53 E-value: 3.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 26 EVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNP--AKEDTEYVNSIQEDVKWLGYEWEEKHFASNYFE 103
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 104 EMYKRAILLIQKGKAYVddqsadqiretrgtltepgqnspyrdrsvednlklfeemragkyqngekvlrakidmaspnin 183
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 184 lrdpviyrishtaHHNTGDTWCIYPMYSYAHPLEDAIEGVTHSLCSLEFED----QRPLYDWVVAEcemenVPHQYEFGR 259
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEYFGWE-----YPETIHWGR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 260 LNLAQTVTSKRKLKLLVDEKHVDGWDDPRMPTISGLRRRGYTPEAIRSFVYETGISKAYGVIDLQVLEHFAREDLKLKAP 339
Cdd:cd09287 160 LKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRAN 239
|
.
gi 309249370 340 R 340
Cdd:cd09287 240 R 240
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
26-94 |
6.21e-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: 71.46 E-value: 6.21e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309249370 26 EVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEE 94
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDE 69
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
28-119 |
1.55e-10 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 62.18 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 28 VTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEE------KHFAsny 101
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGpvlyqsQRHD--- 83
|
90
....*....|....*....
gi 309249370 102 feeMYKRAI-LLIQKGKAY 119
Cdd:PRK05710 84 ---AYRAALdRLRAQGLVY 99
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
26-119 |
7.83e-09 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 58.21 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309249370 26 EVVTRFPPEPNGYLHIGHAKAIWINFSLGDEFGGRTNLRFDDTNPAKEDTEYVNSIQEDVKWLGYEWEE-KHFASNY--- 101
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgPDVGGEYgpy 124
|
90 100
....*....|....*....|...
gi 309249370 102 ----FEEMYKR-AILLIQKGKAY 119
Cdd:PLN02627 125 rqseRNAIYKQyAEKLLESGHVY 147
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
28-95 |
2.11e-07 |
|
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: 49.46 E-value: 2.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309249370 28 VTRFPPEPnGYLHIGHAKAIWINFSLGDEFggrtNLRFDDTNPAK------EDTEYVNSIQEDVKWLGYEWEEK 95
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIADQC----VVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQN 69
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
28-88 |
1.88e-06 |
|
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: 47.47 E-value: 1.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309249370 28 VTRFPPEPNGYLHIGHAKAIWINFSLG-----DEFGGRTNLRFDDTNPAKEDT-------------EYVNSIQEDVKWL 88
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAqayrkLGYKVRCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM 79
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
225-271 |
5.29e-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: 39.83 E-value: 5.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 309249370 225 HSLCSLEFEDQRPLYDWVVAECEMENVPHQYEFGRLNLAQTVTSKRK 271
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
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