|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-548 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1053.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 1 MTSEIKVNKTNFIKNIIKKDLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYI 80
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 81 NAIQEDVEWLGFKWENQPRFASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFE 160
Cdd:PRK05347 82 DSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 161 EMKNGKFAEGSKTLRAKIDMSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRP 240
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 241 FYDWVIEETEFSIKPQQIEFSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQ 320
Cdd:PRK05347 242 LYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 321 DSVIDVSVLEDAVRDDLNKSVLRKNVVLDPIRVSIKDMPDHH---LDVPNHPQEPEFGRREITISSQIFIERDDFVFKLE 397
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQveeLEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 398 KDMKKLSPNGRVRLLNGYVIECQEVITDTNGEVIELKCSYLPETLGGkKPNDGIKPNGIIHWVDANNCLDAEVRIYDRLF 477
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG-NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754269803 478 NDENPANADRIEDVLNPDSLqVIKNAKVERSLESVKAEERFQFNRVGYFIADlKDCSNDTLVFNRIVTLRN 548
Cdd:PRK05347 481 TVPNPAAGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRD 549
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
31-548 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 690.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 31 TRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKMYE 110
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 111 LAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINLRDP 190
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 191 ALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLNLNYTIT 270
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 271 SKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLRKNVVLDP 350
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 351 IRVSIKDMPDHH--LDVPNHPQEPEFGRREITISSQIFIERDDFVFKLEKDMKKLSPNGRVRLLNGYVIECQEVITDTNG 428
Cdd:TIGR00440 323 VEVVIENLSDEYelATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAAG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 429 EVIELKCSYLPETLgGKKPNDGIKPNGIIHWVDANNCLDAEVRIYDRLFNDENPANADRIEDVLNPDSLqVIKNAKVERS 508
Cdd:TIGR00440 403 KITTIFCTYDNKTL-GKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL-VIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 754269803 509 LESVKAEERFQFNRVGYFIADLKDCSNDTLVFNRIVTLRN 548
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKD 520
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
29-343 |
1.11e-140 |
|
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: 405.87 E-value: 1.11e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQpRFASEYFDKM 108
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV-TYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYVcdlsaeeirayrgtlkepgknspyrersitenlelfeemkngkfaegsktlrakidmssgninlr 188
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 189 dpalyrikfshHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSiKPQQIEFSRLNLNYT 268
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803 269 ITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLR 343
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
29-338 |
5.58e-138 |
|
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: 402.08 E-value: 5.58e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKM 108
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYVCDLSAEEIRAYRGTLkePGKNSPYRERSITENLELF-EEMKNGKFAEGSKTLRAKIDMSSgNINL 187
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 188 RDPALYRIKFS---HHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLN 264
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803 265 LNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSV-LEDAVRDDLN 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKsLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
27-531 |
1.57e-121 |
|
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: 365.66 E-value: 1.57e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 27 SSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFD 106
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 107 KMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPY----RERSITENlelfEEMKngkfAEG-SKTLRAKI--- 178
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGePPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 179 -----DMSSG-----NINLRDPALYRikfshhpKTGdkwciYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEE 248
Cdd:COG0008 155 gvvfdDLVRGeitfpNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 249 TEFSIkPqqiEFSRLNLNY----TITSKRKlkylvdnKLVngwddprmpTIKGYRRRGYTPESIRNFCEMIGISKQDS-- 322
Cdd:COG0008 223 LGWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqe 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 323 VIDVSVLEDAVrdDLNKsVLRKNVVLDPIRV------SIKDMPDHHLD---VPNHPQE--PEFGRREITIS--------- 382
Cdd:COG0008 283 IFSLEELIEAF--DLDR-VSRSPAVFDPVKLvwlngpYIRALDDEELAellAPELPEAgiREDLERLVPLVreraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 383 -----SQIFIERDDfvfklEKDMKKLSPNGRVRllngyviecqEVITDTnGEVIELKCSYLPETLggkkpndgikpNGII 457
Cdd:COG0008 360 laelaRFFFIERED-----EKAAKKRLAPEEVR----------KVLKAA-LEVLEAVETWDPETV-----------KGTI 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754269803 458 HWVDAnnclDAEVRiyDRLFndenpANADRIedvlnpdslqVIKNAKVERSL-ESVKA--EERFqFNRVGYFIADLK 531
Cdd:COG0008 413 HWVSA----EAGVK--DGLL-----FMPLRV----------ALTGRTVEPSLfDVLELlgKERV-FERLGYAIDKLA 467
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-548 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1053.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 1 MTSEIKVNKTNFIKNIIKKDLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYI 80
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 81 NAIQEDVEWLGFKWENQPRFASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFE 160
Cdd:PRK05347 82 DSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 161 EMKNGKFAEGSKTLRAKIDMSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRP 240
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 241 FYDWVIEETEFSIKPQQIEFSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQ 320
Cdd:PRK05347 242 LYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 321 DSVIDVSVLEDAVRDDLNKSVLRKNVVLDPIRVSIKDMPDHH---LDVPNHPQEPEFGRREITISSQIFIERDDFVFKLE 397
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQveeLEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 398 KDMKKLSPNGRVRLLNGYVIECQEVITDTNGEVIELKCSYLPETLGGkKPNDGIKPNGIIHWVDANNCLDAEVRIYDRLF 477
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG-NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754269803 478 NDENPANADRIEDVLNPDSLqVIKNAKVERSLESVKAEERFQFNRVGYFIADlKDCSNDTLVFNRIVTLRN 548
Cdd:PRK05347 481 TVPNPAAGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRD 549
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
11-548 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 785.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 11 NFIKNIIKKDLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWL 90
Cdd:PRK14703 14 NFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 91 GFKWENQPRFASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFEEMKNGKFAEG 170
Cdd:PRK14703 94 GFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 171 SKTLRAKIDMSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEET- 249
Cdd:PRK14703 174 AHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLg 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 250 EFSIKPQQIEFSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVL 329
Cdd:PRK14703 254 PWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 330 EDAVRDDLNKSVLRKNVVLDPIRVSIKDMPDHH---LDVPNHPQE-PEFGRREITISSQIFIERDDFVFKLEKDMKKLSP 405
Cdd:PRK14703 334 EFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKveeLDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 406 NGRVRLLNGYVIECQEVITDTNGEVIELKCSYLPETLGGKKPndGIKPNGIIHWVDANNCLDAEVRIYDRLFNDENPANA 485
Cdd:PRK14703 414 GREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT--GRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEAA 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803 486 DR--IEDvLNPDSLQVIKNaKVERSLESVKAEERFQFNRVGYFIADLKDCSNDTLVFNRIVTLRN 548
Cdd:PRK14703 492 DEdfLEF-LNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKD 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
31-548 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 690.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 31 TRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKMYE 110
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 111 LAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINLRDP 190
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 191 ALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLNLNYTIT 270
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 271 SKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLRKNVVLDP 350
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 351 IRVSIKDMPDHH--LDVPNHPQEPEFGRREITISSQIFIERDDFVFKLEKDMKKLSPNGRVRLLNGYVIECQEVITDTNG 428
Cdd:TIGR00440 323 VEVVIENLSDEYelATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAAG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 429 EVIELKCSYLPETLgGKKPNDGIKPNGIIHWVDANNCLDAEVRIYDRLFNDENPANADRIEDVLNPDSLqVIKNAKVERS 508
Cdd:TIGR00440 403 KITTIFCTYDNKTL-GKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL-VIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 754269803 509 LESVKAEERFQFNRVGYFIADLKDCSNDTLVFNRIVTLRN 548
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKD 520
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
29-547 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 543.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGfkWEN-QPRFASEYFDK 107
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WEPfKITYTSDYFQE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 108 MYELAILLIKKGKAYVCDLSAEEIRAYRgtlkEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINL 187
Cdd:PLN02859 343 LYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNM 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 188 RDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFsIKPQQIEFSRLNLNY 267
Cdd:PLN02859 419 YDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGL-YQPYVWEYSRLNVTN 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 268 TITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQD-SVIDVSVLEDAVRDDLNKSVLRKNV 346
Cdd:PLN02859 498 TVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDnSLIRMDRLEHHIREELNKTAPRTMV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 347 VLDPIRVSIKDMPDHHLD------VPNHPQEPEFGRREITISSQIFIERDDFVFKLEKDMKKLSPNGRVRLLNGYVIECQ 420
Cdd:PLN02859 578 VLHPLKVVITNLESGEVIeldakrWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKCT 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 421 EVI-TDTNGEVIELKCSYLPEtlggKKpndgIKPNGIIHWVDAN----NCLDAEVRIYDRLFNDENPANADRIEDVLNPD 495
Cdd:PLN02859 658 DVVlADDNETVVEIRAEYDPE----KK----TKPKGVLHWVAEPspgvEPLKVEVRLFDKLFLSENPAELEDWLEDLNPQ 729
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 754269803 496 SLQVIKNAKVERSLESVKAEERFQFNRVGYFIADlKDCSNDTLVFNRIVTLR 547
Cdd:PLN02859 730 SKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLK 780
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
32-547 |
2.66e-158 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 463.69 E-value: 2.66e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 32 RFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFK--WENqprFASEYFDKMY 109
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKpdWVT---FSSDYFDQLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 110 ELAILLIKKGKAYVCDLSAEEIRAYRgtlkEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINLRD 189
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 190 PALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFsIKPQQIEFSRLNLNYTI 269
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 270 TSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLRKNVVLD 349
Cdd:PTZ00437 287 LSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVID 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 350 PIRVSIKDMP-DHHLDVPNHPQEPEFGRREITISSQIFIERDDfvFKLEKDMKK---LSPNGRVRLL--NGYVIeCQEVI 423
Cdd:PTZ00437 367 PIKVVVDNWKgEREFECPNHPRKPELGSRKVMFTDTFYVDRSD--FRTEDNNSKfygLAPGPRVVGLkySGNVV-CKGFE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 424 TDTNGE--VIELKCSYLPETlggkkpndgiKPNGIIHWVDANNCLDAEVRIYDRLFNDENPANADRIEDVLNPDSlQVIK 501
Cdd:PTZ00437 444 VDAAGQpsVIHVDIDFERKD----------KPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDS-EVVS 512
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 754269803 502 NAKVERSLESVKAEERFQFNRVGYFIADlKDCSNDTLVFNRIVTLR 547
Cdd:PTZ00437 513 HGYAEKGIENAKHFESVQAERFGYFVVD-PDTRPDHLVMNRVLGLR 557
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
29-343 |
1.11e-140 |
|
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: 405.87 E-value: 1.11e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQpRFASEYFDKM 108
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV-TYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYVcdlsaeeirayrgtlkepgknspyrersitenlelfeemkngkfaegsktlrakidmssgninlr 188
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 189 dpalyrikfshHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSiKPQQIEFSRLNLNYT 268
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803 269 ITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLR 343
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
29-338 |
5.58e-138 |
|
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: 402.08 E-value: 5.58e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKM 108
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYVCDLSAEEIRAYRGTLkePGKNSPYRERSITENLELF-EEMKNGKFAEGSKTLRAKIDMSSgNINL 187
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 188 RDPALYRIKFS---HHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLN 264
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803 265 LNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSV-LEDAVRDDLN 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKsLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
27-531 |
1.57e-121 |
|
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: 365.66 E-value: 1.57e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 27 SSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFD 106
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 107 KMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPY----RERSITENlelfEEMKngkfAEG-SKTLRAKI--- 178
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGePPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 179 -----DMSSG-----NINLRDPALYRikfshhpKTGdkwciYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEE 248
Cdd:COG0008 155 gvvfdDLVRGeitfpNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 249 TEFSIkPqqiEFSRLNLNY----TITSKRKlkylvdnKLVngwddprmpTIKGYRRRGYTPESIRNFCEMIGISKQDS-- 322
Cdd:COG0008 223 LGWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqe 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 323 VIDVSVLEDAVrdDLNKsVLRKNVVLDPIRV------SIKDMPDHHLD---VPNHPQE--PEFGRREITIS--------- 382
Cdd:COG0008 283 IFSLEELIEAF--DLDR-VSRSPAVFDPVKLvwlngpYIRALDDEELAellAPELPEAgiREDLERLVPLVreraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 383 -----SQIFIERDDfvfklEKDMKKLSPNGRVRllngyviecqEVITDTnGEVIELKCSYLPETLggkkpndgikpNGII 457
Cdd:COG0008 360 laelaRFFFIERED-----EKAAKKRLAPEEVR----------KVLKAA-LEVLEAVETWDPETV-----------KGTI 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754269803 458 HWVDAnnclDAEVRiyDRLFndenpANADRIedvlnpdslqVIKNAKVERSL-ESVKA--EERFqFNRVGYFIADLK 531
Cdd:COG0008 413 HWVSA----EAGVK--DGLL-----FMPLRV----------ALTGRTVEPSLfDVLELlgKERV-FERLGYAIDKLA 467
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
1-540 |
2.60e-103 |
|
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: 321.77 E-value: 2.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 1 MTSEIKVNKTNFIKniikkDLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYI 80
Cdd:TIGR00463 71 LDIKKKEKKRKGLR-----ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 81 NAIQEDVEWLGFKWEnQPRFASEYFDKMYELAILLIKKGKAYVCDLSAEEIRayrgTLKEPGKNSPYRERSITENLELFE 160
Cdd:TIGR00463 146 DMILEDLEWLGVKWD-EVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFR----ELRNRGEACHCRDRSVEENLERWE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 161 EMKNGKFAEGSKTLRAKIDMSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQD--Q 238
Cdd:TIGR00463 221 EMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 239 RPFYDWVIEETEFsikPQQIEFSRLNLNY--TITSKRKLKYLVDNKLVnGWDDPRMPTIKGYRRRGYTPESIRNFCEMIG 316
Cdd:TIGR00463 301 KQEYIYRYFGWEP---PEFIHWGRLKIDDvrALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 317 ISKQDSVIDVSVLEDAVRDDLNKSVLRKNVVLDPIRVSIKDMPDHHLDV-PNHPQEPEFGRREITISSQIFIERDDFVFK 395
Cdd:TIGR00463 377 VKINDVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRVErPLHPDHPEIGERVLILRGEIYVPKDDLEEG 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 396 LEKdmkklspngrVRLLNGyvieCQEVITDTNGEVIELkcsylpETLGGKKpndgiKPNGIIHWVDANNCLDAevriydr 475
Cdd:TIGR00463 457 VEP----------VRLMDA----VNVIYSKKELRYHSE------GLEGARK-----LGKSIIHWLPAKDAVKV------- 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803 476 lfndenpanadrieDVLNPDSLqvIKNAKVERSLESVKAEERFQFNRVGYFIADLKDcsNDTLVF 540
Cdd:TIGR00463 505 --------------KVIMPDAS--IVEGVIEADASELEVGDVVQFERFGFARLDSAD--KDGMVF 551
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
20-529 |
5.96e-99 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 315.13 E-value: 5.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 20 DLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWEnQPR 99
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 100 FASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTlkepGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKID 179
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 180 MSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEetEFSIKPQQI- 258
Cdd:PLN02907 360 MQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILE--DMGLRKVHIw 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 259 EFSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKqdsviDVSVLEdavRDDL- 337
Cdd:PLN02907 438 EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASK-----NLNLME---WDKLw 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 338 --NKSVL-----RKNVVLDPIRV--SIKDMPDHHL--DVPNHPQEPEFGRREITISSQIFIERDDFVfklekdmkKLSPN 406
Cdd:PLN02907 510 tiNKKIIdpvcpRHTAVLKEGRVllTLTDGPETPFvrIIPRHKKYEGAGKKATTFTNRIWLDYADAE--------AISEG 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 407 GRVRLLN-GYVIeCQEVITDTNGEVIELKCSYLPEtlgGKKPNDGIKpngiIHWV-DANNCLDAEVRIYDRLFNDENPAN 484
Cdd:PLN02907 582 EEVTLMDwGNAI-IKEITKDEGGAVTALSGELHLE---GSVKTTKLK----LTWLpDTNELVPLSLVEFDYLITKKKLEE 653
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 754269803 485 ADRIEDVLNPDSlQVIKNAKVERSLESVKAEERFQFNRVGYFIAD 529
Cdd:PLN02907 654 DDNFLDVLNPCT-KKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
29-529 |
4.98e-94 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 299.18 E-value: 4.98e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKM 108
Cdd:PTZ00402 53 VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDLM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYvCDLSA-EEIRAYRGTlkepGKNSPYRERSITENLELFEEMKNGKfAEGSKT-LRAKIDMSSGNIN 186
Cdd:PTZ00402 133 YEKAEELIKKGLAY-CDKTPrEEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNENKA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 187 LRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSiKPQQIEFSRLNLN 266
Cdd:PTZ00402 207 MRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIR-KPIVEDFSRLNME 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 267 YTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLRKNV 346
Cdd:PTZ00402 286 YSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTV 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 347 VLDPIRVSIKDMPDHHLDV---PNHPQEPEFGRREITISSQIFIERDDFVFKLEKDMKKLSPNGrvrllNGYVIECQEvi 423
Cdd:PTZ00402 366 VSNTLKVRCTVEGQIHLEAcekLLHKKVPDMGEKTYYKSDVIFLDAEDVALLKEGDEVTLMDWG-----NAYIKNIRR-- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 424 TDTNGEVIELKCSYLPEtlggkkpNDGIKPNGIIHWV-DANNCLDAEVRIYDRLFNDENPANADRIEDVLNPDSlQVIKN 502
Cdd:PTZ00402 439 SGEDALITDADIVLHLE-------GDVKKTKFKLTWVpESPKAEVMELNEYDHLLTKKKPDPEESIDDIIAPVT-KYTQE 510
|
490 500
....*....|....*....|....*..
gi 754269803 503 AKVERSLESVKAEERFQFNRVGYFIAD 529
Cdd:PTZ00402 511 VYGEEALSVLKKGDIIQLERRGYYIVD 537
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
31-525 |
1.12e-93 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 297.15 E-value: 1.12e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 31 TRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPD--KEDIEYINAIQEDVEWLGFKWeNQPRFASEYFDKM 108
Cdd:PRK04156 104 MRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKW-DEVVIQSDRLEIY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYVCDLSAEEIRAyrgtLKEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINLR 188
Cdd:PRK04156 183 YEYARKLIEMGGAYVCTCDPEEFKE----LRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 189 DPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQD----QRPFYD---WVIEETefsikpqqIEFS 261
Cdd:PRK04156 259 DWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYDyfgWEYPET--------IHYG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 262 RLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSV 341
Cdd:PRK04156 331 RLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIA 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 342 LRKNVVLDPIRVSIKDMPDHHLDVPNHPQEPEFGRREITISSQIFIERDDFVfklekdmkklSPNGRVRLLNGYVIECQE 421
Cdd:PRK04156 411 NRYFFVRDPVELEIEGAEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLE----------AEGKMVRLMDLFNVEITG 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 422 VITDtngevielKCSYLPETLggkkpnDGIKPNG--IIHWVDANNCLDAEVRIYDRlfndenpanadriedvlnpdslqV 499
Cdd:PRK04156 481 VSVD--------KARYHSDDL------EEARKNKapIIQWVPEDESVPVRVLKPDG-----------------------G 523
|
490 500
....*....|....*....|....*.
gi 754269803 500 IKNAKVERSLESVKAEERFQFNRVGY 525
Cdd:PRK04156 524 DIEGLAEPDVADLEVDDIVQFERFGF 549
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
21-529 |
3.78e-90 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 286.52 E-value: 3.78e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 21 LETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKwENQPRF 100
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 101 ASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEpgknSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDM 180
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 181 SSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSiKPQQIEF 260
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 261 SRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKS 340
Cdd:PLN03233 238 ARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 341 VLRKNVV--LDPIRVSIKDMPD--HHLDVPN--HPQEPEFGRREITISSQIFIERddfvfkleKDMKKLSPNGRVRLLNG 414
Cdd:PLN03233 318 AKRFMAIdkADHTALTVTNADEeaDFAFSETdcHPKDPGFGKRAMRICDEVLLEK--------ADTEDIQLGEDIVLLRW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 415 YVIECQEVITDTNGEVIelkcsylpetlggkkPNDGIK-PNGIIHWV-DANNCLDAEVRIYDRLFNDENPANADRIEDVL 492
Cdd:PLN03233 390 GVIEISKIDGDLEGHFI---------------PDGDFKaAKKKISWIaDVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFI 454
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 754269803 493 NPDSL---QVIKNAkverSLESVKAEERFQFNRVGYFIAD 529
Cdd:PLN03233 455 NPDTLaetDVIGDA----GLKTLKEHDIIQLERRGFYRVD 490
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
29-350 |
1.47e-64 |
|
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: 210.02 E-value: 1.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKM 108
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGkayvcdlsaeeirayrgtlkepgknspyrersitenlelfeemkngkfaegsktlrakidmssgninlr 188
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 189 dpalyrikfshhpktgdkwcIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIkPQQIEFSRLNLNY- 267
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEP-PRFYHFPRLLLEDg 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 268 TITSKRKLKylvdnklvngwddprmPTIKGYRRRGYTPESIRNFCEMIGISKQDSViDVSVLEDAVRDDLNKSVLRKNVV 347
Cdd:cd00418 152 TKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGH-ELFTLEEMIAAFSVERVNSADAT 214
|
...
gi 754269803 348 LDP 350
Cdd:cd00418 215 FDW 217
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
347-529 |
1.21e-58 |
|
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: 192.49 E-value: 1.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 347 VLDPIRVSIKDMPDHH---LDVPNHPQEPEFGRREITISSQIFIERDDFvfklekdmKKLSPNGRVRLLNGYVIECQEVI 423
Cdd:pfam03950 7 VLDPVKVVIENYPEGQeetAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNIKVTEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 424 TDTNGEVIELKCSYLPETLGGKKpndgiKPNG-IIHWVDANNCLDAEVRIYDRLFNDENPANadrieDVLNPDSLQVIKN 502
Cdd:pfam03950 79 KDEDGNVTELHCTYDGDDLGGAR-----KVKGkIIHWVSASDAVPAEVRLYDRLFKDEDDAD-----FLLNPDSLKVLTE 148
|
170 180
....*....|....*....|....*..
gi 754269803 503 AKVERSLESVKAEERFQFNRVGYFIAD 529
Cdd:pfam03950 149 GLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
29-329 |
2.66e-45 |
|
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: 159.44 E-value: 2.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPD--KEDIEYINAIQEDVEWLGFKWEnQPRFASEYFD 106
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 107 KMYELAILLIKKGKAYVcdlsaeeirayrgtlkepgknspyrersitenlelfeemkngkfaegsktlrakidmssgnin 186
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 187 lrdpalyrikfshHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQD----QRPFYD---WvieetefsIKPQQIE 259
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEyfgW--------EYPETIH 156
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 260 FSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVL 329
Cdd:cd09287 157 WGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENL 226
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
31-142 |
1.20e-15 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 77.58 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 31 TRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDkMYE 110
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD-AYR 86
|
90 100 110
....*....|....*....|....*....|...
gi 754269803 111 LAI-LLIKKGKAYVCDLSAEEIRAYRGTLKEPG 142
Cdd:PRK05710 87 AALdRLRAQGLVYPCFCSRKEIAAAAPAPPDGG 119
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
28-340 |
1.64e-13 |
|
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: 70.31 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 28 SILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYfdk 107
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 108 myelaillikkgkayvcdlsaeeirayrgtlkepgknSPYRErsiTENLELFEEmkngkfaegsktlrakidmssgninl 187
Cdd:cd00808 78 -------------------------------------GPYRQ---SERLEIYRK-------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 188 rdpALYRIKfshhpKTGDKwciYPMYTFAHPLEDAIEEITHslctlefqdqrpfydwVIE-ETEFSIKPQQI-------- 258
Cdd:cd00808 92 ---YAEKLL-----EKGDG---FPTYHLANVVDDHLMGITH----------------VIRgEEHLSSTPKQIllyealgw 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 259 ---EFSRLNLnytIT-------SKRKLKYLVDnklvngwddprmptikGYRRRGYTPESIRNFCEMIGISKQDSViDVSV 328
Cdd:cd00808 145 eppKFAHLPL---ILnpdgkklSKRKGDTSIS----------------DYREEGYLPEALLNYLALLGWSPPDGE-EFFT 204
|
330
....*....|....*.
gi 754269803 329 LEDAVR----DDLNKS 340
Cdd:cd00808 205 LEELIElfdlERVSKS 220
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
23-230 |
1.20e-11 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 67.07 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 23 TNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFAS 102
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 103 EY-------FDKMY-ELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFEEMKngkfAEGSK-T 173
Cdd:PLN02627 120 EYgpyrqseRNAIYkQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAEL----AKGTPyT 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754269803 174 LRAKIDmSSGNINLRDpaLYRIKFSHHPKT-GDkWCIY-----PMYTFAHPLEDAIEEITHSL 230
Cdd:PLN02627 196 YRFRVP-KEGSVKIDD--LIRGEVSWNTDTlGD-FVLLrsngqPVYNFCVAVDDATMGITHVI 254
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
31-90 |
4.41e-11 |
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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: 60.96 E-value: 4.41e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754269803 31 TRFPPEPNGYLHIGHAKSICLNFGIAQE-----FDGKCNLRFDDTNPDKED-------------IEYINAIQEDVEWL 90
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDpankkgenakafvERWIERIKEDVEYM 79
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| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
31-97 |
6.06e-10 |
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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: 56.39 E-value: 6.06e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754269803 31 TRFPPEPnGYLHIGHAKSICLNFGIAqefdGKCNLRFDDTNPDK------EDIEYINAIQEDVEWLGFKWENQ 97
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQN 69
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| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
217-274 |
1.05e-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: 41.76 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 217 HPLEDAIEEIT--HSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLNLNYTITSKRK 274
Cdd:cd02156 46 HELEERKESIEedISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
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