|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-551 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1075.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 1 MANEEKEKSLNFIEEIVENDLSSGKHKSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYV 80
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 81 DSIKEDVKWLGFDWASE-HYASDYFDTLYEYAEKLINLGLAYVDDSNSEELAAQKGTPTTPGTNSPFRDRSIEENLTLFR 159
Cdd:PRK05347 82 DSIKEDVRWLGFDWSGElRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 160 EMREGKHEEGSKALRAKIDMASTNMLMRDPIIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRE 239
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 240 LYDWFIAKLEI-FPSKQYEFARLNLGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKR 318
Cdd:PRK05347 242 LYDWVLDNLPIpPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 319 DNMIDASLLEFFIKDHLNKISSRVMAVTDPLKVTITNFPEGQTEDCEIDNNPEDENSGSRMVPFDREIFIEKSDFLEEAP 398
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 399 KKYFRLKPGGVVRLKGAYIIQCDDIVKDENGEVIELKCSFIENSKSGQDTSGVKCKGVIHWVSQKNNVPLELRVYDRLFK 478
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFT 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1407363656 479 EEDvAGYDGDFRDILNENSLEVLKAYGEPSLKDAKLDDKFQFIRKGYYVLDKDSTENQIIFNQTVGMRDSWKK 551
Cdd:PRK05347 482 VPN-PAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
31-549 |
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: 660.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 31 TRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASE-HYASDYFDTLYE 109
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKiRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 110 YAEKLINLGLAYVDDSNSEELAAQKGTPTTPGTNSPFRDRSIEENLTLFREMREGKHEEGSKALRAKIDMASTNMLMRDP 189
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 190 IIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFP-SKQYEFARLNLGYTLM 268
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 269 SKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLEFFIKDHLNKISSRVMAVTDP 348
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 349 LKVTITNFpEGQTEDCEIDNNPEDENSGSRMVPFDREIFIEKSDFLEEAPKKYFRLKPGGVVRLKGAYIIQCDDIVKDEN 428
Cdd:TIGR00440 323 VEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 429 GEVIELKCSFIENSKSGQDTSGVKCKGVIHWVSQKNNVPLELRVYDRLFKEEDvAGYDGDFRDILNENSLEVLKAYGEPS 508
Cdd:TIGR00440 402 GKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPN-PGAPDDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1407363656 509 LKDAKLDDKFQFIRKGYYVLD-KDSTENQIIFNQTVGMRDSW 549
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
29-341 |
7.03e-143 |
|
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: 411.65 E-value: 7.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 29 ILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASEHYASDYFDTLY 108
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 109 EYAEKLINLGLAYVddsnseelaaqkgtpttpgtnspfrdrsieenltlfremregkheegskalrakidmastnmlmrd 188
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 189 piiyrikfakHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFPSKQYEFARLNLGYTLM 268
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVM 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1407363656 269 SKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLEFFIKDHLNKISSR 341
Cdd:cd00807 166 SKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
29-336 |
3.72e-128 |
|
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: 377.04 E-value: 3.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 29 ILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASE-HYASDYFDTL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGpYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 108 YEYAEKLINLGLAYVDDSNSEELAAQKGtpTTPGTNSPFRDRSIEENLTLF-REMREGKHEEGSKALRAKIDMASTnMLM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 187 RDPIIYRIKFA---KHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFPSK-QYEFARLN 262
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1407363656 263 LGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNM-IDASLLEFFIKDHLN 336
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
27-466 |
3.81e-118 |
|
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: 357.18 E-value: 3.81e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 27 KSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASE-HYASDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGpYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 106 TLYEYAEKLINLGLAYVDDSNSEELAAQKGTPTTPGTN----SPFRDRSIEEnltlfREMREGKHEEgsKALRAKI---- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEE-----LERMLAAGEP--PVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 178 ----DMAST-----NMLMRDPIIYRikfakhhrtGDKwciYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKL 248
Cdd:COG0008 156 vvfdDLVRGeitfpNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 249 EIFPSkqyEFARLNL----GYTLMSKRKlrllveeNHVngwddprmpTISGLRRRGYTPKSIRDFCDRIGIAKRDNM--I 322
Cdd:COG0008 224 GWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQeiF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 323 DASLLEFFIkdHLNKIsSRVMAVTDPLKVTITNFPEGQTEDCEIDNN---PEDENSG-----SRMVPFDRE--------- 385
Cdd:COG0008 285 SLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRALDDEELAEllaPELPEAGiredlERLVPLVREraktlsela 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 386 -----IFIEKSDflEEAPKKyfRLKPGGVVRlkgayIIQCDdivkdenGEVIELKCSFIENSKsgqdtsgvkcKGVIHWV 460
Cdd:COG0008 362 elarfFFIERED--EKAAKK--RLAPEEVRK-----VLKAA-------LEVLEAVETWDPETV----------KGTIHWV 415
|
....*.
gi 1407363656 461 SQKNNV 466
Cdd:COG0008 416 SAEAGV 421
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-551 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1075.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 1 MANEEKEKSLNFIEEIVENDLSSGKHKSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYV 80
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 81 DSIKEDVKWLGFDWASE-HYASDYFDTLYEYAEKLINLGLAYVDDSNSEELAAQKGTPTTPGTNSPFRDRSIEENLTLFR 159
Cdd:PRK05347 82 DSIKEDVRWLGFDWSGElRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 160 EMREGKHEEGSKALRAKIDMASTNMLMRDPIIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRE 239
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 240 LYDWFIAKLEI-FPSKQYEFARLNLGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKR 318
Cdd:PRK05347 242 LYDWVLDNLPIpPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 319 DNMIDASLLEFFIKDHLNKISSRVMAVTDPLKVTITNFPEGQTEDCEIDNNPEDENSGSRMVPFDREIFIEKSDFLEEAP 398
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 399 KKYFRLKPGGVVRLKGAYIIQCDDIVKDENGEVIELKCSFIENSKSGQDTSGVKCKGVIHWVSQKNNVPLELRVYDRLFK 478
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFT 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1407363656 479 EEDvAGYDGDFRDILNENSLEVLKAYGEPSLKDAKLDDKFQFIRKGYYVLDKDSTENQIIFNQTVGMRDSWKK 551
Cdd:PRK05347 482 VPN-PAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
7-551 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 833.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 7 EKSLNFIEEIVENDLSSGKHKSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKED 86
Cdd:PRK14703 10 LVSPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 87 VKWLGFDW-ASEHYASDYFDTLYEYAEKLINLGLAYVDDSNSEELAAQKGTPTTPGTNSPFRDRSIEENLTLFREMREGK 165
Cdd:PRK14703 90 VRWLGFDWgEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 166 HEEGSKALRAKIDMASTNMLMRDPIIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFI 245
Cdd:PRK14703 170 FPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 246 AKLEIFPSK--QYEFARLNLGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMID 323
Cdd:PRK14703 250 DHLGPWPPRprQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 324 ASLLEFFIKDHLNKISSRVMAVTDPLKVTITNFPEGQTEDCEIDNNPED-ENSGSRMVPFDREIFIEKSDFLEEAPKKYF 402
Cdd:PRK14703 330 IGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 403 RLKPGGVVRLKGAYIIQCDDIVKDENGEVIELKCSFIENSKSGQDTsGVKCKGVIHWVSQKNNVPLELRVYDRLFKEEDV 482
Cdd:PRK14703 410 RLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQP 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 483 AGYDGDFRDILNENSLEVLKAYGEPSLKDAKLDDKFQFIRKGYYVLDK-DSTENQIIFNQTVGMRDSWKK 551
Cdd:PRK14703 489 EAADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGA 558
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
31-549 |
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: 660.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 31 TRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASE-HYASDYFDTLYE 109
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKiRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 110 YAEKLINLGLAYVDDSNSEELAAQKGTPTTPGTNSPFRDRSIEENLTLFREMREGKHEEGSKALRAKIDMASTNMLMRDP 189
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 190 IIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFP-SKQYEFARLNLGYTLM 268
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 269 SKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLEFFIKDHLNKISSRVMAVTDP 348
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 349 LKVTITNFpEGQTEDCEIDNNPEDENSGSRMVPFDREIFIEKSDFLEEAPKKYFRLKPGGVVRLKGAYIIQCDDIVKDEN 428
Cdd:TIGR00440 323 VEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 429 GEVIELKCSFIENSKSGQDTSGVKCKGVIHWVSQKNNVPLELRVYDRLFKEEDvAGYDGDFRDILNENSLEVLKAYGEPS 508
Cdd:TIGR00440 402 GKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPN-PGAPDDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1407363656 509 LKDAKLDDKFQFIRKGYYVLD-KDSTENQIIFNQTVGMRDSW 549
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
15-551 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 568.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 15 EIVENDLSSGKHKsILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDW 94
Cdd:PLN02859 252 EILEKHLKATGGK-VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 95 ASEHYASDYFDTLYEYAEKLINLGLAYVDDSNSEELAAQKgtptTPGTNSPFRDRSIEENLTLFREMREGKHEEGSKALR 174
Cdd:PLN02859 331 FKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 175 AKIDMASTNMLMRDPIIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFPSK 254
Cdd:PLN02859 407 MKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLYQPY 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 255 QYEFARLNLGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDN-MIDASLLEFFIKD 333
Cdd:PLN02859 487 VWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIRMDRLEHHIRE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 334 HLNKISSRVMAVTDPLKVTITNFPEGQTEDCEID---NNPEDENSGSRMVPFDREIFIEKSDFLEEAPKKYFRLKPGGVV 410
Cdd:PLN02859 567 ELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKrwpDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSV 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 411 RLKGAYIIQCDDIV-KDENGEVIELKCSFiENSKSgqdtsgVKCKGVIHWVSQ----KNNVPLELRVYDRLFKEEDVAGY 485
Cdd:PLN02859 647 LLRYAFPIKCTDVVlADDNETVVEIRAEY-DPEKK------TKPKGVLHWVAEpspgVEPLKVEVRLFDKLFLSENPAEL 719
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1407363656 486 DgDFRDILNENSLEVLK-AYGEPSLKDAKLDDKFQFIRKGYYVLDKDSTENQIIFNQTVGMRDSWKK 551
Cdd:PLN02859 720 E-DWLEDLNPQSKEVISgAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
32-551 |
4.75e-162 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 473.32 E-value: 4.75e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 32 RFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGF--DWASehYASDYFDTLYE 109
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDWVT--FSSDYFDQLHE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 110 YAEKLINLGLAYVDDSNSEELAAQKGTPTtpgtNSPFRDRSIEENLTLFREMREGKHEEGSKALRAKIDMASTNMLMRDP 189
Cdd:PTZ00437 133 FAVQLIKDGKAYVDHSTPDELKQQREQRE----DSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 190 IIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFPSKQYEFARLNLGYTLMS 269
Cdd:PTZ00437 209 IAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFSRLNVTGSLLS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 270 KRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLEFFIKDHLNKISSRVMAVTDPL 349
Cdd:PTZ00437 289 KRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 350 KVTITNFPEGQTEDCEidNNPEDENSGSRMVPFDREIFIEKSDF-LEEAPKKYFRLKPGG-VVRLKGAYIIQCDDIVKDE 427
Cdd:PTZ00437 369 KVVVDNWKGEREFECP--NHPRKPELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPGPrVVGLKYSGNVVCKGFEVDA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 428 NGE--VIELKCSFIENSKSgqdtsgvkcKGVIHWVSQKNNVPLELRVYDRLFKeEDVAGYDGDFRDILNENSLEVLKAYG 505
Cdd:PTZ00437 447 AGQpsVIHVDIDFERKDKP---------KTNISWVSATACTPVEVRLYNALLK-DDRAAIDPEFLKFIDEDSEVVSHGYA 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1407363656 506 EPSLKDAKLDDKFQFIRKGYYVLDKDSTENQIIFNQTVGMRDSWKK 551
Cdd:PTZ00437 517 EKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
29-341 |
7.03e-143 |
|
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: 411.65 E-value: 7.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 29 ILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASEHYASDYFDTLY 108
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 109 EYAEKLINLGLAYVddsnseelaaqkgtpttpgtnspfrdrsieenltlfremregkheegskalrakidmastnmlmrd 188
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 189 piiyrikfakHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFPSKQYEFARLNLGYTLM 268
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVM 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1407363656 269 SKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLEFFIKDHLNKISSR 341
Cdd:cd00807 166 SKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
29-336 |
3.72e-128 |
|
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: 377.04 E-value: 3.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 29 ILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASE-HYASDYFDTL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGpYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 108 YEYAEKLINLGLAYVDDSNSEELAAQKGtpTTPGTNSPFRDRSIEENLTLF-REMREGKHEEGSKALRAKIDMASTnMLM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 187 RDPIIYRIKFA---KHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFPSK-QYEFARLN 262
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1407363656 263 LGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNM-IDASLLEFFIKDHLN 336
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
27-466 |
3.81e-118 |
|
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: 357.18 E-value: 3.81e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 27 KSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASE-HYASDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGpYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 106 TLYEYAEKLINLGLAYVDDSNSEELAAQKGTPTTPGTN----SPFRDRSIEEnltlfREMREGKHEEgsKALRAKI---- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEE-----LERMLAAGEP--PVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 178 ----DMAST-----NMLMRDPIIYRikfakhhrtGDKwciYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKL 248
Cdd:COG0008 156 vvfdDLVRGeitfpNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 249 EIFPSkqyEFARLNL----GYTLMSKRKlrllveeNHVngwddprmpTISGLRRRGYTPKSIRDFCDRIGIAKRDNM--I 322
Cdd:COG0008 224 GWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQeiF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 323 DASLLEFFIkdHLNKIsSRVMAVTDPLKVTITNFPEGQTEDCEIDNN---PEDENSG-----SRMVPFDRE--------- 385
Cdd:COG0008 285 SLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRALDDEELAEllaPELPEAGiredlERLVPLVREraktlsela 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 386 -----IFIEKSDflEEAPKKyfRLKPGGVVRlkgayIIQCDdivkdenGEVIELKCSFIENSKsgqdtsgvkcKGVIHWV 460
Cdd:COG0008 362 elarfFFIERED--EKAAKK--RLAPEEVRK-----VLKAA-------LEVLEAVETWDPETV----------KGTIHWV 415
|
....*.
gi 1407363656 461 SQKNNV 466
Cdd:COG0008 416 SAEAGV 421
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
1-530 |
5.74e-108 |
|
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: 334.10 E-value: 5.74e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 1 MANEEKEKSLNFieeivENDLSSGKHKSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYV 80
Cdd:TIGR00463 71 LDIKKKEKKRKG-----LRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 81 DSIKEDVKWLGFDWASEHYASDYFDTLYEYAEKLINLGLAYVDDSNSEELAAQKGTpttpGTNSPFRDRSIEENLTLFRE 160
Cdd:TIGR00463 146 DMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 161 MREGKHEEGSKALRAKIDMASTNMLMRDPIIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRE- 239
Cdd:TIGR00463 222 MLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRk 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 240 -LYDWFIAKLEIFPSKQYEFARLNLGYTLMSKRKLRLLVEENHVnGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKR 318
Cdd:TIGR00463 302 qEYIYRYFGWEPPEFIHWGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKIN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 319 DNMIDASLLEFFIKDHLNKISSRVMAVTDPLKVTITNFPEGQTEdcEIDNNPEDENSGSRMVPFDREIFIEKSDFLEEAP 398
Cdd:TIGR00463 381 DVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRV--ERPLHPDHPEIGERVLILRGEIYVPKDDLEEGVE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 399 kkyfrlkpggVVRLKGAyiiqCDDIVKDENGEVielkcsfienskSGQDTSGVKCKG--VIHWVSQKNNVPLELRVYDRL 476
Cdd:TIGR00463 459 ----------PVRLMDA----VNVIYSKKELRY------------HSEGLEGARKLGksIIHWLPAKDAVKVKVIMPDAS 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1407363656 477 FKEedvagydgdfrDILNENSLEVlkaygepslkdaKLDDKFQFIRKGYYVLDK 530
Cdd:TIGR00463 513 IVE-----------GVIEADASEL------------EVGDVVQFERFGFARLDS 543
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
18-529 |
6.23e-108 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 339.01 E-value: 6.23e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 18 ENDLSSGKHKSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASE 97
Cdd:PLN02907 203 EVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 98 HYASDYFDTLYEYAEKLINLGLAYVDDSNSEELAAQKGTpttpGTNSPFRDRSIEENLTLFREMREGKHEEGSKALRAKI 177
Cdd:PLN02907 283 TYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 178 DMASTNMLMRDPIIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFPSKQYE 257
Cdd:PLN02907 359 DMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 258 FARLNLGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLEFFIKDHLNK 337
Cdd:PLN02907 439 FSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDP 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 338 ISSRVMAVTDPLKV--TITNFPEgQTEDCEIDNNPEDENSGSRMVPFDREIFIEKSDflEEApkkyfrLKPGGVVRLK-- 413
Cdd:PLN02907 519 VCPRHTAVLKEGRVllTLTDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD--AEA------ISEGEEVTLMdw 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 414 GAYIIQcdDIVKDENGEVIELKCSFieNSKSGQDTSGVKckgvIHWVSQKNN-VPLELRVYDRLFKEEDVAGYDgDFRDI 492
Cdd:PLN02907 590 GNAIIK--EITKDEGGAVTALSGEL--HLEGSVKTTKLK----LTWLPDTNElVPLSLVEFDYLITKKKLEEDD-NFLDV 660
|
490 500 510
....*....|....*....|....*....|....*..
gi 1407363656 493 LNENSLEVLKAYGEPSLKDAKLDDKFQFIRKGYYVLD 529
Cdd:PLN02907 661 LNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
19-530 |
4.39e-106 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 328.12 E-value: 4.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 19 NDLSSGKHKSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASEH 98
Cdd:PLN03233 2 NALEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 99 YASDYFDTLYEYAEKLINLGLAYVDDSNSEELAAQKgtptTPGTNSPFRDRSIEENLTLFREMREGKHEEGSKALRAKID 178
Cdd:PLN03233 82 FTSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKER----ADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKID 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 179 MASTNMLMRDPIIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFPSKQYEF 258
Cdd:PLN03233 158 MQSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 259 ARLNLGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLEFFIKDHLNKI 338
Cdd:PLN03233 238 ARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 339 SSRVMAV--TDPLKVTITNFPEG-QTEDCEIDNNPEDENSGSRMVPFDREIFIEKSDFLEEAPKKYFRLKPGGVVRlkga 415
Cdd:PLN03233 318 AKRFMAIdkADHTALTVTNADEEaDFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDIVLLRWGVIE---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 416 yiiqcddIVKDENGevieLKCSFIENSksgqDTSGVKCKgvIHWVSQ-KNNVPLELRVYDRLFKEEDVAgYDGDFRDILN 494
Cdd:PLN03233 394 -------ISKIDGD----LEGHFIPDG----DFKAAKKK--ISWIADvSDNIPVVLSEFDNLIIKEKLE-EDDKFEDFIN 455
|
490 500 510
....*....|....*....|....*....|....*.
gi 1407363656 495 ENSLEVLKAYGEPSLKDAKLDDKFQFIRKGYYVLDK 530
Cdd:PLN03233 456 PDTLAETDVIGDAGLKTLKEHDIIQLERRGFYRVDR 491
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
17-538 |
7.62e-99 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 311.90 E-value: 7.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 17 VEND---LSSGKHKSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFD 93
Cdd:PTZ00402 38 EENDklqLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 94 WAS-EHYASDYFDTLYEYAEKLINLGLAYVDDSNSEELaaQK----GTPTTpgtnspFRDRSIEENLTLFREMREGKHEE 168
Cdd:PTZ00402 118 WDVgPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEM--QKcrfdGVPTK------YRDISVEETKRLWNEMKKGSAEG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 169 GSKALRAKIDMASTNMLMRDPIIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKL 248
Cdd:PTZ00402 190 QETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 249 EIFPSKQYEFARLNLGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLE 328
Cdd:PTZ00402 270 GIRKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLW 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 329 FFIKDHLNKISSRVMAVTDPLKVTITNFPEGQTEDCEIDNNPEDENSGSrmvpfdreifieksdfleeapKKYFRlkpgg 408
Cdd:PTZ00402 350 YFNTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGE---------------------KTYYK----- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 409 vvrlKGAYIIQCDDIVKDENGEVIELK---CSFIENSK-SGQDTSGVKCKGVIH-------------WVSQKNN-VPLEL 470
Cdd:PTZ00402 404 ----SDVIFLDAEDVALLKEGDEVTLMdwgNAYIKNIRrSGEDALITDADIVLHlegdvkktkfkltWVPESPKaEVMEL 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 471 RVYDRLF--KEEDVagyDGDFRDILNENSLEVLKAYGEPSLKDAKLDDKFQFIRKGYYVLDKDSTENQII 538
Cdd:PTZ00402 480 NEYDHLLtkKKPDP---EESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
4-530 |
1.28e-96 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 304.85 E-value: 1.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 4 EEKEKslnfiEEIVENDLSSGKHKSILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTE--DTEYVD 81
Cdd:PRK04156 82 EEKKE-----EKKGLPPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKrpDPEAYD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 82 SIKEDVKWLGFDWASEHYASDYFDTLYEYAEKLINLGLAYVDDSNSEELAAQK--GTPTtpgtnsPFRDRSIEENLTLFR 159
Cdd:PRK04156 157 MILEDLKWLGVKWDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRdaGKPC------PHRDKSPEENLELWE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 160 EMREGKHEEGSKALRAKIDMASTNMLMRDPIIYRIKFAKHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRE 239
Cdd:PRK04156 231 KMLDGEYKEGEAVVRVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 240 ----LYDWFIAKLEIFpskqYEFARLNLGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGI 315
Cdd:PRK04156 311 kqryIYDYFGWEYPET----IHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGV 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 316 AKRDNMIDASLLEFFIKDHLNKISSRVMAVTDPLKVTITNFPEgqtEDCEIDNNPEDENSGSRMVPFDREIFIEKSDFLE 395
Cdd:PRK04156 387 KETDATISWENLYAINRKLIDPIANRYFFVRDPVELEIEGAEP---LEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEA 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 396 EapkkyfrlkpGGVVRLKGAYIIQcddIVKDENGEVIELKCSFIENSKSGQDtsgvkckgVIHWVSQKNNVPLELRVYDr 475
Cdd:PRK04156 464 E----------GKMVRLMDLFNVE---ITGVSVDKARYHSDDLEEARKNKAP--------IIQWVPEDESVPVRVLKPD- 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1407363656 476 lfkEEDVAGydgdfrdilnenslevlkaYGEPSLKDAKLDDKFQFIRKGYYVLDK 530
Cdd:PRK04156 522 ---GGDIEG-------------------LAEPDVADLEVDDIVQFERFGFVRIDS 554
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
339-529 |
9.32e-68 |
|
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: 216.75 E-value: 9.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 339 SSRVMAVTDPLKVTITNFPEGQTEDCEIDNNPEDENSGSRMVPFDREIFIEKSDFleeapkkyFRLKPGGVVRLKGAYII 418
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 419 QCDDIVKDENGEVIELKCSFIENSKSGQdtsgVKCKG-VIHWVSQKNNVPLELRVYDRLFKEEDvagydgDFRDILNENS 497
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED------DADFLLNPDS 142
|
170 180 190
....*....|....*....|....*....|...
gi 1407363656 498 LEVLK-AYGEPSLKDAKLDDKFQFIRKGYYVLD 529
Cdd:pfam03950 143 LKVLTeGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
29-340 |
2.84e-60 |
|
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: 199.24 E-value: 2.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 29 ILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWaSEH--YASDYFDT 106
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDW-DEGpyRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 107 LYEYAEKLINLGlayvddsnseelaaqkgtpttpgtnspfrdrsieenltlfremregkheegskalrakidmastnmlm 186
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 187 rdpiiyrikfakhhrtgdkwcIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRELYDWFIAKLEIFPSKQYEFARLNLGY- 265
Cdd:cd00418 93 ---------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDg 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1407363656 266 TLMSKRKLRllveenhvngwddprmPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLEFFIKDHLNKISS 340
Cdd:cd00418 152 TKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNS 210
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
29-341 |
2.03e-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: 167.91 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 29 ILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNP--VTEDTEYVDSIKEDVKWLGFDWASEHYASDYFDT 106
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 107 LYEYAEKLINLGLAYVddsnseelaaqkgtpttpgtnspfrdrsieenltlfremregkheegskalrakidmastnmlm 186
Cdd:cd09287 82 YYEYARKLIEMGGAYV---------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 187 rdpiiyrikfakHHRTGDKWCIYPMYDLAHGQSDSIEEITHSVCTLEFVAHRE----LYDWFIAKLEIFpskqYEFARLN 262
Cdd:cd09287 98 ------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEkqryIYEYFGWEYPET----IHWGRLK 161
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1407363656 263 LGYTLMSKRKLRLLVEENHVNGWDDPRMPTISGLRRRGYTPKSIRDFCDRIGIAKRDNMIDASLLEFFIKDHLNKISSR 341
Cdd:cd09287 162 IEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
31-121 |
2.74e-14 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 73.73 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 31 TRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDWASE-HYASDYFDtLYE 109
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPvLYQSQRHD-AYR 86
|
90
....*....|...
gi 1407363656 110 YA-EKLINLGLAY 121
Cdd:PRK05710 87 AAlDRLRAQGLVY 99
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
28-118 |
6.46e-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: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 28 SILTRFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDW------ASEH--- 98
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWdegpdvGGPYgpy 80
|
90 100
....*....|....*....|
gi 1407363656 99 YASDYFDTLYEYAEKLINLG 118
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
32-134 |
8.06e-13 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 70.93 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 32 RFPPEPNGYLHIGHAKSICLNFGLAESYGGKTNLRFDDTNPVTEDTEYVDSIKEDVKWLGFDW------ASEH--YASDY 103
Cdd:PLN02627 49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWdegpdvGGEYgpYRQSE 128
|
90 100 110
....*....|....*....|....*....|..
gi 1407363656 104 FDTLY-EYAEKLINLGLAYVDDSNSEELAAQK 134
Cdd:PLN02627 129 RNAIYkQYAEKLLESGHVYPCFCTDEELEAMK 160
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
31-95 |
1.05e-10 |
|
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: 59.80 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 31 TRFPPEPNGYLHIGHAKSICLNFGLA-----ESYGGKTNLRFDDTNPVTEDT-------------EYVDSIKEDVKWLgF 92
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAqayrkLGYKVRCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM-F 80
|
...
gi 1407363656 93 DWA 95
Cdd:cd00802 81 LQA 83
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
31-94 |
4.24e-09 |
|
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: 54.08 E-value: 4.24e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407363656 31 TRFPPEPnGYLHIGHAKSICLNFGLAesygGKTNLRFDDTNPVT------EDTEYVDSIKEDVKWLGFDW 94
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDF 66
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
221-272 |
6.09e-05 |
|
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: 42.14 E-value: 6.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1407363656 221 SIEEItHSVCTLEFVAHRELYDWFIAKLEIFPS-KQYEFARLNLGYTLMSKRK 272
Cdd:cd02156 54 SIEED-ISVCGEDFQQNRELYRWVKDNITLPVDpEQVELPRLNLETTVMSKRK 105
|
|
| |
