|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
3-560 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1002.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 3 NDNAMETAAAENYMDKLIKEDIESGIYSReICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDME 82
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTR-VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 83 YVKAIIQDIEWLGCSPGEHIYYGSDYSEQIYNSALNLIRKGKAYVCDLSPEEVTAYRGTLTEPGKNSPYRERSVEENLRL 162
Cdd:PRK05347 80 YVDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 163 FSGMREGAYPTGSRVLRAKIDMSSPNINLRDPVIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDH 242
Cdd:PRK05347 160 FERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 243 RPLYEWVLEELGIEEAPRQREFGRVNLTGVVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMV 322
Cdd:PRK05347 240 RPLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 323 RNQTMVDFSMLEHCLRQDLKASVPSIMAVLDPLKVVITNYEAGETEWLPLANNSENAELGVREVPFSGTVYIERDDFMEE 402
Cdd:PRK05347 320 KQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 403 PAPGFRRLVPGGEVRLKGAYIIKCNEVIKDAgTGAVRELRCTYDPLTKSGGANSGRKVKGTLHWVSASHGIPAEVYLYEK 482
Cdd:PRK05347 400 PPKKYFRLVPGKEVRLRNAYVIKCEEVVKDA-DGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDR 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806915762 483 LLEDnEGPkAEGETWEEYINPDSIRLmLSCLLEPFAAGAKPEDKFQFMRQGYFCVDnKLSREDRLVFNRIVPLKDTWK 560
Cdd:PRK05347 479 LFTV-PNP-AAGKDFLDFLNPDSLVI-KQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWA 552
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
35-559 |
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: 634.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 35 TRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEHIYYGSDYSEQIYN 114
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 115 SALNLIRKGKAYVCDLSPEEVTAYRGTLTEPGKNSPYRERSVEENLRLFSGMREGAYPTGSRVLRAKIDMSSPNINLRDP 194
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 195 VIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEEAPRQREFGRVNLTGVVT 274
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 275 GKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQTMVDFSMLEHCLRQDLKASVPSIMAVLDP 354
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 355 LKVVITNYEaGETEWLPLANNSENAELGVREVPFSGTVYIERDDFMEEPAPGFRRLVPGGEVRLKGAYIIKCNEVIKDAg 434
Cdd:TIGR00440 323 VEVVIENLS-DEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 435 TGAVRELRCTYDPLTKSGGANSGRKVKGTLHWVSASHGIPAEVYLYEKLLEdNEGPKAEgETWEEYINPDSIRLMLScLL 514
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFK-VPNPGAP-DDFLSVINPESLVIKQG-FM 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 806915762 515 EPFAAGAKPEDKFQFMRQGYFCVDNKLSREDRLVFNRIVPLKDTW 559
Cdd:TIGR00440 478 EHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
32-346 |
6.50e-120 |
|
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: 353.48 E-value: 6.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 32 EICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGeHIYYGSDYSEQ 111
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 112 IYNSALNLIRKGKAYVcdlspeevtayrgtltepgknspyrersveenlrlfsgmregayptgsrvlrakidmsspninl 191
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 192 rdpviyriihaeHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEeAPRQREFGRVNLTG 271
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806915762 272 VVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQTMVDFSMLEHCLRQDLKASVP 346
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAP 237
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
32-326 |
3.31e-119 |
|
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: 354.70 E-value: 3.31e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 32 EICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEHIYYGSDYSEQ 111
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 112 IYNSALNLIRKGKAYVCDLSPEEVTAYRGTLtePGKNSPYRERSVEENLRLFS-GMREGAYPTGSRVLRAKIDMSSPnIN 190
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 191 LRDPVIYRII---HAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEEAPRQREFGRV 267
Cdd:pfam00749 158 FRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 806915762 268 NLTGVVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQT 326
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFD 296
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
29-473 |
1.29e-114 |
|
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: 348.32 E-value: 1.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 29 YSREICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEHIYYGSDY 108
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 109 SEQIYNSALNLIRKGKAYVCDLSPEEVTAYRGTLTEPGKNSPY----RERSVEENLRLfsgMREGAyptgSRVLRAKI-- 182
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEELERM---LAAGE----PPVLRFKIpe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 183 ------DMSS-----PNINLRDPVIYRiihaehyRTGnawciYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLE 251
Cdd:COG0008 154 egvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 252 ELGIeEAPrqrEFGRVNLT----GVVTGKRYlralvagNYVdgwddprlpTLRGLRRRGFTPESIRSFVREIG--MVRNQ 325
Cdd:COG0008 222 ALGW-EPP---EFAHLPLIlgpdGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGwsKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 326 TMVDFSMLEHCLrqDLKAsVPSIMAVLDPLKVVITNY--------------------EAGETEWL----PLANnsENAEL 381
Cdd:COG0008 282 EIFSLEELIEAF--DLDR-VSRSPAVFDPVKLVWLNGpyiralddeelaellapelpEAGIREDLerlvPLVR--ERAKT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 382 GVREVPFSGTVYIERDDfmEEPAPGfrRLVPgGEVRlkgayiikcnEVIKDAgTGAVRELRcTYDPLTksggansgrkVK 461
Cdd:COG0008 357 LSELAELARFFFIERED--EKAAKK--RLAP-EEVR----------KVLKAA-LEVLEAVE-TWDPET----------VK 409
|
490
....*....|..
gi 806915762 462 GTLHWVSASHGI 473
Cdd:COG0008 410 GTIHWVSAEAGV 421
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
3-560 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1002.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 3 NDNAMETAAAENYMDKLIKEDIESGIYSReICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDME 82
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTR-VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 83 YVKAIIQDIEWLGCSPGEHIYYGSDYSEQIYNSALNLIRKGKAYVCDLSPEEVTAYRGTLTEPGKNSPYRERSVEENLRL 162
Cdd:PRK05347 80 YVDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 163 FSGMREGAYPTGSRVLRAKIDMSSPNINLRDPVIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDH 242
Cdd:PRK05347 160 FERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 243 RPLYEWVLEELGIEEAPRQREFGRVNLTGVVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMV 322
Cdd:PRK05347 240 RPLYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 323 RNQTMVDFSMLEHCLRQDLKASVPSIMAVLDPLKVVITNYEAGETEWLPLANNSENAELGVREVPFSGTVYIERDDFMEE 402
Cdd:PRK05347 320 KQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 403 PAPGFRRLVPGGEVRLKGAYIIKCNEVIKDAgTGAVRELRCTYDPLTKSGGANSGRKVKGTLHWVSASHGIPAEVYLYEK 482
Cdd:PRK05347 400 PPKKYFRLVPGKEVRLRNAYVIKCEEVVKDA-DGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDR 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806915762 483 LLEDnEGPkAEGETWEEYINPDSIRLmLSCLLEPFAAGAKPEDKFQFMRQGYFCVDnKLSREDRLVFNRIVPLKDTWK 560
Cdd:PRK05347 479 LFTV-PNP-AAGKDFLDFLNPDSLVI-KQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWA 552
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
10-559 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 798.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 10 AAAENYMDKLIKEDIESGIYSReICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQ 89
Cdd:PRK14703 10 LVSPNFITEIIEEDLEAGRYPR-VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 90 DIEWLGCSPGEHIYYGSDYSEQIYNSALNLIRKGKAYVCDLSPEEVTAYRGTLTEPGKNSPYRERSVEENLRLFSGMREG 169
Cdd:PRK14703 89 DVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 170 AYPTGSRVLRAKIDMSSPNINLRDPVIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWV 249
Cdd:PRK14703 169 EFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 250 LEELGIEEA-PRQREFGRVNLTGVVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQTMV 328
Cdd:PRK14703 249 LDHLGPWPPrPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 329 DFSMLEHCLRQDLKASVPSIMAVLDPLKVVITNYEAGETEWLPLAN-NSENAELGVREVPFSGTVYIERDDFMEEPAPGF 407
Cdd:PRK14703 329 DIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYwPHDVPKEGSRKVPFTRELYIERDDFSEDPPKGF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 408 RRLVPGGEVRLKGAYIIKCNEVIKDAgTGAVRELRCTYDPLTKSGGAnSGRKVKGTLHWVSASHGIPAEVYLYEKLLEDn 487
Cdd:PRK14703 409 KRLTPGREVRLRGAYIIRCDEVVRDA-DGAVTELRCTYDPESAKGED-TGRKAAGVIHWVSAKHALPAEVRLYDRLFKV- 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 806915762 488 EGPKAEGETWEEYINPDSIRLmLSCLLEPFAAGAKPEDKFQFMRQGYFCVDNKLSREDRLVFNRIVPLKDTW 559
Cdd:PRK14703 486 PQPEAADEDFLEFLNPDSLRV-AQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTW 556
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
35-559 |
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: 634.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 35 TRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEHIYYGSDYSEQIYN 114
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 115 SALNLIRKGKAYVCDLSPEEVTAYRGTLTEPGKNSPYRERSVEENLRLFSGMREGAYPTGSRVLRAKIDMSSPNINLRDP 194
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 195 VIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEEAPRQREFGRVNLTGVVT 274
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 275 GKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQTMVDFSMLEHCLRQDLKASVPSIMAVLDP 354
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 355 LKVVITNYEaGETEWLPLANNSENAELGVREVPFSGTVYIERDDFMEEPAPGFRRLVPGGEVRLKGAYIIKCNEVIKDAg 434
Cdd:TIGR00440 323 VEVVIENLS-DEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 435 TGAVRELRCTYDPLTKSGGANSGRKVKGTLHWVSASHGIPAEVYLYEKLLEdNEGPKAEgETWEEYINPDSIRLMLScLL 514
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFK-VPNPGAP-DDFLSVINPESLVIKQG-FM 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 806915762 515 EPFAAGAKPEDKFQFMRQGYFCVDNKLSREDRLVFNRIVPLKDTW 559
Cdd:TIGR00440 478 EHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
35-563 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 529.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 35 TRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEhIYYGSDYSEQIYN 114
Cdd:PLN02859 267 TRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFK-ITYTSDYFQELYE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 115 SALNLIRKGKAYVCDLSPEEVTAYRgtltEPGKNSPYRERSVEENLRLFSGMREGAYPTGSRVLRAKIDMSSPNINLRDP 194
Cdd:PLN02859 346 LAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYDL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 195 VIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEEaPRQREFGRVNLTGVVT 274
Cdd:PLN02859 422 IAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLYQ-PYVWEYSRLNVTNTVM 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 275 GKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQ-TMVDFSMLEHCLRQDLKASVPSIMAVLD 353
Cdd:PLN02859 501 SKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDnSLIRMDRLEHHIREELNKTAPRTMVVLH 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 354 PLKVVITNYEAGETEWL-----PLANNSENAELgvREVPFSGTVYIERDDFMEEPAPGFRRLVPGGEVRLKGAYIIKCNE 428
Cdd:PLN02859 581 PLKVVITNLESGEVIELdakrwPDAQNDDPSAF--YKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKCTD 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 429 VIKDAGTGAVRELRCTYDPLTKSggansgrKVKGTLHWVS-ASHG---IPAEVYLYEKLLEdNEGPkAEGETWEEYINPD 504
Cdd:PLN02859 659 VVLADDNETVVEIRAEYDPEKKT-------KPKGVLHWVAePSPGvepLKVEVRLFDKLFL-SENP-AELEDWLEDLNPQ 729
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 505 SIRLMLSCLLEPFAAGAKPEDKFQFMRQGYFCVDnKLSREDRLVFNRIVPLKDTW-KSGK 563
Cdd:PLN02859 730 SKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYgKGGK 788
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
36-557 |
1.20e-138 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 413.99 E-value: 1.20e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 36 RFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPgEHIYYGSDYSEQIYNS 115
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKP-DWVTFSSDYFDQLHEF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 116 ALNLIRKGKAYVCDLSPEEVTAYRgtltEPGKNSPYRERSVEENLRLFSGMREGAYPTGSRVLRAKIDMSSPNINLRDPV 195
Cdd:PTZ00437 134 AVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 196 IYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEEaPRQREFGRVNLTGVVTG 275
Cdd:PTZ00437 210 AYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWR-PHVWEFSRLNVTGSLLS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 276 KRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQTMVDFSMLEHCLRQDLKASVPSIMAVLDPL 355
Cdd:PTZ00437 289 KRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 356 KVVITNYEaGETEWLPLaNNSENAELGVREVPFSGTVYIERDDF-MEEPAPGFRRLVPGGE-VRLKGAYIIKCNEV-IKD 432
Cdd:PTZ00437 369 KVVVDNWK-GEREFECP-NHPRKPELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPGPRvVGLKYSGNVVCKGFeVDA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 433 AGTGAVRELRCTYDPLTKSggansgrkvKGTLHWVSASHGIPAEVYLYEKLLEDNEGpkAEGETWEEYINPDSiRLMLSC 512
Cdd:PTZ00437 447 AGQPSVIHVDIDFERKDKP---------KTNISWVSATACTPVEVRLYNALLKDDRA--AIDPEFLKFIDEDS-EVVSHG 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 806915762 513 LLEPFAAGAKPEDKFQFMRQGYFCVDNKlSREDRLVFNRIVPLKD 557
Cdd:PTZ00437 515 YAEKGIENAKHFESVQAERFGYFVVDPD-TRPDHLVMNRVLGLRE 558
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
32-346 |
6.50e-120 |
|
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: 353.48 E-value: 6.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 32 EICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGeHIYYGSDYSEQ 111
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 112 IYNSALNLIRKGKAYVcdlspeevtayrgtltepgknspyrersveenlrlfsgmregayptgsrvlrakidmsspninl 191
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 192 rdpviyriihaeHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEeAPRQREFGRVNLTG 271
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806915762 272 VVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQTMVDFSMLEHCLRQDLKASVP 346
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAP 237
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
32-326 |
3.31e-119 |
|
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: 354.70 E-value: 3.31e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 32 EICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEHIYYGSDYSEQ 111
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 112 IYNSALNLIRKGKAYVCDLSPEEVTAYRGTLtePGKNSPYRERSVEENLRLFS-GMREGAYPTGSRVLRAKIDMSSPnIN 190
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 191 LRDPVIYRII---HAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEEAPRQREFGRV 267
Cdd:pfam00749 158 FRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 806915762 268 NLTGVVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQT 326
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFD 296
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
29-473 |
1.29e-114 |
|
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: 348.32 E-value: 1.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 29 YSREICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEHIYYGSDY 108
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 109 SEQIYNSALNLIRKGKAYVCDLSPEEVTAYRGTLTEPGKNSPY----RERSVEENLRLfsgMREGAyptgSRVLRAKI-- 182
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEELERM---LAAGE----PPVLRFKIpe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 183 ------DMSS-----PNINLRDPVIYRiihaehyRTGnawciYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLE 251
Cdd:COG0008 154 egvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 252 ELGIeEAPrqrEFGRVNLT----GVVTGKRYlralvagNYVdgwddprlpTLRGLRRRGFTPESIRSFVREIG--MVRNQ 325
Cdd:COG0008 222 ALGW-EPP---EFAHLPLIlgpdGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGwsKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 326 TMVDFSMLEHCLrqDLKAsVPSIMAVLDPLKVVITNY--------------------EAGETEWL----PLANnsENAEL 381
Cdd:COG0008 282 EIFSLEELIEAF--DLDR-VSRSPAVFDPVKLVWLNGpyiralddeelaellapelpEAGIREDLerlvPLVR--ERAKT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 382 GVREVPFSGTVYIERDDfmEEPAPGfrRLVPgGEVRlkgayiikcnEVIKDAgTGAVRELRcTYDPLTksggansgrkVK 461
Cdd:COG0008 357 LSELAELARFFFIERED--EKAAKK--RLAP-EEVR----------KVLKAA-LEVLEAVE-TWDPET----------VK 409
|
490
....*....|..
gi 806915762 462 GTLHWVSASHGI 473
Cdd:COG0008 410 GTIHWVSAEAGV 421
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
32-549 |
1.60e-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: 322.93 E-value: 1.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 32 EICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEhIYYGSDYSEQ 111
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDE-VVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 112 IYNSALNLIRKGKAYVCDLSPEEVTAYRGTltepGKNSPYRERSVEENLRLFSGMREGAYPTGSRVLRAKIDMSSPNINL 191
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 192 RDPVIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIeEAPRQREFGRV--NL 269
Cdd:TIGR00463 248 RDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGW-EPPEFIHWGRLkiDD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 270 TGVVTGKRYLRALVAGNYVdGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQTMVDFSMLEHCLRQDLKASVPSIM 349
Cdd:TIGR00463 327 VRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYF 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 350 AVLDPLKVVITNYEAGETEWLPLanNSENAELGVREVPFSGTVYIERDDFMEEPAPgfrrlvpggeVRLkgayiikcnev 429
Cdd:TIGR00463 406 FIWNPVKIEIVGLPEPKRVERPL--HPDHPEIGERVLILRGEIYVPKDDLEEGVEP----------VRL----------- 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 430 iKDAGTGAVRELRCTYDPLTKSGGANSGRKVkgtLHWVSASHGIPAEVylyekLLEDNEgpKAEGetweeyinpdsirlm 509
Cdd:TIGR00463 463 -MDAVNVIYSKKELRYHSEGLEGARKLGKSI---IHWLPAKDAVKVKV-----IMPDAS--IVEG--------------- 516
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 806915762 510 lscLLEPFAAGAKPEDKFQFMRQGYFCVDNKlsREDRLVF 549
Cdd:TIGR00463 517 ---VIEADASELEVGDVVQFERFGFARLDSA--DKDGMVF 551
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
35-549 |
6.68e-101 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 316.41 E-value: 6.68e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 35 TRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPL--KEDMEYVKAIIQDIEWLGCSPGEhIYYGSDYSEQI 112
Cdd:PRK04156 104 MRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDE-VVIQSDRLEIY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 113 YNSALNLIRKGKAYVCDLSPEEVTAYRgtltEPGKNSPYRERSVEENLRLFSGMREGAYPTGSRVLRAKIDMSSPNINLR 192
Cdd:PRK04156 183 YEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 193 DPVIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHslcSLEFKDH-------RPLYE---WvleelgieEAPRQR 262
Cdd:PRK04156 259 DWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTH---VLRGKDHidntekqRYIYDyfgW--------EYPETI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 263 EFGRVNLTGVVTGKRYLRALV-AGNYvDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMvrNQTMVDFSM--LEHCLRQ 339
Cdd:PRK04156 328 HYGRLKIEGFVLSTSKIRKGIeEGEY-SGWDDPRLPTLRALRRRGILPEAIRELIIEVGV--KETDATISWenLYAINRK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 340 DLKASVPSIMAVLDPLKVVITNYEAGETEwLPLANNSEnaELGVREVPFSGTVYIERDDFMEEpapgfrrlvpGGEVRLK 419
Cdd:PRK04156 405 LIDPIANRYFFVRDPVELEIEGAEPLEAK-IPLHPDRP--ERGEREIPVGGKVYVSSDDLEAE----------GKMVRLM 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 420 GAyiikCNEVIKDAGTGAVRELRCTYDpLTKSGGANsgrkvkgTLHWVSASHGIPAEVylyekllednegpkaegetwee 499
Cdd:PRK04156 472 DL----FNVEITGVSVDKARYHSDDLE-EARKNKAP-------IIQWVPEDESVPVRV---------------------- 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 806915762 500 yINPDSIRLMLscLLEPFAAGAKPEDKFQFMRQGYFCVDNKLSREDRLVF 549
Cdd:PRK04156 518 -LKPDGGDIEG--LAEPDVADLEVDDIVQFERFGFVRIDSVEDDEVVAYF 564
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
32-538 |
3.65e-91 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 295.09 E-value: 3.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 32 EICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPgEHIYYGSDYSEQ 111
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKY-DAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 112 IYNSALNLIRKGKAYVCDLSPEEVTAYRGTLTEpgknSPYRERSVEENLRLFSGMREGAYPTGSRVLRAKIDMSSPNINL 191
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKERMDGIE----SKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 192 RDPVIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEEApRQREFGRVNLTG 271
Cdd:PLN02907 368 RDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKV-HIWEFSRLNFVY 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 272 VVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQTMVDFSMLEHCLRQDLKASVPSIMAV 351
Cdd:PLN02907 447 TLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 352 LDPLKVVITNYEAGET-EWLPLANNSENAELGVREVPFSGTVYIERDDfmeepapgFRRLVPGGEVRLK--GAYIIKcnE 428
Cdd:PLN02907 527 LKEGRVLLTLTDGPETpFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD--------AEAISEGEEVTLMdwGNAIIK--E 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 429 VIKDAGtGAVRELRCTYDPltksggANSGRKVKGTLHWVSA-SHGIPAEV----YLY-EKLLEdnegpkaEGETWEEYIN 502
Cdd:PLN02907 597 ITKDEG-GAVTALSGELHL------EGSVKTTKLKLTWLPDtNELVPLSLvefdYLItKKKLE-------EDDNFLDVLN 662
|
490 500 510
....*....|....*....|....*....|....*.
gi 806915762 503 PDSiRLMLSCLLEPFAAGAKPEDKFQFMRQGYFCVD 538
Cdd:PLN02907 663 PCT-KKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
5-544 |
9.16e-88 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 283.01 E-value: 9.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 5 NAMETAAAENY-MDKLIKEDIESGiysrEICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEY 83
Cdd:PTZ00402 28 NTYFTAANANEeNDKLQLTNAEEG----KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 84 VKAIIQDIEWLGCSPGEHIYYGSDYSEQIYNSALNLIRKGKAYvCDLSP-EEVTAYRGTltepGKNSPYRERSVEENLRL 162
Cdd:PTZ00402 104 EQAILDDLATLGVSWDVGPTYSSDYMDLMYEKAEELIKKGLAY-CDKTPrEEMQKCRFD----GVPTKYRDISVEETKRL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 163 FSGMREGAYPTGSRVLRAKIDMSSPNINLRDPVIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDH 242
Cdd:PTZ00402 179 WNEMKKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 243 RPLYEWVLEELGIEEaPRQREFGRVNLTGVVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMV 322
Cdd:PTZ00402 259 NDQYYWFCDALGIRK-PIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMS 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 323 RNQTMVDFSMLEHCLRQDLKASVPSIMAVLDPLKVVITNYEAGETEWLPLANNSENAELGVREVPFSGTVYIERDDFMee 402
Cdd:PTZ00402 338 KTVNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVA-- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 403 papgfrRLVPGGEVRLkgayIIKCNEVIKDAGTGAVRELRCTYDPLTKSGGanSGRKVKGTLHWVSAS-HGIPAEVYLYE 481
Cdd:PTZ00402 416 ------LLKEGDEVTL----MDWGNAYIKNIRRSGEDALITDADIVLHLEG--DVKKTKFKLTWVPESpKAEVMELNEYD 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806915762 482 KLLEDNEgPKAEgETWEEYINPDSiRLMLSCLLEPFAAGAKPEDKFQFMRQGYFCVDNKLSRE 544
Cdd:PTZ00402 484 HLLTKKK-PDPE-ESIDDIIAPVT-KYTQEVYGEEALSVLKKGDIIQLERRGYYIVDDVTPKK 543
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
24-554 |
3.61e-87 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 279.20 E-value: 3.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 24 IESGIYSReICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPgEHIY 103
Cdd:PLN03233 4 LEGAIAGQ-IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKP-DSVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 104 YGSDYSEQIYNSALNLIRKGKAYVCDLSPEEVTAYRGTLTEpgknSPYRERSVEENLRLFSGMREGAYPTGSRVLRAKID 183
Cdd:PLN03233 82 FTSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKID 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 184 MSSPNINLRDPVIYRIIHAEHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEEaPRQRE 263
Cdd:PLN03233 158 MQSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRR-PRIHA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 264 FGRVNLTGVVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMVRNQTMVDFSMLEHCLRQDLKA 343
Cdd:PLN03233 237 FARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 344 SVPSIMAV--LDPLKVVITNYEAG------ETEWLPlannsENAELGVREVPFSGTVYIERDDFmeepapgfRRLVPGGE 415
Cdd:PLN03233 317 RAKRFMAIdkADHTALTVTNADEEadfafsETDCHP-----KDPGFGKRAMRICDEVLLEKADT--------EDIQLGED 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 416 VRLKGAYIIKcnevikdagtgavrelrctydpLTKSGGANSGRKV--------KGTLHWVS-ASHGIPAEVYLYEKLLED 486
Cdd:PLN03233 384 IVLLRWGVIE----------------------ISKIDGDLEGHFIpdgdfkaaKKKISWIAdVSDNIPVVLSEFDNLIIK 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806915762 487 NEgpKAEGETWEEYINPDSIRlMLSCLLEPFAAGAKPEDKFQFMRQGYFCVDNKLSREDRLVFNRIVP 554
Cdd:PLN03233 442 EK--LEEDDKFEDFINPDTLA-ETDVIGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPLILFMIP 506
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
346-538 |
1.35e-66 |
|
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: 213.67 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 346 PSIMAVLDPLKVVITNYEAGETEWLPLANNSENAELGVREVPFSGTVYIERDDfmeepapgFRRLVPGGEVRLKGAYIIK 425
Cdd:pfam03950 2 PRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIERED--------FKRLAPGEEVRLMDAYNIK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 426 CNEVIKDAgTGAVRELRCTYDPLTKSGgansGRKVKG-TLHWVSASHGIPAEVYLYEKLLEDNEGpkaegetWEEYINPD 504
Cdd:pfam03950 74 VTEVVKDE-DGNVTELHCTYDGDDLGG----ARKVKGkIIHWVSASDAVPAEVRLYDRLFKDEDD-------ADFLLNPD 141
|
170 180 190
....*....|....*....|....*....|....
gi 806915762 505 SIRLMLSCLLEPFAAGAKPEDKFQFMRQGYFCVD 538
Cdd:pfam03950 142 SLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
35-334 |
2.33e-52 |
|
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: 178.43 E-value: 2.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 35 TRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEHIYYGSDYSEQIYN 114
Cdd:cd00418 4 TRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLYRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 115 SALNLIRKGkayvcdlspeevtayrgtltepgknspyrersveenlrlfsgmregayptgsrvlrakidmsspninlrdp 194
Cdd:cd00418 84 YAEELIKKG----------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 195 viyriihaehyrtgnawcIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIeEAPRQREFGRVNL-TGVV 273
Cdd:cd00418 93 ------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGW-EPPRFYHFPRLLLeDGTK 153
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806915762 274 TGKRYLRalvagnyvdgwddprlPTLRGLRRRGFTPESIRSFVREIGMVRNQTMVDFSMLE 334
Cdd:cd00418 154 LSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEE 198
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
32-332 |
3.11e-46 |
|
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: 162.52 E-value: 3.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 32 EICTRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNP--LKEDMEYVKAIIQDIEWLGCSPGEhIYYGSDYS 109
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDE-VVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 110 EQIYNSALNLIRKGKAYVcdlspeevtayrgtltepgknspyrersveenlrlfsgmregayptgsrvlrakidmsspni 189
Cdd:cd09287 80 ELYYEYARKLIEMGGAYV-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 190 nlrdpviyriihaeHYRTGNAWCIYPMYDFAHPIQDAIEGITHSLCSLEFKDHRPLYEWVLEELGIEEaPRQREFGRVNL 269
Cdd:cd09287 98 --------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEY-PETIHWGRLKI 162
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806915762 270 TGVVTGKRYLRALVAGNYVDGWDDPRLPTLRGLRRRGFTPESIRSFVREIGMvrNQTMVDFSM 332
Cdd:cd09287 163 EGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGV--KQTDATISW 223
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
35-123 |
1.38e-16 |
|
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: 79.17 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 35 TRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEHIYYGSDY-----S 109
Cdd:cd00808 4 TRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYgpyrqS 83
|
90
....*....|....*..
gi 806915762 110 E--QIYNSALN-LIRKG 123
Cdd:cd00808 84 ErlEIYRKYAEkLLEKG 100
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
35-128 |
2.13e-15 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 76.81 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 35 TRFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCSPGEHIYYGSDYSEqIYN 114
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD-AYR 86
|
90
....*....|....*
gi 806915762 115 SALN-LIRKGKAYVC 128
Cdd:PRK05710 87 AALDrLRAQGLVYPC 101
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
36-234 |
3.31e-13 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 72.08 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 36 RFPPEPNGYLHIGSAFAIHTNYGLAHKYGGTFHLRFDDTNPLKEDMEYVKAIIQDIEWLGCS-------PGEH-IYYGSD 107
Cdd:PLN02627 49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDwdegpdvGGEYgPYRQSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806915762 108 YSEQIYNSALNLIRKGKAYVCDLSPEEVTAYRGTLTEPGKNSPYRER----SVEEnlrLFSGMREG-AY------PTGSR 176
Cdd:PLN02627 129 RNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKwataSDEE---VQAELAKGtPYtyrfrvPKEGS 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 806915762 177 VlraKID-----MSSPNIN-LRDPVIYRiihaehyrtGNAwciYPMYDFAHPIQDAIEGITHSL 234
Cdd:PLN02627 206 V---KIDdlirgEVSWNTDtLGDFVLLR---------SNG---QPVYNFCVAVDDATMGITHVI 254
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
217-269 |
3.74e-06 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 46.70 E-value: 3.74e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 806915762 217 YDFAHPIQDAIEGITH---SLCSLEFKDHRPLYEWVLEELGIEEAPRQREFGRVNL 269
Cdd:cd00802 78 YMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLTFGRVMG 133
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
35-94 |
6.85e-06 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 45.93 E-value: 6.85e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806915762 35 TRFPPEPNGYLHIGSAFAIHTNYGLAH-----KYGGTFHLRFDDTNPLKEDM-------------EYVKAIIQDIEWL 94
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQayrklGYKVRCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM 79
|
|
| |
