|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-545 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1057.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 1 MSEPISNNFIHNFIDKDLEDGVYKEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAI 80
Cdd:PRK05347 5 EAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 81 EEDIKWLGFKWEKKL-WASSYFETMYDAAVALIKKGKAFVDDLTAEQIKEYRGTLKEPGKESPYRNRSVEENLALFEDMR 159
Cdd:PRK05347 85 KEDVRWLGFDWSGELrYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERMR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 160 AGKFADGEKVLRAKIDMSSPNINMRDPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYN 239
Cdd:PRK05347 165 AGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 240 WVLDEVGFwENPPRQIEFARLNLTGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANS 319
Cdd:PRK05347 245 WVLDNLPI-PPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 320 TVESSLLEHCVREDLQDKVESRNVVEDPIKVVITNYPEDKTEMVEVENNKNVPEMGMREIPFSNELYVDGEDFMEVPAKK 399
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 400 YFRLFPGNEVRFKGAYFIKCEEVIKNEDGSIKELHCTYDPATRSGLDFTERKVKGTIHFVDAKTAVQIKIREYDQLLIE- 478
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVp 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 908720483 479 ----DENGNLVPNEASKVEKIAYAEPALAEAKAGERFQFFRHGYYIADsKLNTEDEKVFNKIVGLKSSYKP 545
Cdd:PRK05347 484 npaaGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
26-543 |
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: 655.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 26 VYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKL-WASSYFETM 104
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIrYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 105 YDAAVALIKKGKAFVDDLTAEQIKEYRGTLKEPGKESPYRNRSVEENLALFEDMRAGKFADGEKVLRAKIDMSSPNINMR 184
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 185 DPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFwENPPRQIEFARLNLTG 264
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHI-FPRPAQYEFSRLNLEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 265 TVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEHCVREDLQDKVESRNVV 344
Cdd:TIGR00440 240 TVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 345 EDPIKVVITNYpEDKTEMVEVENNKNVPEMGMREIPFSNELYVDGEDFMEVPAKKYFRLFPGNEVRFKGAYFIKCEEVIK 424
Cdd:TIGR00440 320 IDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 425 NEDGSIKELHCTYDPATRSGLDFTERKVKGTIHFVDAKTAVQIKIREYDQLLIEDENGNL-----VPNEASKVEKIAYAE 499
Cdd:TIGR00440 399 DAAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPddflsVINPESLVIKQGFME 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 908720483 500 PALAEAKAGERFQFFRHGYYIADSKLNTEDEKVFNKIVGLKSSY 543
Cdd:TIGR00440 479 HSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
25-337 |
1.30e-139 |
|
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: 403.17 E-value: 1.30e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 25 EVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKLWASSYFETM 104
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 105 YDAAVALIKKGKAFVddltaeqikeyrgtlkepgkespyrnrsveenlalfedmragkfadgekvlrakidmsspninmr 184
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 185 dpviyriahvtHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFweNPPRQIEFARLNLTG 264
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRL--YRPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 908720483 265 TVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEHCVREDLQDK 337
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPT 235
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
25-336 |
2.75e-138 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 402.85 E-value: 2.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 25 EVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKL-WASSYFET 103
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPyYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 104 MYDAAVALIKKGKAFVDDLTAEQIKEYRGTLkePGKESPYRNRSVEENLALF-EDMRAGKFADGEKVLRAKIDMSSPnIN 182
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 183 MRDPVIYRIA---HVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGfWENPPRQIEFAR 259
Cdd:pfam00749 158 FRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-WEPPPFIHEYLR 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 908720483 260 LNLTGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKA-NSTVESSLLEHCVREDLQD 336
Cdd:pfam00749 237 LNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
24-521 |
1.29e-127 |
|
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: 381.06 E-value: 1.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 24 KEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKW-EKKLWASSYFE 102
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 103 TMYDAAVALIKKGKAFVDDLTAEQIKEYRGTLKEPGKESPY----RNRSVEEnlalfedmRAGKFADGEK-VLRAKI--- 174
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE--------LERMLAAGEPpVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 175 -----DMSS-----PNINMRDPVIYRiahvthhntGDKwciYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDE 244
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 245 VGfWENPprqiEFARLNLT----GTVMSKRllkglvdDGVVegwddprmpTIAGLRRRGYTPEAIRDFCERIGVAKANST 320
Cdd:COG0008 223 LG-WEPP----EFAHLPLIlgpdGTKLSKR-------KGAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 321 VESSL--LEHCVreDLqDKVESRNVVEDPIKVVITNYP-------EDKTEMVEVEN-NKNVPEMGMREIPFSNE------ 384
Cdd:COG0008 282 EIFSLeeLIEAF--DL-DRVSRSPAVFDPVKLVWLNGPyiralddEELAELLAPELpEAGIREDLERLVPLVREraktls 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 385 --------LYVDGEDfmEVPAKKyfRLFPgNEVRFkgayFIKCE-EVIKNEDgsikelhcTYDPATrsgldfterkVKGT 455
Cdd:COG0008 359 elaelarfFFIERED--EKAAKK--RLAP-EEVRK----VLKAAlEVLEAVE--------TWDPET----------VKGT 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 908720483 456 IHFVDAKTavQIKIREYDQLLIEDENGnlvpneaskvekiAYAEPAL---AEAKAGERFqFFRHGYYIA 521
Cdd:COG0008 412 IHWVSAEA--GVKDGLLFMPLRVALTG-------------RTVEPSLfdvLELLGKERV-FERLGYAID 464
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-545 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1057.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 1 MSEPISNNFIHNFIDKDLEDGVYKEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAI 80
Cdd:PRK05347 5 EAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 81 EEDIKWLGFKWEKKL-WASSYFETMYDAAVALIKKGKAFVDDLTAEQIKEYRGTLKEPGKESPYRNRSVEENLALFEDMR 159
Cdd:PRK05347 85 KEDVRWLGFDWSGELrYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERMR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 160 AGKFADGEKVLRAKIDMSSPNINMRDPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYN 239
Cdd:PRK05347 165 AGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 240 WVLDEVGFwENPPRQIEFARLNLTGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANS 319
Cdd:PRK05347 245 WVLDNLPI-PPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 320 TVESSLLEHCVREDLQDKVESRNVVEDPIKVVITNYPEDKTEMVEVENNKNVPEMGMREIPFSNELYVDGEDFMEVPAKK 399
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 400 YFRLFPGNEVRFKGAYFIKCEEVIKNEDGSIKELHCTYDPATRSGLDFTERKVKGTIHFVDAKTAVQIKIREYDQLLIE- 478
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVp 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 908720483 479 ----DENGNLVPNEASKVEKIAYAEPALAEAKAGERFQFFRHGYYIADsKLNTEDEKVFNKIVGLKSSYKP 545
Cdd:PRK05347 484 npaaGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
6-547 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 775.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 6 SNNFIHNFIDKDLEDGVYKEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIK 85
Cdd:PRK14703 12 SPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 86 WLGFKWEKKL-WASSYFETMYDAAVALIKKGKAFVDDLTAEQIKEYRGTLKEPGKESPYRNRSVEENLALFEDMRAGKFA 164
Cdd:PRK14703 92 WLGFDWGEHLyYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 165 DGEKVLRAKIDMSSPNINMRDPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDE 244
Cdd:PRK14703 172 DGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 245 VGFWENPPRQIEFARLNLTGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESS 324
Cdd:PRK14703 252 LGPWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 325 LLEHCVREDLQDKVESRNVVEDPIKVVITNYPEDKTEMVEVEN-NKNVPEMGMREIPFSNELYVDGEDFMEVPAKKYFRL 403
Cdd:PRK14703 332 VLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYwPHDVPKEGSRKVPFTRELYIERDDFSEDPPKGFKRL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 404 FPGNEVRFKGAYFIKCEEVIKNEDGSIKELHCTYDPATRSGLDfTERKVKGTIHFVDAKTAVQIKIREYDQLL------I 477
Cdd:PRK14703 412 TPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGED-TGRKAAGVIHWVSAKHALPAEVRLYDRLFkvpqpeA 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 478 EDENGNLVPNEASKVEKIAYAEPALAEAKAGERFQFFRHGYYIADSKLNTEDEKVFNKIVGLKSSYKPNK 547
Cdd:PRK14703 491 ADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
26-543 |
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: 655.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 26 VYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKL-WASSYFETM 104
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIrYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 105 YDAAVALIKKGKAFVDDLTAEQIKEYRGTLKEPGKESPYRNRSVEENLALFEDMRAGKFADGEKVLRAKIDMSSPNINMR 184
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 185 DPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFwENPPRQIEFARLNLTG 264
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHI-FPRPAQYEFSRLNLEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 265 TVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEHCVREDLQDKVESRNVV 344
Cdd:TIGR00440 240 TVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 345 EDPIKVVITNYpEDKTEMVEVENNKNVPEMGMREIPFSNELYVDGEDFMEVPAKKYFRLFPGNEVRFKGAYFIKCEEVIK 424
Cdd:TIGR00440 320 IDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 425 NEDGSIKELHCTYDPATRSGLDFTERKVKGTIHFVDAKTAVQIKIREYDQLLIEDENGNL-----VPNEASKVEKIAYAE 499
Cdd:TIGR00440 399 DAAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPddflsVINPESLVIKQGFME 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 908720483 500 PALAEAKAGERFQFFRHGYYIADSKLNTEDEKVFNKIVGLKSSY 543
Cdd:TIGR00440 479 HSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
26-545 |
9.87e-179 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 523.17 E-value: 9.87e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 26 VYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKLWASSYFETMY 105
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELY 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 106 DAAVALIKKGKAFVDDLTAEQIKEYRgtlkEPGKESPYRNRSVEENLALFEDMRAGKFADGEKVLRAKIDMSSPNINMRD 185
Cdd:PLN02859 345 ELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYD 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 186 PVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFWEnpPRQIEFARLNLTGT 265
Cdd:PLN02859 421 LIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLYQ--PYVWEYSRLNVTNT 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 266 VMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKA-NSTVESSLLEHCVREDLqDKVESRN-V 343
Cdd:PLN02859 499 VMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdNSLIRMDRLEHHIREEL-NKTAPRTmV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 344 VEDPIKVVITNYPEDKTEMVEVE---NNKNVPEMGMREIPFSNELYVDGEDFMEVPAKKYFRLFPGNEVRFKGAYFIKCE 420
Cdd:PLN02859 578 VLHPLKVVITNLESGEVIELDAKrwpDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKCT 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 421 EVIKNED-GSIKELHCTYDPATRSgldfterKVKGTIHFVDA----KTAVQIKIREYDQL-------LIEDENGNLVPNe 488
Cdd:PLN02859 658 DVVLADDnETVVEIRAEYDPEKKT-------KPKGVLHWVAEpspgVEPLKVEVRLFDKLflsenpaELEDWLEDLNPQ- 729
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 908720483 489 aSK-VEKIAYAEPALAEAKAGERFQFFRHGYYIADsKLNTEDEKVFNKIVGLKSSYKP 545
Cdd:PLN02859 730 -SKeVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
27-540 |
2.08e-162 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 474.09 E-value: 2.08e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 27 YTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKLWASSYFETMYD 106
Cdd:PTZ00437 53 YFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 107 AAVALIKKGKAFVDDLTAEQIKEYRgtlkEPGKESPYRNRSVEENLALFEDMRAGKFADGEKVLRAKIDMSSPNINMRDP 186
Cdd:PTZ00437 133 FAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 187 VIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFWEnpPRQIEFARLNLTGTV 266
Cdd:PTZ00437 209 IAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWR--PHVWEFSRLNVTGSL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 267 MSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEHCVREDLQDKVESRNVVED 346
Cdd:PTZ00437 287 LSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVID 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 347 PIKVVITNYPEDKTemVEVENNKNVPEMGMREIPFSNELYVDGEDF-MEVPAKKYFRLFPGNE-VRFKGAYFIKCEEVIK 424
Cdd:PTZ00437 367 PIKVVVDNWKGERE--FECPNHPRKPELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPGPRvVGLKYSGNVVCKGFEV 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 425 NEDGSIKELHCTydpatrsgLDFTER-KVKGTIHFVDAKTAVQIKIREYDQLLiEDENGNLVP------NEASKVEKIAY 497
Cdd:PTZ00437 445 DAAGQPSVIHVD--------IDFERKdKPKTNISWVSATACTPVEVRLYNALL-KDDRAAIDPeflkfiDEDSEVVSHGY 515
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 908720483 498 AEPALAEAKAGERFQFFRHGYYIADSKlNTEDEKVFNKIVGLK 540
Cdd:PTZ00437 516 AEKGIENAKHFESVQAERFGYFVVDPD-TRPDHLVMNRVLGLR 557
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
25-337 |
1.30e-139 |
|
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: 403.17 E-value: 1.30e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 25 EVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKLWASSYFETM 104
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 105 YDAAVALIKKGKAFVddltaeqikeyrgtlkepgkespyrnrsveenlalfedmragkfadgekvlrakidmsspninmr 184
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 185 dpviyriahvtHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFweNPPRQIEFARLNLTG 264
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRL--YRPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 908720483 265 TVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEHCVREDLQDK 337
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPT 235
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
25-336 |
2.75e-138 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 402.85 E-value: 2.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 25 EVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKL-WASSYFET 103
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPyYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 104 MYDAAVALIKKGKAFVDDLTAEQIKEYRGTLkePGKESPYRNRSVEENLALF-EDMRAGKFADGEKVLRAKIDMSSPnIN 182
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 183 MRDPVIYRIA---HVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGfWENPPRQIEFAR 259
Cdd:pfam00749 158 FRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-WEPPPFIHEYLR 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 908720483 260 LNLTGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKA-NSTVESSLLEHCVREDLQD 336
Cdd:pfam00749 237 LNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
24-521 |
1.29e-127 |
|
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: 381.06 E-value: 1.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 24 KEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKW-EKKLWASSYFE 102
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 103 TMYDAAVALIKKGKAFVDDLTAEQIKEYRGTLKEPGKESPY----RNRSVEEnlalfedmRAGKFADGEK-VLRAKI--- 174
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE--------LERMLAAGEPpVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 175 -----DMSS-----PNINMRDPVIYRiahvthhntGDKwciYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDE 244
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 245 VGfWENPprqiEFARLNLT----GTVMSKRllkglvdDGVVegwddprmpTIAGLRRRGYTPEAIRDFCERIGVAKANST 320
Cdd:COG0008 223 LG-WEPP----EFAHLPLIlgpdGTKLSKR-------KGAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 321 VESSL--LEHCVreDLqDKVESRNVVEDPIKVVITNYP-------EDKTEMVEVEN-NKNVPEMGMREIPFSNE------ 384
Cdd:COG0008 282 EIFSLeeLIEAF--DL-DRVSRSPAVFDPVKLVWLNGPyiralddEELAELLAPELpEAGIREDLERLVPLVREraktls 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 385 --------LYVDGEDfmEVPAKKyfRLFPgNEVRFkgayFIKCE-EVIKNEDgsikelhcTYDPATrsgldfterkVKGT 455
Cdd:COG0008 359 elaelarfFFIERED--EKAAKK--RLAP-EEVRK----VLKAAlEVLEAVE--------TWDPET----------VKGT 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 908720483 456 IHFVDAKTavQIKIREYDQLLIEDENGnlvpneaskvekiAYAEPAL---AEAKAGERFqFFRHGYYIA 521
Cdd:COG0008 412 IHWVSAEA--GVKDGLLFMPLRVALTG-------------RTVEPSLfdvLELLGKERV-FERLGYAID 464
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
17-522 |
1.12e-112 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 350.95 E-value: 1.12e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 17 DLEDGVYKEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKLW 96
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTY 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 97 ASSYFETMYDAAVALIKKGKAFVDDLTAEQIKEYRGTlkepGKESPYRNRSVEENLALFEDMRAGKFADGEKVLRAKIDM 176
Cdd:PLN02907 285 TSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDM 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 177 SSPNINMRDPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFwenPPRQI- 255
Cdd:PLN02907 361 QDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGL---RKVHIw 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 256 EFARLNLTGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLeHCVREDLQ 335
Cdd:PLN02907 438 EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKL-WTINKKII 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 336 DKVESRNV-VEDPIKVVIT--NYPEdKTEMVEVENNKNVPEMGMREIPFSNELYVDGEDFMEVPAkkyfrlfpGNEVRFK 412
Cdd:PLN02907 517 DPVCPRHTaVLKEGRVLLTltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEAISE--------GEEVTLM 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 413 --GAYFIKceEVIKNEDGSIKELHCTYDPatrsgldftERKVKGT----IHFVDAKTAVQIKIREYDQL-----LIEDEN 481
Cdd:PLN02907 588 dwGNAIIK--EITKDEGGAVTALSGELHL---------EGSVKTTklklTWLPDTNELVPLSLVEFDYLitkkkLEEDDN 656
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 908720483 482 GNLVPNEASKVEKIAYAEPALAEAKAGERFQFFRHGYYIAD 522
Cdd:PLN02907 657 FLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
16-533 |
6.03e-112 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 344.53 E-value: 6.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 16 KDLEDGVYKEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPV--KEDVEYVDAIEEDIKWLGFKWEK 93
Cdd:PRK04156 92 PPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 94 KLWASSYFETMYDAAVALIKKGKAFVDDLTAEQIKEyrgtLKEPGKESPYRNRSVEENLALFEDMRAGKFADGEKVLRAK 173
Cdd:PRK04156 172 VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKE----LRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVK 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 174 IDMSSPNINMRDPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGfWEnPPR 253
Cdd:PRK04156 248 TDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFG-WE-YPE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 254 QIEFARLNLTGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLeHCVRED 333
Cdd:PRK04156 326 TIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENL-YAINRK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 334 LQDKVESRNV-VEDPIKVVITNYPEDKtemVEVENNKNVPEMGMREIPFSNELYVDGEDFMEVpakkyfrlfpGNEVRFK 412
Cdd:PRK04156 405 LIDPIANRYFfVRDPVELEIEGAEPLE---AKIPLHPDRPERGEREIPVGGKVYVSSDDLEAE----------GKMVRLM 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 413 GAYFIKCEEVIKNEdgsikelhctydpATRSGLDFTERKVKGT--IHFVDAKTAVQIKIREYDQlliEDENGnlvpneas 490
Cdd:PRK04156 472 DLFNVEITGVSVDK-------------ARYHSDDLEEARKNKApiIQWVPEDESVPVRVLKPDG---GDIEG-------- 527
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 908720483 491 kvekiaYAEPALAEAKAGERFQFFRHGYYIADSKLNTEDEKVF 533
Cdd:PRK04156 528 ------LAEPDVADLEVDDIVQFERFGFVRIDSVEDDEVVAYF 564
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
17-533 |
1.62e-110 |
|
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: 340.26 E-value: 1.62e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 17 DLEDGVYKEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKLW 96
Cdd:TIGR00463 85 ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 97 ASSYFETMYDAAVALIKKGKAFVDDLTAEQIKEyrgtLKEPGKESPYRNRSVEENLALFEDMRAGKFADGEKVLRAKIDM 176
Cdd:TIGR00463 165 QSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRE----LRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 177 SSPNINMRDPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRP-------LYNWVLDEVGFWe 249
Cdd:TIGR00463 241 KHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqeyiyrYFGWEPPEFIHW- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 250 npprqiEFARLNLTGTVMSKRLLKGLVdDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEHC 329
Cdd:TIGR00463 320 ------GRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYAL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 330 VREDLQDKVESRNVVEDPIKVVITNYPEDKTEMVEVenNKNVPEMGMREIPFSNELYVDGEDFMEVPakkyfrlfpgNEV 409
Cdd:TIGR00463 393 NRKIIDEEARRYFFIWNPVKIEIVGLPEPKRVERPL--HPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPV 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 410 RFKGAyfikCEEVIKNEDGSIKELhctydpatrsGLDFTERKVKGTIHFVDAKTAVQIKIREYDQLLIEDengnlvpnea 489
Cdd:TIGR00463 461 RLMDA----VNVIYSKKELRYHSE----------GLEGARKLGKSIIHWLPAKDAVKVKVIMPDASIVEG---------- 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 908720483 490 skvekiaYAEPALAEAKAGERFQFFRHGYYIADSKlnTEDEKVF 533
Cdd:TIGR00463 517 -------VIEADASELEVGDVVQFERFGFARLDSA--DKDGMVF 551
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
18-536 |
2.34e-100 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 315.36 E-value: 2.34e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 18 LEDGVYKEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWE-KKLW 96
Cdd:PTZ00402 45 LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDvGPTY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 97 ASSYFETMYDAAVALIKKGKAFVDDLTAEQIKEYRGTlkepGKESPYRNRSVEENLALFEDMRAGKFADGEKVLRAKIDM 176
Cdd:PTZ00402 125 SSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 177 SSPNINMRDPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFweNPPRQIE 256
Cdd:PTZ00402 201 DNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGI--RKPIVED 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 257 FARLNLTGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEHCVREDLQD 336
Cdd:PTZ00402 279 FSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 337 KVESRNVVEDPIKVVITNYPEDKTEMVEVENNKNVPEMGMREIPFSNELYVDGEDFMevpakkyfRLFPGNEVRFK--GA 414
Cdd:PTZ00402 359 SVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVA--------LLKEGDEVTLMdwGN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 415 YFIKceeVIK--NEDGSIKELHCTYDPatrsgldftERKVKGTIH----FVDAKTAVQIKIREYDQLLIE-----DENGN 483
Cdd:PTZ00402 431 AYIK---NIRrsGEDALITDADIVLHL---------EGDVKKTKFkltwVPESPKAEVMELNEYDHLLTKkkpdpEESID 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 908720483 484 LVPNEASKVEKIAYAEPALAEAKAGERFQFFRHGYYIADsklNTEDEKVFNKI 536
Cdd:PTZ00402 499 DIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVD---DVTPKKVLIAI 548
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
18-522 |
1.28e-85 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 274.96 E-value: 1.28e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 18 LEDGVYKEVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKKLWA 97
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 98 SSYFETMYDAAVALIKKGKAFVDDLTAEQIKEYRGTLkepgKESPYRNRSVEENLALFEDMRAGKFADGEKVLRAKIDMS 177
Cdd:PLN03233 84 SDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADR----AESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 178 SPNINMRDPVIYRIAHVTHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFweNPPRQIEF 257
Cdd:PLN03233 160 SDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGL--RRPRIHAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 258 ARLNLTGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEHCVREDLqDK 337
Cdd:PLN03233 238 ARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEI-DK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 338 VESRNVVEDP---IKVVITNYPEDKT-EMVEVENNKNVPEMGMREIPFSNELYVDGEDFMEVPAkkyfrlfpGNEVRFKG 413
Cdd:PLN03233 317 RAKRFMAIDKadhTALTVTNADEEADfAFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQL--------GEDIVLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 414 AYFIKCEEVikneDGSIkELHCTYDPatrsglDFTERKVKGTiHFVDAKTAVQIKIREYDQLLI-----EDENGNLVPNE 488
Cdd:PLN03233 389 WGVIEISKI----DGDL-EGHFIPDG------DFKAAKKKIS-WIADVSDNIPVVLSEFDNLIIkekleEDDKFEDFINP 456
|
490 500 510
....*....|....*....|....*....|....
gi 908720483 489 ASKVEKIAYAEPALAEAKAGERFQFFRHGYYIAD 522
Cdd:PLN03233 457 DTLAETDVIGDAGLKTLKEHDIIQLERRGFYRVD 490
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
26-345 |
3.09e-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: 198.85 E-value: 3.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 26 VYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKW-EKKLWASSYFETM 104
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWdEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 105 YDAAVALIKKGkafvddltaeqikeyrgtlkepgkespyrnrsveenlalfedmragkfadgekvlrakidmsspninmr 184
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 185 dpviyriahvthhntgdkwcIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGFweNPPRQIEFARLNL-T 263
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGW--EPPRFYHFPRLLLeD 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 264 GTVMSKRllkglvddgvvegwdDPRmPTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEHCVREDLQDKVESRNV 343
Cdd:cd00418 151 GTKLSKR---------------KLN-TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADAT 214
|
..
gi 908720483 344 VE 345
Cdd:cd00418 215 FD 216
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
344-522 |
5.76e-60 |
|
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: 195.95 E-value: 5.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 344 VEDPIKVVITNYPEDKTEMVEVENNKNVPEMGMREIPFSNELYVDGEDFmevpakkyFRLFPGNEVRFKGAYFIKCEEVI 423
Cdd:pfam03950 7 VLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNIKVTEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 424 KNEDGSIKELHCTYDPATRSGldftERKVKG-TIHFVDAKTAVQIKIREYDQLLIEDENGNLVPNEASKVEKI-AYAEPA 501
Cdd:pfam03950 79 KDEDGNVTELHCTYDGDDLGG----ARKVKGkIIHWVSASDAVPAEVRLYDRLFKDEDDADFLLNPDSLKVLTeGLAEPA 154
|
170 180
....*....|....*....|.
gi 908720483 502 LAEAKAGERFQFFRHGYYIAD 522
Cdd:pfam03950 155 LANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
25-321 |
1.44e-56 |
|
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: 189.48 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 25 EVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNP--VKEDVEYVDAIEEDIKWLGFKWEKKLWASSYFE 102
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 103 TMYDAAVALIKKGKAFVddltaeqikeyrgtlkepgkespyrnrsveenlalfedmragkfadgekvlrakidmsspnin 182
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 183 mrdpviyriahvtHHNTGDKWCIYPMYDFAHPIEDAIEGITHSLCSLEFEDHRPLYNWVLDEVGfWEnPPRQIEFARLNL 262
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFG-WE-YPETIHWGRLKI 162
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 908720483 263 TGTVMSKRLLKGLVDDGVVEGWDDPRMPTIAGLRRRGYTPEAIRDFCERIGVAKANSTV 321
Cdd:cd09287 163 EGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATI 221
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
25-328 |
2.97e-15 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 75.32 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 25 EVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWekklwassyfetm 104
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDW------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 105 yDAAVAlikkgkafvddltaeqikeyrgtlkEPGKESPYRNRSveenlalfedmRAGkfadgekvlrakidmsspninmr 184
Cdd:cd00808 68 -DEGPD-------------------------VGGPYGPYRQSE-----------RLE----------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 185 dpvIYRIAHVTHHNTGDKwciYPMYDFAHPIEDAIEGITHslcSLEFEDHRPlynwvldevgfweNPPRQI--------- 255
Cdd:cd00808 88 ---IYRKYAEKLLEKGDG---FPTYHLANVVDDHLMGITH---VIRGEEHLS-------------STPKQIllyealgwe 145
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 908720483 256 --EFARLNL----TGTVMSKRllkglvdDGVVegwddprmpTIAGLRRRGYTPEAIRDFCERIGVAKANSTVESSLLEH 328
Cdd:cd00808 146 ppKFAHLPLilnpDGKKLSKR-------KGDT---------SISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEEL 208
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
28-118 |
4.61e-10 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 61.02 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 28 TRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKWEKK-LWASSYFETmYD 106
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPvLYQSQRHDA-YR 86
|
90
....*....|...
gi 908720483 107 AAVA-LIKKGKAF 118
Cdd:PRK05710 87 AALDrLRAQGLVY 99
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
25-236 |
3.73e-09 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 59.37 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 25 EVYTRFPPEPNGYLHIGHAKAICVNFTTALKYNGKCNLRYDDTNPVKEDVEYVDAIEEDIKWLGFKW--------EKKLW 96
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWdegpdvggEYGPY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 97 ASSYFETMYDA-AVALIKKGKA---FVDDLTAEQIKE----------YRGTL-----------KEPGKESPYRNRSVEEN 151
Cdd:PLN02627 125 RQSERNAIYKQyAEKLLESGHVypcFCTDEELEAMKEeaelkklpprYTGKWatasdeevqaeLAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 152 LALFEDMRAGKFADGEKVLrakidmsspninmRDPVIYRIAHVthhntgdkwciyPMYDFAHPIEDAIEGITHSLCSlef 231
Cdd:PLN02627 205 SVKIDDLIRGEVSWNTDTL-------------GDFVLLRSNGQ------------PVYNFCVAVDDATMGITHVIRA--- 256
|
....*
gi 908720483 232 EDHRP 236
Cdd:PLN02627 257 EEHLP 261
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
28-95 |
3.71e-08 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 51.39 E-value: 3.71e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 908720483 28 TRFPPEPnGYLHIGHAKAICVNFTTAlkynGKCNLRYDDTNPVK------EDVEYVDAIEEDIKWLGFKWEKKL 95
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNR 70
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
28-271 |
4.57e-08 |
|
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: 52.10 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 28 TRFPPEPNGYLHIGHAKAICVNFTTA-----LKYNGKCNLRYDDTNPVKedveyvdaieedikwlgfkwekklwassyfe 102
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAqayrkLGYKVRCIALIDDAGGLI------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 103 tmYDAAVALIKKGKAFVDDLTAEQIKEYrgtlkepgkespyrnrsveenlalfedmragkfadgekvlrakidmsspnin 182
Cdd:cd00802 51 --GDPANKKGENAKAFVERWIERIKEDV---------------------------------------------------- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908720483 183 mrdpviyriahvthhntgdkwciypMYDFAHPIEDAIEGITH---SLCSLEFEDHRPLYNWVLDEVGfWENPPRQIEFAR 259
Cdd:cd00802 77 -------------------------EYMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAG-GPARPFGLTFGR 130
|
250
....*....|...
gi 908720483 260 LNLT-GTVMSKRL 271
Cdd:cd00802 131 VMGAdGTKMSKSK 143
|
|
| |
