|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-551 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1180.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 1 MDNKSLPPNFIRNIILEDIESGRVKEVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVES 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 81 IKEDVRWLGFEW-DKLFFASDYFDEMYNRAVILIKKGKAYVDDLSAEEIRQTRGTLTEPGKESPYRNRSVEENLDLFERM 159
Cdd:PRK05347 84 IKEDVRWLGFDWsGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 160 RKGEFKDGEKVLRAKIDMASPNINMRDPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLY 239
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 240 DWVIEECEMECRPRQYEFARLNLTNTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANS 319
Cdd:PRK05347 244 DWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 320 TVDLKMLEHFIREDLKLKAPRTMAVLRPLKVVITNYPEGQREMLEAENNAENPEMGHRLIPFSREIYIEQDDFMENPPSK 399
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 400 YFRLFPGNEVRLKHAYFIKCHDVIKDAEGRIVELHCTYDPATKSGSGFEGRKVKGTIHWVEATQALPAEFRLFEPLILDD 479
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752664608 480 TTGEDKPFLERINPNSLQVLQGYVEPNMAEARGQDKFQFFRHGYFNVDpKQTTGDKKVFNHIVSLKSSFQLP 551
Cdd:PRK05347 484 NPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-548 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 700.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 27 VVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWD-KLFFASDYFDEM 105
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 106 YNRAVILIKKGKAYVDDLSAEEIRQTRGTLTEPGKESPYRNRSVEENLDLFERMRKGEFKDGEKVLRAKIDMASPNINMR 185
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 186 DPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMECRPRQYEFARLNLTNT 265
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 266 VMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIREDLKLKAPRTMAVL 345
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 346 RPLKVVITNYpEGQREMLEAENNAENPEMGHRLIPFSREIYIEQDDFMENPPSKYFRLFPGNEVRLKHAYFIKCHDVIKD 425
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 426 AEGRIVELHCTYDPATKSGSGFEGRKVKGTIHWVEATQALPAEFRLFEPLILDDTTGEDKPFLERINPNSLQVLQGYVEP 505
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 752664608 506 NMAEARGQDKFQFFRHGYFNVDPKQTTGDKKVFNHIVSLKSSF 548
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
26-340 |
1.41e-147 |
|
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: 423.59 E-value: 1.41e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 26 EVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWDKLFFASDYFDEM 105
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 106 YNRAVILIKKGKAYVddlsaeeirqtrgtltepgkespyrnrsveenldlfermrkgefkdgekvlrakidmaspninmr 185
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 186 dpvlyriahasHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMECrPRQYEFARLNLTNT 265
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752664608 266 VMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIREDLKLKAPR 340
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
26-335 |
9.17e-134 |
|
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: 391.30 E-value: 9.17e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 26 EVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWD-KLFFASDYFDE 104
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 105 MYNRAVILIKKGKAYVDDLSAEEIRQTRGTLtePGKESPYRNRSVEENLDLF-ERMRKGEFKDGEKVLRAKIDMASPnIN 183
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 184 MRDPVLYRIAHAS---HHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMECRPRQYEFARL 260
Cdd:pfam00749 158 FRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752664608 261 NLTNTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDL-KMLEHFIREDLK 335
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLsKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-524 |
1.79e-130 |
|
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: 388.77 E-value: 1.79e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 25 KEVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWD-KLFFASDYFD 103
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDeGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 104 EMYNRAVILIKKGKAYVDDLSAEEIRQTRGTLTEPGKESPY----RNRSVEENldlfERMRkgefKDGEK-VLRAKI--- 175
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGEPpVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 176 -----DMAS-----PNINMRDPVLYRiAHAshhntgdkwciYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEE 245
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-ADG-----------YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 246 CEMEcRPrqyEFARLNLT----NTVMSKRwlKKLVdeaivdgwddprmpTISGLRRRGYTPEAIRAFAREIGVAKANSTV 321
Cdd:COG0008 223 LGWE-PP---EFAHLPLIlgpdGTKLSKR--KGAV--------------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 322 --DLKMLEHFIreDLKlKAPRTMAVLRPLKVVITNYPEGQreMLEAENNAE-----NPEMGH-----RLIPFSRE----- 384
Cdd:COG0008 283 ifSLEELIEAF--DLD-RVSRSPAVFDPVKLVWLNGPYIR--ALDDEELAEllapeLPEAGIredleRLVPLVREraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 385 ---------IYIEQDDfmENPPSKyfRLFPgNEVRLkhayFIKC-HDVIKDAEgrivelhcTYDPATksgsgfegrkVKG 454
Cdd:COG0008 358 selaelarfFFIERED--EKAAKK--RLAP-EEVRK----VLKAaLEVLEAVE--------TWDPET----------VKG 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752664608 455 TIHWVEATqalpAEFR---LFEPLilddttgedkpfleRInpnslqVLQG-YVEP---NMAEARGQDKFqFFRHGYF 524
Cdd:COG0008 411 TIHWVSAE----AGVKdglLFMPL--------------RV------ALTGrTVEPslfDVLELLGKERV-FERLGYA 462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-551 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1180.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 1 MDNKSLPPNFIRNIILEDIESGRVKEVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVES 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 81 IKEDVRWLGFEW-DKLFFASDYFDEMYNRAVILIKKGKAYVDDLSAEEIRQTRGTLTEPGKESPYRNRSVEENLDLFERM 159
Cdd:PRK05347 84 IKEDVRWLGFDWsGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 160 RKGEFKDGEKVLRAKIDMASPNINMRDPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLY 239
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 240 DWVIEECEMECRPRQYEFARLNLTNTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANS 319
Cdd:PRK05347 244 DWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 320 TVDLKMLEHFIREDLKLKAPRTMAVLRPLKVVITNYPEGQREMLEAENNAENPEMGHRLIPFSREIYIEQDDFMENPPSK 399
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 400 YFRLFPGNEVRLKHAYFIKCHDVIKDAEGRIVELHCTYDPATKSGSGFEGRKVKGTIHWVEATQALPAEFRLFEPLILDD 479
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752664608 480 TTGEDKPFLERINPNSLQVLQGYVEPNMAEARGQDKFQFFRHGYFNVDpKQTTGDKKVFNHIVSLKSSFQLP 551
Cdd:PRK05347 484 NPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
8-547 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 870.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 8 PNFIRNIILEDIESGRVKEVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRW 87
Cdd:PRK14703 13 PNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 88 LGFEW-DKLFFASDYFDEMYNRAVILIKKGKAYVDDLSAEEIRQTRGTLTEPGKESPYRNRSVEENLDLFERMRKGEFKD 166
Cdd:PRK14703 93 LGFDWgEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 167 GEKVLRAKIDMASPNINMRDPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEEC 246
Cdd:PRK14703 173 GAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 247 -EMECRPRQYEFARLNLTNTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKM 325
Cdd:PRK14703 253 gPWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 326 LEHFIREDLKLKAPRTMAVLRPLKVVITNYPEGQREMLEAEN-NAENPEMGHRLIPFSREIYIEQDDFMENPPSKYFRLF 404
Cdd:PRK14703 333 LEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYwPHDVPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 405 PGNEVRLKHAYFIKCHDVIKDAEGRIVELHCTYDPATKSGSGfEGRKVKGTIHWVEATQALPAEFRLFEPLI-LDDTTGE 483
Cdd:PRK14703 413 PGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGED-TGRKAAGVIHWVSAKHALPAEVRLYDRLFkVPQPEAA 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752664608 484 DKPFLERINPNSLQVLQGYVEPNMAEARGQDKFQFFRHGYFNVDPKQTTGDKKVFNHIVSLKSS 547
Cdd:PRK14703 492 DEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDT 555
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
27-548 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 700.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 27 VVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWD-KLFFASDYFDEM 105
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 106 YNRAVILIKKGKAYVDDLSAEEIRQTRGTLTEPGKESPYRNRSVEENLDLFERMRKGEFKDGEKVLRAKIDMASPNINMR 185
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 186 DPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMECRPRQYEFARLNLTNT 265
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 266 VMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIREDLKLKAPRTMAVL 345
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 346 RPLKVVITNYpEGQREMLEAENNAENPEMGHRLIPFSREIYIEQDDFMENPPSKYFRLFPGNEVRLKHAYFIKCHDVIKD 425
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 426 AEGRIVELHCTYDPATKSGSGFEGRKVKGTIHWVEATQALPAEFRLFEPLILDDTTGEDKPFLERINPNSLQVLQGYVEP 505
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 752664608 506 NMAEARGQDKFQFFRHGYFNVDPKQTTGDKKVFNHIVSLKSSF 548
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
27-548 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 575.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 27 VVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWDKLFFASDYFDEMY 106
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELY 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 107 NRAVILIKKGKAYVDDLSAEEIRQTRgtltEPGKESPYRNRSVEENLDLFERMRKGEFKDGEKVLRAKIDMASPNINMRD 186
Cdd:PLN02859 345 ELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYD 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 187 PVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMEcRPRQYEFARLNLTNTV 266
Cdd:PLN02859 421 LIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY-QPYVWEYSRLNVTNTV 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 267 MSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKA-NSTVDLKMLEHFIREDLKLKAPRTMAVL 345
Cdd:PLN02859 500 MSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdNSLIRMDRLEHHIREELNKTAPRTMVVL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 346 RPLKVVITNYPEGQREMLEA----ENNAENPEMGHRlIPFSREIYIEQDDFMENPPSKYFRLFPGNEVRLKHAYFIKCHD 421
Cdd:PLN02859 580 HPLKVVITNLESGEVIELDAkrwpDAQNDDPSAFYK-VPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKCTD 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 422 VI-KDAEGRIVELHCTYDPATKSgsgfegrKVKGTIHWV----EATQALPAEFRLFEPLILDDTTGEDKPFLERINPNSL 496
Cdd:PLN02859 659 VVlADDNETVVEIRAEYDPEKKT-------KPKGVLHWVaepsPGVEPLKVEVRLFDKLFLSENPAELEDWLEDLNPQSK 731
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 752664608 497 QVLQG-YVEPNMAEARGQDKFQFFRHGYFNVDpKQTTGDKKVFNHIVSLKSSF 548
Cdd:PLN02859 732 EVISGaYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSY 783
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
30-545 |
2.90e-170 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 494.50 E-value: 2.90e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 30 RFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWDKLFFASDYFDEMYNRA 109
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHEFA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 110 VILIKKGKAYVDDLSAEEIRQTRgtltEPGKESPYRNRSVEENLDLFERMRKGEFKDGEKVLRAKIDMASPNINMRDPVL 189
Cdd:PTZ00437 135 VQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 190 YRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMeCRPRQYEFARLNLTNTVMSK 269
Cdd:PTZ00437 211 YRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSLLSK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 270 RWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIREDLKLKAPRTMAVLRPLK 349
Cdd:PTZ00437 290 RKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPIK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 350 VVITNYpEGQREmLEAENNAENPEMGHRLIPFSREIYIEQDDF-MENPPSKYFRLFPGNE-VRLKHAYFIKCHDVIKDAE 427
Cdd:PTZ00437 370 VVVDNW-KGERE-FECPNHPRKPELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPGPRvVGLKYSGNVVCKGFEVDAA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 428 GRIVELHCTYDPATKSgsgfegrKVKGTIHWVEATQALPAEFRLFEPLILDDTTGEDKPFLERINPNSLQVLQGYVEPNM 507
Cdd:PTZ00437 448 GQPSVIHVDIDFERKD-------KPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEKGI 520
|
490 500 510
....*....|....*....|....*....|....*...
gi 752664608 508 AEARGQDKFQFFRHGYFNVDPkQTTGDKKVFNHIVSLK 545
Cdd:PTZ00437 521 ENAKHFESVQAERFGYFVVDP-DTRPDHLVMNRVLGLR 557
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
26-340 |
1.41e-147 |
|
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: 423.59 E-value: 1.41e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 26 EVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWDKLFFASDYFDEM 105
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 106 YNRAVILIKKGKAYVddlsaeeirqtrgtltepgkespyrnrsveenldlfermrkgefkdgekvlrakidmaspninmr 185
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 186 dpvlyriahasHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMECrPRQYEFARLNLTNT 265
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752664608 266 VMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIREDLKLKAPR 340
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
26-335 |
9.17e-134 |
|
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: 391.30 E-value: 9.17e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 26 EVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWD-KLFFASDYFDE 104
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 105 MYNRAVILIKKGKAYVDDLSAEEIRQTRGTLtePGKESPYRNRSVEENLDLF-ERMRKGEFKDGEKVLRAKIDMASPnIN 183
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 184 MRDPVLYRIAHAS---HHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMECRPRQYEFARL 260
Cdd:pfam00749 158 FRDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752664608 261 NLTNTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDL-KMLEHFIREDLK 335
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLsKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-524 |
1.79e-130 |
|
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: 388.77 E-value: 1.79e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 25 KEVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWD-KLFFASDYFD 103
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDeGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 104 EMYNRAVILIKKGKAYVDDLSAEEIRQTRGTLTEPGKESPY----RNRSVEENldlfERMRkgefKDGEK-VLRAKI--- 175
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGEPpVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 176 -----DMAS-----PNINMRDPVLYRiAHAshhntgdkwciYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEE 245
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-ADG-----------YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 246 CEMEcRPrqyEFARLNLT----NTVMSKRwlKKLVdeaivdgwddprmpTISGLRRRGYTPEAIRAFAREIGVAKANSTV 321
Cdd:COG0008 223 LGWE-PP---EFAHLPLIlgpdGTKLSKR--KGAV--------------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 322 --DLKMLEHFIreDLKlKAPRTMAVLRPLKVVITNYPEGQreMLEAENNAE-----NPEMGH-----RLIPFSRE----- 384
Cdd:COG0008 283 ifSLEELIEAF--DLD-RVSRSPAVFDPVKLVWLNGPYIR--ALDDEELAEllapeLPEAGIredleRLVPLVREraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 385 ---------IYIEQDDfmENPPSKyfRLFPgNEVRLkhayFIKC-HDVIKDAEgrivelhcTYDPATksgsgfegrkVKG 454
Cdd:COG0008 358 selaelarfFFIERED--EKAAKK--RLAP-EEVRK----VLKAaLEVLEAVE--------TWDPET----------VKG 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752664608 455 TIHWVEATqalpAEFR---LFEPLilddttgedkpfleRInpnslqVLQG-YVEP---NMAEARGQDKFqFFRHGYF 524
Cdd:COG0008 411 TIHWVSAE----AGVKdglLFMPL--------------RV------ALTGrTVEPslfDVLELLGKERV-FERLGYA 462
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
16-540 |
2.42e-120 |
|
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: 366.07 E-value: 2.42e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 16 LEDIESGRVKEVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWDKL 95
Cdd:TIGR00463 83 LRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 96 FFASDYFDEMYNRAVILIKKGKAYVDDLSAEEIRQTRGTltepGKESPYRNRSVEENLDLFERMRKGEFKDGEKVLRAKI 175
Cdd:TIGR00463 163 VYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 176 DMASPNINMRDPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDH--RPLYDWVIEECEMEcRPR 253
Cdd:TIGR00463 239 DLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNrrKQEYIYRYFGWEPP-EFI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 254 QYEFARLNLTNTVMSKRWLKKLVDEAIVdGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIRED 333
Cdd:TIGR00463 318 HWGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 334 LKLKAPRTMAVLRPLKVVITNYPEGQREMLEAenNAENPEMGHRLIPFSREIYIEQDDFMENPpskyfrlfpgNEVRLKH 413
Cdd:TIGR00463 397 IDEEARRYFFIWNPVKIEIVGLPEPKRVERPL--HPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRLMD 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 414 AyfikCHDVIKDAEGRIvelhctydpatkSGSGFEGRKVKGT--IHWVEATQALPAEFRLFEPLIlddttgedkpfleri 491
Cdd:TIGR00463 465 A----VNVIYSKKELRY------------HSEGLEGARKLGKsiIHWLPAKDAVKVKVIMPDASI--------------- 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 752664608 492 npnslqvLQGYVEPNMAEARGQDKFQFFRHGYFNVDPKQTTGDKKVFNH 540
Cdd:TIGR00463 514 -------VEGVIEADASELEVGDVVQFERFGFARLDSADKDGMVFVYTH 555
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
18-527 |
1.09e-115 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 359.04 E-value: 1.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 18 DIESGRVKEVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWDKLFF 97
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTY 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 98 ASDYFDEMYNRAVILIKKGKAYVDDLSAEEIRQTRGTltepGKESPYRNRSVEENLDLFERMRKGEFKDGEKVLRAKIDM 177
Cdd:PLN02907 285 TSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDM 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 178 ASPNINMRDPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEecEMECRPRQ-YE 256
Cdd:PLN02907 361 QDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILE--DMGLRKVHiWE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 257 FARLNLTNTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIREDLKL 336
Cdd:PLN02907 439 FSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDP 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 337 KAPRTMAVLRPLKVVIT--NYPEGQrEMLEAENNAENPEMGHRLIPFSREIYIEQDDfmENPPSKyfrlfpGNEVRLK-- 412
Cdd:PLN02907 519 VCPRHTAVLKEGRVLLTltDGPETP-FVRIIPRHKKYEGAGKKATTFTNRIWLDYAD--AEAISE------GEEVTLMdw 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 413 -HAyFIKchDVIKDAEGRIVELHCTYDPAtksGSgfegrkVKGT---IHWVEATQAL-PAEFRLFEPLILDDTTGEDKPF 487
Cdd:PLN02907 590 gNA-IIK--EITKDEGGAVTALSGELHLE---GS------VKTTklkLTWLPDTNELvPLSLVEFDYLITKKKLEEDDNF 657
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 752664608 488 LERINPNSLQVLQGYVEPNMAEARGQDKFQFFRHGYFNVD 527
Cdd:PLN02907 658 LDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
2-540 |
1.44e-109 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 338.36 E-value: 1.44e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 2 DNKSLPPnfirniiLEDIESGRVkevVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPlkeDTRYV--- 78
Cdd:PRK04156 87 EKKGLPP-------LPNAEKGKV---VMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDP---RTKRPdpe 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 79 --ESIKEDVRWLGFEWDKLFFASDYFDEMYNRAVILIKKGKAYVDDLSAEEIRQTRgtltEPGKESPYRNRSVEENLDLF 156
Cdd:PRK04156 154 ayDMILEDLKWLGVKWDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELW 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 157 ERMRKGEFKDGEKVLRAKIDMASPNINMRDPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHsicTLEFEDH- 235
Cdd:PRK04156 230 EKMLDGEYKEGEAVVRVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTH---VLRGKDHi 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 236 ------RPLYD---WvieecEMecrPRQYEFARLNLTNTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIR 306
Cdd:PRK04156 307 dntekqRYIYDyfgW-----EY---PETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIR 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 307 AFAREIGVAKANSTVDLKMLEHFIREDLKLKAPRTMAVLRPLKVVITNYPEgqremLEAEN--NAENPEMGHRLIPFSRE 384
Cdd:PRK04156 379 ELIIEVGVKETDATISWENLYAINRKLIDPIANRYFFVRDPVELEIEGAEP-----LEAKIplHPDRPERGEREIPVGGK 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 385 IYIEQDDFMEnppskyfrlfPGNEVRLKHAYFIKchdvIKDAEGRIVELHctydpatkSGSGFEGRKVKGTI-HWVEATQ 463
Cdd:PRK04156 454 VYVSSDDLEA----------EGKMVRLMDLFNVE----ITGVSVDKARYH--------SDDLEEARKNKAPIiQWVPEDE 511
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752664608 464 ALPAEFRlfeplilddttgedKPFLERINpnslqvlqGYVEPNmAEARGQDKF-QFFRHGYFNVDPKQTTGDKKVFNH 540
Cdd:PRK04156 512 SVPVRVL--------------KPDGGDIE--------GLAEPD-VADLEVDDIvQFERFGFVRIDSVEDDEVVAYFAH 566
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
19-527 |
7.80e-104 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 322.34 E-value: 7.80e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 19 IESGRVKEVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWDKLFFA 98
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 99 SDYFDEMYNRAVILIKKGKAYVDDLSAEEIRQTRGTLtepgKESPYRNRSVEENLDLFERMRKGEFKDGEKVLRAKIDMA 178
Cdd:PLN03233 84 SDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADR----AESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 179 SPNINMRDPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMEcRPRQYEFA 258
Cdd:PLN03233 160 SDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 259 RLNLTNTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIREDLKLKA 338
Cdd:PLN03233 239 RMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 339 PRTMAVLRP--LKVVITNYPEGQREML-EAENNAENPEMGHRLIPFSREIYIEQDDFMEnppskyfrLFPGNEVRLKHAY 415
Cdd:PLN03233 319 KRFMAIDKAdhTALTVTNADEEADFAFsETDCHPKDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLLRWG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 416 FIKCHDVIKDAEGRIVelhctydpatkSGSGFEGRKVKgtIHWV-EATQALPAEFRLFEPLILDDTTGEDKPFLERINPN 494
Cdd:PLN03233 391 VIEISKIDGDLEGHFI-----------PDGDFKAAKKK--ISWIaDVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPD 457
|
490 500 510
....*....|....*....|....*....|...
gi 752664608 495 SLQVLQGYVEPNMAEARGQDKFQFFRHGYFNVD 527
Cdd:PLN03233 458 TLAETDVIGDAGLKTLKEHDIIQLERRGFYRVD 490
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
14-527 |
1.40e-100 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 316.13 E-value: 1.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 14 IILEDIESGRVkevVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWD 93
Cdd:PTZ00402 43 LQLTNAEEGKV---VTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 94 -KLFFASDYFDEMYNRAVILIKKGKAYVDDLSAEEIRQTRGTltepGKESPYRNRSVEENLDLFERMRKGEFKDGEKVLR 172
Cdd:PTZ00402 120 vGPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 173 AKIDMASPNINMRDPVLYRIAHASHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMEcRP 252
Cdd:PTZ00402 196 AKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIR-KP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 253 RQYEFARLNLTNTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIRE 332
Cdd:PTZ00402 275 IVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 333 DLKLKAPRTMAVLRPLKVVITnyPEGQREMLEAEN--NAENPEMGHRLIPFSREIYIEQDDFMenppskyfRLFPGNEVR 410
Cdd:PTZ00402 355 ILDPSVPRYTVVSNTLKVRCT--VEGQIHLEACEKllHKKVPDMGEKTYYKSDVIFLDAEDVA--------LLKEGDEVT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 411 LK---HAYfikchdvIKD-----AEGRIVELHCTYDPatksgsgfEG--RKVKGTIHWV-EATQALPAEFRLFEPLILDD 479
Cdd:PTZ00402 425 LMdwgNAY-------IKNirrsgEDALITDADIVLHL--------EGdvKKTKFKLTWVpESPKAEVMELNEYDHLLTKK 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 752664608 480 TTGEDKPFLERINPNSLQVLQGYVEPNMAEARGQDKFQFFRHGYFNVD 527
Cdd:PTZ00402 490 KPDPEESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVD 537
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
338-527 |
5.44e-72 |
|
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 427609 [Multi-domain] Cd Length: 175 Bit Score: 227.54 E-value: 5.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 338 APRTMAVLRPLKVVITNYPEGQREMLEAENNAENPEMGHRLIPFSREIYIEQDDFmenppskyFRLFPGNEVRLKHAYFI 417
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 418 KCHDVIKDAEGRIVELHCTYDPATKSGSgfegRKVKG-TIHWVEATQALPAEFRLFEPLILDDttgEDKPFLerINPNSL 496
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDE---DDADFL--LNPDSL 143
|
170 180 190
....*....|....*....|....*....|..
gi 752664608 497 QVL-QGYVEPNMAEARGQDKFQFFRHGYFNVD 527
Cdd:pfam03950 144 KVLtEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
27-346 |
8.45e-57 |
|
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: 189.99 E-value: 8.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 27 VVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWDK-LFFASDYFDEM 105
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEgPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 106 YNRAVILIKKGkayvddlsaeeirqtrgtltepgkespyrnrsveenldlfermrkgefkdgekvlrakidmaspninmr 185
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 186 dpvlyriahashhntgdkwcIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMEcRPRQYEFARLNL-TN 264
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLeDG 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 265 TVMSKRwlkklvdeaivdgwdDPRmPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLE---HFIREDLKLKAPR- 340
Cdd:cd00418 152 TKLSKR---------------KLN-TTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEmiaAFSVERVNSADATf 215
|
....*.
gi 752664608 341 TMAVLR 346
Cdd:cd00418 216 DWAKLE 221
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
26-340 |
3.02e-52 |
|
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: 178.31 E-value: 3.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 26 EVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNP--LKEDTRYVESIKEDVRWLGFEWDKLFFASDYFD 103
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 104 EMYNRAVILIKKGKAYVddlsaeeirqtrgtltepgkespyrnrsveenldlfermrkgefkdgekvlrakidmaspnin 183
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 184 mrdpvlyriahasHHNTGDKWCIYPMYDFAHPLEDALEGVTHSICTLEFEDHRPLYDWVIEECEMEcRPRQYEFARLNLT 263
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWE-YPETIHWGRLKIE 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752664608 264 NTVMSKRWLKKLVDEAIVDGWDDPRMPTISGLRRRGYTPEAIRAFAREIGVAKANSTVDLKMLEHFIREDLKLKAPR 340
Cdd:cd09287 164 GGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
26-345 |
3.19e-19 |
|
glutamyl-tRNA synthetase, bacterial 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 bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 90.49 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 26 EVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWD-KLFFASDYFDe 104
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDeGPYYQSQRLD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 105 MYNRAV-ILIKKGKAYVDDLSAEEIRQTRGTLTEPGKESPYRNRSveenLDLFERMRKGEFKDGEK-VLRAKIDM-ASPN 181
Cdd:TIGR00464 80 IYKKYAkELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRC----RNLHEEEIENKLAKGIPpVVRFKIPQeAVVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 182 INmrDPVLYRIAHASHHNT------GDKwciYPMYDFAHPLEDALEGVTHSIctlEFEDHRP-------LYD---WVIee 245
Cdd:TIGR00464 156 FN--DQVRGEITFQNSELDdfvilrSDG---SPTYNFAVVVDDYLMKITHVI---RGEDHISntpkqilIYQalgWKI-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 246 cemecrPRqyeFARLNLTNTV----MSKRwlkklvDEAIvdgwddprmpTISGLRRRGYTPEAIRAF----------ARE 311
Cdd:TIGR00464 226 ------PV---FAHLPMILDEdgkkLSKR------DGAT----------SIMQFKEQGYLPEALINYlallgwsppdDQE 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 752664608 312 I-------------GVAKANSTVDLKMLEHFIREDLKLKAPRTMAVL 345
Cdd:TIGR00464 281 FfsleelieifslnRVSKSPAKFDWKKLQWLNAHYIKELPDEELFEL 327
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
26-93 |
4.75e-13 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 68.77 E-value: 4.75e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752664608 26 EVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWD 93
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWD 68
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
28-119 |
3.22e-12 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 67.57 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 28 VTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNPLKEDTRYVESIKEDVRWLGFEWDK-LFFASDYFDEmY 106
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGpVLYQSQRHDA-Y 85
|
90
....*....|....*
gi 752664608 107 nRAVI--LIKKGKAY 119
Cdd:PRK05710 86 -RAALdrLRAQGLVY 99
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
28-92 |
1.67e-10 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 59.42 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 28 VTRFPPEPNGYLHIGHAKSICLNFELA-----DEFKGRTHLRFDDTNPLKEDT-------------RYVESIKEDVRWLg 89
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAqayrkLGYKVRCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM- 79
|
...
gi 752664608 90 FEW 92
Cdd:cd00802 80 FLQ 82
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
28-92 |
2.48e-09 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 54.85 E-value: 2.48e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752664608 28 VTRFPPEPnGYLHIGHAKSICLNFELADEFkgrtHLRFDDTNPLK------EDTRYVESIKEDVRWLGFEW 92
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIADQC----VVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDF 66
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
26-237 |
6.46e-08 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 55.13 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 26 EVVTRFPPEPNGYLHIGHAKSICLNFELADEFKGRTHLRFDDTNpLKEDTRYVE-SIKEDVRWLGFEWDK---------L 95
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTD-LARSTKESEeAVLRDLKWLGLDWDEgpdvggeygP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 96 FFASDYFDEMYNRAVILIKKGKAYVDDLSAEEIRQTRgTLTEPGKESP-----YRNRSVEEnldLFERMRKGE-----FK 165
Cdd:PLN02627 124 YRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMK-EEAELKKLPPrytgkWATASDEE---VQAELAKGTpytyrFR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752664608 166 --DGEKVlraKID-----MASPNIN-MRDPVLYRiahashhNTGdkwciYPMYDFAHPLEDALEGVTHSIctlEFEDHRP 237
Cdd:PLN02627 200 vpKEGSV---KIDdlirgEVSWNTDtLGDFVLLR-------SNG-----QPVYNFCVAVDDATMGITHVI---RAEEHLP 261
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
225-270 |
2.54e-05 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 43.30 E-value: 2.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 752664608 225 HSICTLEFEDHRPLYDWVIEECEMECRPRQYEFARLNLTNTVMSKR 270
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKR 104
|
|
| |
