|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-588 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1127.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 1 MSQVPPVAPVSNFIRQIIESDLAADRFrgklwagapgpasvqaqgqqdpARIRTRFPPEPNGYLHIGHAKSICLNFGLAR 80
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKH----------------------TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 81 DYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaesgENHLYFASDYFDYMYGFAEALIEAGYAYVDEQSAEEIR 160
Cdd:PRK05347 59 DYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDW-----SGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 161 ANRGSLTEPGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMASPNINLRDPVLYRVRHAHHHRTGDKWCIYPM 240
Cdd:PRK05347 134 EYRGTLTEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 241 YTWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLaelgqLAEPLPHQYEFARLNLSYVVTSKRKLLKLVQDGLVEGW 320
Cdd:PRK05347 214 YDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNL-----PIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGW 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 321 DDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDLDPVAERAVAVLDPIKLIITNYPEGQTEPCH 400
Cdd:PRK05347 289 DDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 401 APRNPHDPAAGQRHFPFSRELWIERDDFREEAPKKYFRLFPGNMVRLKYGYVVKCTGFSKDANGNITEVHAEYLPDTKSG 480
Cdd:PRK05347 369 APNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 481 tPGADSVKVKGNITWVSAAHAVPAEIRLYDRLFSDAFPDAGdKEFLDFLNPDSIKVVRGWLEPGL-QAEPGRAWQFERLG 559
Cdd:PRK05347 449 -NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPNPAAG-KDFLDFLNPDSLVIKQGFVEPSLaDAKPEDRFQFEREG 526
|
570 580
....*....|....*....|....*....
gi 1551428890 560 YFAADRElSRVDAPVINRITTLRDSWAQA 588
Cdd:PRK05347 527 YFCADKD-STPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
52-585 |
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: 670.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 52 IRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWQAEsgenhLYFASD 131
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGK-----IRYSSD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 132 YFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGSLTEPGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMASP 211
Cdd:TIGR00440 76 YFDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 212 NINLRDPVLYRVRHAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgqlAEPLPHQY 291
Cdd:TIGR00440 156 FPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIH-----IFPRPAQY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 292 EFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDLD 371
Cdd:TIGR00440 231 EFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 372 PVAERAVAVLDPIKLIITNYpEGQTEPCHAPRNPHDPAAGQRHFPFSRELWIERDDFREEAPKKYFRLFPGNMVRLKYGY 451
Cdd:TIGR00440 311 ENAPRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 452 VVKCTGFSKDANGNITEVHAEYLPDTKSGTPgADSVKVKGNITWVSAAHAVPAEIRLYDRLFSDAFPDAGDkEFLDFLNP 531
Cdd:TIGR00440 390 VIKAERVEKDAAGKITTIFCTYDNKTLGKEP-ADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPD-DFLSVINP 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1551428890 532 DSIKVVRGWLEPGL-QAEPGRAWQFERLGYFAADRELSRVDAPVINRITTLRDSW 585
Cdd:TIGR00440 468 ESLVIKQGFMEHSLgDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
51-376 |
7.24e-137 |
|
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: 397.78 E-value: 7.24e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaesgeNHLYFAS 130
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP------YKVTYAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 131 DYFDYMYGFAEALIEAGYAYVdeqsaeeiranrgsltepgtdspwrdrpaaeslqrlremrdgkhpdgslvlraridmas 210
Cdd:cd00807 75 DYFDQLYEYAEQLIKKGKAYV----------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 211 pninlrdpvlyrvrhahHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILArlaelgQLAEPLPHQ 290
Cdd:cd00807 96 -----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCD------ALRLYRPHQ 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 291 YEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDL 370
Cdd:cd00807 153 WEFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDL 232
|
....*.
gi 1551428890 371 DPVAER 376
Cdd:cd00807 233 NPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
51-563 |
6.38e-133 |
|
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: 396.09 E-value: 6.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWQAEsgenhLYFAS 130
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEG-----PYYQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 131 DYFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGSLTEPGT----DSPWRDRPAAEslqrLREMRD-GKHPdgslVLRAR 205
Cdd:COG0008 79 DRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKppryDGRCRDLSPEE----LERMLAaGEPP----VLRFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 206 I--------DMAS-----PNINLRDPVLYRVrhahhhrTGdkwciYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDW 272
Cdd:COG0008 151 IpeegvvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIW 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 273 ILArlaelgQLAEPLPhqyEFARLNLSY----VVTSKRKllklvqdGLVegwddprmpTLVGLRRRGYTPSAIRLFCERI 348
Cdd:COG0008 219 LYE------ALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 349 GVARADSR--IDYSLLEQALrdDLDPVAeRAVAVLDPIKLIITNYPEGQTEPCHAPRN---PHDPAAG-----QRHFPFS 418
Cdd:COG0008 274 GWSKSDDQeiFSLEELIEAF--DLDRVS-RSPAVFDPVKLVWLNGPYIRALDDEELAEllaPELPEAGiredlERLVPLV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 419 RE--------------LWIERDDfrEEAPKKyfRLFPGNMVRlkygyVVKCTgfsKDANGNITevhaEYLPDTksgtpga 484
Cdd:COG0008 351 REraktlselaelarfFFIERED--EKAAKK--RLAPEEVRK-----VLKAA---LEVLEAVE----TWDPET------- 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 485 dsvkVKGNITWVSAAhavpAEIRlyDRLFSDafpdagdkefldflnPDSIKVVRGWLEPGLQ--AEP-GRAWQFERLGYF 561
Cdd:COG0008 408 ----VKGTIHWVSAE----AGVK--DGLLFM---------------PLRVALTGRTVEPSLFdvLELlGKERVFERLGYA 462
|
..
gi 1551428890 562 AA 563
Cdd:COG0008 463 ID 464
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
52-372 |
9.26e-126 |
|
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: 372.42 E-value: 9.26e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 52 IRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaesgENHLYFASD 131
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKW-----DYGPYYQSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 132 YFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGslTEPGTDSPWRDRPAAESLQ-RLREMRDGKHPDGSLVLRARIDMAS 210
Cdd:pfam00749 77 RFDIYYKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHlFEEEMKKGSAEGGPATVRAKIPMES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 211 PnINLRDPVLYRVR---HAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgqlAEPL 287
Cdd:pfam00749 155 P-YVFRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-----WEPP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 288 PHQYEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADS-RIDYSLLEQAL 366
Cdd:pfam00749 229 PFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFD 308
|
....*.
gi 1551428890 367 RDDLDP 372
Cdd:pfam00749 309 RKKLDW 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-588 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1127.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 1 MSQVPPVAPVSNFIRQIIESDLAADRFrgklwagapgpasvqaqgqqdpARIRTRFPPEPNGYLHIGHAKSICLNFGLAR 80
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKH----------------------TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 81 DYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaesgENHLYFASDYFDYMYGFAEALIEAGYAYVDEQSAEEIR 160
Cdd:PRK05347 59 DYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDW-----SGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 161 ANRGSLTEPGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMASPNINLRDPVLYRVRHAHHHRTGDKWCIYPM 240
Cdd:PRK05347 134 EYRGTLTEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 241 YTWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLaelgqLAEPLPHQYEFARLNLSYVVTSKRKLLKLVQDGLVEGW 320
Cdd:PRK05347 214 YDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNL-----PIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGW 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 321 DDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDLDPVAERAVAVLDPIKLIITNYPEGQTEPCH 400
Cdd:PRK05347 289 DDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 401 APRNPHDPAAGQRHFPFSRELWIERDDFREEAPKKYFRLFPGNMVRLKYGYVVKCTGFSKDANGNITEVHAEYLPDTKSG 480
Cdd:PRK05347 369 APNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 481 tPGADSVKVKGNITWVSAAHAVPAEIRLYDRLFSDAFPDAGdKEFLDFLNPDSIKVVRGWLEPGL-QAEPGRAWQFERLG 559
Cdd:PRK05347 449 -NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPNPAAG-KDFLDFLNPDSLVIKQGFVEPSLaDAKPEDRFQFEREG 526
|
570 580
....*....|....*....|....*....
gi 1551428890 560 YFAADRElSRVDAPVINRITTLRDSWAQA 588
Cdd:PRK05347 527 YFCADKD-STPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
5-586 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 825.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 5 PPVAPVSNFIRQIIESDLAADRFrgklwagapgpasvqaqgqqdpARIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGG 84
Cdd:PRK14703 7 PRMLVSPNFITEIIEEDLEAGRY----------------------PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 85 VCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaesgENHLYFASDYFDYMYGFAEALIEAGYAYVDEQSAEEIRANRG 164
Cdd:PRK14703 65 RCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDW-----GEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 165 SLTEPGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMASPNINLRDPVLYRVRHAHHHRTGDKWCIYPMYTWA 244
Cdd:PRK14703 140 TVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 245 HPVEDALEGITHSICTLEFEDQRPFYDWILARLAELgqlaEPLPHQYEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPR 324
Cdd:PRK14703 220 HPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPW----PPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 325 MPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDLDPVAERAVAVLDPIKLIITNYPEGQTEPCHAPRN 404
Cdd:PRK14703 296 MPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYW 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 405 PHD-PAAGQRHFPFSRELWIERDDFREEAPKKYFRLFPGNMVRLKYGYVVKCTGFSKDANGNITEVHAEYLPDTKSGTPG 483
Cdd:PRK14703 376 PHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 484 AdsVKVKGNITWVSAAHAVPAEIRLYDRLFSDAFPDAGDKEFLDFLNPDSIKVVRGWLEPGLQAEP-GRAWQFERLGYFA 562
Cdd:PRK14703 456 G--RKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEAADEDFLEFLNPDSLRVAQGRVEPAVRDDPaDTRYQFERQGYFW 533
|
570 580
....*....|....*....|....
gi 1551428890 563 ADRELSRVDAPVINRITTLRDSWA 586
Cdd:PRK14703 534 ADPVDSRPDALVFNRIITLKDTWG 557
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
52-585 |
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: 670.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 52 IRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWQAEsgenhLYFASD 131
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGK-----IRYSSD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 132 YFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGSLTEPGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMASP 211
Cdd:TIGR00440 76 YFDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 212 NINLRDPVLYRVRHAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgqlAEPLPHQY 291
Cdd:TIGR00440 156 FPVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIH-----IFPRPAQY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 292 EFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDLD 371
Cdd:TIGR00440 231 EFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 372 PVAERAVAVLDPIKLIITNYpEGQTEPCHAPRNPHDPAAGQRHFPFSRELWIERDDFREEAPKKYFRLFPGNMVRLKYGY 451
Cdd:TIGR00440 311 ENAPRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 452 VVKCTGFSKDANGNITEVHAEYLPDTKSGTPgADSVKVKGNITWVSAAHAVPAEIRLYDRLFSDAFPDAGDkEFLDFLNP 531
Cdd:TIGR00440 390 VIKAERVEKDAAGKITTIFCTYDNKTLGKEP-ADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPD-DFLSVINP 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1551428890 532 DSIKVVRGWLEPGL-QAEPGRAWQFERLGYFAADRELSRVDAPVINRITTLRDSW 585
Cdd:TIGR00440 468 ESLVIKQGFMEHSLgDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
51-588 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 530.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGfdWQAESgenhLYFAS 130
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WEPFK----ITYTS 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 131 DYFDYMYGFAEALIEAGYAYVDEQSAEEIRANRgsltEPGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMAS 210
Cdd:PLN02859 338 DYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQN 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 211 PNINLRDPVLYRVRHAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAELgqlaepLPHQ 290
Cdd:PLN02859 414 DNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY------QPYV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 291 YEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARAD-SRIDYSLLEQALRDD 369
Cdd:PLN02859 488 WEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDnSLIRMDRLEHHIREE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 370 LDPVAERAVAVLDPIKLIITNYPEGQTEPCHA---PRNPHDPAAGQRHFPFSRELWIERDDFREEAPKKYFRLFPGNMVR 446
Cdd:PLN02859 568 LNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVL 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 447 LKYGYVVKCTGF-SKDANGNITEVHAEYLPDTKSgtpgadsvKVKGNITWVSAA----HAVPAEIRLYDRLFSDAFPDAG 521
Cdd:PLN02859 648 LRYAFPIKCTDVvLADDNETVVEIRAEYDPEKKT--------KPKGVLHWVAEPspgvEPLKVEVRLFDKLFLSENPAEL 719
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1551428890 522 DkEFLDFLNPDSIKVVRG-WLEPGLQ-AEPGRAWQFERLGYFAADRElSRVDAPVINRITTLRDSWAQA 588
Cdd:PLN02859 720 E-DWLEDLNPQSKEVISGaYAVPSLKdAKVGDRFQFERLGYFAVDKD-STPEKLVFNRTVTLKDSYGKG 786
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
55-583 |
2.66e-172 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 501.05 E-value: 2.66e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 55 RFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGF--DWqaesgenhLYFASDY 132
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDW--------VTFSSDY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 133 FDYMYGFAEALIEAGYAYVDEQSAEEIRANRgsltEPGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMASPN 212
Cdd:PTZ00437 127 FDQLHEFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 213 INLRDPVLYRVRHAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILArlaelgQLAEPLPHQYE 292
Cdd:PTZ00437 203 PNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLE------ELNLWRPHVWE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 293 FARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDLDP 372
Cdd:PTZ00437 277 FSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 373 VAERAVAVLDPIKLIITNYPEGQTEPChaPRNPHDPAAGQRHFPFSRELWIERDDFR-EEAPKKYFRLFPG-NMVRLKYG 450
Cdd:PTZ00437 357 RCERRLMVIDPIKVVVDNWKGEREFEC--PNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKYS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 451 YVVKCTGFSKDANGNITEVHAEYLPDTKSgtpgadsvKVKGNITWVSAAHAVPAEIRLYDRLFSDAFPdAGDKEFLDFLN 530
Cdd:PTZ00437 435 GNVVCKGFEVDAAGQPSVIHVDIDFERKD--------KPKTNISWVSATACTPVEVRLYNALLKDDRA-AIDPEFLKFID 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1551428890 531 PDSIKVVRGWLEPGLQ-AEPGRAWQFERLGYFAADRElSRVDAPVINRITTLRD 583
Cdd:PTZ00437 506 EDSEVVSHGYAEKGIEnAKHFESVQAERFGYFVVDPD-TRPDHLVMNRVLGLRE 558
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
51-376 |
7.24e-137 |
|
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: 397.78 E-value: 7.24e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaesgeNHLYFAS 130
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP------YKVTYAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 131 DYFDYMYGFAEALIEAGYAYVdeqsaeeiranrgsltepgtdspwrdrpaaeslqrlremrdgkhpdgslvlraridmas 210
Cdd:cd00807 75 DYFDQLYEYAEQLIKKGKAYV----------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 211 pninlrdpvlyrvrhahHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILArlaelgQLAEPLPHQ 290
Cdd:cd00807 96 -----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCD------ALRLYRPHQ 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 291 YEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDL 370
Cdd:cd00807 153 WEFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDL 232
|
....*.
gi 1551428890 371 DPVAER 376
Cdd:cd00807 233 NPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
51-563 |
6.38e-133 |
|
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: 396.09 E-value: 6.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWQAEsgenhLYFAS 130
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEG-----PYYQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 131 DYFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGSLTEPGT----DSPWRDRPAAEslqrLREMRD-GKHPdgslVLRAR 205
Cdd:COG0008 79 DRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKppryDGRCRDLSPEE----LERMLAaGEPP----VLRFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 206 I--------DMAS-----PNINLRDPVLYRVrhahhhrTGdkwciYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDW 272
Cdd:COG0008 151 IpeegvvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIW 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 273 ILArlaelgQLAEPLPhqyEFARLNLSY----VVTSKRKllklvqdGLVegwddprmpTLVGLRRRGYTPSAIRLFCERI 348
Cdd:COG0008 219 LYE------ALGWEPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 349 GVARADSR--IDYSLLEQALrdDLDPVAeRAVAVLDPIKLIITNYPEGQTEPCHAPRN---PHDPAAG-----QRHFPFS 418
Cdd:COG0008 274 GWSKSDDQeiFSLEELIEAF--DLDRVS-RSPAVFDPVKLVWLNGPYIRALDDEELAEllaPELPEAGiredlERLVPLV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 419 RE--------------LWIERDDfrEEAPKKyfRLFPGNMVRlkygyVVKCTgfsKDANGNITevhaEYLPDTksgtpga 484
Cdd:COG0008 351 REraktlselaelarfFFIERED--EKAAKK--RLAPEEVRK-----VLKAA---LEVLEAVE----TWDPET------- 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 485 dsvkVKGNITWVSAAhavpAEIRlyDRLFSDafpdagdkefldflnPDSIKVVRGWLEPGLQ--AEP-GRAWQFERLGYF 561
Cdd:COG0008 408 ----VKGTIHWVSAE----AGVK--DGLLFM---------------PLRVALTGRTVEPSLFdvLELlGKERVFERLGYA 462
|
..
gi 1551428890 562 AA 563
Cdd:COG0008 463 ID 464
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
52-372 |
9.26e-126 |
|
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: 372.42 E-value: 9.26e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 52 IRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaesgENHLYFASD 131
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKW-----DYGPYYQSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 132 YFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGslTEPGTDSPWRDRPAAESLQ-RLREMRDGKHPDGSLVLRARIDMAS 210
Cdd:pfam00749 77 RFDIYYKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHlFEEEMKKGSAEGGPATVRAKIPMES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 211 PnINLRDPVLYRVR---HAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgqlAEPL 287
Cdd:pfam00749 155 P-YVFRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-----WEPP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 288 PHQYEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADS-RIDYSLLEQAL 366
Cdd:pfam00749 229 PFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFD 308
|
....*.
gi 1551428890 367 RDDLDP 372
Cdd:pfam00749 309 RKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
54-564 |
1.28e-105 |
|
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: 329.09 E-value: 1.28e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 54 TRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaesgeNHLYFASDYF 133
Cdd:TIGR00463 96 MRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKW------DEVVYQSDRI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 134 DYMYGFAEALIEAGYAYVDEQSAEEIRANRGSltepGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMASPNI 213
Cdd:TIGR00463 170 ETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 214 NLRDPVLYRVRHAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFED--QRPFYDWilarlaELGQLAEPLPHQY 291
Cdd:TIGR00463 246 AIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIY------RYFGWEPPEFIHW 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 292 EFARLNLSYVVTSKRKlLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDLD 371
Cdd:TIGR00463 320 GRLKIDDVRALSTSSA-RKGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIID 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 372 PVAERAVAVLDPIKLIITNYPEGQTEpcHAPRNPHDPAAGQRHFPFSRELWIERDDFREEApkkyfrlfpgNMVRLK-YG 450
Cdd:TIGR00463 399 EEARRYFFIWNPVKIEIVGLPEPKRV--ERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRLMdAV 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 451 YVVkctgfskdangnITEVHAEYLPDTKSGtpgaDSVKVKGNITWVSAAHAVPAEIrlydrlfsdAFPDAGDKEflDFLN 530
Cdd:TIGR00463 467 NVI------------YSKKELRYHSEGLEG----ARKLGKSIIHWLPAKDAVKVKV---------IMPDASIVE--GVIE 519
|
490 500 510
....*....|....*....|....*....|....
gi 1551428890 531 PDSIKVvrgwlepglqaEPGRAWQFERLGYFAAD 564
Cdd:TIGR00463 520 ADASEL-----------EVGDVVQFERFGFARLD 542
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
51-575 |
1.61e-103 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 328.61 E-value: 1.61e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWQAesgenhLYFAS 130
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDA------VTYTS 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 131 DYFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGSltepGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMAS 210
Cdd:PLN02907 287 DYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQD 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 211 PNINLRDPVLYRVRHAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWIlarLAELGqlaepLP-- 288
Cdd:PLN02907 363 PNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRI---LEDMG-----LRkv 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 289 HQYEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRD 368
Cdd:PLN02907 435 HIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 369 DLDPVAERAVAVLDPIKLIIT--NYPEgQTEPCHAPRNPHDPAAGQRHFPFSRELWIERDDFREEAPKKYFRLFP-GNMV 445
Cdd:PLN02907 515 IIDPVCPRHTAVLKEGRVLLTltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEAISEGEEVTLMDwGNAI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 446 RLKygyvvkctgFSKDANGNITEVHAEYLPdtksgtpgADSVK-VKGNITWVSA-AHAVPAEIRLYDRLFSDAFPDAGDk 523
Cdd:PLN02907 594 IKE---------ITKDEGGAVTALSGELHL--------EGSVKtTKLKLTWLPDtNELVPLSLVEFDYLITKKKLEEDD- 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1551428890 524 EFLDFLNPDSIKVVRGWLEPGLQA-EPGRAWQFERLGYFAADRELSRVDAPVI 575
Cdd:PLN02907 656 NFLDVLNPCTKKETAALGDSNMRNlKRGEIIQLERKGYYRCDAPFVRSSKPIV 708
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
49-575 |
6.72e-96 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 302.70 E-value: 6.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 49 PARIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWQAESgenhlyF 128
Cdd:PLN03233 9 AGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVS------F 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 129 ASDYFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGSLTEpgtdSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDM 208
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 209 ASPNINLRDPVLYRVRHAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLaelgQLAEPLP 288
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKAL----GLRRPRI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 289 HQyeFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRD 368
Cdd:PLN03233 235 HA--FARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 369 DLDPVAERAVAV--LDPIKLIITNYPEG-----QTEPCHaprnPHDPAAGQRHFPFSRELWIERDDFREEAPKKyfrlfp 441
Cdd:PLN03233 313 EIDKRAKRFMAIdkADHTALTVTNADEEadfafSETDCH----PKDPGFGKRAMRICDEVLLEKADTEDIQLGE------ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 442 gNMVRLKYGyVVKCTGFSKDANGnitevhaEYLPDtksgtpgADSVKVKGNITWVS-AAHAVPAEIRLYDRLFSDAFPDA 520
Cdd:PLN03233 383 -DIVLLRWG-VIEISKIDGDLEG-------HFIPD-------GDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEE 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1551428890 521 GDKeFLDFLNPDSIKVVRGWLEPGLQA-EPGRAWQFERLGYFAADRELSRVDAPVI 575
Cdd:PLN03233 447 DDK-FEDFINPDTLAETDVIGDAGLKTlKEHDIIQLERRGFYRVDRPYMGEEKPLI 501
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
51-579 |
9.45e-94 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 298.30 E-value: 9.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKEN--QEYVDAIKDTVHWLGFDWQAEsgenhlYF 128
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKWDEV------VI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 129 ASDYFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGSltepGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDM 208
Cdd:PRK04156 175 QSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 209 ASPNINLRDPVLYRVRHAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFED----QRPFYD---Wilarlaelg 281
Cdd:PRK04156 251 EHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYDyfgW--------- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 282 qlaePLPHQYEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSL 361
Cdd:PRK04156 322 ----EYPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWEN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 362 LEQALRDDLDPVAERAVAVLDPIKLIITNYPEGQTEPchaPRNPHDPAAGQRHFPFSRELWIERDDFREEapkkyfrlfp 441
Cdd:PRK04156 398 LYAINRKLIDPIANRYFFVRDPVELEIEGAEPLEAKI---PLHPDRPERGEREIPVGGKVYVSSDDLEAE---------- 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 442 GNMVRLKYGYVVKCTGFSKDAngniTEVHAEYLPDTKsgtpgadsvKVKGNIT-WVSAAHAVPAEIRLydrlfsdafPDA 520
Cdd:PRK04156 465 GKMVRLMDLFNVEITGVSVDK----ARYHSDDLEEAR---------KNKAPIIqWVPEDESVPVRVLK---------PDG 522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 521 GDKEfldflnpdsikvvrGWLEPGLQA-EPGRAWQFERLGYfaadrelSRVDAPVINRIT 579
Cdd:PRK04156 523 GDIE--------------GLAEPDVADlEVDDIVQFERFGF-------VRIDSVEDDEVV 561
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
51-569 |
3.80e-86 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 279.54 E-value: 3.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaESGENhlyFAS 130
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSW--DVGPT---YSS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 131 DYFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGSltepGTDSPWRDRPAAESLQRLREMRDGKHPDGSLVLRARIDMAS 210
Cdd:PTZ00402 127 DYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 211 PNINLRDPVLYRVRHAHHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgqLAEPLPHq 290
Cdd:PTZ00402 203 ENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALG----IRKPIVE- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 291 yEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDDL 370
Cdd:PTZ00402 278 -DFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQIL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 371 DPVAERAVAVLDPIKLIITNYPEGQTEPCHAPRNPHDPAAGQRHFPFSRELWIERDDfreeapkkyfrlfpgnMVRLKYG 450
Cdd:PTZ00402 357 DPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAED----------------VALLKEG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 451 YVVKCTGFSKDANGNITEVHAEYLPDTKSGT--PGADSVKVKGNITWVSAA-HAVPAEIRLYDRLFSDAFPDAgDKEFLD 527
Cdd:PTZ00402 421 DEVTLMDWGNAYIKNIRRSGEDALITDADIVlhLEGDVKKTKFKLTWVPESpKAEVMELNEYDHLLTKKKPDP-EESIDD 499
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1551428890 528 FLNPDSIKVVRGWLEPGLQA-EPGRAWQFERLGYFAADRELSR 569
Cdd:PTZ00402 500 IIAPVTKYTQEVYGEEALSVlKKGDIIQLERRGYYIVDDVTPK 542
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
374-564 |
2.22e-71 |
|
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: 226.77 E-value: 2.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 374 AERAVAVLDPIKLIITNYPEGQTEPCHAPRNPHDPAAGQRHFPFSRELWIERDDFreeapkkyFRLFPGNMVRLKYGYVV 453
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 454 KCTGFSKDANGNITEVHAEYLPDTKSGTpgadsVKVKGN-ITWVSAAHAVPAEIRLYDRLFSDafpdagDKEFLDFLNPD 532
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA-----RKVKGKiIHWVSASDAVPAEVRLYDRLFKD------EDDADFLLNPD 141
|
170 180 190
....*....|....*....|....*....|....
gi 1551428890 533 SIKVV-RGWLEPGL-QAEPGRAWQFERLGYFAAD 564
Cdd:pfam03950 142 SLKVLtEGLAEPALaNLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
51-386 |
1.55e-59 |
|
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: 198.08 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWqaesgENHLYFAS 130
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDW-----DEGPYRQS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 131 DYFDYMYGFAEALIEAGyayvdeqsaeeiranrgsltepgtdspwrdrpaaeslqrlremrdgkhpdgslvlraridmas 210
Cdd:cd00418 76 DRFDLYRAYAEELIKKG--------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 211 pninlrdpvlyrvrhahhhrtgdkwcIYPMYTWAHPVEDALEGITHSICTLEFEDQRPFYDWILArlaelgQLAEPLPHQ 290
Cdd:cd00418 93 --------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYE------ALGWEPPRF 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 291 YEFARLNLSY-VVTSKRKLlklvqdglvegwddprMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSLLEQALRDD 369
Cdd:cd00418 141 YHFPRLLLEDgTKLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFS 204
|
330
....*....|....*..
gi 1551428890 370 LDPVAeRAVAVLDPIKL 386
Cdd:cd00418 205 VERVN-SADATFDWAKL 220
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
51-376 |
1.02e-45 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 161.36 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 51 RIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPE--KENQEYVDAIKDTVHWLGFDWQAEsgenhlYF 128
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEV------VI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 129 ASDYFDYMYGFAEALIEAGYAYVdeqsaeeiranrgsltepgtdspwrdrpaaeslqrlremrdgkhpdgslvlraridm 208
Cdd:cd09287 75 ASDRIELYYEYARKLIEMGGAYV--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 209 aspninlrdpvlyrvrhahHHRTGDKWCIYPMYTWAHPVEDALEGITHSICTLEFED----QRPFYD---WILarlaelg 281
Cdd:cd09287 98 -------------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEyfgWEY------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 282 qlaeplPHQYEFARLNLSYVVTSKRKLLKLVQDGLVEGWDDPRMPTLVGLRRRGYTPSAIRLFCERIGVARADSRIDYSL 361
Cdd:cd09287 152 ------PETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWEN 225
|
330
....*....|....*
gi 1551428890 362 LEQALRDDLDPVAER 376
Cdd:cd09287 226 LYAINRKLIDPRANR 240
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
52-147 |
1.36e-17 |
|
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: 82.25 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 52 IRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDW---QAESGENHLYF 128
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWdegPDVGGPYGPYR 81
|
90
....*....|....*....
gi 1551428890 129 ASDYFDYMYGFAEALIEAG 147
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG 100
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
49-256 |
2.91e-14 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 73.73 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 49 PARIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDWQAEsgenhLYF 128
Cdd:PRK05710 3 MTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGP-----VLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 129 ASDYFDYmYGFA-EALIEAGYAYVDEQSAEEIRANRGSLTEPGTDSPWRDRPAAESLQRLREMrdgkhpdgslvlraRID 207
Cdd:PRK05710 78 QSQRHDA-YRAAlDRLRAQGLVYPCFCSRKEIAAAAPAPPDGGGIYPGTCRDLLHGPRNPPAW--------------RLR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1551428890 208 MASPNINLRDPVLYRVRHAHHHRTGDkwCI------YPMYTWAHPVEDALEGITH 256
Cdd:PRK05710 143 VPDAVIAFDDRLQGRQHQDLALAVGD--FVlrradgLFAYQLAVVVDDALQGVTH 195
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
38-258 |
3.18e-14 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 75.55 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 38 PASVQAQGQQDPARIRTRFPPEPNGYLHIGHAKSICLNFGLARDYGGVCHLRFDDTNPEKENQEYVDAIKDTVHWLGFDW 117
Cdd:PLN02627 32 SVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 118 QA---ESGENHLYFASDYFDYMYGFAEALIEAGYAYVDEQSAEEIRANRGSLTE----PGTDSPWRDRPAAESLQrlrEM 190
Cdd:PLN02627 112 DEgpdVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELkklpPRYTGKWATASDEEVQA---EL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 191 RDG-------KHPDGSlvlRARID-----MASPNIN-LRDPVLYRvrhahhhRTGdkwciYPMYTWAHPVEDALEGITHS 257
Cdd:PLN02627 189 AKGtpytyrfRVPKEG---SVKIDdlirgEVSWNTDtLGDFVLLR-------SNG-----QPVYNFCVAVDDATMGITHV 253
|
.
gi 1551428890 258 I 258
Cdd:PLN02627 254 I 254
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
54-117 |
6.22e-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: 57.87 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1551428890 54 TRFPPEPNGYLHIGHAKSICLNFGLARD-----YGGVCHLRFDDTNPEKENQ---------EYVDA----IKDTVHWLgF 115
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDPankkgenakAFVERwierIKEDVEYM-F 80
|
..
gi 1551428890 116 DW 117
Cdd:cd00802 81 LQ 82
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
54-118 |
4.00e-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: 54.47 E-value: 4.00e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1551428890 54 TRFPPEPnGYLHIGHAKSICLNFGLArdygGVCHLRFDDTNPEKENQ------EYVDAIKDTVHWLGFDWQ 118
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQdpheleERKESIEEDISVCGEDFQ 67
|
|
| |
