|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
2-568 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1156.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 2 NTDRNDAPAPSNFIRNIIEDDNRSGKWsQRVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVE 81
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKH-TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 82 YVDSIIDAVKWLGFEWNkngtEHKYFASDYYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGIDSPYRTRTPDE 161
Cdd:PRK05347 80 YVDSIKEDVRWLGFDWS----GELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 162 NLDLFRRMKAGEFKEGEHVLRAKIDMGSPNFNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLE 241
Cdd:PRK05347 156 NLDLFERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 242 FEDHRPLYDWFLAQLaddgvFERPLPQQIEFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIR 321
Cdd:PRK05347 236 FEDHRPLYDWVLDNL-----PIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 322 LMVERVGVTKVDSWIDMSILEGALRDDLDDKAPRAIAVLDPLKLIIDNYPEGQSEACSAPVHPHHPDRGVRSFPFSRELW 401
Cdd:PRK05347 311 EFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 402 IEREDFQETPPKGYFRLFPGNKVRLKYGFVVECTGADKDENGNVIAVHCNYFPDSRSGtEGANNYKVKGTIHWVSAASAY 481
Cdd:PRK05347 391 IEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG-NPADGRKVKGTIHWVSAAHAV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 482 AAEVRLYDRLFKEPQPGAGGaEFLDALNPDSKRVVNAYLEPSAREANAEDRFQFERHGYFVADRvDSQPGKPVFNRIVGL 561
Cdd:PRK05347 470 PAEVRLYDRLFTVPNPAAGK-DFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADK-DSTPGKLVFNRTVGL 547
|
....*..
gi 636794924 562 RDSWGKP 568
Cdd:PRK05347 548 RDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
32-565 |
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: 698.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 32 VETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNKNGTehkyFASDY 111
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIR----YSSDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 112 YDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGIDSPYRTRTPDENLDLFRRMKAGEFKEGEHVLRAKIDMGSPN 191
Cdd:TIGR00440 77 FDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 192 FNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLaqladDGVFERPLPQQIE 271
Cdd:TIGR00440 157 PVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVL-----DNIHIFPRPAQYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 272 FSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDDLDD 351
Cdd:TIGR00440 232 FSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 352 KAPRAIAVLDPLKLIIDNYpEGQSEACSAPVHPHHPDRGVRSFPFSRELWIEREDFQETPPKGYFRLFPGNKVRLKYGFV 431
Cdd:TIGR00440 312 NAPRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 432 VECTGADKDENGNVIAVHCNYFPDSRsGTEGANNYKVKGTIHWVSAASAYAAEVRLYDRLFKEPQPGAgGAEFLDALNPD 511
Cdd:TIGR00440 391 IKAERVEKDAAGKITTIFCTYDNKTL-GKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGA-PDDFLSVINPE 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 636794924 512 SKRVVNAYLEPSAREANAEDRFQFERHGYFVADRVDSQPGKPVFNRIVGLRDSW 565
Cdd:TIGR00440 469 SLVIKQGFMEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
31-355 |
3.91e-139 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 402.79 E-value: 3.91e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNkngteHKYFASD 110
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-----KVTYASD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 111 YYDKLYEYAEMLIKKGQAYVdsqtaeemratrgsateagidspyrtrtpdenldlfrrmkagefkegehvlrakidmgsp 190
Cdd:cd00807 76 YFDQLYEYAEQLIKKGKAYV------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 nfnmrdpviyrirfahHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLAQLaddgvfERPLPQQI 270
Cdd:cd00807 96 ----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL------RLYRPHQW 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 271 EFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDDLD 350
Cdd:cd00807 154 EFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLN 233
|
....*
gi 636794924 351 DKAPR 355
Cdd:cd00807 234 PTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
29-543 |
1.25e-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: 389.54 E-value: 1.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 29 SQRVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNkngtEHKYFA 108
Cdd:COG0008 2 GMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWD----EGPYYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 109 SDYYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGI----DSPYRTRTPDEnldLFRRMKAGEfkegEHVLRAK 184
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKppryDGRCRDLSPEE---LERMLAAGE----PPVLRFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 185 I--------DMGS-----PNFNMRDPVIYRirfahhyRTGdtwciYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDW 251
Cdd:COG0008 151 IpeegvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIW 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 252 FLAQLAddgvFERPlpqqiEFSRLNLTY----AITSKRKllqlvqdNHVegwddprmpTIVGVRRRGFTPESIRLMVERV 327
Cdd:COG0008 219 LYEALG----WEPP-----EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 328 GVTKVDSW--IDMSILEGALrdDLDDKaPRAIAVLDPLKLIIDNYPEGQS---EACSAPVHPHHPDRGVRS-----FPFS 397
Cdd:COG0008 274 GWSKSDDQeiFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlddEELAELLAPELPEAGIREdlerlVPLV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 398 RE--------------LWIEREDfqETPPKGyfRLFPGNkVRlkygFVVECTGAdkdengnVIAVHCNYFPDSrsgtega 463
Cdd:COG0008 351 REraktlselaelarfFFIERED--EKAAKK--RLAPEE-VR----KVLKAALE-------VLEAVETWDPET------- 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 464 nnykVKGTIHWVSAasayAAEVRlyDRLFKEPqpgaggaefldalnpdsKRVV--NAYLEPSAR---EANAEDRFqFERH 538
Cdd:COG0008 408 ----VKGTIHWVSA----EAGVK--DGLLFMP-----------------LRVAltGRTVEPSLFdvlELLGKERV-FERL 459
|
....*
gi 636794924 539 GYFVA 543
Cdd:COG0008 460 GYAID 464
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
32-351 |
1.72e-128 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 378.59 E-value: 1.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 32 VETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNkngtEHKYFASDY 111
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD----YGPYYQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 112 YDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGidSPYRTRTPDENLDLFRR-MKAGEFKEGEHVLRAKIDMGSP 190
Cdd:pfam00749 78 FDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALG--SPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMESP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 nFNMRDPVIYRIRFA---HHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLAQLaddGVfeRPLP 267
Cdd:pfam00749 156 -YVFRDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDAL---GW--EPPP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 268 QQIEFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSW-IDMSILEGALR 346
Cdd:pfam00749 230 FIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDR 309
|
....*
gi 636794924 347 DDLDD 351
Cdd:pfam00749 310 KKLDW 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
2-568 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1156.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 2 NTDRNDAPAPSNFIRNIIEDDNRSGKWsQRVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVE 81
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKH-TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 82 YVDSIIDAVKWLGFEWNkngtEHKYFASDYYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGIDSPYRTRTPDE 161
Cdd:PRK05347 80 YVDSIKEDVRWLGFDWS----GELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 162 NLDLFRRMKAGEFKEGEHVLRAKIDMGSPNFNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLE 241
Cdd:PRK05347 156 NLDLFERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 242 FEDHRPLYDWFLAQLaddgvFERPLPQQIEFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIR 321
Cdd:PRK05347 236 FEDHRPLYDWVLDNL-----PIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 322 LMVERVGVTKVDSWIDMSILEGALRDDLDDKAPRAIAVLDPLKLIIDNYPEGQSEACSAPVHPHHPDRGVRSFPFSRELW 401
Cdd:PRK05347 311 EFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 402 IEREDFQETPPKGYFRLFPGNKVRLKYGFVVECTGADKDENGNVIAVHCNYFPDSRSGtEGANNYKVKGTIHWVSAASAY 481
Cdd:PRK05347 391 IEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG-NPADGRKVKGTIHWVSAAHAV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 482 AAEVRLYDRLFKEPQPGAGGaEFLDALNPDSKRVVNAYLEPSAREANAEDRFQFERHGYFVADRvDSQPGKPVFNRIVGL 561
Cdd:PRK05347 470 PAEVRLYDRLFTVPNPAAGK-DFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADK-DSTPGKLVFNRTVGL 547
|
....*..
gi 636794924 562 RDSWGKP 568
Cdd:PRK05347 548 RDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
1-569 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 869.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 1 MNTDRNDAPAPSNFIRNIIEDDNRSGKWsQRVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESV 80
Cdd:PRK14703 2 SDAPRPRMLVSPNFITEIIEEDLEAGRY-PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 81 EYVDSIIDAVKWLGFEWNkngtEHKYFASDYYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGIDSPYRTRTPD 160
Cdd:PRK14703 81 EYVEAIKDDVRWLGFDWG----EHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 161 ENLDLFRRMKAGEFKEGEHVLRAKIDMGSPNFNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTL 240
Cdd:PRK14703 157 ENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 241 EFEDHRPLYDWFLAQLADdgvfERPLPQQIEFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESI 320
Cdd:PRK14703 237 EFENNRAIYDWVLDHLGP----WPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 321 RLMVERVGVTKVDSWIDMSILEGALRDDLDDKAPRAIAVLDPLKLIIDNYPEGQSEACSAPVHPHHPDR-GVRSFPFSRE 399
Cdd:PRK14703 313 RDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKeGSRKVPFTRE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 400 LWIEREDFQETPPKGYFRLFPGNKVRLKYGFVVECTGADKDENGNVIAVHCNYFPDSRSGTEGANnyKVKGTIHWVSAAS 479
Cdd:PRK14703 393 LYIERDDFSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDTGR--KAAGVIHWVSAKH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 480 AYAAEVRLYDRLFKEPQPGAGGAEFLDALNPDSKRVVNAYLEPSAREANAEDRFQFERHGYFVADRVDSQPGKPVFNRIV 559
Cdd:PRK14703 471 ALPAEVRLYDRLFKVPQPEAADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRII 550
|
570
....*....|
gi 636794924 560 GLRDSWGKPA 569
Cdd:PRK14703 551 TLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
32-565 |
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: 698.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 32 VETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNKNGTehkyFASDY 111
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIR----YSSDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 112 YDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGIDSPYRTRTPDENLDLFRRMKAGEFKEGEHVLRAKIDMGSPN 191
Cdd:TIGR00440 77 FDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 192 FNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLaqladDGVFERPLPQQIE 271
Cdd:TIGR00440 157 PVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVL-----DNIHIFPRPAQYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 272 FSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDDLDD 351
Cdd:TIGR00440 232 FSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 352 KAPRAIAVLDPLKLIIDNYpEGQSEACSAPVHPHHPDRGVRSFPFSRELWIEREDFQETPPKGYFRLFPGNKVRLKYGFV 431
Cdd:TIGR00440 312 NAPRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 432 VECTGADKDENGNVIAVHCNYFPDSRsGTEGANNYKVKGTIHWVSAASAYAAEVRLYDRLFKEPQPGAgGAEFLDALNPD 511
Cdd:TIGR00440 391 IKAERVEKDAAGKITTIFCTYDNKTL-GKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGA-PDDFLSVINPE 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 636794924 512 SKRVVNAYLEPSAREANAEDRFQFERHGYFVADRVDSQPGKPVFNRIVGLRDSW 565
Cdd:TIGR00440 469 SLVIKQGFMEHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
31-568 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 572.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNKngtehKYFASD 110
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFK-----ITYTSD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 111 YYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRgsatEAGIDSPYRTRTPDENLDLFRRMKAGEFKEGEHVLRAKIDMGSP 190
Cdd:PLN02859 339 YFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQND 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 NFNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLAQLaddGVFerpLPQQI 270
Cdd:PLN02859 415 NFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL---GLY---QPYVW 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 271 EFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVD-SWIDMSILEGALRDDL 349
Cdd:PLN02859 489 EYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDnSLIRMDRLEHHIREEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 350 DDKAPRAIAVLDPLKLIIDNYPEGQSEACSAPVHPHHPDRGVRSF---PFSRELWIEREDFQETPPKGYFRLFPGNKVRL 426
Cdd:PLN02859 569 NKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFykvPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 427 KYGFVVECTG-ADKDENGNVIAVHCNYFPDSRSgtegannyKVKGTIHWVSAAS----AYAAEVRLYDRLFKEPQPgAGG 501
Cdd:PLN02859 649 RYAFPIKCTDvVLADDNETVVEIRAEYDPEKKT--------KPKGVLHWVAEPSpgvePLKVEVRLFDKLFLSENP-AEL 719
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636794924 502 AEFLDALNPDSKRVVN-AYLEPSAREANAEDRFQFERHGYFVADRvDSQPGKPVFNRIVGLRDSWGKP 568
Cdd:PLN02859 720 EDWLEDLNPQSKEVISgAYAVPSLKDAKVGDRFQFERLGYFAVDK-DSTPEKLVFNRTVTLKDSYGKG 786
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
35-569 |
9.30e-167 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 486.03 E-value: 9.30e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 35 RFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFE--WNKngtehkyFASDYY 112
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKpdWVT-------FSSDYF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 113 DKLYEYAEMLIKKGQAYVDSQTAEEMRATRgsatEAGIDSPYRTRTPDENLDLFRRMKAGEFKEGEHVLRAKIDMGSPNF 192
Cdd:PTZ00437 128 DQLHEFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 193 NMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLAQLAddgvFERplPQQIEF 272
Cdd:PTZ00437 204 NMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELN----LWR--PHVWEF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 273 SRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDDLDDK 352
Cdd:PTZ00437 278 SRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDER 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 353 APRAIAVLDPLKLIIDNYpEGQSEAcSAPVHPHHPDRGVRSFPFSRELWIEREDFQ-ETPPKGYFRLFPGNK-VRLKYGF 430
Cdd:PTZ00437 358 CERRLMVIDPIKVVVDNW-KGEREF-ECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGPRvVGLKYSG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 431 VVECTGADKDENGNVIAVHCNyfpdsrsgTEGANNYKVKGTIHWVSAASAYAAEVRLYDRLFKEPQpGAGGAEFLDALNP 510
Cdd:PTZ00437 436 NVVCKGFEVDAAGQPSVIHVD--------IDFERKDKPKTNISWVSATACTPVEVRLYNALLKDDR-AAIDPEFLKFIDE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 636794924 511 DSKRVVNAYLEPSAREANAEDRFQFERHGYFVADRvDSQPGKPVFNRIVGLRDSWGKPA 569
Cdd:PTZ00437 507 DSEVVSHGYAEKGIENAKHFESVQAERFGYFVVDP-DTRPDHLVMNRVLGLREDKEKAT 564
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
31-355 |
3.91e-139 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 402.79 E-value: 3.91e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNkngteHKYFASD 110
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-----KVTYASD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 111 YYDKLYEYAEMLIKKGQAYVdsqtaeemratrgsateagidspyrtrtpdenldlfrrmkagefkegehvlrakidmgsp 190
Cdd:cd00807 76 YFDQLYEYAEQLIKKGKAYV------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 nfnmrdpviyrirfahHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLAQLaddgvfERPLPQQI 270
Cdd:cd00807 96 ----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL------RLYRPHQW 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 271 EFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDDLD 350
Cdd:cd00807 154 EFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLN 233
|
....*
gi 636794924 351 DKAPR 355
Cdd:cd00807 234 PTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
29-543 |
1.25e-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: 389.54 E-value: 1.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 29 SQRVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNkngtEHKYFA 108
Cdd:COG0008 2 GMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWD----EGPYYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 109 SDYYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGI----DSPYRTRTPDEnldLFRRMKAGEfkegEHVLRAK 184
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKppryDGRCRDLSPEE---LERMLAAGE----PPVLRFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 185 I--------DMGS-----PNFNMRDPVIYRirfahhyRTGdtwciYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDW 251
Cdd:COG0008 151 IpeegvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIW 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 252 FLAQLAddgvFERPlpqqiEFSRLNLTY----AITSKRKllqlvqdNHVegwddprmpTIVGVRRRGFTPESIRLMVERV 327
Cdd:COG0008 219 LYEALG----WEPP-----EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 328 GVTKVDSW--IDMSILEGALrdDLDDKaPRAIAVLDPLKLIIDNYPEGQS---EACSAPVHPHHPDRGVRS-----FPFS 397
Cdd:COG0008 274 GWSKSDDQeiFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlddEELAELLAPELPEAGIREdlerlVPLV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 398 RE--------------LWIEREDfqETPPKGyfRLFPGNkVRlkygFVVECTGAdkdengnVIAVHCNYFPDSrsgtega 463
Cdd:COG0008 351 REraktlselaelarfFFIERED--EKAAKK--RLAPEE-VR----KVLKAALE-------VLEAVETWDPET------- 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 464 nnykVKGTIHWVSAasayAAEVRlyDRLFKEPqpgaggaefldalnpdsKRVV--NAYLEPSAR---EANAEDRFqFERH 538
Cdd:COG0008 408 ----VKGTIHWVSA----EAGVK--DGLLFMP-----------------LRVAltGRTVEPSLFdvlELLGKERV-FERL 459
|
....*
gi 636794924 539 GYFVA 543
Cdd:COG0008 460 GYAID 464
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
32-351 |
1.72e-128 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 378.59 E-value: 1.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 32 VETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNkngtEHKYFASDY 111
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWD----YGPYYQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 112 YDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGidSPYRTRTPDENLDLFRR-MKAGEFKEGEHVLRAKIDMGSP 190
Cdd:pfam00749 78 FDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQEALG--SPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMESP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 nFNMRDPVIYRIRFA---HHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLAQLaddGVfeRPLP 267
Cdd:pfam00749 156 -YVFRDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDAL---GW--EPPP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 268 QQIEFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSW-IDMSILEGALR 346
Cdd:pfam00749 230 FIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDR 309
|
....*
gi 636794924 347 DDLDD 351
Cdd:pfam00749 310 KKLDW 314
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
31-554 |
1.91e-107 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 338.24 E-value: 1.91e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNKngtehKYFASD 110
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDA-----VTYTSD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 111 YYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGsateAGIDSPYRTRTPDENLDLFRRMKAGEFKEGEHVLRAKIDMGSP 190
Cdd:PLN02907 288 YFPQLMEMAEKLIKEGKAYVDDTPREQMRKERM----DGIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDP 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 NFNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFlaqLADDGVfeRPLpqQI 270
Cdd:PLN02907 364 NKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRI---LEDMGL--RKV--HI 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 271 -EFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDDL 349
Cdd:PLN02907 437 wEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKII 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 350 DDKAPRAIAVLDPLKLIID--NYPEgQSEACSAPVHPHHPDRGVRSFPFSRELWIEREDfQETPPKGyfrlfpgnkvrlk 427
Cdd:PLN02907 517 DPVCPRHTAVLKEGRVLLTltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD-AEAISEG------------- 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 428 ygfvVECTGAD----------KDENGNVIAVHCNYFPdsrsgtEGAnnykVKGT---IHWVSAASAYaAEVRL--YDRLF 492
Cdd:PLN02907 582 ----EEVTLMDwgnaiikeitKDEGGAVTALSGELHL------EGS----VKTTklkLTWLPDTNEL-VPLSLveFDYLI 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636794924 493 KEPQPGAGGaEFLDALNPDSKRVVNAYLEPSAREANAEDRFQFERHGYFVADRVDSQPGKPV 554
Cdd:PLN02907 647 TKKKLEEDD-NFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSSKPI 707
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
31-554 |
3.96e-104 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 324.88 E-value: 3.96e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVE---YvDSIIDAVKWLGFEWNKngtehKYF 107
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPDpeaY-DMILEDLKWLGVKWDE-----VVI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 108 ASDYYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRgsatEAGIDSPYRTRTPDENLDLFRRMKAGEFKEGEHVLRAKIDM 187
Cdd:PRK04156 175 QSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 188 GSPNFNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHslcTLEFEDH-------RPLYDWFlaqladdg 260
Cdd:PRK04156 251 EHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTH---VLRGKDHidntekqRYIYDYF-------- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 261 vfERPLPQQIEFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIR-LMVErVGVTKVDSWIDMS 339
Cdd:PRK04156 320 --GWEYPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIReLIIE-VGVKETDATISWE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 340 ILEGALRDDLDDKAPRAIAVLDPLKLIIDNYPEGQSEacsAPVHPHHPDRGVRSFPFSRELWIEREDFQETppkgyfrlf 419
Cdd:PRK04156 397 NLYAINRKLIDPIANRYFFVRDPVELEIEGAEPLEAK---IPLHPDRPERGEREIPVGGKVYVSSDDLEAE--------- 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 420 pGNKVRLKYGFVVECTGADKDEngnvIAVHCNYFPDSRSgtegaNNYKVkgtIHWVSAASAYAAEVRlydrlfkEPQPGa 499
Cdd:PRK04156 465 -GKMVRLMDLFNVEITGVSVDK----ARYHSDDLEEARK-----NKAPI---IQWVPEDESVPVRVL-------KPDGG- 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 636794924 500 ggaefldalnpdskrVVNAYLEPSAREANAEDRFQFERHGyFVadRVDSQPGKPV 554
Cdd:PRK04156 524 ---------------DIEGLAEPDVADLEVDDIVQFERFG-FV--RIDSVEDDEV 560
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
31-553 |
1.16e-100 |
|
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: 315.61 E-value: 1.16e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNKngtehKYFASD 110
Cdd:TIGR00463 93 EVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDE-----VVYQSD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 111 YYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSateaGIDSPYRTRTPDENLDLFRRMKAGEFKEGEHVLRAKIDMGSP 190
Cdd:TIGR00463 168 RIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 NFNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDH--RPLYDWFLAQLaddgvfERPLPQ 268
Cdd:TIGR00463 244 NPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNrrKQEYIYRYFGW------EPPEFI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 269 QIEFSRLNLTYAITSKRKlLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDD 348
Cdd:TIGR00463 318 HWGRLKIDDVRALSTSSA-RKGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 349 LDDKAPRAIAVLDPLKLIIDNYPEGQSEacSAPVHPHHPDRGVRSFPFSRELWIEREDFQETPpkgyfrlfpgNKVRLKy 428
Cdd:TIGR00463 397 IDEEARRYFFIWNPVKIEIVGLPEPKRV--ERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRLM- 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 429 gfvvectgadkdENGNVI--AVHCNYFPDsrsGTEGANNYKvKGTIHWVSAASAYAAEVRLYDRLFKEpqpgaggaefld 506
Cdd:TIGR00463 464 ------------DAVNVIysKKELRYHSE---GLEGARKLG-KSIIHWLPAKDAVKVKVIMPDASIVE------------ 515
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 636794924 507 alnpdskrvvnAYLEPSAREANAEDRFQFERHGYFVADRVDsQPGKP 553
Cdd:TIGR00463 516 -----------GVIEADASELEVGDVVQFERFGFARLDSAD-KDGMV 550
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
31-552 |
1.88e-94 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 300.73 E-value: 1.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNKNGTehkyFASD 110
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPT----YSSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 111 YYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSateaGIDSPYRTRTPDENLDLFRRMKAGEFKEGEHVLRAKIDMGSP 190
Cdd:PTZ00402 128 YMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 NFNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLAQLAddgvFERPLPQqi 270
Cdd:PTZ00402 204 NKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALG----IRKPIVE-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 271 EFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDDLD 350
Cdd:PTZ00402 278 DFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 351 DKAPRAIAVLDPLKLIIDNYPEGQSEACSAPVHPHHPDRGVRSFPFSRELWIEREDFQetppkgyfRLFPGNKVRL---- 426
Cdd:PTZ00402 358 PSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVA--------LLKEGDEVTLmdwg 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 427 -KYGFVVECTGADKDENGNVIAVHcnyfpdsrsgTEGaNNYKVKGTIHWVSAA-SAYAAEVRLYDRLF--KEPQPgaggA 502
Cdd:PTZ00402 430 nAYIKNIRRSGEDALITDADIVLH----------LEG-DVKKTKFKLTWVPESpKAEVMELNEYDHLLtkKKPDP----E 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 636794924 503 EFLDA-LNPDSKRVVNAYLEPSAREANAEDRFQFERHGYFVADrvDSQPGK 552
Cdd:PTZ00402 495 ESIDDiIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVD--DVTPKK 543
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
31-554 |
1.66e-91 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 290.76 E-value: 1.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEwnkngTEHKYFASD 110
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-----PDSVSFTSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 111 YYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEagidSPYRTRTPDENLDLFRRMKAGEFKEGEHVLRAKIDMGSP 190
Cdd:PLN03233 86 YFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 NFNMRDPVIYRIRFAHHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLAQLAddgvFERPLPQQi 270
Cdd:PLN03233 162 NGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALG----LRRPRIHA- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 271 eFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDDLD 350
Cdd:PLN03233 237 -FARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 351 DKAPRAIAV--LDPLKLIIDNYPEGQSEA-CSAPVHPHHPDRGVRSFPFSRELWIEREDFQEtppkgyfrLFPGNKVRLK 427
Cdd:PLN03233 316 KRAKRFMAIdkADHTALTVTNADEEADFAfSETDCHPKDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 428 YGFVVECTGADKDENGNVIavhcnyfPDSrsgteganNYK-VKGTIHWVSAASAyAAEVRLY--DRLFKEPQPGAGGaEF 504
Cdd:PLN03233 388 RWGVIEISKIDGDLEGHFI-------PDG--------DFKaAKKKISWIADVSD-NIPVVLSefDNLIIKEKLEEDD-KF 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 636794924 505 LDALNPDSKRVVNAYLEPSAREANAEDRFQFERHGYFVADRVDSQPGKPV 554
Cdd:PLN03233 451 EDFINPDTLAETDVIGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPL 500
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
353-544 |
8.89e-74 |
|
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: 232.55 E-value: 8.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 353 APRAIAVLDPLKLIIDNYPEGQSEACSAPVHPHHPDRGVRSFPFSRELWIEREDFqetppkgyFRLFPGNKVRLKYGFVV 432
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 433 ECTGADKDENGNVIAVHCNYFPDSRSGteganNYKVKG-TIHWVSAASAYAAEVRLYDRLFKEPQpgagGAEFLdaLNPD 511
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGG-----ARKVKGkIIHWVSASDAVPAEVRLYDRLFKDED----DADFL--LNPD 141
|
170 180 190
....*....|....*....|....*....|....
gi 636794924 512 SKRVV-NAYLEPSAREANAEDRFQFERHGYFVAD 544
Cdd:pfam03950 142 SLKVLtEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
31-365 |
2.24e-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: 191.92 E-value: 2.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNkngtEHKYFASD 110
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWD----EGPYRQSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 111 YYDKLYEYAEMLIKKGqayvdsqtaeemratrgsateagidspyrtrtpdenldlfrrmkagefkegehvlrakidmgsp 190
Cdd:cd00418 77 RFDLYRAYAEELIKKG---------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 191 nfnmrdpviyrirfahhyrtgdtwcIYPMYDYAHCVSDAIENITHSLCTLEFEDHRPLYDWFLAQladdgvFERPLPQQI 270
Cdd:cd00418 93 -------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEA------LGWEPPRFY 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 271 EFSRLNLTYA-ITSKRKLlqlvqdnhvegwddprMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGALRDDL 349
Cdd:cd00418 142 HFPRLLLEDGtKLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSV 205
|
330
....*....|....*.
gi 636794924 350 DDKAPrAIAVLDPLKL 365
Cdd:cd00418 206 ERVNS-ADATFDWAKL 220
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
31-355 |
1.20e-44 |
|
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: 158.28 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 31 RVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESV--EYVDSIIDAVKWLGFEWNKngtehKYFA 108
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDE-----VVIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 109 SDYYDKLYEYAEMLIKKGQAYVdsqtaeemratrgsateagidspyrtrtpdenldlfrrmkagefkegehvlrakidmg 188
Cdd:cd09287 76 SDRIELYYEYARKLIEMGGAYV---------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 189 spnfnmrdpviyrirfahHYRTGDTWCIYPMYDYAHCVSDAIENITHSLCTLEFED----HRPLYDWFLAQLaddgvfer 264
Cdd:cd09287 98 ------------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEYFGWEY-------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 265 plPQQIEFSRLNLTYAITSKRKLLQLVQDNHVEGWDDPRMPTIVGVRRRGFTPESIRLMVERVGVTKVDSWIDMSILEGA 344
Cdd:cd09287 152 --PETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAI 229
|
330
....*....|.
gi 636794924 345 LRDDLDDKAPR 355
Cdd:cd09287 230 NRKLIDPRANR 240
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
32-126 |
4.46e-18 |
|
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: 83.79 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 32 VETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWN----KNGTEHKYF 107
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDegpdVGGPYGPYR 81
|
90
....*....|....*....
gi 636794924 108 ASDYYDKLYEYAEMLIKKG 126
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
29-247 |
1.83e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 69.77 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 29 SQRVETRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWN----KNGTEH 104
Cdd:PLN02627 43 GGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdVGGEYG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 105 KYFASDYYDKLYEYAEMLIKKGQAYVDSQTAEEMRATRGSATEAGIDSPY----RTRTPDEnldlfrrmkagefkegehv 180
Cdd:PLN02627 123 PYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYtgkwATASDEE------------------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 181 LRAKIDMGSP-NFNMRDPVIYRIRFAHHYRTGDTWCI-------------YPMYDYAHCVSDAIENITHslcTLEFEDHR 246
Cdd:PLN02627 184 VQAELAKGTPyTYRFRVPKEGSVKIDDLIRGEVSWNTdtlgdfvllrsngQPVYNFCVAVDDATMGITH---VIRAEEHL 260
|
.
gi 636794924 247 P 247
Cdd:PLN02627 261 P 261
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
34-129 |
4.19e-10 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 61.02 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 34 TRFPPEPNGYLHIGHAKSICVNFGLAAQYGGVCHLRFDDTNPEKESVEYVDSIIDAVKWLGFEWNkngtEHKYFASDYYD 113
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWD----GPVLYQSQRHD 83
|
90
....*....|....*..
gi 636794924 114 kLYEYA-EMLIKKGQAY 129
Cdd:PRK05710 84 -AYRAAlDRLRAQGLVY 99
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
34-114 |
1.98e-08 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 53.25 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 34 TRFPPEPNGYLHIGHAKSICVNFGLA-----AQYGGVCHLRFDDTNP------------EKESVE-YVDSIIDAVKWLgf 95
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAqayrkLGYKVRCIALIDDAGGligdpankkgenAKAFVErWIERIKEDVEYM-- 79
|
90
....*....|....*....
gi 636794924 96 ewnkngTEHKYFASDYYDK 114
Cdd:cd00802 80 ------FLQAADFLLLYET 92
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
34-121 |
4.12e-07 |
|
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: 48.69 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636794924 34 TRFPPEPnGYLHIGHAKSICVNFGLAaqygGVCHLRFDDTNPEK------ESVEYVDSIIDAVKWLGFEWNKNgtehkyf 107
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQN------- 69
|
90
....*....|....
gi 636794924 108 aSDYYDKLYEYAEM 121
Cdd:cd02156 70 -RELYRWVKDNITL 82
|
|
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