|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-587 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1125.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 1 MTHAPTPPAASNFLRPIIEDDLQANRFQgklwagkpgpaalqaqgqpdpaRIRTRFPPEPNGYLHIGHAKSICVNFGLAR 80
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHT----------------------RVHTRFPPEPNGYLHIGHAKSICLNFGLAQ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 81 DYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgNDNLYFASDYFEFMYEFAEALVQAGHAYVDEQSAEEIRA 160
Cdd:PRK05347 59 DYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDW----SGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIRE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 161 SRGTLTEPGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASPNINLRDPVMYRVRHATHHRTGNAWCIYPMY 240
Cdd:PRK05347 135 YRGTLTEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 241 SWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLaelgkLARPLPHQYEFARLNLTYVVTSKRKLLQLVREGYVDGWD 320
Cdd:PRK05347 215 DFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNL-----PIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 321 DPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLDPVAPRSVAVLDPLKLVITNYPEGRSETCSA 400
Cdd:PRK05347 290 DPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 401 PRNPHDPQAGVREFPFTRELWIEQDDFREEPPKKYFRLFPGNTVRLKYGYVVRCTGFTKDESGKVVEVQAEYLPDTKSGt 480
Cdd:PRK05347 370 PNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 481 PGADSVKVKGNITWVSAAHAVPAQVHLYDRLFADAHPDGGdKDFLACLNPNSKQTVQAWLEPGI-EAVPGATWQFERLGY 559
Cdd:PRK05347 449 NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPNPAAG-KDFLDFLNPDSLVIKQGFVEPSLaDAKPEDRFQFEREGY 527
|
570 580
....*....|....*....|....*...
gi 489917582 560 FTVDsKDSRPEAPVLNRIVTLRDSWQAA 587
Cdd:PRK05347 528 FCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
52-584 |
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: 657.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 52 IRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWQAdgndNLYFASDY 131
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEG----KIRYSSDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 132 FEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTLTEPGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASPN 211
Cdd:TIGR00440 77 FDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 212 INLRDPVMYRVRHATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgklARPLPHQYE 291
Cdd:TIGR00440 157 PVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIH-----IFPRPAQYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 292 FARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLDP 371
Cdd:TIGR00440 232 FSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 372 VAPRSVAVLDPLKLVITNYpEGRSETCSAPRNPHDPQAGVREFPFTRELWIEQDDFREEPPKKYFRLFPGNTVRLKYGYV 451
Cdd:TIGR00440 312 NAPRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 452 VRCTGFTKDESGKVVEVQAEYLPDTKSGTPgADSVKVKGNITWVSAAHAVPAQVHLYDRLFADAHPdGGDKDFLACLNPN 531
Cdd:TIGR00440 391 IKAERVEKDAAGKITTIFCTYDNKTLGKEP-ADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNP-GAPDDFLSVINPE 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 489917582 532 SKQTVQAWLEPGI-EAVPGATWQFERLGYFTVDSKDSRPEAPVLNRIVTLRDSW 584
Cdd:TIGR00440 469 SLVIKQGFMEHSLgDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
51-375 |
4.24e-138 |
|
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: 400.86 E-value: 4.24e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgnDNLYFASD 130
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-----YKVTYASD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 131 YFEFMYEFAEALVQAGHAYVdeqsaeeirasrgtltepgtdspwrdrpadesllrlremrdgkhpdgslvlraridmasp 210
Cdd:cd00807 76 YFDQLYEYAEQLIKKGKAYV------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 211 ninlrdpvmyrvrhatHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILArlaelgKLARPLPHQY 290
Cdd:cd00807 96 ----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCD------ALRLYRPHQW 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 291 EFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLD 370
Cdd:cd00807 154 EFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLN 233
|
....*
gi 489917582 371 PVAPR 375
Cdd:cd00807 234 PTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
51-501 |
9.49e-135 |
|
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: 401.09 E-value: 9.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgNDNLYFASD 130
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDW----DEGPYYQSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 131 YFEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTLTEPGT----DSPWRDRPADEsllrLREMRD-GKHPdgslVLRARI 205
Cdd:COG0008 80 RFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKppryDGRCRDLSPEE----LERMLAaGEPP----VLRFKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 206 --------DMAS-----PNINLRDPVMYRVrhathhrTGnawciYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWI 272
Cdd:COG0008 152 peegvvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 273 LARLAElgklarPLPhqyEFARLNLTY----VVTSKRKllqlvreGYVdgwddprmpTLFGLRRRGYTPSSIRLFCDRTA 348
Cdd:COG0008 220 YEALGW------EPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 349 VSKSDSR--IDYSLLEQAVrdDLDPVaPRSVAVLDPLKLVITNYPEGR-------SETCSaprnPHDPQAGV-----REF 414
Cdd:COG0008 275 WSKSDDQeiFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRalddeelAELLA----PELPEAGIredleRLV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 415 PFTRE--------------LWIEQDDfrEEPPKKyfRLFPGNTVRlkygyVVRCTgftkdesGKVVEVQAEYLPDTksgt 480
Cdd:COG0008 348 PLVREraktlselaelarfFFIERED--EKAAKK--RLAPEEVRK-----VLKAA-------LEVLEAVETWDPET---- 407
|
490 500
....*....|....*....|.
gi 489917582 481 pgadsvkVKGNITWVSAAHAV 501
Cdd:COG0008 408 -------VKGTIHWVSAEAGV 421
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
52-371 |
5.08e-127 |
|
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: 375.50 E-value: 5.08e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 52 IRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgNDNLYFASDY 131
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKW----DYGPYYQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 132 FEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTLtePGTDSPWRDRPADESL-LRLREMRDGKHPDGSLVLRARIDMASP 210
Cdd:pfam00749 78 FDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLhLFEEEMKKGSAEGGPATVRAKIPMESP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 211 nINLRDPVMYRVR---HATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgklARPLP 287
Cdd:pfam00749 156 -YVFRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-----WEPPP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 288 HQYEFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDS-RIDYSLLEQAVR 366
Cdd:pfam00749 230 FIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDR 309
|
....*
gi 489917582 367 DDLDP 371
Cdd:pfam00749 310 KKLDW 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-587 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1125.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 1 MTHAPTPPAASNFLRPIIEDDLQANRFQgklwagkpgpaalqaqgqpdpaRIRTRFPPEPNGYLHIGHAKSICVNFGLAR 80
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHT----------------------RVHTRFPPEPNGYLHIGHAKSICLNFGLAQ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 81 DYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgNDNLYFASDYFEFMYEFAEALVQAGHAYVDEQSAEEIRA 160
Cdd:PRK05347 59 DYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDW----SGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIRE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 161 SRGTLTEPGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASPNINLRDPVMYRVRHATHHRTGNAWCIYPMY 240
Cdd:PRK05347 135 YRGTLTEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 241 SWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLaelgkLARPLPHQYEFARLNLTYVVTSKRKLLQLVREGYVDGWD 320
Cdd:PRK05347 215 DFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNL-----PIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 321 DPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLDPVAPRSVAVLDPLKLVITNYPEGRSETCSA 400
Cdd:PRK05347 290 DPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 401 PRNPHDPQAGVREFPFTRELWIEQDDFREEPPKKYFRLFPGNTVRLKYGYVVRCTGFTKDESGKVVEVQAEYLPDTKSGt 480
Cdd:PRK05347 370 PNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 481 PGADSVKVKGNITWVSAAHAVPAQVHLYDRLFADAHPDGGdKDFLACLNPNSKQTVQAWLEPGI-EAVPGATWQFERLGY 559
Cdd:PRK05347 449 NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPNPAAG-KDFLDFLNPDSLVIKQGFVEPSLaDAKPEDRFQFEREGY 527
|
570 580
....*....|....*....|....*...
gi 489917582 560 FTVDsKDSRPEAPVLNRIVTLRDSWQAA 587
Cdd:PRK05347 528 FCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
1-584 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 828.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 1 MTHAPTP--PAASNFLRPIIEDDLQANRFQgklwagkpgpaalqaqgqpdpaRIRTRFPPEPNGYLHIGHAKSICVNFGL 78
Cdd:PRK14703 1 MSDAPRPrmLVSPNFITEIIEEDLEAGRYP----------------------RVVTRFPPEPNGYLHIGHAKSILLNFGI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 79 ARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgNDNLYFASDYFEFMYEFAEALVQAGHAYVDEQSAEEI 158
Cdd:PRK14703 59 ARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDW----GEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 159 RASRGTLTEPGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASPNINLRDPVMYRVRHATHHRTGNAWCIYP 238
Cdd:PRK14703 135 RELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 239 MYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAELgklaRPLPHQYEFARLNLTYVVTSKRKLLQLVREGYVDG 318
Cdd:PRK14703 215 MYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPW----PPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 319 WDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLDPVAPRSVAVLDPLKLVITNYPEGRSETC 398
Cdd:PRK14703 291 WDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEEL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 399 SAPRNPHD-PQAGVREFPFTRELWIEQDDFREEPPKKYFRLFPGNTVRLKYGYVVRCTGFTKDESGKVVEVQAEYLPDTK 477
Cdd:PRK14703 371 DLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 478 SGTPGAdsVKVKGNITWVSAAHAVPAQVHLYDRLFADAHPDGGDKDFLACLNPNSKQTVQAWLEPGIEAVPGAT-WQFER 556
Cdd:PRK14703 451 KGEDTG--RKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEAADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTrYQFER 528
|
570 580
....*....|....*....|....*...
gi 489917582 557 LGYFTVDSKDSRPEAPVLNRIVTLRDSW 584
Cdd:PRK14703 529 QGYFWADPVDSRPDALVFNRIITLKDTW 556
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
52-584 |
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: 657.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 52 IRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWQAdgndNLYFASDY 131
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEG----KIRYSSDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 132 FEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTLTEPGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASPN 211
Cdd:TIGR00440 77 FDELYRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 212 INLRDPVMYRVRHATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgklARPLPHQYE 291
Cdd:TIGR00440 157 PVMRDPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIH-----IFPRPAQYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 292 FARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLDP 371
Cdd:TIGR00440 232 FSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 372 VAPRSVAVLDPLKLVITNYpEGRSETCSAPRNPHDPQAGVREFPFTRELWIEQDDFREEPPKKYFRLFPGNTVRLKYGYV 451
Cdd:TIGR00440 312 NAPRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 452 VRCTGFTKDESGKVVEVQAEYLPDTKSGTPgADSVKVKGNITWVSAAHAVPAQVHLYDRLFADAHPdGGDKDFLACLNPN 531
Cdd:TIGR00440 391 IKAERVEKDAAGKITTIFCTYDNKTLGKEP-ADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNP-GAPDDFLSVINPE 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 489917582 532 SKQTVQAWLEPGI-EAVPGATWQFERLGYFTVDSKDSRPEAPVLNRIVTLRDSW 584
Cdd:TIGR00440 469 SLVIKQGFMEHSLgDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
51-584 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 551.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGfdWQADgndNLYFASD 130
Cdd:PLN02859 264 KVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WEPF---KITYTSD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 131 YFEFMYEFAEALVQAGHAYVDEQSAEEIRASRgtltEPGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASP 210
Cdd:PLN02859 339 YFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQND 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 211 NINLRDPVMYRVRHATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAELgklarpLPHQY 290
Cdd:PLN02859 415 NFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY------QPYVW 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 291 EFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSD-SRIDYSLLEQAVRDDL 369
Cdd:PLN02859 489 EYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDnSLIRMDRLEHHIREEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 370 DPVAPRSVAVLDPLKLVITNYPEGRSETCSA---PRNPHDPQAGVREFPFTRELWIEQDDFREEPPKKYFRLFPGNTVRL 446
Cdd:PLN02859 569 NKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 447 KYGYVVRCTGFT-KDESGKVVEVQAEYLPDTKSgtpgadsvKVKGNITWVSAA----HAVPAQVHLYDRLFADAHPDGGD 521
Cdd:PLN02859 649 RYAFPIKCTDVVlADDNETVVEIRAEYDPEKKT--------KPKGVLHWVAEPspgvEPLKVEVRLFDKLFLSENPAELE 720
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917582 522 kDFLACLNPNSKQTVQ-AWLEPGI-EAVPGATWQFERLGYFTVDsKDSRPEAPVLNRIVTLRDSW 584
Cdd:PLN02859 721 -DWLEDLNPQSKEVISgAYAVPSLkDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSY 783
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
55-582 |
3.58e-167 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 487.95 E-value: 3.58e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 55 RFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGfdWQADGndnLYFASDYFEF 134
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMG--WKPDW---VTFSSDYFDQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 135 MYEFAEALVQAGHAYVDEQSAEEIRASRgtltEPGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASPNINL 214
Cdd:PTZ00437 130 LHEFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 215 RDPVMYRVRHATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLaelgKLARplPHQYEFAR 294
Cdd:PTZ00437 206 RDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEEL----NLWR--PHVWEFSR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 295 LNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLDPVAP 374
Cdd:PTZ00437 280 LNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 375 RSVAVLDPLKLVITNYPEGRSETCsaPRNPHDPQAGVREFPFTRELWIEQDDFR-EEPPKKYFRLFPG-NTVRLKYGYVV 452
Cdd:PTZ00437 360 RRLMVIDPIKVVVDNWKGEREFEC--PNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKYSGNV 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 453 RCTGFTKDESGK--VVEVQAEYLPDTKSGTpgadsvkvkgNITWVSAAHAVPAQVHLYDRLFADAHPdGGDKDFLACLNP 530
Cdd:PTZ00437 438 VCKGFEVDAAGQpsVIHVDIDFERKDKPKT----------NISWVSATACTPVEVRLYNALLKDDRA-AIDPEFLKFIDE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489917582 531 NSKQTVQAWLEPGIEAVPG-ATWQFERLGYFTVDSkDSRPEAPVLNRIVTLRD 582
Cdd:PTZ00437 507 DSEVVSHGYAEKGIENAKHfESVQAERFGYFVVDP-DTRPDHLVMNRVLGLRE 558
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
51-375 |
4.24e-138 |
|
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: 400.86 E-value: 4.24e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgnDNLYFASD 130
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-----YKVTYASD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 131 YFEFMYEFAEALVQAGHAYVdeqsaeeirasrgtltepgtdspwrdrpadesllrlremrdgkhpdgslvlraridmasp 210
Cdd:cd00807 76 YFDQLYEYAEQLIKKGKAYV------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 211 ninlrdpvmyrvrhatHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILArlaelgKLARPLPHQY 290
Cdd:cd00807 96 ----------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCD------ALRLYRPHQW 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 291 EFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLD 370
Cdd:cd00807 154 EFSRLNLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLN 233
|
....*
gi 489917582 371 PVAPR 375
Cdd:cd00807 234 PTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
51-501 |
9.49e-135 |
|
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: 401.09 E-value: 9.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgNDNLYFASD 130
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDW----DEGPYYQSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 131 YFEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTLTEPGT----DSPWRDRPADEsllrLREMRD-GKHPdgslVLRARI 205
Cdd:COG0008 80 RFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKppryDGRCRDLSPEE----LERMLAaGEPP----VLRFKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 206 --------DMAS-----PNINLRDPVMYRVrhathhrTGnawciYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWI 272
Cdd:COG0008 152 peegvvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 273 LARLAElgklarPLPhqyEFARLNLTY----VVTSKRKllqlvreGYVdgwddprmpTLFGLRRRGYTPSSIRLFCDRTA 348
Cdd:COG0008 220 YEALGW------EPP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 349 VSKSDSR--IDYSLLEQAVrdDLDPVaPRSVAVLDPLKLVITNYPEGR-------SETCSaprnPHDPQAGV-----REF 414
Cdd:COG0008 275 WSKSDDQeiFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRalddeelAELLA----PELPEAGIredleRLV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 415 PFTRE--------------LWIEQDDfrEEPPKKyfRLFPGNTVRlkygyVVRCTgftkdesGKVVEVQAEYLPDTksgt 480
Cdd:COG0008 348 PLVREraktlselaelarfFFIERED--EKAAKK--RLAPEEVRK-----VLKAA-------LEVLEAVETWDPET---- 407
|
490 500
....*....|....*....|.
gi 489917582 481 pgadsvkVKGNITWVSAAHAV 501
Cdd:COG0008 408 -------VKGTIHWVSAEAGV 421
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
52-371 |
5.08e-127 |
|
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: 375.50 E-value: 5.08e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 52 IRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgNDNLYFASDY 131
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKW----DYGPYYQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 132 FEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTLtePGTDSPWRDRPADESL-LRLREMRDGKHPDGSLVLRARIDMASP 210
Cdd:pfam00749 78 FDIYYKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLhLFEEEMKKGSAEGGPATVRAKIPMESP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 211 nINLRDPVMYRVR---HATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgklARPLP 287
Cdd:pfam00749 156 -YVFRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-----WEPPP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 288 HQYEFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDS-RIDYSLLEQAVR 366
Cdd:pfam00749 230 FIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDR 309
|
....*
gi 489917582 367 DDLDP 371
Cdd:pfam00749 310 KKLDW 314
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
51-573 |
2.03e-105 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 333.61 E-value: 2.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgnDNLYFASD 130
Cdd:PLN02907 213 KVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKY-----DAVTYTSD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 131 YFEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTltepGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASP 210
Cdd:PLN02907 288 YFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDP 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 211 NINLRDPVMYRVRHATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAeLGKLarplpHQY 290
Cdd:PLN02907 364 NKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMG-LRKV-----HIW 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 291 EFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLD 370
Cdd:PLN02907 438 EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIID 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 371 PVAPRSVAVLDPLKLVIT--NYPEGrSETCSAPRNPHDPQAGVREFPFTRELWIEQDDFREeppkkyfrLFPGNTVRL-K 447
Cdd:PLN02907 518 PVCPRHTAVLKEGRVLLTltDGPET-PFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLmD 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 448 YGYVVrCTGFTKDESGKVVEVQAEYLPdtksgtpgADSVK-VKGNITWVSA-AHAVPAQVHLYDRLFADAHPDGGDkDFL 525
Cdd:PLN02907 589 WGNAI-IKEITKDEGGAVTALSGELHL--------EGSVKtTKLKLTWLPDtNELVPLSLVEFDYLITKKKLEEDD-NFL 658
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489917582 526 ACLNPNSKQTVQAWLEPGIEAVP-GATWQFERLGYFTVDSKDSRPEAPV 573
Cdd:PLN02907 659 DVLNPCTKKETAALGDSNMRNLKrGEIIQLERKGYYRCDAPFVRSSKPI 707
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
54-566 |
1.25e-102 |
|
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: 321.39 E-value: 1.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 54 TRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgnDNLYFASDYFE 133
Cdd:TIGR00463 96 MRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKW-----DEVVYQSDRIE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 134 FMYEFAEALVQAGHAYVDEQSAEEIRASRGTltepGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASPNIN 213
Cdd:TIGR00463 171 TYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 214 LRDPVMYRVRHATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFED--QRPFYDWilarlaELGKLARPLPHQYE 291
Cdd:TIGR00463 247 IRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIY------RYFGWEPPEFIHWG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 292 FARLNLTYVVTSKRKLLQLVREGYVdGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLDP 371
Cdd:TIGR00463 321 RLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 372 VAPRSVAVLDPLKLVITNYPEGRSETcsAPRNPHDPQAGVREFPFTRELWIEQDDFREEPpkkyfrlfpgNTVRLKygyv 451
Cdd:TIGR00463 400 EARRYFFIWNPVKIEIVGLPEPKRVE--RPLHPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRLM---- 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 452 vrctgftkdESGKVV--EVQAEYLPDTKSGtpgaDSVKVKGNITWVSAAHAVPAQVHLYDRLFADahpDGGDKDFlacln 529
Cdd:TIGR00463 464 ---------DAVNVIysKKELRYHSEGLEG----ARKLGKSIIHWLPAKDAVKVKVIMPDASIVE---GVIEADA----- 522
|
490 500 510
....*....|....*....|....*....|....*..
gi 489917582 530 pnSKQTVqawlepgieavpGATWQFERLGYFTVDSKD 566
Cdd:TIGR00463 523 --SELEV------------GDVVQFERFGFARLDSAD 545
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
49-574 |
1.50e-95 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 301.93 E-value: 1.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 49 PARIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDwqadgNDNLYFA 128
Cdd:PLN03233 9 AGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-----PDSVSFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 129 SDYFEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTLTEpgtdSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMA 208
Cdd:PLN03233 84 SDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 209 SPNINLRDPVMYRVRHATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLaelgKLARPLPH 288
Cdd:PLN03233 160 SDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKAL----GLRRPRIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 289 QyeFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDD 368
Cdd:PLN03233 236 A--FARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 369 LDPVAPRSVAV--LDPLKLVITNYPEG----RSETCSAPRnphDPQAGVREFPFTRELWIEQDDFREeppkkyfrLFPGN 442
Cdd:PLN03233 314 IDKRAKRFMAIdkADHTALTVTNADEEadfaFSETDCHPK---DPGFGKRAMRICDEVLLEKADTED--------IQLGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 443 TVRLKYGYVVRCTGFTKDESGKVVevqaeylpdtksgtPGADSVKVKGNITWVS-AAHAVPAQVHLYDRLFADAHPDGGD 521
Cdd:PLN03233 383 DIVLLRWGVIEISKIDGDLEGHFI--------------PDGDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDD 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 489917582 522 KdFLACLNPNSKQTVQAWLEPGIEAVPGA-TWQFERLGYFTVDSKDSRPEAPVL 574
Cdd:PLN03233 449 K-FEDFINPDTLAETDVIGDAGLKTLKEHdIIQLERRGFYRVDRPYMGEEKPLI 501
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
51-567 |
1.74e-92 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 295.22 E-value: 1.74e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPE--KEEQEYVDAIIEAVHWLGFDWqadgnDNLYFA 128
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKW-----DEVVIQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 129 SDYFEFMYEFAEALVQAGHAYVDEQSAEEIRAsrgtLTEPGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMA 208
Cdd:PRK04156 176 SDRLEIYYEYARKLIEMGGAYVCTCDPEEFKE----LRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 209 SPNINLRDPVMYRVRHATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFED----QRPFYD---Wilarlaelgk 281
Cdd:PRK04156 252 HPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYDyfgW---------- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 282 larPLPHQYEFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLL 361
Cdd:PRK04156 322 ---EYPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 362 EQAVRDDLDPVAPRSVAVLDPLKLVITNYPEGRSEtcsAPRNPHDPQAGVREFPFTRELWIEQDDFREEppkkyfrlfpG 441
Cdd:PRK04156 399 YAINRKLIDPIANRYFFVRDPVELEIEGAEPLEAK---IPLHPDRPERGEREIPVGGKVYVSSDDLEAE----------G 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 442 NTVRLKYGYVVRCTGftkdesgkVVEVQAEYLPDTKsgtpgADSVKVKGNIT-WVSAAHAVPAQVHLydrlfadahPDGG 520
Cdd:PRK04156 466 KMVRLMDLFNVEITG--------VSVDKARYHSDDL-----EEARKNKAPIIqWVPEDESVPVRVLK---------PDGG 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489917582 521 DKDFLAclnpnskqtvqawlEPGIEAV-PGATWQFERLGYFTVDSKDS 567
Cdd:PRK04156 524 DIEGLA--------------EPDVADLeVDDIVQFERFGFVRIDSVED 557
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
51-568 |
2.31e-89 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 288.01 E-value: 2.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWQADGNdnlyFASD 130
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPT----YSSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 131 YFEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTltepGTDSPWRDRPADESLLRLREMRDGKHPDGSLVLRARIDMASP 210
Cdd:PTZ00402 128 YMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 211 NINLRDPVMYRVRHATHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILARLAelgkLARPLPHqy 290
Cdd:PTZ00402 204 NKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALG----IRKPIVE-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 291 EFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDLD 370
Cdd:PTZ00402 278 DFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 371 PVAPRSVAVLDPLKLVITNYPEGRSETCSAPRNPHDPQAGVREFPFTRELWIEQDDFReeppkkyfRLFPGNTVRL-KYG 449
Cdd:PTZ00402 358 PSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDVA--------LLKEGDEVTLmDWG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 450 yvvrcTGFTKD-----ESGKVVEVQAEYLPDtksgtpgADSVKVKGNITWVSAA-HAVPAQVHLYDRLFADAHPDGGDK- 522
Cdd:PTZ00402 430 -----NAYIKNirrsgEDALITDADIVLHLE-------GDVKKTKFKLTWVPESpKAEVMELNEYDHLLTKKKPDPEESi 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489917582 523 -DFLAclnPNSKQTVQAWLEPGIEAV-PGATWQFERLGYFTVDSKDSR 568
Cdd:PTZ00402 498 dDIIA---PVTKYTQEVYGEEALSVLkKGDIIQLERRGYYIVDDVTPK 542
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
373-563 |
2.44e-67 |
|
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: 216.37 E-value: 2.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 373 APRSVAVLDPLKLVITNYPEGRSETCSAPRNPHDPQAGVREFPFTRELWIEQDDFreeppkkyFRLFPGNTVRLKYGYVV 452
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 453 RCTGFTKDESGKVVEVQAEYLPDTKSGTpgadsVKVKGN-ITWVSAAHAVPAQVHLYDRLFADAHpdggDKDFLacLNPN 531
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA-----RKVKGKiIHWVSASDAVPAEVRLYDRLFKDED----DADFL--LNPD 141
|
170 180 190
....*....|....*....|....*....|....
gi 489917582 532 SKQTV-QAWLEPGIEAV-PGATWQFERLGYFTVD 563
Cdd:pfam03950 142 SLKVLtEGLAEPALANLkPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
51-385 |
1.33e-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: 1.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWqadgNDNLYFASD 130
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDW----DEGPYRQSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 131 YFEFMYEFAEALVQAGhayvdeqsaeeirasrgtltepgtdspwrdrpadesllrlremrdgkhpdgslvlraridmasp 210
Cdd:cd00418 77 RFDLYRAYAEELIKKG---------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 211 ninlrdpvmyrvrhathhrtgnawcIYPMYSWAHPVEDALEGITHSICTLEFEDQRPFYDWILArlaelgKLARPLPHQY 290
Cdd:cd00418 93 -------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYE------ALGWEPPRFY 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 291 EFARLNLTY-VVTSKRKLlqlvregyvdgwddprMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLLEQAVRDDL 369
Cdd:cd00418 142 HFPRLLLEDgTKLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSV 205
|
330
....*....|....*.
gi 489917582 370 DPVAPrSVAVLDPLKL 385
Cdd:cd00418 206 ERVNS-ADATFDWAKL 220
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
51-375 |
6.31e-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: 159.44 E-value: 6.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 51 RIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPE--KEEQEYVDAIIEAVHWLGFDWqadgnDNLYFA 128
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKW-----DEVVIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 129 SDYFEFMYEFAEALVQAGHAYVdeqsaeeirasrgtltepgtdspwrdrpadesllrlremrdgkhpdgslvlraridma 208
Cdd:cd09287 76 SDRIELYYEYARKLIEMGGAYV---------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 209 spninlrdpvmyrvrhatHHRTGNAWCIYPMYSWAHPVEDALEGITHSICTLEFED----QRPFYD---WILarlaelgk 281
Cdd:cd09287 98 ------------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEyfgWEY-------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 282 larplPHQYEFARLNLTYVVTSKRKLLQLVREGYVDGWDDPRMPTLFGLRRRGYTPSSIRLFCDRTAVSKSDSRIDYSLL 361
Cdd:cd09287 152 -----PETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENL 226
|
330
....*....|....
gi 489917582 362 EQAVRDDLDPVAPR 375
Cdd:cd09287 227 YAINRKLIDPRANR 240
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
52-146 |
9.11e-19 |
|
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: 85.72 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 52 IRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDW----QADGNDNLYF 127
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWdegpDVGGPYGPYR 81
|
90
....*....|....*....
gi 489917582 128 ASDYFEFMYEFAEALVQAG 146
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
38-257 |
4.67e-15 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 78.24 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 38 PAALQAQGQPDPARIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDW 117
Cdd:PLN02627 32 SVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 118 Q----ADGNDNLYFASDYFEFMYEFAEALVQAGHAYVDEQSAEEIRASRGTLTE----PGTDSPWRDRPADESllrLREM 189
Cdd:PLN02627 112 DegpdVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELkklpPRYTGKWATASDEEV---QAEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 190 RDG-------KHPDGSlvlRARID-----MASPNIN-LRDPVMYRvrhathhrtGNAwciYPMYSWAHPVEDALEGITHS 256
Cdd:PLN02627 189 AKGtpytyrfRVPKEG---SVKIDdlirgEVSWNTDtLGDFVLLR---------SNG---QPVYNFCVAVDDATMGITHV 253
|
.
gi 489917582 257 I 257
Cdd:PLN02627 254 I 254
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
49-187 |
5.50e-14 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 72.96 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 49 PARIRTRFPPEPNGYLHIGHAKSICVNFGLARDYGGVCHLRFDDTNPEKEEQEYVDAIIEAVHWLGFDWQADgndnLYFA 128
Cdd:PRK05710 3 MTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGP----VLYQ 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917582 129 SDYFEFMYEFAEALVQAGHAYVDEQSAEEIRASR-----GTLTEPGT----DSPWRDRPAdeslLRLR 187
Cdd:PRK05710 79 SQRHDAYRAALDRLRAQGLVYPCFCSRKEIAAAApappdGGGIYPGTcrdlLHGPRNPPA----WRLR 142
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
54-120 |
1.56e-10 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 59.42 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917582 54 TRFPPEPNGYLHIGHAKSICVNFGLARD-----YGGVCHLRFDDTNPEKEEQ---------EYVDA----IIEAVHWLgF 115
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDPankkgenakAFVERwierIKEDVEYM-F 80
|
....*
gi 489917582 116 DWQAD 120
Cdd:cd00802 81 LQAAD 85
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
54-120 |
1.25e-08 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 52.93 E-value: 1.25e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917582 54 TRFPPEPnGYLHIGHAKSICVNFGLArdygGVCHLRFDDTNPEKEEQ------EYVDAIIEAVHWLGFDWQAD 120
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQdpheleERKESIEEDISVCGEDFQQN 69
|
|
| |
