|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-565 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1113.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 1 MAEEIKERSNNFIENIIEEDLAGGfSANNLRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEY 80
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASG-KHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 81 VDAIRRDVAWLGYKW-DKECYASDYFQELYDWAVMLIKKGKAYVDKQTSEEIAAQKGTPTTAGTESPYRNTSPEENLALF 159
Cdd:PRK05347 81 VDSIKEDVRWLGFDWsGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 160 ERMKNGEFANGTYVLRAKIDMASPNMLMRDPIIYRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHR 239
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 240 ELYDWFLDQVIpasaladgkEVVRPKQREFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRK 319
Cdd:PRK05347 241 PLYDWVLDNLP---------IPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIRE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 320 FADTIGIAKRENLIDVSLLEFCVREDLNKKANRVMGVLDPVKVIITNYPEGKEEWLEAENNPEVSPMTYRKVPFSRELYI 399
Cdd:PRK05347 312 FCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 400 EREDFREEADKKYFRLKLGGEVRLKNAYIIKAESVVKDSEGNILEIHCTYDPDSRSGSGsqASTRKVKGTLHWVSVPHAL 479
Cdd:PRK05347 392 EREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNP--ADGRKVKGTIHWVSAAHAV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 480 TVEARLYDRLFTVAEPDRQEDsFLNYINPDSLKVITAYVEPSLQTAKAGDIVQFQRLGYFCVDPDSTPDKLVFNKTVGLK 559
Cdd:PRK05347 470 PAEVRLYDRLFTVPNPAAGKD-FLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLR 548
|
....*.
gi 1242566642 560 DTWEKV 565
Cdd:PRK05347 549 DSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
30-562 |
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: 686.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 30 LRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKEC-YASDYFQEL 108
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIrYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 109 YDWAVMLIKKGKAYVDKQTSEEIAAQKGTPTTAGTESPYRNTSPEENLALFERMKNGEFANGTYVLRAKIDMASPNMLMR 188
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 189 DPIIYRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQV-IPasaladgkevVRPKQR 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIhIF----------PRPAQY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 268 EFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCVREDLN 347
Cdd:TIGR00440 231 EFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 348 KKANRVMGVLDPVKVIITNYpEGKEEWLEAENNPEVSPMTYRKVPFSRELYIEREDFREEADKKYFRLKLGGEVRLKNAY 427
Cdd:TIGR00440 311 ENAPRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 428 IIKAESVVKDSEGNILEIHCTYDPDSRSGSGSQAstRKVKGTLHWVSVPHALTVEARLYDRLFTVAEPDRQEDsFLNYIN 507
Cdd:TIGR00440 390 VIKAERVEKDAAGKITTIFCTYDNKTLGKEPADG--RKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDD-FLSVIN 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1242566642 508 PDSLKVITAYVEPSLQTAKAGDIVQFQRLGYFCVDP-DSTPDKLVFNKTVGLKDTW 562
Cdd:TIGR00440 467 PESLVIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
33-352 |
1.18e-131 |
|
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: 383.53 E-value: 1.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 33 RFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKECYASDYFQELYDWA 112
Cdd:cd00807 5 RFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLYEYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 113 VMLIKKGKAYVdkqtseeiaaqkgtpttagtespyrntspeenlalfermkngefangtyvlrakidmaspnmlmrdpii 192
Cdd:cd00807 85 EQLIKKGKAYV--------------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 193 yrimnasHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQVipasaladgkEVVRPKQREFARR 272
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL----------RLYRPHQWEFSRL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 273 NLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCVREDLNKKANR 352
Cdd:cd00807 159 NLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-539 |
7.87e-121 |
|
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: 364.50 E-value: 7.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 26 SANNLRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKE-CYASDY 104
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGpYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 105 FQELYDWAVMLIKKGKAYVDKQTSEEIAAQKGTPTTAGTESPY----RNTSPEEnlaLFERMKNGEfangTYVLRAKI-- 178
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE---LERMLAAGE----PPVLRFKIpe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 179 ------DMAS-----PNMLMRDPIIYRimnashhrtGDKwhiYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLD 247
Cdd:COG0008 154 egvvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 248 qvipasALadGKEVvrPkqrEFARRNLSH----TIVSKRKllqlvteKYVagwddprmpTISGLRRRGYTPEAIRKFADT 323
Cdd:COG0008 222 ------AL--GWEP--P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLAL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 324 IGIAKREN--LIDVSLLEFCVreDLNKKaNRVMGVLDPVKVIITNYPEGKE-------EWLeAENNPEVSPMTY--RKVP 392
Cdd:COG0008 273 LGWSKSDDqeIFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlddeelaELL-APELPEAGIREDleRLVP 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 393 FSRE--------------LYIEREDfrEEADKKYFRLKlggEVRlknAYIIKAESVVKDSEgnileihcTYDPDSrsgsg 458
Cdd:COG0008 349 LVREraktlselaelarfFFIERED--EKAAKKRLAPE---EVR---KVLKAALEVLEAVE--------TWDPET----- 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 459 sqastrkVKGTLHWVSvphaltVEARLYDRLFTVAepdrqedsflnyinpdsLKVIT--AYVEPSL-QTAKA--GDIVqF 533
Cdd:COG0008 408 -------VKGTIHWVS------AEAGVKDGLLFMP-----------------LRVALtgRTVEPSLfDVLELlgKERV-F 456
|
....*.
gi 1242566642 534 QRLGYF 539
Cdd:COG0008 457 ERLGYA 462
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
30-347 |
6.27e-119 |
|
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: 354.32 E-value: 6.27e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 30 LRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWD-KECYASDYFQEL 108
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 109 YDWAVMLIKKGKAYVDKQTSEEIAAQKGTPTTAGteSPYRNTSPEENLALF-ERMKNGEFANGTYVLRAKIDMASPnMLM 187
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQEALG--SPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 188 RDPIIYRIMNAS---HHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQV-IPasaladgkevVR 263
Cdd:pfam00749 159 RDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALgWE----------PP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 264 PKQREFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKR-ENLIDVSLLEFCV 342
Cdd:pfam00749 229 PFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFD 308
|
....*
gi 1242566642 343 REDLN 347
Cdd:pfam00749 309 RKKLD 313
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-565 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1113.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 1 MAEEIKERSNNFIENIIEEDLAGGfSANNLRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEY 80
Cdd:PRK05347 2 MMSEAEARPSNFIRQIIDEDLASG-KHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 81 VDAIRRDVAWLGYKW-DKECYASDYFQELYDWAVMLIKKGKAYVDKQTSEEIAAQKGTPTTAGTESPYRNTSPEENLALF 159
Cdd:PRK05347 81 VDSIKEDVRWLGFDWsGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 160 ERMKNGEFANGTYVLRAKIDMASPNMLMRDPIIYRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHR 239
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 240 ELYDWFLDQVIpasaladgkEVVRPKQREFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRK 319
Cdd:PRK05347 241 PLYDWVLDNLP---------IPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIRE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 320 FADTIGIAKRENLIDVSLLEFCVREDLNKKANRVMGVLDPVKVIITNYPEGKEEWLEAENNPEVSPMTYRKVPFSRELYI 399
Cdd:PRK05347 312 FCERIGVTKQDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 400 EREDFREEADKKYFRLKLGGEVRLKNAYIIKAESVVKDSEGNILEIHCTYDPDSRSGSGsqASTRKVKGTLHWVSVPHAL 479
Cdd:PRK05347 392 EREDFMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNP--ADGRKVKGTIHWVSAAHAV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 480 TVEARLYDRLFTVAEPDRQEDsFLNYINPDSLKVITAYVEPSLQTAKAGDIVQFQRLGYFCVDPDSTPDKLVFNKTVGLK 559
Cdd:PRK05347 470 PAEVRLYDRLFTVPNPAAGKD-FLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLR 548
|
....*.
gi 1242566642 560 DTWEKV 565
Cdd:PRK05347 549 DSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
7-568 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 820.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 7 ERSNNFIENIIEEDLAGGfSANNLRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRR 86
Cdd:PRK14703 10 LVSPNFITEIIEEDLEAG-RYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 87 DVAWLGYKW-DKECYASDYFQELYDWAVMLIKKGKAYVDKQTSEEIAAQKGTPTTAGTESPYRNTSPEENLALFERMKNG 165
Cdd:PRK14703 89 DVRWLGFDWgEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 166 EFANGTYVLRAKIDMASPNMLMRDPIIYRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWF 245
Cdd:PRK14703 169 EFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 246 LDQVIPASAladgkevvRPKQREFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIG 325
Cdd:PRK14703 249 LDHLGPWPP--------RPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 326 IAKRENLIDVSLLEFCVREDLNKKANRVMGVLDPVKVIITNYPEGKEEWLEAENNP-EVSPMTYRKVPFSRELYIEREDF 404
Cdd:PRK14703 321 VAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPhDVPKEGSRKVPFTRELYIERDDF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 405 REEADKKYFRLKLGGEVRLKNAYIIKAESVVKDSEGNILEIHCTYDPDSRSGsgsQASTRKVKGTLHWVSVPHALTVEAR 484
Cdd:PRK14703 401 SEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKG---EDTGRKAAGVIHWVSAKHALPAEVR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 485 LYDRLFTVAEPDRQEDSFLNYINPDSLKVITAYVEPSLQTAKAGDIVQFQRLGYFCVDP-DSTPDKLVFNKTVGLKDTWE 563
Cdd:PRK14703 478 LYDRLFKVPQPEAADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWG 557
|
....*
gi 1242566642 564 KVKSE 568
Cdd:PRK14703 558 ARARE 562
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
30-562 |
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: 686.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 30 LRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKEC-YASDYFQEL 108
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIrYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 109 YDWAVMLIKKGKAYVDKQTSEEIAAQKGTPTTAGTESPYRNTSPEENLALFERMKNGEFANGTYVLRAKIDMASPNMLMR 188
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 189 DPIIYRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQV-IPasaladgkevVRPKQR 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIhIF----------PRPAQY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 268 EFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCVREDLN 347
Cdd:TIGR00440 231 EFSRLNLEGTVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 348 KKANRVMGVLDPVKVIITNYpEGKEEWLEAENNPEVSPMTYRKVPFSRELYIEREDFREEADKKYFRLKLGGEVRLKNAY 427
Cdd:TIGR00440 311 ENAPRAMAVIDPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 428 IIKAESVVKDSEGNILEIHCTYDPDSRSGSGSQAstRKVKGTLHWVSVPHALTVEARLYDRLFTVAEPDRQEDsFLNYIN 507
Cdd:TIGR00440 390 VIKAERVEKDAAGKITTIFCTYDNKTLGKEPADG--RKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDD-FLSVIN 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1242566642 508 PDSLKVITAYVEPSLQTAKAGDIVQFQRLGYFCVDP-DSTPDKLVFNKTVGLKDTW 562
Cdd:TIGR00440 467 PESLVIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
33-564 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 559.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 33 RFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKECYASDYFQELYDWA 112
Cdd:PLN02859 268 RFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 113 VMLIKKGKAYVDKQTSEEIAAQKgtptTAGTESPYRNTSPEENLALFERMKNGEFANGTYVLRAKIDMASPNMLMRDPII 192
Cdd:PLN02859 348 VELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYDLIA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 193 YRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQVipasaladgkEVVRPKQREFARR 272
Cdd:PLN02859 424 YRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL----------GLYQPYVWEYSRL 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 273 NLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKREN-LIDVSLLEFCVREDLNKKAN 351
Cdd:PLN02859 494 NVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIRMDRLEHHIREELNKTAP 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 352 RVMGVLDPVKVIITNYPEGKEEWLEAE---NNPEVSPMTYRKVPFSRELYIEREDFREEADKKYFRLKLGGEVRLKNAYI 428
Cdd:PLN02859 574 RTMVVLHPLKVVITNLESGEVIELDAKrwpDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFP 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 429 IKAESVV-KDSEGNILEIHCTYDPDSRSgsgsqastrKVKGTLHWVSVP----HALTVEARLYDRLFTVAEPDRQEDsFL 503
Cdd:PLN02859 654 IKCTDVVlADDNETVVEIRAEYDPEKKT---------KPKGVLHWVAEPspgvEPLKVEVRLFDKLFLSENPAELED-WL 723
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1242566642 504 NYINPDSLKVIT-AYVEPSLQTAKAGDIVQFQRLGYFCVDPDSTPDKLVFNKTVGLKDTWEK 564
Cdd:PLN02859 724 EDLNPQSKEVISgAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
32-564 |
7.37e-160 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 468.31 E-value: 7.37e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 32 FRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKECYASDYFQELYDW 111
Cdd:PTZ00437 54 FRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHEF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 112 AVMLIKKGKAYVDKQTSEEIAAQKgtptTAGTESPYRNTSPEENLALFERMKNGEFANGTYVLRAKIDMASPNMLMRDPI 191
Cdd:PTZ00437 134 AVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 192 IYRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQVipasaladgkEVVRPKQREFAR 271
Cdd:PTZ00437 210 AYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEEL----------NLWRPHVWEFSR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 272 RNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCVREDLNKKAN 351
Cdd:PTZ00437 280 LNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 352 RVMGVLDPVKVIITNYpEGKEEwLEAENNPEVSPMTYRKVPFSRELYIEREDFR-EEADKKYFRLKLGGE-VRLKNAYII 429
Cdd:PTZ00437 360 RRLMVIDPIKVVVDNW-KGERE-FECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGPRvVGLKYSGNV 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 430 KAESVVKDSEGNILEIHCTYDPDsrsgsgsqaSTRKVKGTLHWVSVPHALTVEARLYDRLFtvaEPDRQ--EDSFLNYIN 507
Cdd:PTZ00437 438 VCKGFEVDAAGQPSVIHVDIDFE---------RKDKPKTNISWVSATACTPVEVRLYNALL---KDDRAaiDPEFLKFID 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1242566642 508 PDSLKVITAYVEPSLQTAKAGDIVQFQRLGYFCVDPDSTPDKLVFNKTVGLKDTWEK 564
Cdd:PTZ00437 506 EDSEVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
33-352 |
1.18e-131 |
|
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: 383.53 E-value: 1.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 33 RFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKECYASDYFQELYDWA 112
Cdd:cd00807 5 RFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLYEYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 113 VMLIKKGKAYVdkqtseeiaaqkgtpttagtespyrntspeenlalfermkngefangtyvlrakidmaspnmlmrdpii 192
Cdd:cd00807 85 EQLIKKGKAYV--------------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 193 yrimnasHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQVipasaladgkEVVRPKQREFARR 272
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDAL----------RLYRPHQWEFSRL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 273 NLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCVREDLNKKANR 352
Cdd:cd00807 159 NLTYTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-539 |
7.87e-121 |
|
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: 364.50 E-value: 7.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 26 SANNLRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKE-CYASDY 104
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGpYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 105 FQELYDWAVMLIKKGKAYVDKQTSEEIAAQKGTPTTAGTESPY----RNTSPEEnlaLFERMKNGEfangTYVLRAKI-- 178
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEE---LERMLAAGE----PPVLRFKIpe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 179 ------DMAS-----PNMLMRDPIIYRimnashhrtGDKwhiYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLD 247
Cdd:COG0008 154 egvvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 248 qvipasALadGKEVvrPkqrEFARRNLSH----TIVSKRKllqlvteKYVagwddprmpTISGLRRRGYTPEAIRKFADT 323
Cdd:COG0008 222 ------AL--GWEP--P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLAL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 324 IGIAKREN--LIDVSLLEFCVreDLNKKaNRVMGVLDPVKVIITNYPEGKE-------EWLeAENNPEVSPMTY--RKVP 392
Cdd:COG0008 273 LGWSKSDDqeIFSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRAlddeelaELL-APELPEAGIREDleRLVP 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 393 FSRE--------------LYIEREDfrEEADKKYFRLKlggEVRlknAYIIKAESVVKDSEgnileihcTYDPDSrsgsg 458
Cdd:COG0008 349 LVREraktlselaelarfFFIERED--EKAAKKRLAPE---EVR---KVLKAALEVLEAVE--------TWDPET----- 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 459 sqastrkVKGTLHWVSvphaltVEARLYDRLFTVAepdrqedsflnyinpdsLKVIT--AYVEPSL-QTAKA--GDIVqF 533
Cdd:COG0008 408 -------VKGTIHWVS------AEAGVKDGLLFMP-----------------LRVALtgRTVEPSLfDVLELlgKERV-F 456
|
....*.
gi 1242566642 534 QRLGYF 539
Cdd:COG0008 457 ERLGYA 462
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
30-347 |
6.27e-119 |
|
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: 354.32 E-value: 6.27e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 30 LRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWD-KECYASDYFQEL 108
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 109 YDWAVMLIKKGKAYVDKQTSEEIAAQKGTPTTAGteSPYRNTSPEENLALF-ERMKNGEFANGTYVLRAKIDMASPnMLM 187
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQEALG--SPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 188 RDPIIYRIMNAS---HHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQV-IPasaladgkevVR 263
Cdd:pfam00749 159 RDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALgWE----------PP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 264 PKQREFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKR-ENLIDVSLLEFCV 342
Cdd:pfam00749 229 PFIHEYLRLNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFD 308
|
....*
gi 1242566642 343 REDLN 347
Cdd:pfam00749 309 RKKLD 313
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
33-542 |
3.69e-101 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 321.67 E-value: 3.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 33 RFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKECYASDYFQELYDWA 112
Cdd:PLN02907 217 RFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 113 VMLIKKGKAYVDKQTSEEIAAQKGtpttAGTESPYRNTSPEENLALFERMKNGEFANGTYVLRAKIDMASPNMLMRDPII 192
Cdd:PLN02907 297 EKLIKEGKAYVDDTPREQMRKERM----DGIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVY 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 193 YRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFldqvipasaLADGKevVRPKQ-REFAR 271
Cdd:PLN02907 373 YRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRI---------LEDMG--LRKVHiWEFSR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 272 RNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLefcvrEDLNKK-- 349
Cdd:PLN02907 442 LNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKL-----WTINKKii 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 350 ---ANRVMGVLDPVKVIIT--NYPEgKEEWLEAENNPEVSPMTYRKVPFSRELYIEREDFREeadkkyfrLKLGGEVRLK 424
Cdd:PLN02907 517 dpvCPRHTAVLKEGRVLLTltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLM 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 425 ---NAyIIKaeSVVKDSEGNILEIHCTYDPdsrsgsgsQASTRKVKGTLHWV-SVPHALTVEARLYDRLFTVAEPDrQED 500
Cdd:PLN02907 588 dwgNA-IIK--EITKDEGGAVTALSGELHL--------EGSVKTTKLKLTWLpDTNELVPLSLVEFDYLITKKKLE-EDD 655
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1242566642 501 SFLNYINPDSLKVITAYVEPSLQTAKAGDIVQFQRLGYFCVD 542
Cdd:PLN02907 656 NFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
33-542 |
5.31e-96 |
|
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: 303.67 E-value: 5.31e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 33 RFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKECYASDYFQELYDWA 112
Cdd:TIGR00463 97 RFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 113 VMLIKKGKAYVDKQTSEEIAAQKgtptTAGTESPYRNTSPEENLALFERMKNGEFANGTYVLRAKIDMASPNMLMRDPII 192
Cdd:TIGR00463 177 RKLIEMGKAYVCDCRPEEFRELR----NRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 193 YRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRE--LYDWFLdqvipasalaDGKEVVRPKQREFA 270
Cdd:TIGR00463 253 FRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqEYIYRY----------FGWEPPEFIHWGRL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 271 RRNLSHTIVSKRKLLQLVTEKYVaGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCVREDLNKKA 350
Cdd:TIGR00463 323 KIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 351 NRVMGVLDPVKVIITNYPEGKEEwlEAENNPEVSPMTYRKVPFSRELYIEREDFREeadkkyfrlkLGGEVRLKNAYIIK 430
Cdd:TIGR00463 402 RRYFFIWNPVKIEIVGLPEPKRV--ERPLHPDHPEIGERVLILRGEIYVPKDDLEE----------GVEPVRLMDAVNVI 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 431 AESvvKDSEGNILEIhctydpdsrsgsgsQASTRKVKGTLHWVSVPHALTVEArlydrlftvaepdrqedsflnyINPDS 510
Cdd:TIGR00463 470 YSK--KELRYHSEGL--------------EGARKLGKSIIHWLPAKDAVKVKV----------------------IMPDA 511
|
490 500 510
....*....|....*....|....*....|..
gi 1242566642 511 LKViTAYVEPSLQTAKAGDIVQFQRLGYFCVD 542
Cdd:TIGR00463 512 SIV-EGVIEADASELEVGDVVQFERFGFARLD 542
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
29-552 |
1.43e-95 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 302.54 E-value: 1.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 29 NLRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPS--KEEQEYVDAIRRDVAWLGYKWDKECYASDYFQ 106
Cdd:PRK04156 101 KVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDEVVIQSDRLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 107 ELYDWAVMLIKKGKAYVDKQTSEEIAAQKgtptTAGTESPYRNTSPEENLALFERMKNGEFANGTYVLRAKIDMASPNML 186
Cdd:PRK04156 181 IYYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 187 MRDPIIYRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRE----LYDWFldqvipasaladGKEVv 262
Cdd:PRK04156 257 VRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEkqryIYDYF------------GWEY- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 263 rPKQREFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIakRENLIDVSL--LEF 340
Cdd:PRK04156 324 -PETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGV--KETDATISWenLYA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 341 CVREDLNKKANRVMGVLDPVKVIITNYPEgkeewLEAEN--NPEVSPMTYRKVPFSRELYIEREDFREeadkkyfrlkLG 418
Cdd:PRK04156 401 INRKLIDPIANRYFFVRDPVELEIEGAEP-----LEAKIplHPDRPERGEREIPVGGKVYVSSDDLEA----------EG 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 419 GEVRLKNAYIIKaesvVKDSEGNILEIHctydpdsrsgSGSQASTRKVKGTL-HWVSVPHALTVEarlydrlftVAEPDR 497
Cdd:PRK04156 466 KMVRLMDLFNVE----ITGVSVDKARYH----------SDDLEEARKNKAPIiQWVPEDESVPVR---------VLKPDG 522
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1242566642 498 qedsflnyinpdslKVITAYVEPSLQTAKAGDIVQFQRLGYFCVDpDSTPDKLVF 552
Cdd:PRK04156 523 --------------GDIEGLAEPDVADLEVDDIVQFERFGFVRID-SVEDDEVVA 562
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
33-565 |
2.09e-95 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 303.42 E-value: 2.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 33 RFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWD-KECYASDYFQELYDW 111
Cdd:PTZ00402 56 RFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDvGPTYSSDYMDLMYEK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 112 AVMLIKKGKAYVDKQTSEEIaaQK----GTPTTagtespYRNTSPEENLALFERMKNGEFANGTYVLRAKIDMASPNMLM 187
Cdd:PTZ00402 136 AEELIKKGLAYCDKTPREEM--QKcrfdGVPTK------YRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNENKAM 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 188 RDPIIYRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDqvipasALAdgkeVVRPKQR 267
Cdd:PTZ00402 208 RDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCD------ALG----IRKPIVE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 268 EFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCVREDLN 347
Cdd:PTZ00402 278 DFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 348 KKANRVMGVLDPVKVIITNYPEG---KEEWLEAENNPEVSPMTYRKvpfSRELYIEREDFReeadkkyfRLKLGGEVRLK 424
Cdd:PTZ00402 358 PSVPRYTVVSNTLKVRCTVEGQIhleACEKLLHKKVPDMGEKTYYK---SDVIFLDAEDVA--------LLKEGDEVTLM 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 425 ---NAYI--IKAESvvkdSEGNILEIHCTYDPdsrsgsgsQASTRKVKGTLHWV-SVPHALTVEARLYDRLFTVAEPDrQ 498
Cdd:PTZ00402 427 dwgNAYIknIRRSG----EDALITDADIVLHL--------EGDVKKTKFKLTWVpESPKAEVMELNEYDHLLTKKKPD-P 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1242566642 499 EDSFLNYINPDSLKVITAYVEPSLQTAKAGDIVQFQRLGYFCVDpDSTPDKLVfnktVGLKDTWEKV 565
Cdd:PTZ00402 494 EESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVD-DVTPKKVL----IAIPDGREKV 555
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
33-549 |
3.90e-95 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 300.39 E-value: 3.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 33 RFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKECYASDYFQELYDWA 112
Cdd:PLN03233 15 RFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPIRCYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 113 VMLIKKGKAYVDKQTSEEIAAQKgtptTAGTESPYRNTSPEENLALFERMKNGEFANGTYVLRAKIDMASPNMLMRDPII 192
Cdd:PLN03233 95 IILIEEGLAYMDDTPQEEMKKER----ADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLRDPVL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 193 YRIMNASHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQVipasaladgkEVVRPKQREFARR 272
Cdd:PLN03233 171 FRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKAL----------GLRRPRIHAFARM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 273 NLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCVREDLNKKANR 352
Cdd:PLN03233 241 NFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 353 VMGV--LDPVKVIITNYPEGKE-EWLEAENNPEVSPMTYRKVPFSRELYIEREDFREeadkkyfrLKLGGEVRLKNAYII 429
Cdd:PLN03233 321 FMAIdkADHTALTVTNADEEADfAFSETDCHPKDPGFGKRAMRICDEVLLEKADTED--------IQLGEDIVLLRWGVI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 430 KAESVVKDSEGNILeihctydPDsrsgsgsqASTRKVKGTLHWVS-VPHALTVEARLYDRLfTVAEPDRQEDSFLNYINP 508
Cdd:PLN03233 393 EISKIDGDLEGHFI-------PD--------GDFKAAKKKISWIAdVSDNIPVVLSEFDNL-IIKEKLEEDDKFEDFINP 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1242566642 509 DSLKVITAYVEPSLQTAKAGDIVQFQRLGYFCVD-PDSTPDK 549
Cdd:PLN03233 457 DTLAETDVIGDAGLKTLKEHDIIQLERRGFYRVDrPYMGEEK 498
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
350-542 |
1.15e-78 |
|
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: 245.26 E-value: 1.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 350 ANRVMGVLDPVKVIITNYPEGKEEWLEAENNPEVSPMTYRKVPFSRELYIEREDFreeadkkyFRLKLGGEVRLKNAYII 429
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 430 KAESVVKDSEGNILEIHCTYDPDSRSGsgsqasTRKVKG-TLHWVSVPHALTVEARLYDRLFTVAEpdrqEDSFLnyINP 508
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGG------ARKVKGkIIHWVSASDAVPAEVRLYDRLFKDED----DADFL--LNP 140
|
170 180 190
....*....|....*....|....*....|....*
gi 1242566642 509 DSLKVIT-AYVEPSLQTAKAGDIVQFQRLGYFCVD 542
Cdd:pfam03950 141 DSLKVLTeGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
31-353 |
1.76e-44 |
|
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: 157.63 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 31 RFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKECY-ASDYFQELY 109
Cdd:cd00418 3 VTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYrQSDRFDLYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 110 DWAVMLIKKGkayvdkqtseeiaaqkgtpttagtespyrntspeenlalfermkngefangtyvlrakidmaspnmlmrd 189
Cdd:cd00418 83 AYAEELIKKG---------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 190 piiyrimnashhrtgdkwhIYPMYDWAHGESDYLEQISHSLCTLEFLPHRELYDWFLDQVIpasaladgkeVVRPKQREF 269
Cdd:cd00418 93 -------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALG----------WEPPRFYHF 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 270 ARRNLSH-TIVSKRKLlqlvtekyvagwddprMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCVR---ED 345
Cdd:cd00418 144 PRLLLEDgTKLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAfsvER 207
|
....*...
gi 1242566642 346 LNKKANRV 353
Cdd:cd00418 208 VNSADATF 215
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
29-352 |
2.56e-37 |
|
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: 138.25 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 29 NLRFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNP--SKEEQEYVDAIRRDVAWLGYKWDKECYASDYFQ 106
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 107 ELYDWAVMLIKKGKAYVdkqtseeiaaqkgtpttagtespyrntspeenlalfermkngefangtyvlrakidmaspnml 186
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 187 mrdpiiyrimnasHHRTGDKWHIYPMYDWAHGESDYLEQISHSLCTLEFLPHRE----LYDWFldqvipasaladGKEvv 262
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEkqryIYEYF------------GWE-- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 263 RPKQREFARRNLSHTIVSKRKLLQLVTEKYVAGWDDPRMPTISGLRRRGYTPEAIRKFADTIGIAKRENLIDVSLLEFCV 342
Cdd:cd09287 151 YPETIHWGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAIN 230
|
330
....*....|
gi 1242566642 343 REDLNKKANR 352
Cdd:cd09287 231 RKLIDPRANR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
31-122 |
1.64e-10 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 62.18 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 31 RFRFPPEPNGYLHLGHASSICLNF-------GLGLrynapvnLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDKEC-YAS 102
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWldarahgGRWL-------LRIEDIDPPREVPGAADAILADLEWLGLHWDGPVlYQS 79
|
90 100
....*....|....*....|.
gi 1242566642 103 DYFqELYDWAV-MLIKKGKAY 122
Cdd:PRK05710 80 QRH-DAYRAALdRLRAQGLVY 99
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
31-135 |
1.22e-09 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 60.91 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 31 RFRFPPEPNGYLHLGHASSICLNFGLGLRYNAPVNLRFDDTNPSKEEQEYVDAIRRDVAWLGYKWDK------EC--YAS 102
Cdd:PLN02627 47 RVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgpdvggEYgpYRQ 126
|
90 100 110
....*....|....*....|....*....|....
gi 1242566642 103 DYFQELY-DWAVMLIKKGKAYVDKQTSEEIAAQK 135
Cdd:PLN02627 127 SERNAIYkQYAEKLLESGHVYPCFCTDEELEAMK 160
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
33-117 |
1.30e-06 |
|
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: 47.15 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 33 RFPPEPnGYLHLGHASSICLNFGLGlrYNapVNLRFDDTNPSKEEQ------EYVDAIRRDVAWLGYKWDKEcyasdyfQ 106
Cdd:cd02156 3 RFPGEP-GYLHIGHAKLICRAKGIA--DQ--CVVRIDDNPPVKVWQdpheleERKESIEEDISVCGEDFQQN-------R 70
|
90
....*....|.
gi 1242566642 107 ELYDWAVMLIK 117
Cdd:cd02156 71 ELYRWVKDNIT 81
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
33-111 |
1.29e-05 |
|
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: 45.16 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242566642 33 RFPPEPNGYLHLGHASSICLNFGLG-----LRYNAPVNLRFDDTNPSKEEQeyvdairRDVAWLGYKWDKECYaSDYFQE 107
Cdd:cd00802 3 FSGITPNGYLHIGHLRTIVTFDFLAqayrkLGYKVRCIALIDDAGGLIGDP-------ANKKGENAKAFVERW-IERIKE 74
|
....
gi 1242566642 108 LYDW 111
Cdd:cd00802 75 DVEY 78
|
|
| |
