|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-552 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1137.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 1 MSNETNSSNFIKNIIINDLETGKHDSIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVES 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 81 IKEDVKWLGFDWN-ELNFASNYFDEMYKRALILIKKGKAYVCDLTQEEMREYRGTLTEPGKESPHRNRTIEENLDLFERM 159
Cdd:PRK05347 84 IKEDVRWLGFDWSgELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 160 KNGEFKDGEKTLRAKIDMSSPNINLRDPIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLY 239
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 240 DWFVKECEMENIPRQIEFARLNINNTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNS 319
Cdd:PRK05347 244 DWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 320 TVDSQMLDYFLRENLQPKAPLTMGVLRPLKLIITNYPEDKIEMLEIENNAKDESQGKRLVPFSRELYIEQDDFMEEPVKK 399
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 400 YFRFFPGNEVRLKGAYFVKCTDVIKDENGNVVEIHGTYDPETKSGSGFTGRKVKSTIHWVDAKSAIPCEFRLFEPLILDD 479
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524214 480 IPEnEGKHFLEQINPNSLEILQGFVEPTqIKDAKPFDKFQFVRNGFFSIDnKYTTDEKFVFNRIVPLKSSFKP 552
Cdd:PRK05347 484 NPA-AGKDFLDFLNPDSLVIKQGFVEPS-LADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAK 553
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
29-550 |
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: 667.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 29 TRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWN-ELNFASNYFDEMYK 107
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 108 RALILIKKGKAYVCDLTQEEMREYRGTLTEPGKESPHRNRTIEENLDLFERMKNGEFKDGEKTLRAKIDMSSPNINLRDP 187
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 188 IIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMENIPRQIEFARLNINNTVM 267
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 268 SKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQMLDYFLRENLQPKAPLTMGVLRP 347
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 348 LKLIITNYpEDKIEMLEIENNAKDESQGKRLVPFSRELYIEQDDFMEEPVKKYFRFFPGNEVRLKGAYFVKCTDVIKDEN 427
Cdd:TIGR00440 323 VEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 428 GNVVEIHGTYDPETKSGSGFTGRKVKSTIHWVDAKSAIPCEFRLFEPLILDDIPENEgKHFLEQINPNSLEILQGFVEPT 507
Cdd:TIGR00440 402 GKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAP-DDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489524214 508 qIKDAKPFDKFQFVRNGFFSIDNKYTTDEKFVFNRIVPLKSSF 550
Cdd:TIGR00440 481 -LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-339 |
3.34e-142 |
|
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: 410.10 E-value: 3.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 27 IITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNELNFASNYFDEMY 106
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 107 KRALILIKKGKAYVcdltqeemreyrgtltepgkesphrnrtieenldlfermkngefkdgektlrakidmsspninlrd 186
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 187 piiyrishstHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMENiPRQIEFARLNINNTV 266
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYTV 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524214 267 MSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQMLDYFLRENLQPKAP 339
Cdd:cd00807 165 MSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAP 237
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
29-336 |
6.05e-136 |
|
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: 397.07 E-value: 6.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 29 TRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNE-LNFASNYFDEMYK 107
Cdd:pfam00749 4 TRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYgPYYQSDRFDIYYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 108 RALILIKKGKAYVCDLTQEEMREYRGTLtePGKESPHRNRTIEENLDLF-ERMKNGEFKDGEKTLRAKIDMSSPnINLRD 186
Cdd:pfam00749 84 YAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 187 PIIYRI---SHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMENIPRQIEFARLNIN 263
Cdd:pfam00749 161 PVRGRIkftPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524214 264 NTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSK-VNSTVDSQMLDYFLRENLQP 336
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKsFDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-475 |
9.62e-129 |
|
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: 384.53 E-value: 9.62e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 25 DSIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNE-LNFASNYFD 103
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 104 EMYKRALILIKKGKAYVCDLTQEEMREYRGTLTEPGKE----SPHRNRTIEEnldLFERMKNGEfkdgEKTLRAKI---- 175
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEE---LERMLAAGE----PPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 176 ----DMSS-----PNINLRDPIIYRishsthhntGDKwciYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKEC 246
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 247 EMEnIPrqiEFARLNI----NNTVMSKRKlkqlvdeGIVdgwddprvpTISGIRRKGYTAEALRNFCSEIGVSKVNSTV- 321
Cdd:COG0008 224 GWE-PP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEi 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 322 --DSQMLDYFLRENLqPKApltMGVLRPLKLIITNYP-------EDKIEMLEIEN-NAKDESQGKRLVPFSRE------- 384
Cdd:COG0008 284 fsLEELIEAFDLDRV-SRS---PAVFDPVKLVWLNGPyiralddEELAELLAPELpEAGIREDLERLVPLVREraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 385 -------LYIEQDDfmEEPVKKyfRFFPgNEVRLkgayFVKCTdvikdenGNVVEIHGTYDPETksgsgftgrkVKSTIH 457
Cdd:COG0008 360 laelarfFFIERED--EKAAKK--RLAP-EEVRK----VLKAA-------LEVLEAVETWDPET----------VKGTIH 413
|
490 500
....*....|....*....|.
gi 489524214 458 WVDAKSaipcEFR---LFEPL 475
Cdd:COG0008 414 WVSAEA----GVKdglLFMPL 430
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-552 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1137.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 1 MSNETNSSNFIKNIIINDLETGKHDSIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVES 80
Cdd:PRK05347 4 SEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 81 IKEDVKWLGFDWN-ELNFASNYFDEMYKRALILIKKGKAYVCDLTQEEMREYRGTLTEPGKESPHRNRTIEENLDLFERM 159
Cdd:PRK05347 84 IKEDVRWLGFDWSgELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 160 KNGEFKDGEKTLRAKIDMSSPNINLRDPIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLY 239
Cdd:PRK05347 164 RAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 240 DWFVKECEMENIPRQIEFARLNINNTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNS 319
Cdd:PRK05347 244 DWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 320 TVDSQMLDYFLRENLQPKAPLTMGVLRPLKLIITNYPEDKIEMLEIENNAKDESQGKRLVPFSRELYIEQDDFMEEPVKK 399
Cdd:PRK05347 324 VIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPKK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 400 YFRFFPGNEVRLKGAYFVKCTDVIKDENGNVVEIHGTYDPETKSGSGFTGRKVKSTIHWVDAKSAIPCEFRLFEPLILDD 479
Cdd:PRK05347 404 YFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524214 480 IPEnEGKHFLEQINPNSLEILQGFVEPTqIKDAKPFDKFQFVRNGFFSIDnKYTTDEKFVFNRIVPLKSSFKP 552
Cdd:PRK05347 484 NPA-AGKDFLDFLNPDSLVIKQGFVEPS-LADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
7-554 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 827.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 7 SSNFIKNIIINDLETGKHDSIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVK 86
Cdd:PRK14703 12 SPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 87 WLGFDWNE-LNFASNYFDEMYKRALILIKKGKAYVCDLTQEEMREYRGTLTEPGKESPHRNRTIEENLDLFERMKNGEFK 165
Cdd:PRK14703 92 WLGFDWGEhLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 166 DGEKTLRAKIDMSSPNINLRDPIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKE 245
Cdd:PRK14703 172 DGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 246 C-EMENIPRQIEFARLNINNTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQ 324
Cdd:PRK14703 252 LgPWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 325 MLDYFLRENLQPKAPLTMGVLRPLKLIITNYPEDKIEMLEIENNAKD-ESQGKRLVPFSRELYIEQDDFMEEPVKKYFRF 403
Cdd:PRK14703 332 VLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKRL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 404 FPGNEVRLKGAYFVKCTDVIKDENGNVVEIHGTYDPETKSGSGfTGRKVKSTIHWVDAKSAIPCEFRLFEPLILDDIPEN 483
Cdd:PRK14703 412 TPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGED-TGRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEA 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524214 484 EGKHFLEQINPNSLEILQGFVEPTqIKDAKPFDKFQFVRNGFFSIDNKYTTDEKFVFNRIVPLKSSFKPGK 554
Cdd:PRK14703 491 ADEDFLEFLNPDSLRVAQGRVEPA-VRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
29-550 |
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: 667.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 29 TRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWN-ELNFASNYFDEMYK 107
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 108 RALILIKKGKAYVCDLTQEEMREYRGTLTEPGKESPHRNRTIEENLDLFERMKNGEFKDGEKTLRAKIDMSSPNINLRDP 187
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 188 IIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMENIPRQIEFARLNINNTVM 267
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 268 SKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQMLDYFLRENLQPKAPLTMGVLRP 347
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 348 LKLIITNYpEDKIEMLEIENNAKDESQGKRLVPFSRELYIEQDDFMEEPVKKYFRFFPGNEVRLKGAYFVKCTDVIKDEN 427
Cdd:TIGR00440 323 VEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 428 GNVVEIHGTYDPETKSGSGFTGRKVKSTIHWVDAKSAIPCEFRLFEPLILDDIPENEgKHFLEQINPNSLEILQGFVEPT 507
Cdd:TIGR00440 402 GKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAP-DDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489524214 508 qIKDAKPFDKFQFVRNGFFSIDNKYTTDEKFVFNRIVPLKSSF 550
Cdd:TIGR00440 481 -LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
27-554 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 555.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 27 IITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNELNFASNYFDEMY 106
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELY 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 107 KRALILIKKGKAYVCDLTQEEMREYRgtltEPGKESPHRNRTIEENLDLFERMKNGEFKDGEKTLRAKIDMSSPNINLRD 186
Cdd:PLN02859 345 ELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYD 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 187 PIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMEnIPRQIEFARLNINNTV 266
Cdd:PLN02859 421 LIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY-QPYVWEYSRLNVTNTV 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 267 MSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKV-NSTVDSQMLDYFLRENLQPKAPLTMGVL 345
Cdd:PLN02859 500 MSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdNSLIRMDRLEHHIREELNKTAPRTMVVL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 346 RPLKLIITNYPEDKIEMLEIE---NNAKDESQGKRLVPFSRELYIEQDDFMEEPVKKYFRFFPGNEVRLKGAYFVKCTDV 422
Cdd:PLN02859 580 HPLKVVITNLESGEVIELDAKrwpDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKCTDV 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 423 I-KDENGNVVEIHGTYDPETKSgsgftgrKVKSTIHWVDAKS----AIPCEFRLFEPLILDDIPeNEGKHFLEQINPNSL 497
Cdd:PLN02859 660 VlADDNETVVEIRAEYDPEKKT-------KPKGVLHWVAEPSpgvePLKVEVRLFDKLFLSENP-AELEDWLEDLNPQSK 731
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524214 498 EILQGFVEPTQIKDAKPFDKFQFVRNGFFSIDnKYTTDEKFVFNRIVPLKSSFKPGK 554
Cdd:PLN02859 732 EVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
23-547 |
4.97e-150 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 442.88 E-value: 4.97e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 23 KHDSIIT-----RFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNELNF 97
Cdd:PTZ00437 43 KHEAVTGgkpyfRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 98 ASNYFDEMYKRALILIKKGKAYVCDLTQEEMREYRgtltEPGKESPHRNRTIEENLDLFERMKNGEFKDGEKTLRAKIDM 177
Cdd:PTZ00437 123 SSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 178 SSPNINLRDPIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMENiPRQIEF 257
Cdd:PTZ00437 199 KSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWR-PHVWEF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 258 ARLNINNTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQMLDYFLRENLQPK 337
Cdd:PTZ00437 278 SRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDER 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 338 APLTMGVLRPLKLIITNYPEDKIemLEIENNAKDESQGKRLVPFSRELYIEQDDF-MEEPVKKYFRFFPGNE-VRLKGAY 415
Cdd:PTZ00437 358 CERRLMVIDPIKVVVDNWKGERE--FECPNHPRKPELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPGPRvVGLKYSG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 416 FVKCTDVIKDENGNVVEIHGTYDPETKSgsgftgrKVKSTIHWVDAKSAIPCEFRLFEPLILDDIPENEgKHFLEQINPN 495
Cdd:PTZ00437 436 NVVCKGFEVDAAGQPSVIHVDIDFERKD-------KPKTNISWVSATACTPVEVRLYNALLKDDRAAID-PEFLKFIDED 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489524214 496 SLEILQGFVEPtQIKDAKPFDKFQFVRNGFFSIDNKyTTDEKFVFNRIVPLK 547
Cdd:PTZ00437 508 SEVVSHGYAEK-GIENAKHFESVQAERFGYFVVDPD-TRPDHLVMNRVLGLR 557
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-339 |
3.34e-142 |
|
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: 410.10 E-value: 3.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 27 IITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNELNFASNYFDEMY 106
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 107 KRALILIKKGKAYVcdltqeemreyrgtltepgkesphrnrtieenldlfermkngefkdgektlrakidmsspninlrd 186
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 187 piiyrishstHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMENiPRQIEFARLNINNTV 266
Cdd:cd00807 96 ----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYTV 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524214 267 MSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQMLDYFLRENLQPKAP 339
Cdd:cd00807 165 MSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAP 237
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
29-336 |
6.05e-136 |
|
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: 397.07 E-value: 6.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 29 TRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNE-LNFASNYFDEMYK 107
Cdd:pfam00749 4 TRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYgPYYQSDRFDIYYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 108 RALILIKKGKAYVCDLTQEEMREYRGTLtePGKESPHRNRTIEENLDLF-ERMKNGEFKDGEKTLRAKIDMSSPnINLRD 186
Cdd:pfam00749 84 YAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 187 PIIYRI---SHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMENIPRQIEFARLNIN 263
Cdd:pfam00749 161 PVRGRIkftPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524214 264 NTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSK-VNSTVDSQMLDYFLRENLQP 336
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKsFDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
25-475 |
9.62e-129 |
|
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: 384.53 E-value: 9.62e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 25 DSIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNE-LNFASNYFD 103
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 104 EMYKRALILIKKGKAYVCDLTQEEMREYRGTLTEPGKE----SPHRNRTIEEnldLFERMKNGEfkdgEKTLRAKI---- 175
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPprydGRCRDLSPEE---LERMLAAGE----PPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 176 ----DMSS-----PNINLRDPIIYRishsthhntGDKwciYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKEC 246
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR---------ADG---YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 247 EMEnIPrqiEFARLNI----NNTVMSKRKlkqlvdeGIVdgwddprvpTISGIRRKGYTAEALRNFCSEIGVSKVNSTV- 321
Cdd:COG0008 224 GWE-PP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEi 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 322 --DSQMLDYFLRENLqPKApltMGVLRPLKLIITNYP-------EDKIEMLEIEN-NAKDESQGKRLVPFSRE------- 384
Cdd:COG0008 284 fsLEELIEAFDLDRV-SRS---PAVFDPVKLVWLNGPyiralddEELAELLAPELpEAGIREDLERLVPLVREraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 385 -------LYIEQDDfmEEPVKKyfRFFPgNEVRLkgayFVKCTdvikdenGNVVEIHGTYDPETksgsgftgrkVKSTIH 457
Cdd:COG0008 360 laelarfFFIERED--EKAAKK--RLAP-EEVRK----VLKAA-------LEVLEAVETWDPET----------VKGTIH 413
|
490 500
....*....|....*....|.
gi 489524214 458 WVDAKSaipcEFR---LFEPL 475
Cdd:COG0008 414 WVSAEA----GVKdglLFMPL 430
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
18-482 |
1.39e-114 |
|
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: 351.05 E-value: 1.39e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 18 DLETGKHDSIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNELNF 97
Cdd:TIGR00463 85 ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 98 ASNYFDEMYKRALILIKKGKAYVCDLTQEEMREYRGTltepGKESPHRNRTIEENLDLFERMKNGEFKDGEKTLRAKIDM 177
Cdd:TIGR00463 165 QSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 178 SSPNINLRDPIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFED--QRPLYDWFVKECEMeniPRQI 255
Cdd:TIGR00463 241 KHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEP---PEFI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 256 EFARLNIN--NTVMSKRKLKQLVDeGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQMLDYFLREN 333
Cdd:TIGR00463 318 HWGRLKIDdvRALSTSSARKGILR-GEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 334 LQPKAPLTMGVLRPLKLIITNYPEDKIEMLEIenNAKDESQGKRLVPFSRELYIEQDDFMEEPvkkyfrffpgNEVRLKG 413
Cdd:TIGR00463 397 IDEEARRYFFIWNPVKIEIVGLPEPKRVERPL--HPDHPEIGERVLILRGEIYVPKDDLEEGV----------EPVRLMD 464
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524214 414 AYfvkctDVIKDENGNVVeihgtydpetkSGSGFTG--RKVKSTIHWVDAKSAIPCEFRLFEPLILDDIPE 482
Cdd:TIGR00463 465 AV-----NVIYSKKELRY-----------HSEGLEGarKLGKSIIHWLPAKDAVKVKVIMPDASIVEGVIE 519
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
18-540 |
3.14e-112 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 345.30 E-value: 3.14e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 18 DLETGKHDSIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPL--KEDVEYVESIKEDVKWLGFDWNEL 95
Cdd:PRK04156 93 PLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDEV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 96 NFASNYFDEMYKRALILIKKGKAYVCDLTQEEMREYRgtltEPGKESPHRNRTIEENLDLFERMKNGEFKDGEKTLRAKI 175
Cdd:PRK04156 173 VIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 176 DMSSPNINLRDPIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFED----QRPLYDWFVKEcemenI 251
Cdd:PRK04156 249 DLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYDYFGWE-----Y 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 252 PRQIEFARLNINNTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQMLDYFLR 331
Cdd:PRK04156 324 PETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINR 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 332 ENLQPKAPLTMGVLRPLKLIITNYPEDKIemlEIENNAKDESQGKRLVPFSRELYIEQDDFMEEpvkkyfrffpGNEVRL 411
Cdd:PRK04156 404 KLIDPIANRYFFVRDPVELEIEGAEPLEA---KIPLHPDRPERGEREIPVGGKVYVSSDDLEAE----------GKMVRL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 412 KGAYFVKctdvIKDENGNVVEIHGTYDPETKSGsgftgrKVKsTIHWVDAKSAIPCEFRlfeplilddIPENegkhfleq 491
Cdd:PRK04156 471 MDLFNVE----ITGVSVDKARYHSDDLEEARKN------KAP-IIQWVPEDESVPVRVL---------KPDG-------- 522
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489524214 492 inpnslEILQGFVEPtQIKDAKPFDKFQFVRNGFFSIDNKYTTDEKFVF 540
Cdd:PRK04156 523 ------GDIEGLAEP-DVADLEVDDIVQFERFGFVRIDSVEDDEVVAYF 564
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
18-496 |
4.24e-111 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 347.10 E-value: 4.24e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 18 DLETGKHDSIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNELNF 97
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTY 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 98 ASNYFDEMYKRALILIKKGKAYVCDLTQEEMREYRGTltepGKESPHRNRTIEENLDLFERMKNGEFKDGEKTLRAKIDM 177
Cdd:PLN02907 285 TSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDM 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 178 SSPNINLRDPIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMENIprQI-E 256
Cdd:PLN02907 361 QDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKV--HIwE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 257 FARLNINNTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNS--------TVDSQMLDy 328
Cdd:PLN02907 439 FSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNlmewdklwTINKKIID- 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 329 flrenlqPKAPLTMGVLRPLKLIIT--NYPEdKIEMLEIENNAKDESQGKRLVPFSRELYIEQDDfmEEPVKKyfrffpG 406
Cdd:PLN02907 518 -------PVCPRHTAVLKEGRVLLTltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD--AEAISE------G 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 407 NEVRLK--GAYFVKctDVIKDENGNVVEIHGTYDPEtksGSgftgrkVKST---IHWV-DAKSAIPCEFRLFEPLILDDI 480
Cdd:PLN02907 582 EEVTLMdwGNAIIK--EITKDEGGAVTALSGELHLE---GS------VKTTklkLTWLpDTNELVPLSLVEFDYLITKKK 650
|
490
....*....|....*.
gi 489524214 481 PEnEGKHFLEQINPNS 496
Cdd:PLN02907 651 LE-EDDNFLDVLNPCT 665
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
16-545 |
1.54e-104 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 324.27 E-value: 1.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 16 INDLETGKHDSIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNEL 95
Cdd:PLN03233 1 MNALEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 96 NFASNYFDEMYKRALILIKKGKAYVCDLTQEEMREYRGTLtepgKESPHRNRTIEENLDLFERMKNGEFKDGEKTLRAKI 175
Cdd:PLN03233 81 SFTSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADR----AESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 176 DMSSPNINLRDPIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMENiPRQI 255
Cdd:PLN03233 157 DMQSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRR-PRIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 256 EFARLNINNTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSK--VNstvdsqmLDY--FLR 331
Cdd:PLN03233 236 AFARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRrvVN-------LDWakFWA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 332 EN---LQPKAPLTMGVLRP--LKLIITNYPED-KIEMLEIENNAKDESQGKRLVPFSRELYIEQDDFMEEPVkkyfrffp 405
Cdd:PLN03233 309 ENkkeIDKRAKRFMAIDKAdhTALTVTNADEEaDFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQL-------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 406 GNEVRLKGAYFVKCTDVIKDENGNVVEihgtyDPETKSGsgftgrkvKSTIHWV-DAKSAIPCEFRLFEPLILDDIPENE 484
Cdd:PLN03233 381 GEDIVLLRWGVIEISKIDGDLEGHFIP-----DGDFKAA--------KKKISWIaDVSDNIPVVLSEFDNLIIKEKLEED 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524214 485 GKhFLEQINPNSLEILQgFVEPTQIKDAKPFDKFQFVRNGFFSIDNKYTTDEKFVFNRIVP 545
Cdd:PLN03233 448 DK-FEDFINPDTLAETD-VIGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPLILFMIP 506
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
14-530 |
3.23e-93 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 297.26 E-value: 3.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 14 IIINDLETGKhdsIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWN 93
Cdd:PTZ00402 43 LQLTNAEEGK---VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 94 E-LNFASNYFDEMYKRALILIKKGKAYvCDLT-QEEMREYRGTltepGKESPHRNRTIEENLDLFERMKNGEFKDGEKTL 171
Cdd:PTZ00402 120 VgPTYSSDYMDLMYEKAEELIKKGLAY-CDKTpREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 172 RAKIDMSSPNINLRDPIIYRISHSTHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFvkeCEMENI 251
Cdd:PTZ00402 195 RAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWF---CDALGI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 252 PRQI--EFARLNINNTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQMLDYF 329
Cdd:PTZ00402 272 RKPIveDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 330 LRENLQPKAPLTMGVLRPLKLIITNYPEDKIEMLEIENNAKDESQGKRLVPFSRELYIEQDD--FMEEpvkkyfrffpGN 407
Cdd:PTZ00402 352 NTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDvaLLKE----------GD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 408 EVRLK--GAYFVKctDVIK-DENGNVVEIHGTYDPETKSgsgftgRKVKSTIHWV-DAKSAIPCEFRLFEPLILDDIPEN 483
Cdd:PTZ00402 422 EVTLMdwGNAYIK--NIRRsGEDALITDADIVLHLEGDV------KKTKFKLTWVpESPKAEVMELNEYDHLLTKKKPDP 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 489524214 484 EGKhfLEQINPNSLEILQGFVEPTQIKDAKPFDKFQFVRNGFFSIDN 530
Cdd:PTZ00402 494 EES--IDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDD 538
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
338-529 |
2.31e-65 |
|
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: 210.21 E-value: 2.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 338 APLTMGVLRPLKLIITNYPEDKIEMLEIENNAKDESQGKRLVPFSRELYIEQDDFmeepvkkyFRFFPGNEVRLKGAYFV 417
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 418 KCTDVIKDENGNVVEIHGTYDPETKSGSgftgRKVK-STIHWVDAKSAIPCEFRLFEPLILDDipenEGKHFLeqINPNS 496
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKgKIIHWVSASDAVPAEVRLYDRLFKDE----DDADFL--LNPDS 142
|
170 180 190
....*....|....*....|....*....|....
gi 489524214 497 LEIL-QGFVEPtQIKDAKPFDKFQFVRNGFFSID 529
Cdd:pfam03950 143 LKVLtEGLAEP-ALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
27-316 |
4.87e-58 |
|
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: 193.07 E-value: 4.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 27 IITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNE-LNFASNYFDEM 105
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEgPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 106 YKRALILIKKGkayvcdltqeemreyrgtltepgkesphrnrtieenldlfermkngefkdgektlrakidmsspninlr 185
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 186 dpiiyrishsthhntgdkwcIYPMYAFAHPIEDAIEGITHSICTLEFEDQRPLYDWFVKECEMEnIPRQIEFARLNI-NN 264
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLeDG 151
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489524214 265 TVMSKRKLkqlvdegivdgwddprVPTISGIRRKGYTAEALRNFCSEIGVSK 316
Cdd:cd00418 152 TKLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSK 187
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
27-339 |
1.92e-54 |
|
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: 184.09 E-value: 1.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 27 IITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNP--LKEDVEYVESIKEDVKWLGFDWNELNFASNYFDE 104
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 105 MYKRALILIKKGKAYVcdltqeemreyrgtltepgkesphrnrtieenldlfermkngefkdgektlrakidmsspninl 184
Cdd:cd09287 82 YYEYARKLIEMGGAYV---------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 185 rdpiiyrishstHHNTGDKWCIYPMYAFAHPIEDAIEGITHSICTLEFED----QRPLYDWFVKEcemenIPRQIEFARL 260
Cdd:cd09287 98 ------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEYFGWE-----YPETIHWGRL 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524214 261 NINNTVMSKRKLKQLVDEGIVDGWDDPRVPTISGIRRKGYTAEALRNFCSEIGVSKVNSTVDSQMLDYFLRENLQPKAP 339
Cdd:cd09287 161 KIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRAN 239
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
26-315 |
3.76e-15 |
|
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: 74.93 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 26 SIITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNElnfasnyfdem 105
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 106 ykralilikkgkayvcdltqeemREYRGTLTEPGKESphrnrtieenldlfERmkNGEFKDGEKTLRAKidmsspninlr 185
Cdd:cd00808 70 -----------------------GPDVGGPYGPYRQS--------------ER--LEIYRKYAEKLLEK----------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 186 dpiiyrishsthhntGDKwciYPMYAFAHPIEDAIEGITHSIctlefedqRPlYDWFVkecemeNIPRQI---------- 255
Cdd:cd00808 100 ---------------GDG---FPTYHLANVVDDHLMGITHVI--------RG-EEHLS------STPKQIllyealgwep 146
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524214 256 -EFARL----NINNTVMSKRKLKQLvdegivdgwddprvptISGIRRKGYTAEALRNFCSEIGVS 315
Cdd:cd00808 147 pKFAHLplilNPDGKKLSKRKGDTS----------------ISDYREEGYLPEALLNYLALLGWS 195
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
28-139 |
8.08e-13 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 69.11 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 28 ITRFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWN-ELNFASNYFDEmY 106
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDgPVLYQSQRHDA-Y 85
|
90 100 110
....*....|....*....|....*....|....
gi 489524214 107 KRAL-ILIKKGKAYVCDLTQEEMREYRGTLTEPG 139
Cdd:PRK05710 86 RAALdRLRAQGLVYPCFCSRKEIAAAAPAPPDGG 119
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
30-130 |
5.11e-12 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 68.23 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 30 RFPPEPNGYLHIGHAKSICLNFGLAKEFNGKANLRFDDTNPLKEDVEYVESIKEDVKWLGFDWNELNFASNYF------- 102
Cdd:PLN02627 49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYgpyrqse 128
|
90 100 110
....*....|....*....|....*....|...
gi 489524214 103 -DEMYKR-ALILIKKGKAYVCDLTQEE---MRE 130
Cdd:PLN02627 129 rNAIYKQyAEKLLESGHVYPCFCTDEEleaMKE 161
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
28-103 |
7.89e-11 |
|
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: 60.19 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 28 ITRFPPEPNGYLHIGHAKSICLNFGLAKE-----FNGKANLRFDDTNPLKEDV-------------EYVESIKEDVKWLg 89
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDPankkgenakafveRWIERIKEDVEYM- 79
|
90
....*....|....*.
gi 489524214 90 FDW--NELNFASNYFD 103
Cdd:cd00802 80 FLQaaDFLLLYETECD 95
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
29-92 |
2.75e-09 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 54.85 E-value: 2.75e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524214 29 TRFPPEPnGYLHIGHAKSICLNFGLAkefnGKANLRFDDTNPLK------EDVEYVESIKEDVKWLGFDW 92
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDF 66
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| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
225-271 |
5.65e-05 |
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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: 42.53 E-value: 5.65e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489524214 225 HSICTLEFEDQRPLYDWFVKECEMENIPRQIEFARLNINNTVMSKRK 271
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
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