|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-553 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1235.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 1 MSEAEARPTNFIRQIIDEDLATGKHNTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVE 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 81 SIKHDVQWLGFDWSGDIHYSSDYFDQLHAYALELINKGLAYVDELSPDQIREYRGSLTSPGKNSPYRDRSVEENIALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 161 MRNGEFAEGAACLRAKIDMASPFFVMRDPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 241 YDWVLDNISIPCHPRQYEFSRLNLEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 321 NNVEMMALESCIRDDLNENAPRAMAVINPVKVIIENFTGDDVQRVKMPNHPSKPEMGTREVPFTREIYIDQADFREEANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 401 QYKRLVLGKEVRLRNAYVIKAERIEKDAEGNITTIFCSYDIDTLSKDPADGRKVKGVIHWVSASEGKPAEFRLYDRLFSV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2169659252 481 ANPGQAEDFLTTINPESLVISHGFVEPSLVAAQAEISLQFEREGYFCADsRYSRAEHLVFNRTVGLRDTWESK 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-550 |
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: 965.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDIHYSSDYFDQL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 108 HAYALELINKGLAYVDELSPDQIREYRGSLTSPGKNSPYRDRSVEENIALFEKMRNGEFAEGAACLRAKIDMASPFFVMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 188 DPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIPCHPRQYEFSRLNLEYS 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 268 IMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNNVEMMALESCIRDDLNENAPRAMAVI 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 348 NPVKVIIENFTgDDVQRVKMPNHPSKPEMGTREVPFTREIYIDQADFREEANKQYKRLVLGKEVRLRNAYVIKAERIEKD 427
Cdd:TIGR00440 321 DPVEVVIENLS-DEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 428 AEGNITTIFCSYDIDTLSKDPADGRKVKGVIHWVSASEGKPAEFRLYDRLFSVANPGQAEDFLTTINPESLVISHGFVEP 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2169659252 508 SLVAAQAEISLQFEREGYFCADSRYSRAEHLVFNRTVGLRDTW 550
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
2.39e-163 |
|
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: 466.80 E-value: 2.39e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDIHYSSDYFDQL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 108 HAYALELINKGLAYVDELSPDQIREYRGslTSPGKNSPYRDRSVEENIALF-EKMRNGEFAEGAACLRAKIDMASPFfVM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESPY-VF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 187 RDPVLYRIKFAE---HHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIPCHPRQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2169659252 264 LEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQ-DNNVEMMALESCIRDDLNE 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-342 |
2.31e-151 |
|
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: 433.60 E-value: 2.31e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWsGDIHYSSDYFDQ 106
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 107 LHAYALELINKGLAYVdelspdqireyrgsltspgknspyrdrsveenialfekmrngefaegaaclrakidmaspffvm 186
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 187 rdpvlyrikfaeHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIPChPRQYEFSRLNLEY 266
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2169659252 267 SIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNNVEMMALESCIRDDLNENAPR 342
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-526 |
2.84e-128 |
|
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: 383.37 E-value: 2.84e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 26 NTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDIHYSSDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 106 QLHAYALELINKGLAYVDELSPDQIREYRGSLTSPGKNSPY----RDRSVEENialfEKMRngefAEG-AACLRAKI--- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGePPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 178 -----DMAS-----PFFVMRDPVLYRikfaehhQTGkkwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDN 247
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 248 ISIPcHPrqyEFSRLNLEY----SIMSKRKlnqlvteKIVegwddprmpTVSGLRRRGYTAASIREFCRRIGVTKQDNNV 323
Cdd:COG0008 223 LGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 324 --EMMALESCIrdDLNENaPRAMAVINPVKVIIEN------FTGDDVQRVKMPNHPSK--PEMGTREVPFTRE------- 386
Cdd:COG0008 283 ifSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAgiREDLERLVPLVREraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 387 -------IYIDQADfrEEANKqyKRLVLgKEVRLrnayVIKAERiekDAEGNITTifcsYDIDTlskdpadgrkVKGVIH 459
Cdd:COG0008 360 laelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL---EVLEAVET----WDPET----------VKGTIH 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 460 WVSASEGkpaefrLYDRLFSVanpgqaedflttinPESLVISHGFVEPSLvAAQAEISLQ---FEREGYF 526
Cdd:COG0008 414 WVSAEAG------VKDGLLFM--------------PLRVALTGRTVEPSL-FDVLELLGKervFERLGYA 462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-553 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1235.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 1 MSEAEARPTNFIRQIIDEDLATGKHNTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVE 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 81 SIKHDVQWLGFDWSGDIHYSSDYFDQLHAYALELINKGLAYVDELSPDQIREYRGSLTSPGKNSPYRDRSVEENIALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 161 MRNGEFAEGAACLRAKIDMASPFFVMRDPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 241 YDWVLDNISIPCHPRQYEFSRLNLEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 321 NNVEMMALESCIRDDLNENAPRAMAVINPVKVIIENFTGDDVQRVKMPNHPSKPEMGTREVPFTREIYIDQADFREEANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 401 QYKRLVLGKEVRLRNAYVIKAERIEKDAEGNITTIFCSYDIDTLSKDPADGRKVKGVIHWVSASEGKPAEFRLYDRLFSV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2169659252 481 ANPGQAEDFLTTINPESLVISHGFVEPSLVAAQAEISLQFEREGYFCADsRYSRAEHLVFNRTVGLRDTWESK 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-550 |
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: 965.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDIHYSSDYFDQL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 108 HAYALELINKGLAYVDELSPDQIREYRGSLTSPGKNSPYRDRSVEENIALFEKMRNGEFAEGAACLRAKIDMASPFFVMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 188 DPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIPCHPRQYEFSRLNLEYS 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 268 IMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNNVEMMALESCIRDDLNENAPRAMAVI 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 348 NPVKVIIENFTgDDVQRVKMPNHPSKPEMGTREVPFTREIYIDQADFREEANKQYKRLVLGKEVRLRNAYVIKAERIEKD 427
Cdd:TIGR00440 321 DPVEVVIENLS-DEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 428 AEGNITTIFCSYDIDTLSKDPADGRKVKGVIHWVSASEGKPAEFRLYDRLFSVANPGQAEDFLTTINPESLVISHGFVEP 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2169659252 508 SLVAAQAEISLQFEREGYFCADSRYSRAEHLVFNRTVGLRDTW 550
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
1-550 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 864.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 1 MSEAEaRPT-----NFIRQIIDEDLATGKHNTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKED 75
Cdd:PRK14703 1 MSDAP-RPRmlvspNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 76 IEFVESIKHDVQWLGFDWSGDIHYSSDYFDQLHAYALELINKGLAYVDELSPDQIREYRGSLTSPGKNSPYRDRSVEENI 155
Cdd:PRK14703 80 TEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 156 ALFEKMRNGEFAEGAACLRAKIDMASPFFVMRDPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQ 235
Cdd:PRK14703 160 DLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 236 DNRRLYDWVLDNIS-IPCHPRQYEFSRLNLEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRI 314
Cdd:PRK14703 240 NNRAIYDWVLDHLGpWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 315 GVTKQDNNVEMMALESCIRDDLNENAPRAMAVINPVKVIIENFTGDDVQRVKMPNHPSK-PEMGTREVPFTREIYIDQAD 393
Cdd:PRK14703 320 GVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 394 FREEANKQYKRLVLGKEVRLRNAYVIKAERIEKDAEGNITTIFCSYDIDTLSKDPAdGRKVKGVIHWVSASEGKPAEFRL 473
Cdd:PRK14703 400 FSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2169659252 474 YDRLFSVANP-GQAEDFLTTINPESLVISHGFVEPSLVAAQAEISLQFEREGYFCADSRYSRAEHLVFNRTVGLRDTW 550
Cdd:PRK14703 479 YDRLFKVPQPeAADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTW 556
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
7-550 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 593.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 7 RPTNfIRQIIDEDL-ATGkhNTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHD 85
Cdd:PLN02859 246 RPSN-TKEILEKHLkATG--GKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 86 VQWLGfdWSG-DIHYSSDYFDQLHAYALELINKGLAYVDELSPDQIREYRGSLtspgKNSPYRDRSVEENIALFEKMRNG 164
Cdd:PLN02859 323 VEWMG--WEPfKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKK----MNSPWRDRPIEESLKLFEDMRRG 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 165 EFAEGAACLRAKIDMASPFFVMRDPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWV 244
Cdd:PLN02859 397 LIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 245 LDNISIpCHPRQYEFSRLNLEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNN-V 323
Cdd:PLN02859 477 LDSLGL-YQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSlI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 324 EMMALESCIRDDLNENAPRAMAVINPVKVIIENFTGDDVQRV---KMPNHPSKPEMGTREVPFTREIYIDQADFREEANK 400
Cdd:PLN02859 556 RMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSK 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 401 QYKRLVLGKEVRLRNAYVIK-AERIEKDAEGNITTIFCSYdidtlskDPADGRKVKGVIHWVS-ASEGK---PAEFRLYD 475
Cdd:PLN02859 636 DYYGLAPGKSVLLRYAFPIKcTDVVLADDNETVVEIRAEY-------DPEKKTKPKGVLHWVAePSPGVeplKVEVRLFD 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2169659252 476 RLFSVANPGQAEDFLTTINPES-LVISHGFVEPSLVAAQAEISLQFEREGYFCADsRYSRAEHLVFNRTVGLRDTW 550
Cdd:PLN02859 709 KLFLSENPAELEDWLEDLNPQSkEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSY 783
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
24-548 |
8.17e-179 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 516.46 E-value: 8.17e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 24 KHNTV-----HTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGF--DWsgd 96
Cdd:PTZ00437 43 KHEAVtggkpYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDW--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 97 IHYSSDYFDQLHAYALELINKGLAYVDELSPDQIREYRGSLtspgKNSPYRDRSVEENIALFEKMRNGEFAEGAACLRAK 176
Cdd:PTZ00437 120 VTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQR----EDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 177 IDMASPFFVMRDPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIpCHPRQ 256
Cdd:PTZ00437 196 ADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 257 YEFSRLNLEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNNVEMMALESCIRDDL 336
Cdd:PTZ00437 275 WEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 337 NENAPRAMAVINPVKVIIENFTGDdvQRVKMPNHPSKPEMGTREVPFTREIYIDQADFR-EEANKQYKRLVLG-KEVRLR 414
Cdd:PTZ00437 355 DERCERRLMVIDPIKVVVDNWKGE--REFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 415 NAYVIKAERIEKDAEGNITTIFCsyDIDTLSKDpadgrKVKGVIHWVSASEGKPAEFRLYDRLFSVANPGQAEDFLTTIN 494
Cdd:PTZ00437 433 YSGNVVCKGFEVDAAGQPSVIHV--DIDFERKD-----KPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFID 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2169659252 495 PESLVISHGFVEPSLVAAQAEISLQFEREGYFCADSRySRAEHLVFNRTVGLRD 548
Cdd:PTZ00437 506 EDSEVVSHGYAEKGIENAKHFESVQAERFGYFVVDPD-TRPDHLVMNRVLGLRE 558
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
2.39e-163 |
|
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: 466.80 E-value: 2.39e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDIHYSSDYFDQL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 108 HAYALELINKGLAYVDELSPDQIREYRGslTSPGKNSPYRDRSVEENIALF-EKMRNGEFAEGAACLRAKIDMASPFfVM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESPY-VF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 187 RDPVLYRIKFAE---HHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIPCHPRQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2169659252 264 LEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQ-DNNVEMMALESCIRDDLNE 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-342 |
2.31e-151 |
|
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: 433.60 E-value: 2.31e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWsGDIHYSSDYFDQ 106
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 107 LHAYALELINKGLAYVdelspdqireyrgsltspgknspyrdrsveenialfekmrngefaegaaclrakidmaspffvm 186
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 187 rdpvlyrikfaeHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIPChPRQYEFSRLNLEY 266
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2169659252 267 SIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNNVEMMALESCIRDDLNENAPR 342
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-526 |
2.84e-128 |
|
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: 383.37 E-value: 2.84e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 26 NTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDIHYSSDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 106 QLHAYALELINKGLAYVDELSPDQIREYRGSLTSPGKNSPY----RDRSVEENialfEKMRngefAEG-AACLRAKI--- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGePPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 178 -----DMAS-----PFFVMRDPVLYRikfaehhQTGkkwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDN 247
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 248 ISIPcHPrqyEFSRLNLEY----SIMSKRKlnqlvteKIVegwddprmpTVSGLRRRGYTAASIREFCRRIGVTKQDNNV 323
Cdd:COG0008 223 LGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 324 --EMMALESCIrdDLNENaPRAMAVINPVKVIIEN------FTGDDVQRVKMPNHPSK--PEMGTREVPFTRE------- 386
Cdd:COG0008 283 ifSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAgiREDLERLVPLVREraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 387 -------IYIDQADfrEEANKqyKRLVLgKEVRLrnayVIKAERiekDAEGNITTifcsYDIDTlskdpadgrkVKGVIH 459
Cdd:COG0008 360 laelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL---EVLEAVET----WDPET----------VKGTIH 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 460 WVSASEGkpaefrLYDRLFSVanpgqaedflttinPESLVISHGFVEPSLvAAQAEISLQ---FEREGYF 526
Cdd:COG0008 414 WVSAEAG------VKDGLLFM--------------PLRVALTGRTVEPSL-FDVLELLGKervFERLGYA 462
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
19-556 |
2.92e-118 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 365.97 E-value: 2.92e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 19 DLATGKHNTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSgDIH 98
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 99 YSSDYFDQLHAYALELINKGLAYVDELSPDQIREYRGSltspGKNSPYRDRSVEENIALFEKMRNGEFAEGAACLRAKID 178
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 179 MASPFFVMRDPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIPcHPRQYE 258
Cdd:PLN02907 360 MQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHIWE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 259 FSRLNLEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNNVEMMALESCIRDDLNE 338
Cdd:PLN02907 439 FSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDP 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 339 NAPRAMAVINPVKVIIENFTGDDVQRVKM-PNHPSKPEMGTREVPFTREIYIDQADFREeankqykrLVLGKEVRLR--- 414
Cdd:PLN02907 519 VCPRHTAVLKEGRVLLTLTDGPETPFVRIiPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLMdwg 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 415 NAYVikaERIEKDAEGNITTIFCSYDIDtlskdpADGRKVKGVIHWVSA-SEGKPAEFRLYDRLFSVANPGQAEDFLTTI 493
Cdd:PLN02907 591 NAII---KEITKDEGGAVTALSGELHLE------GSVKTTKLKLTWLPDtNELVPLSLVEFDYLITKKKLEEDDNFLDVL 661
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2169659252 494 NPESLVISHGFVEPSLVAAQAEISLQFEREGYFCADSRYSRAehlvfnrtvglrdtweSKPVV 556
Cdd:PLN02907 662 NPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRS----------------SKPIV 708
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
2-530 |
8.73e-115 |
|
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: 351.82 E-value: 8.73e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 2 SEAEARPTNFIRqiideDLATGKHNTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVES 81
Cdd:TIGR00463 73 IKKKEKKRKGLR-----ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 82 IKHDVQWLGFDWSgDIHYSSDYFDQLHAYALELINKGLAYVDELSPDQIREYRGSltspGKNSPYRDRSVEENIALFEKM 161
Cdd:TIGR00463 148 ILEDLEWLGVKWD-EVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 162 RNGEFAEGAACLRAKIDMASPFFVMRDPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR-- 239
Cdd:TIGR00463 223 LEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkq 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 240 LYDWVLDNISIPcHPRQYEFSRLNLEYSIMSKRKLnQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQ 319
Cdd:TIGR00463 303 EYIYRYFGWEPP-EFIHWGRLKIDDVRALSTSSAR-KGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKIN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 320 DNNVEMMALESCIRDDLNENAPRAMAVINPVKVIIENFTGDdvQRVKMPNHPSKPEMGTREVPFTREIYIDQADFREean 399
Cdd:TIGR00463 381 DVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEP--KRVERPLHPDHPEIGERVLILRGEIYVPKDDLEE--- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 400 kqykrlvLGKEVRLRNAYVIKAEriEKDAEgnittiFCSYDIDtlskdpADGRKVKGVIHWVSASEGKPAEFRLYDRLfs 479
Cdd:TIGR00463 456 -------GVEPVRLMDAVNVIYS--KKELR------YHSEGLE------GARKLGKSIIHWLPAKDAVKVKVIMPDAS-- 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2169659252 480 vanpgqaedflttinpeslvISHGFVEPSLVAAQAEISLQFEREGYFCADS 530
Cdd:TIGR00463 513 --------------------IVEGVIEADASELEVGDVVQFERFGFARLDS 543
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
28-525 |
9.35e-108 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 333.74 E-value: 9.35e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPA--KEDIEFVESIKHDVQWLGFDWSgDIHYSSDYFD 105
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 106 QLHAYALELINKGLAYVDELSPDQIREYRGSltspGKNSPYRDRSVEENIALFEKMRNGEFAEGAACLRAKIDMASPFFV 185
Cdd:PRK04156 181 IYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 186 MRDPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDN----RRLYD---WVLdnisipchPRQYE 258
Cdd:PRK04156 257 VRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNtekqRYIYDyfgWEY--------PETIH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 259 FSRLNLEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNNVEMMALESCIRDDLNE 338
Cdd:PRK04156 329 YGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 339 NAPRAMAVINPVKVIIEnftGDDVQRVKMPNHPSKPEMGTREVPFTREIYIDQADFREeankqykrlvLGKEVRLRNAYV 418
Cdd:PRK04156 409 IANRYFFVRDPVELEIE---GAEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEA----------EGKMVRLMDLFN 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 419 IKAERIEKDAegnitTIFCSYDIDtlskdpaDGRKVKG-VIHWVSASEGKPaefrlydrlfsvanpgqaedfLTTINPES 497
Cdd:PRK04156 476 VEITGVSVDK-----ARYHSDDLE-------EARKNKApIIQWVPEDESVP---------------------VRVLKPDG 522
|
490 500
....*....|....*....|....*...
gi 2169659252 498 LVIShGFVEPSLVAAQAEISLQFEREGY 525
Cdd:PRK04156 523 GDIE-GLAEPDVADLEVDDIVQFERFGF 549
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
1-530 |
1.95e-105 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 328.85 E-value: 1.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 1 MSEAEARPTNFIRQiidedLATGKHNTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVE 80
Cdd:PTZ00402 31 FTAANANEENDKLQ-----LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 81 SIKHDVQWLGFDWSGDIHYSSDYFDQLHAYALELINKGLAYVDELSPDQIREYRGSltspGKNSPYRDRSVEENIALFEK 160
Cdd:PTZ00402 106 AILDDLATLGVSWDVGPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 161 MRNGEfAEGA-ACLRAKIDMASPFFVMRDPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR 239
Cdd:PTZ00402 182 MKKGS-AEGQeTCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRND 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 240 LYDWVLDNISIPcHPRQYEFSRLNLEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQ 319
Cdd:PTZ00402 261 QYYWFCDALGIR-KPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 320 DNNVEMMALESCIRDDLNENAPRAMAVINPVKV--IIENFTGddVQRVKMPNHPSKPEMGTREVPFTREIYIDQADFree 397
Cdd:PTZ00402 340 VNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVrcTVEGQIH--LEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDV--- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 398 ankqyKRLVLGKEVRLR---NAYVikaERIEKDAEGNITTifcsyDIDTLSKDPADGRKVKGVIHWVSAS-EGKPAEFRL 473
Cdd:PTZ00402 415 -----ALLKEGDEVTLMdwgNAYI---KNIRRSGEDALIT-----DADIVLHLEGDVKKTKFKLTWVPESpKAEVMELNE 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2169659252 474 YDRLFSVANPGQAEDFLTTINPESLVISHGFVEPSLVAAQAEISLQFEREGYFCADS 530
Cdd:PTZ00402 482 YDHLLTKKKPDPEESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDD 538
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
28-532 |
3.84e-97 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 305.01 E-value: 3.84e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDwSGDIHYSSDYFDQL 107
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 108 HAYALELINKGLAYVDELSPDQIREYRGSLtspgKNSPYRDRSVEENIALFEKMRNGEFAEGAACLRAKIDMASPFFVMR 187
Cdd:PLN03233 91 RCYAIILIEEGLAYMDDTPQEEMKKERADR----AESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 188 DPVLYRIKFAEHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIPcHPRQYEFSRLNLEYS 267
Cdd:PLN03233 167 DPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAFARMNFMNT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 268 IMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNNVEMMALESCIRDDLNENAPRAMAV- 346
Cdd:PLN03233 246 VLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAId 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 347 -INPVKVIIENF-TGDDVQRVKMPNHPSKPEMGTREVPFTREIYIDQADfreeankqYKRLVLGKEVRLRNAYVIKAERI 424
Cdd:PLN03233 326 kADHTALTVTNAdEEADFAFSETDCHPKDPGFGKRAMRICDEVLLEKAD--------TEDIQLGEDIVLLRWGVIEISKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 425 EKDAEGNITTifcsydidtlskdPADGRKVKGVIHWVS-ASEGKPAEFRLYDRLFSVANPGQAEDFLTTINPESLVISHG 503
Cdd:PLN03233 398 DGDLEGHFIP-------------DGDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDV 464
|
490 500
....*....|....*....|....*....
gi 2169659252 504 FVEPSLVAAQAEISLQFEREGYFCADSRY 532
Cdd:PLN03233 465 IGDAGLKTLKEHDIIQLERRGFYRVDRPY 493
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
340-529 |
2.48e-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: 244.10 E-value: 2.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 340 APRAMAVINPVKVIIENFTGDDVQRVKMPNHPSKPEMGTREVPFTREIYIDQADFreeankqyKRLVLGKEVRLRNAYVI 419
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 420 KAERIEKDAEGNITTIFCSYDIDTLSKDpadgRKVKG-VIHWVSASEGKPAEFRLYDRLFSVANpgqAEDFLttINPESL 498
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED---DADFL--LNPDSL 143
|
170 180 190
....*....|....*....|....*....|..
gi 2169659252 499 -VISHGFVEPSLVAAQAEISLQFEREGYFCAD 529
Cdd:pfam03950 144 kVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
27-338 |
7.46e-78 |
|
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: 245.07 E-value: 7.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDIHYSSDYFDQ 106
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 107 LHAYALELINKGlayvdelspdqireyrgsltspgknspyrdrsveenialfekmrngefaegaaclrakidmaspffvm 186
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 187 rdpvlyrikfaehhqtgkkwcIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNISIPcHPRQYEFSRLNLEY 266
Cdd:cd00418 93 ---------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLED 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 267 S-IMSKRKLNqlvtekivegwddprmPTVSGLRRRGYTAASIREFCRRIGVTK-----------------------QDNN 322
Cdd:cd00418 151 GtKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKpdghelftleemiaafsvervnsADAT 214
|
330
....*....|....*.
gi 2169659252 323 VEMMALESCIRDDLNE 338
Cdd:cd00418 215 FDWAKLEWLNREYIRE 230
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
28-342 |
2.42e-46 |
|
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: 162.52 E-value: 2.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNP--AKEDIEFVESIKHDVQWLGFDWSgDIHYSSDYFD 105
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 106 QLHAYALELINKGLAYVdelspdqireyrgsltspgknspyrdrsveenialfekmrngefaegaaclrakidmaspffv 185
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 186 mrdpvlyrikfaeHHQTGKKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR----LYD---WVldnisipcHPRQYE 258
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEkqryIYEyfgWE--------YPETIH 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 259 FSRLNLEYSIMSKRKLNQLVTEKIVEGWDDPRMPTVSGLRRRGYTAASIREFCRRIGVTKQDNNVEMMALESCIRDDLNE 338
Cdd:cd09287 157 WGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDP 236
|
....
gi 2169659252 339 NAPR 342
Cdd:cd09287 237 RANR 240
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
29-273 |
2.54e-17 |
|
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: 78.68 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 29 HTRFPPEPNGYLHIGHAKSICLNFGIAQD-----YQGQCNLRFDDTNPAKE--DIEFVESIKHdvqwlgfdwsgdihyss 101
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGdpANKKGENAKA----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 102 dyfdqlhayalelinkglayvdelspdqireyrgsltspgknspYRDRSVEENIALFEkmrngefaegaaclrakidmas 181
Cdd:cd00802 64 --------------------------------------------FVERWIERIKEDVE---------------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 182 pffvmrdpvlyrikfaehhqtgkkwciypmYDFTHCISDALEGITH---SLCTLEFQDNRRLYDWVLDNISIPCHPRQYE 258
Cdd:cd00802 78 ------------------------------YMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLT 127
|
250
....*....|....*.
gi 2169659252 259 FSRLNLEYS-IMSKRK 273
Cdd:cd00802 128 FGRVMGADGtKMSKSK 143
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
30-121 |
7.04e-15 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 75.27 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDIHYSSDYFDqlhA 109
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD---A 84
|
90
....*....|....*
gi 2169659252 110 Y--ALE-LINKGLAY 121
Cdd:PRK05710 85 YraALDrLRAQGLVY 99
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
27-118 |
1.66e-13 |
|
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: 70.31 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDI--------H 98
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPdvggpygpY 80
|
90 100
....*....|....*....|
gi 2169659252 99 YSSDYFDQLHAYALELINKG 118
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG 100
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
29-105 |
1.63e-12 |
|
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: 63.71 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 29 HTRFPPEPnGYLHIGHAKSICLNFGIAqdyqGQCNLRFDDTNPAK------EDIEFVESIKHDVQWLGFDWSGDIHYSSD 102
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNRELYRW 75
|
...
gi 2169659252 103 YFD 105
Cdd:cd02156 76 VKD 78
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
227-273 |
9.21e-12 |
|
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: 61.79 E-value: 9.21e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2169659252 227 HSLCTLEFQDNRRLYDWVLDNISIPCHPRQYEFSRLNLEYSIMSKRK 273
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
21-121 |
4.37e-09 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 58.98 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169659252 21 ATGKHNTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVESIKHDVQWLGFDWSGDIHYS 100
Cdd:PLN02627 39 GESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVG 118
|
90 100
....*....|....*....|....*....
gi 2169659252 101 SDY--FDQ------LHAYALELINKGLAY 121
Cdd:PLN02627 119 GEYgpYRQsernaiYKQYAEKLLESGHVY 147
|
|
| |
