|
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: 1272.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 1 MSEAEARPTNFIRQIIDEDLANGKHTSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVD 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 81 SIKHDVEWLGFHWSGNVRYSSDYFDQLFNYAVELVNKGLAYVDELTPEQIREYRGSLTAPGKNSPYRDRSVEENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 161 MRNGEFAEGTACLRAKIDMASPFIVMRDPVIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 241 YDWVLDNITIPVHPRQYEFSRLNLEYSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 321 NTVEMAALESCIRDDLNENAPRAMAVLDPVKVIIENFPQGEVEMVTMPNHPNKPEMGSRQVPFSREIYIDRADFREEANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 401 QYKRLVLGKEVRLRNAYVIKADRVEKDEAGNITVLHCSYDPDTLSKDPADGRKVKGVIHWVSAEHALPVEIRLYDRLFSV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495120059 481 ANPGAAEDFLATINPESLVIKQGFVEPSLQNAEKGKAYQFEREGYFCLDsRLATAEKLVFNRTVGLRDTWAKI 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
30-550 |
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: 1004.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSGNVRYSSDYFDQLFN 109
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 110 YAVELVNKGLAYVDELTPEQIREYRGSLTAPGKNSPYRDRSVEENLALFEKMRNGEFAEGTACLRAKIDMASPFIVMRDP 189
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 190 VIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYSIM 269
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 270 SKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNTVEMAALESCIRDDLNENAPRAMAVLDP 349
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 350 VKVIIENFpQGEVEMVTMPNHPNKPEMGSRQVPFSREIYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKADRVEKDEA 429
Cdd:TIGR00440 323 VEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 430 GNITVLHCSYDPDTLSKDPADGRKVKGVIHWVSAEHALPVEIRLYDRLFSVANPGAAEDFLATINPESLVIKQGFVEPSL 509
Cdd:TIGR00440 402 GKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHSL 481
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1495120059 510 QNAEKGKAYQFEREGYFCLDSRLATAEKLVFNRTVGLRDTW 550
Cdd:TIGR00440 482 GDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
30-338 |
4.39e-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: 466.41 E-value: 4.39e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSGNVRYSSDYFDQLFN 109
Cdd:pfam00749 4 TRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 110 YAVELVNKGLAYVDELTPEQIREYRGslTAPGKNSPYRDRSVEENLALF-EKMRNGEFAEGTACLRAKIDMASPfIVMRD 188
Cdd:pfam00749 84 YAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 189 PVIYRIKFAE---HHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLE 265
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495120059 266 YSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQ-DNTVEMAALESCIRDDLNE 338
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-342 |
6.88e-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: 432.06 E-value: 6.88e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 28 ICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWsGNVRYSSDYFDQL 107
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 108 FNYAVELVNKGLAYVdeltpeqireyrgsltapgknspyrdrsveenlalfekmrngefaegtaclrakidmaspfivmr 187
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 188 dpviyrikfaeHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEYS 267
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495120059 268 IMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNTVEMAALESCIRDDLNENAPR 342
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-526 |
2.89e-133 |
|
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: 396.09 E-value: 2.89e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 26 TSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSGNVRYSSDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 106 QLFNYAVELVNKGLAYVDELTPEQIREYRGSLTAPGKNSPY----RDRSVEENlalfEKMRngefAEG-TACLRAKI--- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGePPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 178 -----DMAS-----PFIVMRDPVIYRikfaehhQTGtkwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDN 247
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 248 ITIPVhPrqyEFSRLNLEY----SIMSKRKlnllvteKVVegwddprmpTISGLRRRGYTAGSIREFCKRIGVTKQDNTV 323
Cdd:COG0008 223 LGWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 324 --EMAALESCIrdDLNENaPRAMAVLDPVKVIIENFP---QGEVEMVT---MPNHPNK--PEMGSRQVPFSRE------- 386
Cdd:COG0008 283 ifSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPyirALDDEELAellAPELPEAgiREDLERLVPLVREraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 387 -------IYIDRADfrEEANKqyKRLVLgKEVRLrnayVIKADRvEKDEAgnitvlHCSYDPDTlskdpadgrkVKGVIH 459
Cdd:COG0008 360 laelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL-EVLEA------VETWDPET----------VKGTIH 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495120059 460 WVSAEHalpvEIRlyDRLFSVanpgaaedflatinPESLVIKQGFVEPSLQNAEK--GKAYQFEREGYF 526
Cdd:COG0008 414 WVSAEA----GVK--DGLLFM--------------PLRVALTGRTVEPSLFDVLEllGKERVFERLGYA 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: 1272.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 1 MSEAEARPTNFIRQIIDEDLANGKHTSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVD 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 81 SIKHDVEWLGFHWSGNVRYSSDYFDQLFNYAVELVNKGLAYVDELTPEQIREYRGSLTAPGKNSPYRDRSVEENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 161 MRNGEFAEGTACLRAKIDMASPFIVMRDPVIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 241 YDWVLDNITIPVHPRQYEFSRLNLEYSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 321 NTVEMAALESCIRDDLNENAPRAMAVLDPVKVIIENFPQGEVEMVTMPNHPNKPEMGSRQVPFSREIYIDRADFREEANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 401 QYKRLVLGKEVRLRNAYVIKADRVEKDEAGNITVLHCSYDPDTLSKDPADGRKVKGVIHWVSAEHALPVEIRLYDRLFSV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495120059 481 ANPGAAEDFLATINPESLVIKQGFVEPSLQNAEKGKAYQFEREGYFCLDsRLATAEKLVFNRTVGLRDTWAKI 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
30-550 |
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: 1004.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSGNVRYSSDYFDQLFN 109
Cdd:TIGR00440 3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 110 YAVELVNKGLAYVDELTPEQIREYRGSLTAPGKNSPYRDRSVEENLALFEKMRNGEFAEGTACLRAKIDMASPFIVMRDP 189
Cdd:TIGR00440 83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 190 VIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYSIM 269
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 270 SKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNTVEMAALESCIRDDLNENAPRAMAVLDP 349
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 350 VKVIIENFpQGEVEMVTMPNHPNKPEMGSRQVPFSREIYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKADRVEKDEA 429
Cdd:TIGR00440 323 VEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 430 GNITVLHCSYDPDTLSKDPADGRKVKGVIHWVSAEHALPVEIRLYDRLFSVANPGAAEDFLATINPESLVIKQGFVEPSL 509
Cdd:TIGR00440 402 GKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHSL 481
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1495120059 510 QNAEKGKAYQFEREGYFCLDSRLATAEKLVFNRTVGLRDTW 550
Cdd:TIGR00440 482 GDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
1-552 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 875.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 1 MSEAEaRPT-----NFIRQIIDEDLANGKHTSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKED 75
Cdd:PRK14703 1 MSDAP-RPRmlvspNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 76 IEFVDSIKHDVEWLGFHWSGNVRYSSDYFDQLFNYAVELVNKGLAYVDELTPEQIREYRGSLTAPGKNSPYRDRSVEENL 155
Cdd:PRK14703 80 TEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 156 ALFEKMRNGEFAEGTACLRAKIDMASPFIVMRDPVIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQ 235
Cdd:PRK14703 160 DLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 236 DNRRLYDWVLDNIT-IPVHPRQYEFSRLNLEYSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRI 314
Cdd:PRK14703 240 NNRAIYDWVLDHLGpWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 315 GVTKQDNTVEMAALESCIRDDLNENAPRAMAVLDPVKVIIENFPQGEVEMVTMPNHPNK-PEMGSRQVPFSREIYIDRAD 393
Cdd:PRK14703 320 GVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 394 FREEANKQYKRLVLGKEVRLRNAYVIKADRVEKDEAGNITVLHCSYDPDTLSKDPAdGRKVKGVIHWVSAEHALPVEIRL 473
Cdd:PRK14703 400 FSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 474 YDRLFSVANP-GAAEDFLATINPESLVIKQGFVEPSLQNAEKGKAYQFEREGYFCLDSRLATAEKLVFNRTVGLRDTWAK 552
Cdd:PRK14703 479 YDRLFKVPQPeAADEDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGA 558
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
7-554 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 612.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 7 RPTNfIRQIIDEDLangKHTS--ICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKH 84
Cdd:PLN02859 246 RPSN-TKEILEKHL---KATGgkVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 85 DVEWLGfhWSG-NVRYSSDYFDQLFNYAVELVNKGLAYVDELTPEQIREYRGSLtapgKNSPYRDRSVEENLALFEKMRN 163
Cdd:PLN02859 322 IVEWMG--WEPfKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKK----MNSPWRDRPIEESLKLFEDMRR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 164 GEFAEGTACLRAKIDMASPFIVMRDPVIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDW 243
Cdd:PLN02859 396 GLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYW 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 244 VLDNITIpVHPRQYEFSRLNLEYSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNT- 322
Cdd:PLN02859 476 LLDSLGL-YQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSl 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 323 VEMAALESCIRDDLNENAPRAMAVLDPVKVIIENFPQGEVEMV---TMPNHPNKPEMGSRQVPFSREIYIDRADFREEAN 399
Cdd:PLN02859 555 IRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELdakRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDS 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 400 KQYKRLVLGKEVRLRNAYVIK-ADRVEKDEAGNITVLHCSYDPDTLSKDpadgrkvKGVIHWVSA----EHALPVEIRLY 474
Cdd:PLN02859 635 KDYYGLAPGKSVLLRYAFPIKcTDVVLADDNETVVEIRAEYDPEKKTKP-------KGVLHWVAEpspgVEPLKVEVRLF 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 475 DRLFSVANPGAAEDFLATINPES-LVIKQGFVEPSLQNAEKGKAYQFEREGYFCLDsRLATAEKLVFNRTVGLRDTWAKI 553
Cdd:PLN02859 708 DKLFLSENPAELEDWLEDLNPQSkEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYGKG 786
|
.
gi 1495120059 554 G 554
Cdd:PLN02859 787 G 787
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
31-548 |
4.28e-180 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 519.54 E-value: 4.28e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 31 RFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGfhWSGN-VRYSSDYFDQLFN 109
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMG--WKPDwVTFSSDYFDQLHE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 110 YAVELVNKGLAYVDELTPEQIREYRGSLtapgKNSPYRDRSVEENLALFEKMRNGEFAEGTACLRAKIDMASPFIVMRDP 189
Cdd:PTZ00437 133 FAVQLIKDGKAYVDHSTPDELKQQREQR----EDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 190 VIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIpVHPRQYEFSRLNLEYSIM 269
Cdd:PTZ00437 209 IAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSLL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 270 SKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNTVEMAALESCIRDDLNENAPRAMAVLDP 349
Cdd:PTZ00437 288 SKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 350 VKVIIENFpQGEVEmVTMPNHPNKPEMGSRQVPFSREIYIDRADFR-EEANKQYKRLVLG-KEVRLRNAYVIKADRVEKD 427
Cdd:PTZ00437 368 IKVVVDNW-KGERE-FECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKYSGNVVCKGFEVD 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 428 EAGNITVLHCSYDPDTLSKDpadgrkvKGVIHWVSAEHALPVEIRLYDRLFSVANPGAAEDFLATINPESLVIKQGFVEP 507
Cdd:PTZ00437 446 AAGQPSVIHVDIDFERKDKP-------KTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEK 518
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1495120059 508 SLQNAEKGKAYQFEREGYFCLDSRlATAEKLVFNRTVGLRD 548
Cdd:PTZ00437 519 GIENAKHFESVQAERFGYFVVDPD-TRPDHLVMNRVLGLRE 558
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
30-338 |
4.39e-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: 466.41 E-value: 4.39e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSGNVRYSSDYFDQLFN 109
Cdd:pfam00749 4 TRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 110 YAVELVNKGLAYVDELTPEQIREYRGslTAPGKNSPYRDRSVEENLALF-EKMRNGEFAEGTACLRAKIDMASPfIVMRD 188
Cdd:pfam00749 84 YAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 189 PVIYRIKFAE---HHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLE 265
Cdd:pfam00749 161 PVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495120059 266 YSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQ-DNTVEMAALESCIRDDLNE 338
Cdd:pfam00749 241 GTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-342 |
6.88e-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: 432.06 E-value: 6.88e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 28 ICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWsGNVRYSSDYFDQL 107
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 108 FNYAVELVNKGLAYVdeltpeqireyrgsltapgknspyrdrsveenlalfekmrngefaegtaclrakidmaspfivmr 187
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 188 dpviyrikfaeHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEYS 267
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495120059 268 IMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNTVEMAALESCIRDDLNENAPR 342
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-526 |
2.89e-133 |
|
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: 396.09 E-value: 2.89e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 26 TSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSGNVRYSSDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 106 QLFNYAVELVNKGLAYVDELTPEQIREYRGSLTAPGKNSPY----RDRSVEENlalfEKMRngefAEG-TACLRAKI--- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGePPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 178 -----DMAS-----PFIVMRDPVIYRikfaehhQTGtkwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDN 247
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 248 ITIPVhPrqyEFSRLNLEY----SIMSKRKlnllvteKVVegwddprmpTISGLRRRGYTAGSIREFCKRIGVTKQDNTV 323
Cdd:COG0008 223 LGWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 324 --EMAALESCIrdDLNENaPRAMAVLDPVKVIIENFP---QGEVEMVT---MPNHPNK--PEMGSRQVPFSRE------- 386
Cdd:COG0008 283 ifSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPyirALDDEELAellAPELPEAgiREDLERLVPLVREraktlse 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 387 -------IYIDRADfrEEANKqyKRLVLgKEVRLrnayVIKADRvEKDEAgnitvlHCSYDPDTlskdpadgrkVKGVIH 459
Cdd:COG0008 360 laelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL-EVLEA------VETWDPET----------VKGTIH 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495120059 460 WVSAEHalpvEIRlyDRLFSVanpgaaedflatinPESLVIKQGFVEPSLQNAEK--GKAYQFEREGYF 526
Cdd:COG0008 414 WVSAEA----GVK--DGLLFM--------------PLRVALTGRTVEPSLFDVLEllGKERVFERLGYA 462
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
19-529 |
1.90e-125 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 384.46 E-value: 1.90e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 19 DLANGKHTSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSgNVR 98
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 99 YSSDYFDQLFNYAVELVNKGLAYVDELTPEQIREYRGSltapGKNSPYRDRSVEENLALFEKMRNGEfAEGTAC-LRAKI 177
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGS-ERGLQCcVRGKL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 178 DMASPFIVMRDPVIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIP-VHprQ 256
Cdd:PLN02907 359 DMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRkVH--I 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 257 YEFSRLNLEYSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNTVEMAALESCIRDDL 336
Cdd:PLN02907 437 WEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKII 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 337 NENAPRAMAVLDPVKVI--IENFPQGEvEMVTMPNHPNKPEMGSRQVPFSREIYIDRADFREeankqykrLVLGKEVRLR 414
Cdd:PLN02907 517 DPVCPRHTAVLKEGRVLltLTDGPETP-FVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLM 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 415 ---NAyVIKAdrVEKDEAGNITVLHCSYDPDtlskdpADGRKVKGVIHWVSAEHAL-PVEIRLYDRLFSVANPGAAEDFL 490
Cdd:PLN02907 588 dwgNA-IIKE--ITKDEGGAVTALSGELHLE------GSVKTTKLKLTWLPDTNELvPLSLVEFDYLITKKKLEEDDNFL 658
|
490 500 510
....*....|....*....|....*....|....*....
gi 1495120059 491 ATINPESLVIKQGFVEPSLQNAEKGKAYQFEREGYFCLD 529
Cdd:PLN02907 659 DVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
2-530 |
7.76e-123 |
|
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: 372.23 E-value: 7.76e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 2 SEAEARPTNFIRqiideDLANGKHTSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDS 81
Cdd:TIGR00463 73 IKKKEKKRKGLR-----ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 82 IKHDVEWLGFHWSgNVRYSSDYFDQLFNYAVELVNKGLAYVDELTPEQIREYRGSltapGKNSPYRDRSVEENLALFEKM 161
Cdd:TIGR00463 148 ILEDLEWLGVKWD-EVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 162 RNGEFAEGTACLRAKIDMASPFIVMRDPVIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR-- 239
Cdd:TIGR00463 223 LEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkq 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 240 LYDWVLDNITIPVHpRQYEFSRLNLEYSIMSKRKLNLLVtEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQ 319
Cdd:TIGR00463 303 EYIYRYFGWEPPEF-IHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKIN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 320 DNTVEMAALESCIRDDLNENAPRAMAVLDPVKVIIENFPQGEVEMvtMPNHPNKPEMGSRQVPFSREIYIDRADFREean 399
Cdd:TIGR00463 381 DVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRVE--RPLHPDHPEIGERVLILRGEIYVPKDDLEE--- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 400 kqykrlvLGKEVRLRNAYVIKADRVEKDEAGnitvlhcsydpDTLSKDPADGRKvkgVIHWVSAEHALPVEIRLYDRLfs 479
Cdd:TIGR00463 456 -------GVEPVRLMDAVNVIYSKKELRYHS-----------EGLEGARKLGKS---IIHWLPAKDAVKVKVIMPDAS-- 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1495120059 480 vanpgaaedflatinpeslvIKQGFVEPSLQNAEKGKAYQFEREGYFCLDS 530
Cdd:TIGR00463 513 --------------------IVEGVIEADASELEVGDVVQFERFGFARLDS 543
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
19-530 |
1.20e-113 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 349.15 E-value: 1.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 19 DLANGKHTSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPA--KEDIEFVDSIKHDVEWLGFHWSgN 96
Cdd:PRK04156 93 PLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-E 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 97 VRYSSDYFDQLFNYAVELVNKGLAYVDELTPEQIREYRGSltapGKNSPYRDRSVEENLALFEKMRNGEFAEGTACLRAK 176
Cdd:PRK04156 172 VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVK 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 177 IDMASPFIVMRDPVIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDN----RRLYD---WVLdnit 249
Cdd:PRK04156 248 TDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNtekqRYIYDyfgWEY---- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 250 ipvhPRQYEFSRLNLEYSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNTVEMAALE 329
Cdd:PRK04156 324 ----PETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLY 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 330 SCIRDDLNENAPRAMAVLDPVKVIIENFPQGEVEmvtMPNHPNKPEMGSRQVPFSREIYIDRADFREeankqykrlvLGK 409
Cdd:PRK04156 400 AINRKLIDPIANRYFFVRDPVELEIEGAEPLEAK---IPLHPDRPERGEREIPVGGKVYVSSDDLEA----------EGK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 410 EVRLRNAYVIKADRVEKDEAgnitVLHcsydpdtlSKDPADGRKVKG-VIHWVSAEHALPVEIRLYDRlfsvanpgaaed 488
Cdd:PRK04156 467 MVRLMDLFNVEITGVSVDKA----RYH--------SDDLEEARKNKApIIQWVPEDESVPVRVLKPDG------------ 522
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1495120059 489 flatinpeslVIKQGFVEPSLQNAEKGKAYQFEREGYFCLDS 530
Cdd:PRK04156 523 ----------GDIEGLAEPDVADLEVDDIVQFERFGFVRIDS 554
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
1-539 |
3.96e-112 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 346.18 E-value: 3.96e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 1 MSEAEARPTNFIRQiidedLANGKHTSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVD 80
Cdd:PTZ00402 31 FTAANANEENDKLQ-----LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 81 SIKHDVEWLGFHWSGNVRYSSDYFDQLFNYAVELVNKGLAYVDELTPEQIREYRGSltapGKNSPYRDRSVEENLALFEK 160
Cdd:PTZ00402 106 AILDDLATLGVSWDVGPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 161 MRNGEfAEGT-ACLRAKIDMASPFIVMRDPVIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR 239
Cdd:PTZ00402 182 MKKGS-AEGQeTCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRND 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 240 LYDWVLDNITIPvHPRQYEFSRLNLEYSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQ 319
Cdd:PTZ00402 261 QYYWFCDALGIR-KPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 320 DNTVEMAALESCIRDDLNENAPRAMAVLDPVKVIIENFPQGEVEMVTMPNHPNKPEMGSRQVPFSREIYIDRADFreean 399
Cdd:PTZ00402 340 VNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDV----- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 400 kqyKRLVLGKEVRLR---NAYVIKADRveKDEAGNITvlhcsyDPDTLSKDPADGRKVKGVIHWV-SAEHALPVEIRLYD 475
Cdd:PTZ00402 415 ---ALLKEGDEVTLMdwgNAYIKNIRR--SGEDALIT------DADIVLHLEGDVKKTKFKLTWVpESPKAEVMELNEYD 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495120059 476 RLFSVANPGAAEDFLATINPESLVIKQGFVEPSLQNAEKGKAYQFEREGYFCLDSrlATAEKLV 539
Cdd:PTZ00402 484 HLLTKKKPDPEESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDD--VTPKKVL 545
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
28-537 |
5.96e-99 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 309.63 E-value: 5.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 28 ICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHwSGNVRYSSDYFDQL 107
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 108 FNYAVELVNKGLAYVDELTPEQIREYRgsltAPGKNSPYRDRSVEENLALFEKMRNGEFAEGTACLRAKIDMASPFIVMR 187
Cdd:PLN03233 91 RCYAIILIEEGLAYMDDTPQEEMKKER----ADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 188 DPVIYRIKFAEHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEYS 267
Cdd:PLN03233 167 DPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAFARMNFMNT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 268 IMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNTVEMAALESCIRDDLNENAPRAMAV- 346
Cdd:PLN03233 246 VLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAId 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 347 -LDPVKVIIENFPQG-EVEMVTMPNHPNKPEMGSRQVPFSREIYIDRADfreeankqYKRLVLGKEVRLRNAYVIKADRV 424
Cdd:PLN03233 326 kADHTALTVTNADEEaDFAFSETDCHPKDPGFGKRAMRICDEVLLEKAD--------TEDIQLGEDIVLLRWGVIEISKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 425 EKDEAGNitvlhcsYDPDtlskdpADGRKVKGVIHWVS-AEHALPVEIRLYDRLFSVANPGAAEDFLATINPESLVIKQG 503
Cdd:PLN03233 398 DGDLEGH-------FIPD------GDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDV 464
|
490 500 510
....*....|....*....|....*....|....
gi 1495120059 504 FVEPSLQNAEKGKAYQFEREGYFCLDSRLATAEK 537
Cdd:PLN03233 465 IGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEK 498
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
340-529 |
9.28e-87 |
|
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: 265.67 E-value: 9.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 340 APRAMAVLDPVKVIIENFPQGEVEMVTMPNHPNKPEMGSRQVPFSREIYIDRADFreeankqyKRLVLGKEVRLRNAYVI 419
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 420 KADRVEKDEAGNITVLHCSYDPDTLSKDpadgRKVKG-VIHWVSAEHALPVEIRLYDRLFSVANpgaAEDFLatINPESL 498
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED---DADFL--LNPDSL 143
|
170 180 190
....*....|....*....|....*....|..
gi 1495120059 499 -VIKQGFVEPSLQNAEKGKAYQFEREGYFCLD 529
Cdd:pfam03950 144 kVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
30-338 |
8.73e-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: 244.69 E-value: 8.73e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSGNVRYSSDYFDQLFN 109
Cdd:cd00418 4 TRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLYRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 110 YAVELVNKGlayvdeltpeqireyrgsltapgknspyrdrsveenlalfekmrngefaegtaclrakidmaspfivmrdp 189
Cdd:cd00418 84 YAEELIKKG----------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 190 viyrikfaehhqtgtkwcIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEYS-I 268
Cdd:cd00418 93 ------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLEDGtK 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 269 MSKRKLNllvtekvvegwddprmPTISGLRRRGYTAGSIREFCKRIGVTK-----------------------QDNTVEM 325
Cdd:cd00418 154 LSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKpdghelftleemiaafsvervnsADATFDW 217
|
330
....*....|...
gi 1495120059 326 AALESCIRDDLNE 338
Cdd:cd00418 218 AKLEWLNREYIRE 230
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
28-342 |
7.73e-48 |
|
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: 166.37 E-value: 7.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 28 ICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNP--AKEDIEFVDSIKHDVEWLGFHWSgNVRYSSDYFD 105
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 106 QLFNYAVELVNKGLAYVdeltpeqireyrgsltapgknspyrdrsveenlalfekmrngefaegtaclrakidmaspfiv 185
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 186 mrdpviyrikfaeHHQTGTKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR----LYD---WVldnitipvHPRQYE 258
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEkqryIYEyfgWE--------YPETIH 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 259 FSRLNLEYSIMSKRKLNLLVTEKVVEGWDDPRMPTISGLRRRGYTAGSIREFCKRIGVTKQDNTVEMAALESCIRDDLNE 338
Cdd:cd09287 157 WGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDP 236
|
....
gi 1495120059 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 ... |
30-273 |
3.33e-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: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 30 TRFPPEPNGYLHIGHAKSICLNFGIAQD-----YQGQCNLRFDDTNPAKEDiefvdsikhdvewlgfhwsgnvryssdyf 104
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGD----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 105 dqlfnyavelvnkglayvdeltPEQireyrgsltAPGKNSP-YRDRSVEENLALFEkmrngefaegtaclrakidmaspf 183
Cdd:cd00802 53 ----------------------PAN---------KKGENAKaFVERWIERIKEDVE------------------------ 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 184 ivmrdpviyrikfaehhqtgtkwciypmYDFTHCISDALEGITH---SLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFS 260
Cdd:cd00802 78 ----------------------------YMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLTFG 129
|
250
....*....|....
gi 1495120059 261 RLNLEYS-IMSKRK 273
Cdd:cd00802 130 RVMGADGtKMSKSK 143
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
26-121 |
9.50e-17 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 81.05 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 26 TSICTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSGNVRYSSDYFD 105
Cdd:PRK05710 4 TPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD 83
|
90
....*....|....*..
gi 1495120059 106 qLFNYAVE-LVNKGLAY 121
Cdd:PRK05710 84 -AYRAALDrLRAQGLVY 99
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
227-273 |
6.98e-13 |
|
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: 64.87 E-value: 6.98e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1495120059 227 HSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYSIMSKRK 273
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
30-118 |
2.88e-11 |
|
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: 63.76 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWSGNVR--------YSS 101
Cdd:cd00808 4 TRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDvggpygpyRQS 83
|
90
....*....|....*..
gi 1495120059 102 DYFDQLFNYAVELVNKG 118
Cdd:cd00808 84 ERLEIYRKYAEKLLEKG 100
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
30-108 |
8.87e-11 |
|
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: 59.09 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 30 TRFPPEPnGYLHIGHAKSICLNFGIAqdyqGQCNLRFDDTNPAK------EDIEFVDSIKHDVEWLGFHWSGNVRYSSDY 103
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNRELYRWV 76
|
....*
gi 1495120059 104 FDQLF 108
Cdd:cd02156 77 KDNIT 81
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
31-229 |
6.62e-09 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 58.60 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 31 RFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPAKEDIEFVDSIKHDVEWLGFHWS---------GNVRYS- 100
Cdd:PLN02627 49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvggeyGPYRQSe 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495120059 101 -SDYFDQlfnYAVELVNKGLAYVDELTPEQIREYRGslTAPGKNSP------YRDRSVEENLAlfekmrngEFAEGTA-C 172
Cdd:PLN02627 129 rNAIYKQ---YAEKLLESGHVYPCFCTDEELEAMKE--EAELKKLPprytgkWATASDEEVQA--------ELAKGTPyT 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495120059 173 LRAKIDMASPfIVMRDPViyRIKFAEHHQTGTKWCIY-----PMYDFTHCISDALEGITHSL 229
Cdd:PLN02627 196 YRFRVPKEGS-VKIDDLI--RGEVSWNTDTLGDFVLLrsngqPVYNFCVAVDDATMGITHVI 254
|
|
| |
