|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-552 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1278.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 1 MSEAEARPTNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVE 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 81 SIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 161 MRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 241 YDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 321 NTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENY-QGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANK 399
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYpEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 400 QYKRLVLGKEVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSV 479
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383404143 480 PNPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDsRHSTAEKPVFNRTVGLRDTWAKV 552
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-549 |
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: 1062.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 108 HAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 188 DPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYT 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 268 VMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVI 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 348 DPVKLVIENYQGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 427
Cdd:TIGR00440 321 DPVEVVIENLSDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 428 EGNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPS 507
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 383404143 508 LKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRDTW 549
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
4.67e-170 |
|
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: 483.74 E-value: 4.67e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 108 HAYAIELINKGLAYVDELTPEQIREYRGTltQPGKNSPYRDRSVEENLALF-EKMRAGGFEEGKACLRAKIDMASPfIVM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREE--QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 187 RDPVLYRIKFAE---HHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383404143 264 LEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQ-DNTIEMASLESCIREDLNE 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-342 |
1.64e-155 |
|
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: 444.00 E-value: 1.64e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWsGNVRYSSDYFDQ 106
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 107 LHAYAIELINKGLAYVdeltpeqireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivm 186
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 187 rdpvlyrikfaeHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEY 266
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383404143 267 TVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPR 342
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-525 |
6.33e-140 |
|
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: 413.03 E-value: 6.33e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 26 TTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 106 QLHAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPY----RDRSVEENlalfEKMRAGGFEegkACLRAKI---- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERMLAAGEP---PVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 178 ----DMAS-----PFIVMRDPVLYRikfaehhQTGnkwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNI 248
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 249 TIPVhPrqyEFSRLNLEY----TVMSKRKlnllvadKHVegwddprmpTISGLRRRGYTAASIREFCKRIGVTKQDNT-- 322
Cdd:COG0008 224 GWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQei 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 323 IEMASLESCIreDLNENaPRAMAVIDPVKLVIENYQgegEMVTMPN-------HPNKPEMG-----SRQVPFSGE----- 385
Cdd:COG0008 284 FSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGP---YIRALDDeelaellAPELPEAGiredlERLVPLVREraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 386 ---------IWIDRADfrEEANKqyKRLVLgKEVRLrnayVIKAERvekDAEGNITtifcTYDADTlskdpadgrkVKGV 456
Cdd:COG0008 358 selaelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL---EVLEAVE----TWDPET----------VKGT 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383404143 457 IHWVSAAHalpvEIRlyDRLFSVPnpgaaddfLSVinpeslVIKQGFAEPSLKD--AVAGKAFQFEREGYF 525
Cdd:COG0008 412 IHWVSAEA----GVK--DGLLFMP--------LRV------ALTGRTVEPSLFDvlELLGKERVFERLGYA 462
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
1-552 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1278.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 1 MSEAEARPTNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVE 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 81 SIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 161 MRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 241 YDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 321 NTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENY-QGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANK 399
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYpEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 400 QYKRLVLGKEVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSV 479
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383404143 480 PNPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDsRHSTAEKPVFNRTVGLRDTWAKV 552
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-549 |
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: 1062.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 108 HAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 188 DPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYT 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 268 VMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVI 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 348 DPVKLVIENYQGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 427
Cdd:TIGR00440 321 DPVEVVIENLSDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 428 EGNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPS 507
Cdd:TIGR00440 401 AGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEHS 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 383404143 508 LKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRDTW 549
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
1-551 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 869.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 1 MSEAEaRPT-----NFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKED 75
Cdd:PRK14703 1 MSDAP-RPRmlvspNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 76 IEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENL 155
Cdd:PRK14703 80 TEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 156 ALFEKMRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQ 235
Cdd:PRK14703 160 DLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 236 DNRRLYDWVLDNIT-IPVHPRQYEFSRLNLEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRI 314
Cdd:PRK14703 240 NNRAIYDWVLDHLGpWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 315 GVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQGEG-EMVTMPNHPNK-PEMGSRQVPFSGEIWIDRAD 392
Cdd:PRK14703 320 GVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKvEELDLPYWPHDvPKEGSRKVPFTRELYIERDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 393 FREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLSKDPAdGRKVKGVIHWVSAAHALPVEIRL 472
Cdd:PRK14703 400 FSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 473 YDRLFSVPNPGAAD-DFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRDTWAK 551
Cdd:PRK14703 479 YDRLFKVPQPEAADeDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGA 558
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
7-553 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 615.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 7 RPTNfIRQIIDEDL--ASGKhttVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKN 84
Cdd:PLN02859 246 RPSN-TKEILEKHLkaTGGK---VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 85 DVEWLGfhWSG-NVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRgtltQPGKNSPYRDRSVEENLALFEKMRA 163
Cdd:PLN02859 322 IVEWMG--WEPfKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 164 GGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDW 243
Cdd:PLN02859 396 GLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYW 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 244 VLDNITIpVHPRQYEFSRLNLEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNT- 322
Cdd:PLN02859 476 LLDSLGL-YQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSl 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 323 IEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQG----EGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEAN 398
Cdd:PLN02859 555 IRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESgeviELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDS 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 399 KQYKRLVLGKEVRLRNAYVIK-AERVEKDAEGNITTIFCTYdadtlskDPADGRKVKGVIHWVSAA----HALPVEIRLY 473
Cdd:PLN02859 635 KDYYGLAPGKSVLLRYAFPIKcTDVVLADDNETVVEIRAEY-------DPEKKTKPKGVLHWVAEPspgvEPLKVEVRLF 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 474 DRLFSVPNPGAADDFLSVINPES-LVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDsRHSTAEKPVFNRTVGLRDTWAKV 552
Cdd:PLN02859 708 DKLFLSENPAELEDWLEDLNPQSkEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYGKG 786
|
.
gi 383404143 553 G 553
Cdd:PLN02859 787 G 787
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
31-547 |
5.80e-179 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 516.84 E-value: 5.80e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 31 RFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGfhWSGN-VRYSSDYFDQLHA 109
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMG--WKPDwVTFSSDYFDQLHE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 110 YAIELINKGLAYVDELTPEQIREYRgtltQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMRDP 189
Cdd:PTZ00437 133 FAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 190 VLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIpVHPRQYEFSRLNLEYTVM 269
Cdd:PTZ00437 209 IAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSLL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 270 SKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDP 349
Cdd:PTZ00437 288 SKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 350 VKLVIENYQGEGEmVTMPNHPNKPEMGSRQVPFSGEIWIDRADFR-EEANKQYKRLVLG-KEVRLRNAYVIKAERVEKDA 427
Cdd:PTZ00437 368 IKVVVDNWKGERE-FECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKYSGNVVCKGFEVDA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 428 EGNITTIFCtyDADTLSKDpadgrKVKGVIHWVSAAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPS 507
Cdd:PTZ00437 447 AGQPSVIHV--DIDFERKD-----KPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEKG 519
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 383404143 508 LKDAVAGKAFQFEREGYFCLDSrHSTAEKPVFNRTVGLRD 547
Cdd:PTZ00437 520 IENAKHFESVQAERFGYFVVDP-DTRPDHLVMNRVLGLRE 558
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
4.67e-170 |
|
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: 483.74 E-value: 4.67e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 108 HAYAIELINKGLAYVDELTPEQIREYRGTltQPGKNSPYRDRSVEENLALF-EKMRAGGFEEGKACLRAKIDMASPfIVM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREE--QEALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 187 RDPVLYRIKFAE---HHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383404143 264 LEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQ-DNTIEMASLESCIREDLNE 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
27-342 |
1.64e-155 |
|
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: 444.00 E-value: 1.64e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWsGNVRYSSDYFDQ 106
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKP-YKVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 107 LHAYAIELINKGLAYVdeltpeqireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivm 186
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 187 rdpvlyrikfaeHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEY 266
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTY 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383404143 267 TVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPR 342
Cdd:cd00807 163 TVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-525 |
6.33e-140 |
|
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: 413.03 E-value: 6.33e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 26 TTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 106 QLHAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPY----RDRSVEENlalfEKMRAGGFEegkACLRAKI---- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERMLAAGEP---PVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 178 ----DMAS-----PFIVMRDPVLYRikfaehhQTGnkwciYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNI 248
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 249 TIPVhPrqyEFSRLNLEY----TVMSKRKlnllvadKHVegwddprmpTISGLRRRGYTAASIREFCKRIGVTKQDNT-- 322
Cdd:COG0008 224 GWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQei 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 323 IEMASLESCIreDLNENaPRAMAVIDPVKLVIENYQgegEMVTMPN-------HPNKPEMG-----SRQVPFSGE----- 385
Cdd:COG0008 284 FSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGP---YIRALDDeelaellAPELPEAGiredlERLVPLVREraktl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 386 ---------IWIDRADfrEEANKqyKRLVLgKEVRLrnayVIKAERvekDAEGNITtifcTYDADTlskdpadgrkVKGV 456
Cdd:COG0008 358 selaelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL---EVLEAVE----TWDPET----------VKGT 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383404143 457 IHWVSAAHalpvEIRlyDRLFSVPnpgaaddfLSVinpeslVIKQGFAEPSLKD--AVAGKAFQFEREGYF 525
Cdd:COG0008 412 IHWVSAEA----GVK--DGLLFMP--------LRV------ALTGRTVEPSLFDvlELLGKERVFERLGYA 462
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
19-538 |
2.68e-125 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 384.08 E-value: 2.68e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 19 DLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSgNVR 98
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 99 YSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTltqpGKNSPYRDRSVEENLALFEKMRAGGfEEGKAC-LRAKI 177
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGS-ERGLQCcVRGKL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 178 DMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIP-VHprQ 256
Cdd:PLN02907 359 DMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRkVH--I 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 257 YEFSRLNLEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDL 336
Cdd:PLN02907 437 WEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKII 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 337 NENAPRAMAVIDP--VKLVIENYQGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREeankqykrLVLGKEVRLR- 413
Cdd:PLN02907 517 DPVCPRHTAVLKEgrVLLTLTDGPETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLMd 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 414 --NAYVikaERVEKDAEGNITTIFCTYDADtlskdpADGRKVKGVIHWVSAAHAL-PVEIRLYDRLFSVPNPGAADDFLS 490
Cdd:PLN02907 589 wgNAII---KEITKDEGGAVTALSGELHLE------GSVKTTKLKLTWLPDTNELvPLSLVEFDYLITKKKLEEDDNFLD 659
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 383404143 491 VINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPV 538
Cdd:PLN02907 660 VLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSSKPI 707
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
2-529 |
5.30e-117 |
|
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: 357.21 E-value: 5.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 2 SEAEARPTNFIRqiideDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVES 81
Cdd:TIGR00463 73 IKKKEKKRKGLR-----ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 82 IKNDVEWLGFHWSgNVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTltqpGKNSPYRDRSVEENLALFEKM 161
Cdd:TIGR00463 148 ILEDLEWLGVKWD-EVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 162 RAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR-- 239
Cdd:TIGR00463 223 LEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkq 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 240 LYDWVLDNITIPVHpRQYEFSRLNLEYTVMSKRKLNLLVaDKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQ 319
Cdd:TIGR00463 303 EYIYRYFGWEPPEF-IHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKIN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 320 DNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQGEGEmVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREeank 399
Cdd:TIGR00463 381 DVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKR-VERPLHPDHPEIGERVLILRGEIYVPKDDLEE---- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 400 qykrlvLGKEVRLRNAYVIKAErvEKDAEgnittifctYDADTLSKDPADGRKvkgVIHWVSAAHALPVEirlydrlfsv 479
Cdd:TIGR00463 456 ------GVEPVRLMDAVNVIYS--KKELR---------YHSEGLEGARKLGKS---IIHWLPAKDAVKVK---------- 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 383404143 480 pnpgaaddflsVINPESLvIKQGFAEPSLKDAVAGKAFQFEREGYFCLDS 529
Cdd:TIGR00463 506 -----------VIMPDAS-IVEGVIEADASELEVGDVVQFERFGFARLDS 543
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
28-529 |
3.60e-110 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 339.91 E-value: 3.60e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPV--KEDIEYVESIKNDVEWLGFHWSgNVRYSSDYFD 105
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 106 QLHAYAIELINKGLAYVDELTPEQIREYRGTltqpGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIV 185
Cdd:PRK04156 181 IYYEYARKLIEMGGAYVCTCDPEEFKELRDA----GKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 186 MRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDN----RRLYD---WVLdnitipvhPRQYE 258
Cdd:PRK04156 257 VRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNtekqRYIYDyfgWEY--------PETIH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 259 FSRLNLEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNE 338
Cdd:PRK04156 329 YGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 339 NAPRAMAVIDPVKLVIENYqgEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREeankqykrlvLGKEVRLRNAYVI 418
Cdd:PRK04156 409 IANRYFFVRDPVELEIEGA--EPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEA----------EGKMVRLMDLFNV 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 419 KAERVEKDAegnittifctydADTLSKDPADGRKVKG-VIHWVSAAHALPVEirlydrlfsvpnpgaaddflsVINPESl 497
Cdd:PRK04156 477 EITGVSVDK------------ARYHSDDLEEARKNKApIIQWVPEDESVPVR---------------------VLKPDG- 522
|
490 500 510
....*....|....*....|....*....|..
gi 383404143 498 VIKQGFAEPSLKDAVAGKAFQFEREGYFCLDS 529
Cdd:PRK04156 523 GDIEGLAEPDVADLEVDDIVQFERFGFVRIDS 554
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
1-529 |
2.67e-109 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 338.86 E-value: 2.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 1 MSEAEARPTNFIRQiidedLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVE 80
Cdd:PTZ00402 31 FTAANANEENDKLQ-----LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 81 SIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTltqpGKNSPYRDRSVEENLALFEK 160
Cdd:PTZ00402 106 AILDDLATLGVSWDVGPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 161 MRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL 240
Cdd:PTZ00402 182 MKKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 241 YDWVLDNITIPvHPRQYEFSRLNLEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQD 320
Cdd:PTZ00402 262 YYWFCDALGIR-KPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 321 NTIEMASLESCIREDLNENAPRAMAVIDPVKL--VIENyQGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFreean 398
Cdd:PTZ00402 341 NFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVrcTVEG-QIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDV----- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 399 kqyKRLVLGKEVRLR---NAYVIKAERveKDAEGNITtifctyDADTLSKDPADGRKVKGVIHWVSAA-HALPVEIRLYD 474
Cdd:PTZ00402 415 ---ALLKEGDEVTLMdwgNAYIKNIRR--SGEDALIT------DADIVLHLEGDVKKTKFKLTWVPESpKAEVMELNEYD 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 383404143 475 RLFSVPNPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDS 529
Cdd:PTZ00402 484 HLLTKKKPDPEESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDD 538
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
28-538 |
1.27e-106 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 329.66 E-value: 1.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHwSGNVRYSSDYFDQL 107
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 108 HAYAIELINKGLAYVDELTPEQIREYRGTLTQpgknSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMR 187
Cdd:PLN03233 91 RCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 188 DPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEYT 267
Cdd:PLN03233 167 DPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAFARMNFMNT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 268 VMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAV- 346
Cdd:PLN03233 246 VLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAId 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 347 -IDPVKLVIENYQGEGEMVTMPN--HPNKPEMGSRQVPFSGEIWIDRADfreeankqYKRLVLGKEVRLRNAYVIKAERV 423
Cdd:PLN03233 326 kADHTALTVTNADEEADFAFSETdcHPKDPGFGKRAMRICDEVLLEKAD--------TEDIQLGEDIVLLRWGVIEISKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 424 EKDAEGNITTifctydadtlskdPADGRKVKGVIHWVS-AAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVIKQG 502
Cdd:PLN03233 398 DGDLEGHFIP-------------DGDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDV 464
|
490 500 510
....*....|....*....|....*....|....*.
gi 383404143 503 FAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPV 538
Cdd:PLN03233 465 IGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPL 500
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
27-338 |
1.57e-86 |
|
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: 267.42 E-value: 1.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQ 106
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 107 LHAYAIELINKGlayvdeltpeqireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivm 186
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 187 rdpvlyrikfaehhqtgnkwcIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPvHPRQYEFSRLNLEY 266
Cdd:cd00418 93 ---------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLED 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 267 -TVMSKRKLNllvadkhvegwddprmPTISGLRRRGYTAASIREFCKRIGVTK-----------------------QDNT 322
Cdd:cd00418 151 gTKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKpdghelftleemiaafsvervnsADAT 214
|
330
....*....|....*.
gi 383404143 323 IEMASLESCIREDLNE 338
Cdd:cd00418 215 FDWAKLEWLNREYIRE 230
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
340-528 |
1.72e-81 |
|
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: 252.19 E-value: 1.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 340 APRAMAVIDPVKLVIENY-QGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFreeankqyKRLVLGKEVRLRNAYVI 418
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYpEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 419 KAERVEKDAEGNITTIFCTYDADTLSKDpadgRKVKG-VIHWVSAAHALPVEIRLYDRLFSVPNpgaadDFLSVINPESL 497
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED-----DADFLLNPDSL 143
|
170 180 190
....*....|....*....|....*....|..
gi 383404143 498 -VIKQGFAEPSLKDAVAGKAFQFEREGYFCLD 528
Cdd:pfam03950 144 kVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
28-342 |
3.04e-49 |
|
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: 170.22 E-value: 3.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNP--VKEDIEYVESIKNDVEWLGFHWSgNVRYSSDYFD 105
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 106 QLHAYAIELINKGLAYVdeltpeqireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfiv 185
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 186 mrdpvlyrikfaeHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRR----LYD---WVldnitipvHPRQYE 258
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEkqryIYEyfgWE--------YPETIH 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 259 FSRLNLEYTVMSKRKLNLLVADKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNE 338
Cdd:cd09287 157 WGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDP 236
|
....
gi 383404143 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 |
2.49e-19 |
|
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: 84.45 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 29 HTRFPPEPNGYLHIGHAKSICLNFGIAQD-----YKGQCNLRFDDTNPVKEdieyvesikndvewlgfhWSGNVryssdy 103
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIG------------------DPANK------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 104 fdqlhayaielinkglayvdeltpeqireyrgtltqPGKNSP-YRDRSVEENLALFEkmraggfeegkaclrakidmasp 182
Cdd:cd00802 57 ------------------------------------KGENAKaFVERWIERIKEDVE----------------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 183 fivmrdpvlyrikfaehhqtgnkwciypmYDFTHCISDALEGITH---SLCTLEFQDNRRLYDWVLDNITIPVHPRQYEF 259
Cdd:cd00802 78 -----------------------------YMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLTF 128
|
250
....*....|....*
gi 383404143 260 SRLNLEY-TVMSKRK 273
Cdd:cd00802 129 GRVMGADgTKMSKSK 143
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
30-121 |
1.66e-14 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 74.12 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDqlhA 109
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD---A 84
|
90
....*....|....*
gi 383404143 110 Y--AIE-LINKGLAY 121
Cdd:PRK05710 85 YraALDrLRAQGLVY 99
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
29-105 |
5.95e-14 |
|
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: 67.95 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 29 HTRFPPEPnGYLHIGHAKSICLNFGIAqdykGQCNLRFDDTNPVK------EDIEYVESIKNDVEWLGFHWSGNVRYSSD 102
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNRELYRW 75
|
...
gi 383404143 103 YFD 105
Cdd:cd02156 76 VKD 78
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
27-118 |
1.00e-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: 71.08 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 27 TVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVR-------- 98
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDvggpygpy 80
|
90 100
....*....|....*....|
gi 383404143 99 YSSDYFDQLHAYAIELINKG 118
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG 100
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
227-273 |
1.87e-13 |
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nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 66.41 E-value: 1.87e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 383404143 227 HSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRK 273
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
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| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
21-229 |
3.66e-08 |
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glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 55.90 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 21 ASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYS 100
Cdd:PLN02627 39 GESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVG 118
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383404143 101 SDY--FDQ------LHAYAIELINKGLAYVDELTPEQIREYRGtlTQPGKNSP------YRDRSVEENLALFEK------ 160
Cdd:PLN02627 119 GEYgpYRQsernaiYKQYAEKLLESGHVYPCFCTDEELEAMKE--EAELKKLPprytgkWATASDEEVQAELAKgtpyty 196
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170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383404143 161 ---MRAGGFEEGKACLRAKI----DMASPFIVMRdpvlyrikfaehhQTGNkwciyPMYDFTHCISDALEGITHSL 229
Cdd:PLN02627 197 rfrVPKEGSVKIDDLIRGEVswntDTLGDFVLLR-------------SNGQ-----PVYNFCVAVDDATMGITHVI 254
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