|
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: 1276.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 1 MSEADARPSNFIRQIIDKDLADGKHTSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVE 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 81 SIKKDVNWLGFEWDGEVCYSSNYFDKLYEYAIELINKGLAYVDELSPEQIREYRGTLKEPGKPSPYRDRSVEENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 161 MRAGEFEEGKACLRAKIDMGSSFMVMRDPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 241 YDWVLDNITIDCRPHQYEFSRLNLEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQE 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 321 NMIEFSSLESCIRDDLNENAPRAMAVLDPVKVVIENFEEGAVENLTLANHPNKPEMGEREVPFTREVWIEREDFREEANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 401 KYKRLVLGKEVRLRGAYVIKAERVEKDAEGNITTIYCTYDPETLGKNPADGRKVKGVIHWVSADKALPAEIRLYDRLFTV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797005916 481 PNPAAAEDFASTINPDSLVVINGFVEPSLASAEAEQGYQFERMGYFCADsKDSTANNLVFNRTVGLRDTWAKI 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-550 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 957.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNYFDKL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 108 YEYAIELINKGLAYVDELSPEQIREYRGTLKEPGKPSPYRDRSVEENLALFEKMRAGEFEEGKACLRAKIDMGSSFMVMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 188 DPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDCRPHQYEFSRLNLEYT 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 268 VMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSLESCIRDDLNENAPRAMAVL 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 348 DPVKVVIENFeEGAVENLTLANHPNKPEMGEREVPFTREVWIEREDFREEANKKYKRLVLGKEVRLRGAYVIKAERVEKD 427
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 428 AEGNITTIYCTYDPETLGKNPADGRKVKGVIHWVSADKALPAEIRLYDRLFTVPNPAAAEDFASTINPDSLVVINGFVEP 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1797005916 508 SLASAEAEQGYQFERMGYFCADSKDSTANNLVFNRTVGLRDTW 550
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
1.90e-164 |
|
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: 469.88 E-value: 1.90e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNYFDKL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 108 YEYAIELINKGLAYVDELSPEQIREYRGTLkePGKPSPYRDRSVEENLALF-EKMRAGEFEEGKACLRAKIDMGSSfMVM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 187 RDPVLYRVRFA---THHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDCRPHQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1797005916 264 LEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQ-ENMIEFSSLESCIRDDLNE 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-342 |
1.02e-154 |
|
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: 442.08 E-value: 1.02e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDgEVCYSSNYFDKL 107
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 108 YEYAIELINKGLAYVdelspeqireyrgtlkepgkpspyrdrsveenlalfekmragefeegkaclrakidmgssfmvmr 187
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 188 dpvlyrvrfatHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDCrPHQYEFSRLNLEYT 267
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1797005916 268 VMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSLESCIRDDLNENAPR 342
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-526 |
9.10e-141 |
|
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: 415.35 E-value: 9.10e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 26 TSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 106 KLYEYAIELINKGLAYVDELSPEQIREYRGTLKEPGKPSPY----RDRSVEENlalfEKMRA-GEfeegKACLRAKI--- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERMLAaGE----PPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 178 -----DMGS-----SFMVMRDPVLYRVrfathhqTGdkwciYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDN 247
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 248 ITIDcRPhqyEFSRLNLEY----TVMSKRKlnqlvteKLVngwddprmpTVSGLRRRGFTPASIREFCKRIGVTKQENMI 323
Cdd:COG0008 223 LGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 324 EFS--SLESCIrdDLNENaPRAMAVLDPVKVVIEN------FEEGAVENLTLanhPNKPEMG-----EREVPFTRE---- 386
Cdd:COG0008 283 IFSleELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLA---PELPEAGiredlERLVPLVRErakt 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 387 ----------VWIEREDfrEEANKkyKRLVLgKEVRLrgayVIKAERvekDAEGNITtiycTYDPETlgknpadgrkVKG 456
Cdd:COG0008 357 lselaelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL---EVLEAVE----TWDPET----------VKG 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797005916 457 VIHWVSADkalpAEIRlyDRLFTVPnpaaaedfastinpdsL-VVING-FVEPSLA-SAEAEQGYQ-FERMGYF 526
Cdd:COG0008 411 TIHWVSAE----AGVK--DGLLFMP----------------LrVALTGrTVEPSLFdVLELLGKERvFERLGYA 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: 1276.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 1 MSEADARPSNFIRQIIDKDLADGKHTSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVE 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 81 SIKKDVNWLGFEWDGEVCYSSNYFDKLYEYAIELINKGLAYVDELSPEQIREYRGTLKEPGKPSPYRDRSVEENLALFEK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 161 MRAGEFEEGKACLRAKIDMGSSFMVMRDPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 241 YDWVLDNITIDCRPHQYEFSRLNLEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQE 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 321 NMIEFSSLESCIRDDLNENAPRAMAVLDPVKVVIENFEEGAVENLTLANHPNKPEMGEREVPFTREVWIEREDFREEANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 401 KYKRLVLGKEVRLRGAYVIKAERVEKDAEGNITTIYCTYDPETLGKNPADGRKVKGVIHWVSADKALPAEIRLYDRLFTV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797005916 481 PNPAAAEDFASTINPDSLVVINGFVEPSLASAEAEQGYQFERMGYFCADsKDSTANNLVFNRTVGLRDTWAKI 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
28-550 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 957.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNYFDKL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 108 YEYAIELINKGLAYVDELSPEQIREYRGTLKEPGKPSPYRDRSVEENLALFEKMRAGEFEEGKACLRAKIDMGSSFMVMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 188 DPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDCRPHQYEFSRLNLEYT 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 268 VMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSLESCIRDDLNENAPRAMAVL 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 348 DPVKVVIENFeEGAVENLTLANHPNKPEMGEREVPFTREVWIEREDFREEANKKYKRLVLGKEVRLRGAYVIKAERVEKD 427
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 428 AEGNITTIYCTYDPETLGKNPADGRKVKGVIHWVSADKALPAEIRLYDRLFTVPNPAAAEDFASTINPDSLVVINGFVEP 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1797005916 508 SLASAEAEQGYQFERMGYFCADSKDSTANNLVFNRTVGLRDTW 550
Cdd:TIGR00440 480 SLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
1-556 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 905.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 1 MSEAdARPS-----NFIRQIIDKDLADGKHTSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKED 75
Cdd:PRK14703 1 MSDA-PRPRmlvspNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 76 IEYVESIKKDVNWLGFEWDGEVCYSSNYFDKLYEYAIELINKGLAYVDELSPEQIREYRGTLKEPGKPSPYRDRSVEENL 155
Cdd:PRK14703 80 TEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 156 ALFEKMRAGEFEEGKACLRAKIDMGSSFMVMRDPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFM 235
Cdd:PRK14703 160 DLFRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 236 DNRRLYDWVLDNIT-IDCRPHQYEFSRLNLEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRI 314
Cdd:PRK14703 240 NNRAIYDWVLDHLGpWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 315 GVTKQENMIEFSSLESCIRDDLNENAPRAMAVLDPVKVVIENFEEGAVENLTLANHPNK-PEMGEREVPFTREVWIERED 393
Cdd:PRK14703 320 GVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 394 FREEANKKYKRLVLGKEVRLRGAYVIKAERVEKDAEGNITTIYCTYDPETLGKNPAdGRKVKGVIHWVSADKALPAEIRL 473
Cdd:PRK14703 400 FSEDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 474 YDRLFTVPNPAAAE-DFASTINPDSLVVINGFVEPSLASAEAEQGYQFERMGYFCADSKDSTANNLVFNRTVGLRDTWAK 552
Cdd:PRK14703 479 YDRLFKVPQPEAADeDFLEFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGA 558
|
....
gi 1797005916 553 IENQ 556
Cdd:PRK14703 559 RARE 562
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
7-552 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 626.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 7 RPSNfIRQIIDKDLadgKHTS--VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKK 84
Cdd:PLN02859 246 RPSN-TKEILEKHL---KATGgkVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 85 DVNWLGFEwDGEVCYSSNYFDKLYEYAIELINKGLAYVDELSPEQIREYRgtlkEPGKPSPYRDRSVEENLALFEKMRAG 164
Cdd:PLN02859 322 IVEWMGWE-PFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRG 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 165 EFEEGKACLRAKIDMGSSFMVMRDPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWV 244
Cdd:PLN02859 397 LIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 245 LDNITIdCRPHQYEFSRLNLEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQEN-MI 323
Cdd:PLN02859 477 LDSLGL-YQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 324 EFSSLESCIRDDLNENAPRAMAVLDPVKVVIENFEEGAVENLTLANHPNKPEMGERE---VPFTREVWIEREDFREEANK 400
Cdd:PLN02859 556 RMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAfykVPFSRVVYIERSDFRLKDSK 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 401 KYKRLVLGKEVRLRGAYVIK-AERVEKDAEGNITTIYCTYDPEtlgknpaDGRKVKGVIHWVSAD----KALPAEIRLYD 475
Cdd:PLN02859 636 DYYGLAPGKSVLLRYAFPIKcTDVVLADDNETVVEIRAEYDPE-------KKTKPKGVLHWVAEPspgvEPLKVEVRLFD 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1797005916 476 RLFTVPNPAAAEDFASTINPDSLVVING-FVEPSLASAEAEQGYQFERMGYFCADsKDSTANNLVFNRTVGLRDTWAK 552
Cdd:PLN02859 709 KLFLSENPAELEDWLEDLNPQSKEVISGaYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLKDSYGK 785
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
24-548 |
4.01e-177 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 512.22 E-value: 4.01e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 24 KHTSV-----HTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGeVC 98
Cdd:PTZ00437 43 KHEAVtggkpYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDW-VT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 99 YSSNYFDKLYEYAIELINKGLAYVDELSPEQIREYRgtlkEPGKPSPYRDRSVEENLALFEKMRAGEFEEGKACLRAKID 178
Cdd:PTZ00437 122 FSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 179 MGSSFMVMRDPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIdCRPHQYE 258
Cdd:PTZ00437 198 MKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 259 FSRLNLEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSLESCIRDDLNE 338
Cdd:PTZ00437 277 FSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 339 NAPRAMAVLDPVKVVIENFE-EGAVENLtlaNHPNKPEMGEREVPFTREVWIEREDFR-EEANKKYKRLVLG-KEVRLRG 415
Cdd:PTZ00437 357 RCERRLMVIDPIKVVVDNWKgEREFECP---NHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKY 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 416 AYVIKAERVEKDAEGNITTIYCTYDPETLGKNpadgrkvKGVIHWVSADKALPAEIRLYDRLFTVPNPAAAEDFASTINP 495
Cdd:PTZ00437 434 SGNVVCKGFEVDAAGQPSVIHVDIDFERKDKP-------KTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1797005916 496 DSLVVINGFVEPSLASAEAEQGYQFERMGYFCADSkDSTANNLVFNRTVGLRD 548
Cdd:PTZ00437 507 DSEVVSHGYAEKGIENAKHFESVQAERFGYFVVDP-DTRPDHLVMNRVLGLRE 558
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-338 |
1.90e-164 |
|
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: 469.88 E-value: 1.90e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNYFDKL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 108 YEYAIELINKGLAYVDELSPEQIREYRGTLkePGKPSPYRDRSVEENLALF-EKMRAGEFEEGKACLRAKIDMGSSfMVM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 187 RDPVLYRVRFA---THHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDCRPHQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1797005916 264 LEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQ-ENMIEFSSLESCIRDDLNE 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLDW 314
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-342 |
1.02e-154 |
|
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: 442.08 E-value: 1.02e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDgEVCYSSNYFDKL 107
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 108 YEYAIELINKGLAYVdelspeqireyrgtlkepgkpspyrdrsveenlalfekmragefeegkaclrakidmgssfmvmr 187
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 188 dpvlyrvrfatHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDCrPHQYEFSRLNLEYT 267
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYR-PHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1797005916 268 VMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSLESCIRDDLNENAPR 342
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
26-526 |
9.10e-141 |
|
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: 415.35 E-value: 9.10e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 26 TSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNYFD 105
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 106 KLYEYAIELINKGLAYVDELSPEQIREYRGTLKEPGKPSPY----RDRSVEENlalfEKMRA-GEfeegKACLRAKI--- 177
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERMLAaGE----PPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 178 -----DMGS-----SFMVMRDPVLYRVrfathhqTGdkwciYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDN 247
Cdd:COG0008 155 gvvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 248 ITIDcRPhqyEFSRLNLEY----TVMSKRKlnqlvteKLVngwddprmpTVSGLRRRGFTPASIREFCKRIGVTKQENMI 323
Cdd:COG0008 223 LGWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 324 EFS--SLESCIrdDLNENaPRAMAVLDPVKVVIEN------FEEGAVENLTLanhPNKPEMG-----EREVPFTRE---- 386
Cdd:COG0008 283 IFSleELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLA---PELPEAGiredlERLVPLVRErakt 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 387 ----------VWIEREDfrEEANKkyKRLVLgKEVRLrgayVIKAERvekDAEGNITtiycTYDPETlgknpadgrkVKG 456
Cdd:COG0008 357 lselaelarfFFIERED--EKAAK--KRLAP-EEVRK----VLKAAL---EVLEAVE----TWDPET----------VKG 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797005916 457 VIHWVSADkalpAEIRlyDRLFTVPnpaaaedfastinpdsL-VVING-FVEPSLA-SAEAEQGYQ-FERMGYF 526
Cdd:COG0008 411 TIHWVSAE----AGVK--DGLLFMP----------------LrVALTGrTVEPSLFdVLELLGKERvFERLGYA 462
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
19-532 |
2.90e-120 |
|
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: 365.68 E-value: 2.90e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 19 DLADGKHTSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDgEVC 98
Cdd:TIGR00463 85 ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 99 YSSNYFDKLYEYAIELINKGLAYVDELSPEQIREyrgtLKEPGKPSPYRDRSVEENLALFEKMRAGEFEEGKACLRAKID 178
Cdd:TIGR00463 164 YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRE----LRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 179 MGSSFMVMRDPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRR--LYDWVLDNITIDcRPHQ 256
Cdd:TIGR00463 240 LKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqEYIYRYFGWEPP-EFIH 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 257 YEFSRLNLEYTVMSKRKLnQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSLESCIRDDL 336
Cdd:TIGR00463 319 WGRLKIDDVRALSTSSAR-KGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKII 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 337 NENAPRAMAVLDPVKVVIENFEEGAVENLTLanHPNKPEMGEREVPFTREVWIEREDFREeankkykrlvLGKEVRLrga 416
Cdd:TIGR00463 398 DEEARRYFFIWNPVKIEIVGLPEPKRVERPL--HPDHPEIGERVLILRGEIYVPKDDLEE----------GVEPVRL--- 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 417 yvikaerveKDAeGNIttIYCTYDPETLGKNPADGRKV-KGVIHWVSADKALPAEIrlydrlftvpnpaaaedfastINP 495
Cdd:TIGR00463 463 ---------MDA-VNV--IYSKKELRYHSEGLEGARKLgKSIIHWLPAKDAVKVKV---------------------IMP 509
|
490 500 510
....*....|....*....|....*....|....*..
gi 1797005916 496 DSLVViNGFVEPSLASAEAEQGYQFERMGYFCADSKD 532
Cdd:TIGR00463 510 DASIV-EGVIEADASELEVGDVVQFERFGFARLDSAD 545
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
19-529 |
1.90e-119 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 369.05 E-value: 1.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 19 DLADGKHTSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDgEVC 98
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 99 YSSNYFDKLYEYAIELINKGLAYVDELSPEQIREYRGTLKEpgkpSPYRDRSVEENLALFEKMRAGEfEEGKAC-LRAKI 177
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIE----SKCRNNSVEENLRLWKEMIAGS-ERGLQCcVRGKL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 178 DMGSSFMVMRDPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDcRPHQY 257
Cdd:PLN02907 359 DMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHIW 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 258 EFSRLNLEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSLESCIRDDLN 337
Cdd:PLN02907 438 EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIID 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 338 ENAPRAMAVLDPVKVVienfeegavenLTLANHPNKPEM------------GEREVPFTREVWIEREDfrEEANKKykrl 405
Cdd:PLN02907 518 PVCPRHTAVLKEGRVL-----------LTLTDGPETPFVriiprhkkyegaGKKATTFTNRIWLDYAD--AEAISE---- 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 406 vlGKEVRLR--GAYVIKAerVEKDAEGNITTIYCTYDPEtlgknpADGRKVKGVIHWVSADKAL-PAEIRLYDRLFTVPN 482
Cdd:PLN02907 581 --GEEVTLMdwGNAIIKE--ITKDEGGAVTALSGELHLE------GSVKTTKLKLTWLPDTNELvPLSLVEFDYLITKKK 650
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1797005916 483 PAAAEDFASTINPDSLVVINGFVEPSLASAEAEQGYQFERMGYFCAD 529
Cdd:PLN02907 651 LEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
18-533 |
4.15e-115 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 353.00 E-value: 4.15e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 18 KDLADGKHTSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPE--KEDIEYVESIKKDVNWLGFEWDg 95
Cdd:PRK04156 92 PPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 96 EVCYSSNYFDKLYEYAIELINKGLAYVDELSPEQIREyrgtLKEPGKPSPYRDRSVEENLALFEKMRAGEFEEGKACLRA 175
Cdd:PRK04156 171 EVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKE----LRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 176 KIDMGSSFMVMRDPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDN----RRLYD---WVLdni 248
Cdd:PRK04156 247 KTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNtekqRYIYDyfgWEY--- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 249 tidcrPHQYEFSRLNLEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSL 328
Cdd:PRK04156 324 -----PETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 329 ESCIRDDLNENAPRAMAVLDPVKVVIENFEEGAVEnltLANHPNKPEMGEREVPFTREVWIEREDFREeankkykrlvLG 408
Cdd:PRK04156 399 YAINRKLIDPIANRYFFVRDPVELEIEGAEPLEAK---IPLHPDRPERGEREIPVGGKVYVSSDDLEA----------EG 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 409 KEVRLRGAYVIKAERVEkdaegnitTIYCTYDPETLgknpADGRKVKG-VIHWVSADKALPAEIrlydrlftvpnpaaae 487
Cdd:PRK04156 466 KMVRLMDLFNVEITGVS--------VDKARYHSDDL----EEARKNKApIIQWVPEDESVPVRV---------------- 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1797005916 488 dfastINPDSlVVINGFVEPSLASAEAEQGYQFERMGYFCADSKDS 533
Cdd:PRK04156 518 -----LKPDG-GDIEGLAEPDVADLEVDDIVQFERFGFVRIDSVED 557
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
1-530 |
9.21e-110 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 340.02 E-value: 9.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 1 MSEADARPSNfirqiiDK-DLADGKHTSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYV 79
Cdd:PTZ00402 31 FTAANANEEN------DKlQLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 80 ESIKKDVNWLGFEWDGEVCYSSNYFDKLYEYAIELINKGLAYVDELSPEQIREYRGTlkepGKPSPYRDRSVEENLALFE 159
Cdd:PTZ00402 105 QAILDDLATLGVSWDVGPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 160 KMRAGEFEEGKACLRAKIDMGSSFMVMRDPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRR 239
Cdd:PTZ00402 181 EMKKGSAEGQETCLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRND 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 240 LYDWVLDNITIDcRPHQYEFSRLNLEYTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQ 319
Cdd:PTZ00402 261 QYYWFCDALGIR-KPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 320 ENMIEFSSLESCIRDDLNENAPRAMAVLDPVKV--VIENfeEGAVENLTLANHPNKPEMGEREVPFTREVWIEREDFree 397
Cdd:PTZ00402 340 VNFMEWSKLWYFNTQILDPSVPRYTVVSNTLKVrcTVEG--QIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAEDV--- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 398 ankkyKRLVLGKEVRLR---GAYVIKAERveKDAEGNITTIYCTYDPEtlgknpADGRKVKGVIHWV-SADKALPAEIRL 473
Cdd:PTZ00402 415 -----ALLKEGDEVTLMdwgNAYIKNIRR--SGEDALITDADIVLHLE------GDVKKTKFKLTWVpESPKAEVMELNE 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1797005916 474 YDRLFTVPNPAAAEDFASTINPDSLVVINGFVEPSLASAEAEQGYQFERMGYFCADS 530
Cdd:PTZ00402 482 YDHLLTKKKPDPEESIDDIIAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDD 538
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
28-529 |
3.04e-101 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 315.80 E-value: 3.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDgEVCYSSNYFDKL 107
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPD-SVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 108 YEYAIELINKGLAYVDELSPEQIREYRGTLKEpgkpSPYRDRSVEENLALFEKMRAGEFEEGKACLRAKIDMGSSFMVMR 187
Cdd:PLN03233 91 RCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 188 DPVLYRVRFATHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDcRPHQYEFSRLNLEYT 267
Cdd:PLN03233 167 DPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAFARMNFMNT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 268 VMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSLESCIRDDLNENAPRAMAV- 346
Cdd:PLN03233 246 VLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAId 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 347 -LDPVKVVIENFEEGA-VENLTLANHPNKPEMGEREVPFTREVWIEREDfreeankkYKRLVLGKEVRLRGAYVIKAERV 424
Cdd:PLN03233 326 kADHTALTVTNADEEAdFAFSETDCHPKDPGFGKRAMRICDEVLLEKAD--------TEDIQLGEDIVLLRWGVIEISKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 425 EKDAEGNittiyctYDPEtlgknpADGRKVKGVIHWVS-ADKALPAEIRLYDRLFTVPNPAAAEDFASTINPDSLVVING 503
Cdd:PLN03233 398 DGDLEGH-------FIPD------GDFKAAKKKISWIAdVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDV 464
|
490 500
....*....|....*....|....*.
gi 1797005916 504 FVEPSLASAEAEQGYQFERMGYFCAD 529
Cdd:PLN03233 465 IGDAGLKTLKEHDIIQLERRGFYRVD 490
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
340-529 |
1.65e-84 |
|
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: 259.90 E-value: 1.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 340 APRAMAVLDPVKVVIENFEEGAVENLTLANHPNKPEMGEREVPFTREVWIEREDFreeankkyKRLVLGKEVRLRGAYVI 419
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 420 KAERVEKDAEGNITTIYCTYDPETLGKNpadgRKVKG-VIHWVSADKALPAEIRLYDRLFTVPNpaaaeDFASTINPDSL 498
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED-----DADFLLNPDSL 143
|
170 180 190
....*....|....*....|....*....|..
gi 1797005916 499 VVI-NGFVEPSLASAEAEQGYQFERMGYFCAD 529
Cdd:pfam03950 144 KVLtEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
28-338 |
3.61e-78 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 245.84 E-value: 3.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNYFDKL 107
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 108 YEYAIELINKGlayvdelspeqireyrgtlkepgkpspyrdrsveenlalfekmragefeegkaclrakidmgssfmvmr 187
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 188 dpvlyrvrfathhqtgdkwcIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDcRPHQYEFSRLNLEY- 266
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-PPRFYHFPRLLLEDg 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 267 TVMSKRKLNqlvteklvngwddprmPTVSGLRRRGFTPASIREFCKRIGVTKQE-----------------------NMI 323
Cdd:cd00418 152 TKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDghelftleemiaafsvervnsadATF 215
|
330
....*....|....*
gi 1797005916 324 EFSSLESCIRDDLNE 338
Cdd:cd00418 216 DWAKLEWLNREYIRE 230
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
28-342 |
8.96e-51 |
|
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: 174.46 E-value: 8.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 28 VHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPE--KEDIEYVESIKKDVNWLGFEWDgEVCYSSNYFD 105
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 106 KLYEYAIELINKGLAYVdelspeqireyrgtlkepgkpspyrdrsveenlalfekmragefeegkaclrakidmgssfmv 185
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 186 mrdpvlyrvrfatHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFMDNRRLYDWVLDNITIDcRPHQYEFSRLNLE 265
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWE-YPETIHWGRLKIE 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1797005916 266 YTVMSKRKLNQLVTEKLVNGWDDPRMPTVSGLRRRGFTPASIREFCKRIGVTKQENMIEFSSLESCIRDDLNENAPR 342
Cdd:cd09287 164 GGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
27-229 |
1.60e-22 |
|
glutamyl-tRNA synthetase, bacterial 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 bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 100.50 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 27 SVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNYFDK 106
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 107 LYEYAIELINKGLAYVDELSPEQIREYRGTLKEPGKPSPYRDRSveenLALFEKMRAGEFEEGKAC-LRAKIDMGSSFmV 185
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRC----RNLHEEEIENKLAKGIPPvVRFKIPQEAVV-S 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1797005916 186 MRDPVLYRVRFAThhQTGDKWCIY-----PMYDFTHCISDALEGITHSI 229
Cdd:TIGR00464 156 FNDQVRGEITFQN--SELDDFVILrsdgsPTYNFAVVVDDYLMKITHVI 202
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
29-273 |
1.34e-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: 79.45 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 29 HTRFPPEPNGYLHIGHAKSICLNFGIAQD-----YQGQCNLRFDDTNPEKEDieyvesiKKDVNWLGFEwdgevcyssny 103
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGD-------PANKKGENAK----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 104 fdklyeyaielinkglAYVDELSPEQIREYrgtlkepgkpspyrdrsveenlalfekmragefeegkaclrakidmgssf 183
Cdd:cd00802 63 ----------------AFVERWIERIKEDV-------------------------------------------------- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 184 mvmrdpvlyrvrfathhqtgdkwciypMYDFTHCISDALEGITH---SICTLEFMDNRRLYDWVLDNITIDCRPHQYEFS 260
Cdd:cd00802 77 ---------------------------EYMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLTFG 129
|
250
....*....|....
gi 1797005916 261 RLNLEY-TVMSKRK 273
Cdd:cd00802 130 RVMGADgTKMSKSK 143
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
30-121 |
3.20e-17 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 82.21 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 30 TRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNYFDkLYE 109
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD-AYR 86
|
90
....*....|...
gi 1797005916 110 YAIE-LINKGLAY 121
Cdd:PRK05710 87 AALDrLRAQGLVY 99
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
27-118 |
3.25e-15 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 75.32 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 27 SVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWDGEVCYSSNY--- 103
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYgpy 80
|
90 100
....*....|....*....|
gi 1797005916 104 -----FDKLYEYAIELINKG 118
Cdd:cd00808 81 rqserLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
21-237 |
2.93e-13 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 72.08 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 21 ADGKHTSVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKEDIEYVESIKKDVNWLGFEWD------ 94
Cdd:PLN02627 39 GESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005916 95 GEVC-YSSNYFDKLY-EYAIELINKGLAYVDELSPEQIREYRGTLKEPGKPSPY----RDRSVEENLAlfekmragEFEE 168
Cdd:PLN02627 119 GEYGpYRQSERNAIYkQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYtgkwATASDEEVQA--------ELAK 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1797005916 169 GKA-CLRAKIDMGSSfMVMRDpvLYRVRFATHHQT-GDkWCIY-----PMYDFTHCISDALEGITHSICTLEFMDN 237
Cdd:PLN02627 191 GTPyTYRFRVPKEGS-VKIDD--LIRGEVSWNTDTlGD-FVLLrsngqPVYNFCVAVDDATMGITHVIRAEEHLPN 262
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
29-95 |
3.58e-12 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 62.94 E-value: 3.58e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797005916 29 HTRFPPEPnGYLHIGHAKSICLNFGIAqdyqGQCNLRFDDTNPEK------EDIEYVESIKKDVNWLGFEWDG 95
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQ 68
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
227-273 |
1.51e-09 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 55.62 E-value: 1.51e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1797005916 227 HSICTLEFMDNRRLYDWVLDNITIDCRPHQYEFSRLNLEYTVMSKRK 273
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
|
|
| |
