|
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: 1178.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 1 MAETEHRPTNFIRQIIDKDLANGVHESIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVN 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 81 SIKEDVKWLGFEWDGEERYSSNYFDQLHGFANELIDKGLAYVDFSTQDVMRELRGTLTAPGKNSPYRDTDVETNQREFAK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 161 MTAGEYKEGECSLRAKIDMASPFMCMRDPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 241 YDWVIENITIDSTPRQYEFSRLNLEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 321 NMVEMSMLEACVREDLNVNAPRAMAVLDPIKLVIENYPENDSETLVAPNHPSDESMGTREISFGREIWIEAEDFRESANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 401 KFKRLVLDKEVRLRNAYVVKANRVEKDADGNVTTVYCTYDADTLGKDPADGRKVKGVIHWVDAGTAQQAEFRLYDRLFNV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 996038741 481 PNPAAEENFTDVINPESLTVLTGWAEAGLAKRGSEAgAWQFERTGYFCLDADSTDDKPVFNRTVGLRDTWAKI 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPED-RFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 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: 840.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 28 IKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNYFDQL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 108 HGFANELIDKGLAYVDFSTQDVMRELRGTLTAPGKNSPYRDTDVETNQREFAKMTAGEYKEGECSLRAKIDMASPFMCMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 188 DPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIDSTPRQYEFSRLNLEYT 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 268 VLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSMLEACVREDLNVNAPRAMAVL 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 348 DPIKLVIENYpENDSETLVAPNHPSDESMGTREISFGREIWIEAEDFRESANKKFKRLVLDKEVRLRNAYVVKANRVEKD 427
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 428 ADGNVTTVYCTYDADTLGKDPADGRKVKGVIHWVDAGTAQQAEFRLYDRLFNVPNPAAEENFTDVINPESLTVLTGWAEA 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 996038741 508 GLAKRGSEAGaWQFERTGYFCLDA-DSTDDKPVFNRTVGLRDTW 550
Cdd:TIGR00440 480 SLGDAVANKR-FQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-337 |
5.28e-145 |
|
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: 420.19 E-value: 5.28e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 28 IKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNYFDQL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 108 HGFANELIDKGLAYVDFSTQDVMRELRGTLtaPGKNSPYRDTDVETNQREFA-KMTAGEYKEGECSLRAKIDMASPfMCM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 187 RDPVIYRVK---HAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIDSTPRQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 996038741 264 LEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNM-VEMSMLEACVREDLN 337
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-342 |
3.28e-143 |
|
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: 412.80 E-value: 3.28e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 28 IKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDgEERYSSNYFDQL 107
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 108 HGFANELIDKGLAYVdfstqdvmrelrgtltapgknspyrdtdvetnqrefakmtageykegecslrakidmaspfmcmr 187
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 188 dpviyrvkhahHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIdSTPRQYEFSRLNLEYT 267
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRL-YRPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 996038741 268 VLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSMLEACVREDLNVNAPR 342
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
27-481 |
6.26e-127 |
|
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: 379.91 E-value: 6.26e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 27 SIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNYFDQ 106
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 107 LHGFANELIDKGLAYVDFSTQDVMRELRGTLTAPGKNSPY----RDTDVEtnqrEFAKM-TAGEykegECSLRAKI---- 177
Cdd:COG0008 84 YYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPE----ELERMlAAGE----PPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 178 ----DMAS-----PFMCMRDPVIYRVkhahhhqTGdkwcvYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENI 248
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 249 TIDsTPrqyEFSRLNLEY----TVLSKRRliqlveeNHVsgwddprmpTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVE 324
Cdd:COG0008 224 GWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 325 MSM--LEACVreDLNvNAPRAMAVLDPIKLVIENYP---ENDSETLVAPNHPSDESMG-----TREISFGRE-------- 386
Cdd:COG0008 284 FSLeeLIEAF--DLD-RVSRSPAVFDPVKLVWLNGPyirALDDEELAELLAPELPEAGiredlERLVPLVREraktlsel 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 387 ------IWIEAEDfrESANKKfkrlvldkevRLRNAYVVKANRVEKDADGNVTtvycTYDADTlgkdpadgrkVKGVIHW 460
Cdd:COG0008 361 aelarfFFIERED--EKAAKK----------RLAPEEVRKVLKAALEVLEAVE----TWDPET----------VKGTIHW 414
|
490 500
....*....|....*....|.
gi 996038741 461 VdagtaqQAEFRLYDRLFNVP 481
Cdd:COG0008 415 V------SAEAGVKDGLLFMP 429
|
|
| |
|
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: 1178.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 1 MAETEHRPTNFIRQIIDKDLANGVHESIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVN 80
Cdd:PRK05347 3 MSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 81 SIKEDVKWLGFEWDGEERYSSNYFDQLHGFANELIDKGLAYVDFSTQDVMRELRGTLTAPGKNSPYRDTDVETNQREFAK 160
Cdd:PRK05347 83 SIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 161 MTAGEYKEGECSLRAKIDMASPFMCMRDPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRL 240
Cdd:PRK05347 163 MRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 241 YDWVIENITIDSTPRQYEFSRLNLEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMD 320
Cdd:PRK05347 243 YDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 321 NMVEMSMLEACVREDLNVNAPRAMAVLDPIKLVIENYPENDSETLVAPNHPSDESMGTREISFGREIWIEAEDFRESANK 400
Cdd:PRK05347 323 SVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPPK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 401 KFKRLVLDKEVRLRNAYVVKANRVEKDADGNVTTVYCTYDADTLGKDPADGRKVKGVIHWVDAGTAQQAEFRLYDRLFNV 480
Cdd:PRK05347 403 KYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 996038741 481 PNPAAEENFTDVINPESLTVLTGWAEAGLAKRGSEAgAWQFERTGYFCLDADSTDDKPVFNRTVGLRDTWAKI 553
Cdd:PRK05347 483 PNPAAGKDFLDFLNPDSLVIKQGFVEPSLADAKPED-RFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 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: 840.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 28 IKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNYFDQL 107
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 108 HGFANELIDKGLAYVDFSTQDVMRELRGTLTAPGKNSPYRDTDVETNQREFAKMTAGEYKEGECSLRAKIDMASPFMCMR 187
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 188 DPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIDSTPRQYEFSRLNLEYT 267
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 268 VLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSMLEACVREDLNVNAPRAMAVL 347
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 348 DPIKLVIENYpENDSETLVAPNHPSDESMGTREISFGREIWIEAEDFRESANKKFKRLVLDKEVRLRNAYVVKANRVEKD 427
Cdd:TIGR00440 321 DPVEVVIENL-SDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 428 ADGNVTTVYCTYDADTLGKDPADGRKVKGVIHWVDAGTAQQAEFRLYDRLFNVPNPAAEENFTDVINPESLTVLTGWAEA 507
Cdd:TIGR00440 400 AAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFMEH 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 996038741 508 GLAKRGSEAGaWQFERTGYFCLDA-DSTDDKPVFNRTVGLRDTW 550
Cdd:TIGR00440 480 SLGDAVANKR-FQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
3-555 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 813.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 3 ETEHRPT-----NFIRQIIDKDLANGVHESIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIA 77
Cdd:PRK14703 2 SDAPRPRmlvspNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 78 FVNSIKEDVKWLGFEWDGEERYSSNYFDQLHGFANELIDKGLAYVDFSTQDVMRELRGTLTAPGKNSPYRDTDVETNQRE 157
Cdd:PRK14703 82 YVEAIKDDVRWLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 158 FAKMTAGEYKEGECSLRAKIDMASPFMCMRDPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDN 237
Cdd:PRK14703 162 FRRMRAGEFPDGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 238 RRLYDWVIENIT-IDSTPRQYEFSRLNLEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGV 316
Cdd:PRK14703 242 RAIYDWVLDHLGpWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 317 TKMDNMVEMSMLEACVREDLNVNAPRAMAVLDPIKLVIENYPENDSETLVAPNHPSD-ESMGTREISFGREIWIEAEDFR 395
Cdd:PRK14703 322 AKTNSTVDIGVLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 396 ESANKKFKRLVLDKEVRLRNAYVVKANRVEKDADGNVTTVYCTYDADTLGKDPAdGRKVKGVIHWVDAGTAQQAEFRLYD 475
Cdd:PRK14703 402 EDPPKGFKRLTPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRLYD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 476 RLFNVPNP-AAEENFTDVINPESLTVLTGWAEAglAKRGSEAGA-WQFERTGYFCLD-ADSTDDKPVFNRTVGLRDTWAK 552
Cdd:PRK14703 481 RLFKVPQPeAADEDFLEFLNPDSLRVAQGRVEP--AVRDDPADTrYQFERQGYFWADpVDSRPDALVFNRIITLKDTWGA 558
|
...
gi 996038741 553 IGD 555
Cdd:PRK14703 559 RAR 561
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
7-554 |
1.91e-174 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 512.77 E-value: 1.91e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 7 RPTNfIRQIIDKDL-ANGvhESIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKED 85
Cdd:PLN02859 246 RPSN-TKEILEKHLkATG--GKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 86 VKWLGFEwDGEERYSSNYFDQLHGFANELIDKGLAYVDFSTQDVMRELRGTLtapgKNSPYRDTDVETNQREFAKMTAGE 165
Cdd:PLN02859 323 VEWMGWE-PFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKK----MNSPWRDRPIEESLKLFEDMRRGL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 166 YKEGECSLRAKIDMASPFMCMRDPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVI 245
Cdd:PLN02859 398 IEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 246 ENITIdSTPRQYEFSRLNLEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDN-MVE 324
Cdd:PLN02859 478 DSLGL-YQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIR 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 325 MSMLEACVREDLNVNAPRAMAVLDPIKLVIENYPENDSETLVA---PNHPSDESMGTREISFGREIWIEAEDFRESANKK 401
Cdd:PLN02859 557 MDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAkrwPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKD 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 402 FKRLVLDKEVRLRNAYVVK-ANRVEKDADGNVTTVYCTYdadtlgkDPADGRKVKGVIHWVDAGTAQQ----AEFRLYDR 476
Cdd:PLN02859 637 YYGLAPGKSVLLRYAFPIKcTDVVLADDNETVVEIRAEY-------DPEKKTKPKGVLHWVAEPSPGVeplkVEVRLFDK 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 996038741 477 LFNVPNPAAEENFTDVINPESLTVLTGwAEAGLAKRGSEAG-AWQFERTGYFCLDADSTDDKPVFNRTVGLRDTWAKIG 554
Cdd:PLN02859 710 LFLSENPAELEDWLEDLNPQSKEVISG-AYAVPSLKDAKVGdRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
31-548 |
2.43e-154 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 453.67 E-value: 2.43e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 31 RFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEErYSSNYFDQLHGF 110
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVT-FSSDYFDQLHEF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 111 ANELIDKGLAYVDFSTQDVMRELRGTLtapgKNSPYRDTDVETNQREFAKMTAGEYKEGECSLRAKIDMASPFMCMRDPV 190
Cdd:PTZ00437 134 AVQLIKDGKAYVDHSTPDELKQQREQR----EDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 191 IYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIdSTPRQYEFSRLNLEYTVLS 270
Cdd:PTZ00437 210 AYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSLLS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 271 KRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSMLEACVREDLNVNAPRAMAVLDPI 350
Cdd:PTZ00437 289 KRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDPI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 351 KLVIENYpenDSE-TLVAPNHPSDESMGTREISFGREIWIEAEDFR-ESANKKFKRLVLD-KEVRLRNAYVVKANRVEKD 427
Cdd:PTZ00437 369 KVVVDNW---KGErEFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKYSGNVVCKGFEVD 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 428 ADGNVTTVYCtyDADTLGKDpadgrKVKGVIHWVDAGTAQQAEFRLYDRLFNVPNPAAEENFTDVINPESLTVLTGWAEA 507
Cdd:PTZ00437 446 AAGQPSVIHV--DIDFERKD-----KPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEK 518
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 996038741 508 GLaKRGSEAGAWQFERTGYFCLDADSTDDKPVFNRTVGLRD 548
Cdd:PTZ00437 519 GI-ENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLRE 558
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
28-337 |
5.28e-145 |
|
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: 420.19 E-value: 5.28e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 28 IKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNYFDQL 107
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 108 HGFANELIDKGLAYVDFSTQDVMRELRGTLtaPGKNSPYRDTDVETNQREFA-KMTAGEYKEGECSLRAKIDMASPfMCM 186
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESP-YVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 187 RDPVIYRVK---HAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIDSTPRQYEFSRLN 263
Cdd:pfam00749 159 RDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 996038741 264 LEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNM-VEMSMLEACVREDLN 337
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVnRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
28-342 |
3.28e-143 |
|
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: 412.80 E-value: 3.28e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 28 IKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDgEERYSSNYFDQL 107
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 108 HGFANELIDKGLAYVdfstqdvmrelrgtltapgknspyrdtdvetnqrefakmtageykegecslrakidmaspfmcmr 187
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 188 dpviyrvkhahHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIdSTPRQYEFSRLNLEYT 267
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRL-YRPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 996038741 268 VLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSMLEACVREDLNVNAPR 342
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
27-481 |
6.26e-127 |
|
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: 379.91 E-value: 6.26e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 27 SIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNYFDQ 106
Cdd:COG0008 4 KVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 107 LHGFANELIDKGLAYVDFSTQDVMRELRGTLTAPGKNSPY----RDTDVEtnqrEFAKM-TAGEykegECSLRAKI---- 177
Cdd:COG0008 84 YYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPE----ELERMlAAGE----PPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 178 ----DMAS-----PFMCMRDPVIYRVkhahhhqTGdkwcvYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENI 248
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 249 TIDsTPrqyEFSRLNLEY----TVLSKRRliqlveeNHVsgwddprmpTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVE 324
Cdd:COG0008 224 GWE-PP---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 325 MSM--LEACVreDLNvNAPRAMAVLDPIKLVIENYP---ENDSETLVAPNHPSDESMG-----TREISFGRE-------- 386
Cdd:COG0008 284 FSLeeLIEAF--DLD-RVSRSPAVFDPVKLVWLNGPyirALDDEELAELLAPELPEAGiredlERLVPLVREraktlsel 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 387 ------IWIEAEDfrESANKKfkrlvldkevRLRNAYVVKANRVEKDADGNVTtvycTYDADTlgkdpadgrkVKGVIHW 460
Cdd:COG0008 361 aelarfFFIERED--EKAAKK----------RLAPEEVRKVLKAALEVLEAVE----TWDPET----------VKGTIHW 414
|
490 500
....*....|....*....|.
gi 996038741 461 VdagtaqQAEFRLYDRLFNVP 481
Cdd:COG0008 415 V------SAEAGVKDGLLFMP 429
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
28-531 |
1.11e-108 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 340.93 E-value: 1.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 28 IKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDgEERYSSNYFDQL 107
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVTYTSDYFPQL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 108 HGFANELIDKGLAYVDFSTQDVMRELRGTltapGKNSPYRDTDVETNQREFAKMTAGEYKEGECSLRAKIDMASPFMCMR 187
Cdd:PLN02907 293 MEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 188 DPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIdstpRQ---YEFSRLNL 264
Cdd:PLN02907 369 DPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGL----RKvhiWEFSRLNF 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 265 EYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSMLEACVREDLNVNAPRAM 344
Cdd:PLN02907 445 VYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHT 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 345 AVLDPIK--LVIENYPENdSETLVAPNHPSDESMGTREISFGREIWIEAEDFREsankkfkrLVLDKEVRLR---NAYVV 419
Cdd:PLN02907 525 AVLKEGRvlLTLTDGPET-PFVRIIPRHKKYEGAGKKATTFTNRIWLDYADAEA--------ISEGEEVTLMdwgNAIIK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 420 KanrVEKDADGNVTTVYCTYDADtlgkdpADGRKVKGVIHWVdAGTAQQAEFRL--YDRLFNVPNPAAEENFTDVINP-- 495
Cdd:PLN02907 596 E---ITKDEGGAVTALSGELHLE------GSVKTTKLKLTWL-PDTNELVPLSLveFDYLITKKKLEEDDNFLDVLNPct 665
|
490 500 510
....*....|....*....|....*....|....*...
gi 996038741 496 --ESLTVltGWAEAGLAKRGSeagAWQFERTGYFCLDA 531
Cdd:PLN02907 666 kkETAAL--GDSNMRNLKRGE---IIQLERKGYYRCDA 698
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
20-532 |
5.70e-104 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 324.99 E-value: 5.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 20 LANGVHESIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERY 99
Cdd:PTZ00402 45 LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 100 SSNYFDQLHGFANELIDKGLAYVDFSTQDVMRELRgtltAPGKNSPYRDTDVETNQREFAKMTAGEYKEGECSLRAKIDM 179
Cdd:PTZ00402 125 SSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCR----FDGVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 180 ASPFMCMRDPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIdSTPRQYEF 259
Cdd:PTZ00402 201 DNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGI-RKPIVEDF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 260 SRLNLEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSMLEACVREDLNVN 339
Cdd:PTZ00402 280 SRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 340 APRAMAVLDPIKLVIENYPENDSETLVAPNHPSDESMGTREISFGREIWIEAEDfresankkfkrLVLDK---EVRLR-- 414
Cdd:PTZ00402 360 VPRYTVVSNTLKVRCTVEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAED-----------VALLKegdEVTLMdw 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 415 -NAYVVKANRveKDADGNVTtvyctyDADTLGKDPADGRKVKGVIHWV-DAGTAQQAEFRLYDRLFNVPNPAAEENFTDV 492
Cdd:PTZ00402 429 gNAYIKNIRR--SGEDALIT------DADIVLHLEGDVKKTKFKLTWVpESPKAEVMELNEYDHLLTKKKPDPEESIDDI 500
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 996038741 493 INPESLTVLTGWAEAGLA--KRGSEAgawQFERTGYFCLDAD 532
Cdd:PTZ00402 501 IAPVTKYTQEVYGEEALSvlKKGDII---QLERRGYYIVDDV 539
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
18-536 |
4.49e-103 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 321.80 E-value: 4.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 18 KDLANGVHESIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPA--KEDIAFVNSIKEDVKWLGFEWDg 95
Cdd:PRK04156 92 PPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 96 EERYSSNYFDQLHGFANELIDKGLAYVDFSTQDVMRELRgtltAPGKNSPYRDTDVETNQREFAKMTAGEYKEGECSLRA 175
Cdd:PRK04156 171 EVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 176 KIDMASPFMCMRDPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDN----RRLYD---Wvieni 248
Cdd:PRK04156 247 KTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNtekqRYIYDyfgW----- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 249 tidSTPRQYEFSRLNLEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSML 328
Cdd:PRK04156 322 ---EYPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 329 EACVREDLNVNAPRAMAVLDPIKLVIENYPENDSEtlvAPNHPSDESMGTREISFGREIWIEAEDFREsankkfkrlvLD 408
Cdd:PRK04156 399 YAINRKLIDPIANRYFFVRDPVELEIEGAEPLEAK---IPLHPDRPERGEREIPVGGKVYVSSDDLEA----------EG 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 409 KEVRLRNAYVVKANRVEKDadgnvttvYCTYDADTLgkdpADGRKVKG-VIHWVdagtaqqaefrlydrlfnvpnPAAEE 487
Cdd:PRK04156 466 KMVRLMDLFNVEITGVSVD--------KARYHSDDL----EEARKNKApIIQWV---------------------PEDES 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 996038741 488 NFTDVINPESlTVLTGWAEAGLAKRgsEAGAW-QFERTGYFCLDADSTDD 536
Cdd:PRK04156 513 VPVRVLKPDG-GDIEGLAEPDVADL--EVDDIvQFERFGFVRIDSVEDDE 559
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
3-538 |
6.23e-101 |
|
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: 315.99 E-value: 6.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 3 ETEHRPTNFIRqiidkDLANGVHESIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSI 82
Cdd:TIGR00463 74 KKKEKKRKGLR-----ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 83 KEDVKWLGFEWDgEERYSSNYFDQLHGFANELIDKGLAYVDFSTQDVMRELRGTltapGKNSPYRDTDVETNQREFAKMT 162
Cdd:TIGR00463 149 LEDLEWLGVKWD-EVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNR----GEACHCRDRSVEENLERWEEML 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 163 AGEYKEGECSLRAKIDMASPFMCMRDPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRR--L 240
Cdd:TIGR00463 224 EGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 241 YDWVIENITIDSTpRQYEFSRLNlEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMD 320
Cdd:TIGR00463 304 YIYRYFGWEPPEF-IHWGRLKID-DVRALSTSSARKGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKIND 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 321 NMVEMSMLEACVREDLNVNAPRAMAVLDPIKLVIENYPENDSETLvaPNHPSDESMGTREISFGREIWIEAEDFREsank 400
Cdd:TIGR00463 382 VTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRVER--PLHPDHPEIGERVLILRGEIYVPKDDLEE---- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 401 kfkrlvLDKEVRLRNAyvvkanrvekdadGNVttVYCTYDADTLGKDPADGRKV-KGVIHWVDAGTAQQAEFRLYDRLFN 479
Cdd:TIGR00463 456 ------GVEPVRLMDA-------------VNV--IYSKKELRYHSEGLEGARKLgKSIIHWLPAKDAVKVKVIMPDASIV 514
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 996038741 480 ---VPNPAAEENFTDVInpesltvltgwaeaglakrgseagawQFERTGYFCLDADSTDDKP 538
Cdd:TIGR00463 515 egvIEADASELEVGDVV--------------------------QFERFGFARLDSADKDGMV 550
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
20-530 |
1.56e-94 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 298.08 E-value: 1.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 20 LANGVHESIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEErY 99
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVS-F 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 100 SSNYFDQLHGFANELIDKGLAYVDFSTQDVMRELRgtltAPGKNSPYRDTDVETNQREFAKMTAGEYKEGECSLRAKIDM 179
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKER----ADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 180 ASPFMCMRDPVIYRVKHAHHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIdSTPRQYEF 259
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGL-RRPRIHAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 260 SRLNLEYTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSMLEACVREDLNVN 339
Cdd:PLN03233 238 ARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 340 APRAMAV--LDPIKLVIENYPENDSETLVAPN-HPSDESMGTREISFGREIWIEAEDfresankkFKRLVLDKEVRLRNA 416
Cdd:PLN03233 318 AKRFMAIdkADHTALTVTNADEEADFAFSETDcHPKDPGFGKRAMRICDEVLLEKAD--------TEDIQLGEDIVLLRW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 417 YVVKANRVEKDADGNVTTvyctydadtlgkdPADGRKVKGVIHWV-DAGTAQQAEFRLYDRLFNVPNPAAEENFTDVINP 495
Cdd:PLN03233 390 GVIEISKIDGDLEGHFIP-------------DGDFKAAKKKISWIaDVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFINP 456
|
490 500 510
....*....|....*....|....*....|....*
gi 996038741 496 ESLTVLTGWAEAGLaKRGSEAGAWQFERTGYFCLD 530
Cdd:PLN03233 457 DTLAETDVIGDAGL-KTLKEHDIIQLERRGFYRVD 490
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
340-530 |
1.70e-73 |
|
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: 231.39 E-value: 1.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 340 APRAMAVLDPIKLVIENYPENDSETLVAPNHPSDESMGTREISFGREIWIEAEDfresankkFKRLVLDKEVRLRNAYVV 419
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIERED--------FKRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 420 KANRVEKDADGNVTTVYCTYDADTLGKDpadgRKVKG-VIHWVDAGTAQQAEFRLYDRLFNVPNpaaeeNFTDVINPESL 498
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGA----RKVKGkIIHWVSASDAVPAEVRLYDRLFKDED-----DADFLLNPDSL 143
|
170 180 190
....*....|....*....|....*....|....
gi 996038741 499 TVLT-GWAEAGLAkrGSEAG-AWQFERTGYFCLD 530
Cdd:pfam03950 144 KVLTeGLAEPALA--NLKPGdIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
28-337 |
2.62e-67 |
|
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: 217.73 E-value: 2.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 28 IKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNYFDQL 107
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 108 HGFANELIDKGlayvdfstqdvmrelrgtltapgknspyrdtdvetnqrefakmtageykegecslrakidmaspfmcmr 187
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 188 dpviyrvkhahhhqtgdkwcVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIdSTPRQYEFSRLNLEY- 266
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGW-EPPRFYHFPRLLLEDg 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 267 TVLSKRRLiqlveenhvsgwddprMPTVAGLRRRGYTAGSVREFCKRIGVTKMD-----------------------NMV 323
Cdd:cd00418 152 TKLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSKPDghelftleemiaafsvervnsadATF 215
|
330
....*....|....
gi 996038741 324 EMSMLEACVREDLN 337
Cdd:cd00418 216 DWAKLEWLNREYIR 229
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
28-342 |
1.05e-48 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 168.68 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 28 IKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNP--AKEDIAFVNSIKEDVKWLGFEWDgEERYSSNYFD 105
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 106 QLHGFANELIDKGLAYVdfstqdvmrelrgtltapgknspyrdtdvetnqrefakmtageykegecslrakidmaspfmc 185
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 186 mrdpviyrvkhahHHQTGDKWCVYPMYDFTHCISDAIEGITHSLCTLEFQDNRRLYDWVIENITIDsTPRQYEFSRLNLE 265
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWE-YPETIHWGRLKIE 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 996038741 266 YTVLSKRRLIQLVEENHVSGWDDPRMPTVAGLRRRGYTAGSVREFCKRIGVTKMDNMVEMSMLEACVREDLNVNAPR 342
Cdd:cd09287 164 GGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
27-256 |
1.52e-17 |
|
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: 85.48 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 27 SIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNYFDQ 106
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 107 LHGFANELIDKGLAYVDFSTQDVMRELRGTLTAPGKNSPYRDTDVETNQREFAKMTAgeyKEGECSLRAKIDMASPFM-- 184
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLA---KGIPPVVRFKIPQEAVVSfn 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 185 ------------CMRDPVIYRvkhahhhqtGDKwcvYPMYDFTHCISDAIEGITHSLctlefqdnrRLYDWvienitIDS 252
Cdd:TIGR00464 158 dqvrgeitfqnsELDDFVILR---------SDG---SPTYNFAVVVDDYLMKITHVI---------RGEDH------ISN 210
|
....
gi 996038741 253 TPRQ 256
Cdd:TIGR00464 211 TPKQ 214
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
27-118 |
2.62e-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: 69.54 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 27 SIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNY--- 103
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYgpy 80
|
90 100
....*....|....*....|
gi 996038741 104 -----FDQLHGFANELIDKG 118
Cdd:cd00808 81 rqserLEIYRKYAEKLLEKG 100
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
30-121 |
1.75e-12 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 68.34 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 30 TRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWDGEERYSSNYFDQLHG 109
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHDAYRA 87
|
90
....*....|..
gi 996038741 110 FANELIDKGLAY 121
Cdd:PRK05710 88 ALDRLRAQGLVY 99
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
30-272 |
1.30e-11 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 62.50 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 30 TRFPPEPNGFLHIGHAKSICLNFGVAQD-----YSGSCNLRFDDTNPAKEDIAfvnsikeDVKWLGFEwdgeeryssnyf 104
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDPA-------NKKGENAK------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 105 dqlhgfanelidkglAYVDFSTqdvmrelrgtltapgknspyrdtdvetnqREFAKMTAgeykegecslrakidmaspfm 184
Cdd:cd00802 63 ---------------AFVERWI-----------------------------ERIKEDVE--------------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 185 cmrdpviyrvkhahhhqtgdkwcvypmYDFTHCISDAIEGITH---SLCTLEFQDNRRLYDWVIENITIDSTPRQYEFSR 261
Cdd:cd00802 78 ---------------------------YMFLQAADFLLLYETEcdiHLGGSDQLGHIELGLELLKKAGGPARPFGLTFGR 130
|
250
....*....|..
gi 996038741 262 LNLEY-TVLSKR 272
Cdd:cd00802 131 VMGADgTKMSKS 142
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
26-229 |
3.27e-11 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 65.92 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 26 ESIKTRFPPEPNGFLHIGHAKSICLNFGVAQDYSGSCNLRFDDTNPAKEDIAFVNSIKEDVKWLGFEWD---------GE 96
Cdd:PLN02627 44 GPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvggeyGP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996038741 97 ERYS--SNYFDQLhgfANELIDKGLAYVDFSTQ---DVMRElrgtlTAPGKNSP------YRDTDVETNQREFAKMTAGE 165
Cdd:PLN02627 124 YRQSerNAIYKQY---AEKLLESGHVYPCFCTDeelEAMKE-----EAELKKLPprytgkWATASDEEVQAELAKGTPYT 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 996038741 166 Y-----KEGecslRAKIDmaspfmcmrDPViyRVKHAHHHQT-GD----KWCVYPMYDFTHCISDAIEGITHSL 229
Cdd:PLN02627 196 YrfrvpKEG----SVKID---------DLI--RGEVSWNTDTlGDfvllRSNGQPVYNFCVAVDDATMGITHVI 254
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
227-272 |
1.28e-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: 1.28e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 996038741 227 HSLCTLEFQDNRRLYDWVIENITIDSTPRQYEFSRLNLEYTVLSKR 272
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKR 104
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
29-99 |
2.57e-09 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 54.85 E-value: 2.57e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 996038741 29 KTRFPPEPnGFLHIGHAKSICLNFGVAqdysGSCNLRFDDTNPAK------EDIAFVNSIKEDVKWLGFEWDGEERY 99
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNREL 72
|
|
| |
