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Conserved domains on  [gi|754269803|gb|AJI60409|]
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glutamine--tRNA ligase [Francisella tularensis subsp. novicida U112]

Protein Classification

glutamine--tRNA ligase( domain architecture ID 11480771)

glutamine--tRNA ligase catalyzes the attachment of glutamine to tRNA(Gln)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05347 PRK05347
glutaminyl-tRNA synthetase; Provisional
1-548 0e+00

glutaminyl-tRNA synthetase; Provisional


:

Pssm-ID: 235424 [Multi-domain]  Cd Length: 554  Bit Score: 1053.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803   1 MTSEIKVNKTNFIKNIIKKDLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYI 80
Cdd:PRK05347   2 MMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  81 NAIQEDVEWLGFKWENQPRFASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFE 160
Cdd:PRK05347  82 DSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 161 EMKNGKFAEGSKTLRAKIDMSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRP 240
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 241 FYDWVIEETEFSIKPQQIEFSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQ 320
Cdd:PRK05347 242 LYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 321 DSVIDVSVLEDAVRDDLNKSVLRKNVVLDPIRVSIKDMPDHH---LDVPNHPQEPEFGRREITISSQIFIERDDFVFKLE 397
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQveeLEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 398 KDMKKLSPNGRVRLLNGYVIECQEVITDTNGEVIELKCSYLPETLGGkKPNDGIKPNGIIHWVDANNCLDAEVRIYDRLF 477
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG-NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754269803 478 NDENPANADRIEDVLNPDSLqVIKNAKVERSLESVKAEERFQFNRVGYFIADlKDCSNDTLVFNRIVTLRN 548
Cdd:PRK05347 481 TVPNPAAGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRD 549
 
Name Accession Description Interval E-value
PRK05347 PRK05347
glutaminyl-tRNA synthetase; Provisional
1-548 0e+00

glutaminyl-tRNA synthetase; Provisional


Pssm-ID: 235424 [Multi-domain]  Cd Length: 554  Bit Score: 1053.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803   1 MTSEIKVNKTNFIKNIIKKDLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYI 80
Cdd:PRK05347   2 MMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  81 NAIQEDVEWLGFKWENQPRFASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFE 160
Cdd:PRK05347  82 DSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 161 EMKNGKFAEGSKTLRAKIDMSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRP 240
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 241 FYDWVIEETEFSIKPQQIEFSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQ 320
Cdd:PRK05347 242 LYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 321 DSVIDVSVLEDAVRDDLNKSVLRKNVVLDPIRVSIKDMPDHH---LDVPNHPQEPEFGRREITISSQIFIERDDFVFKLE 397
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQveeLEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 398 KDMKKLSPNGRVRLLNGYVIECQEVITDTNGEVIELKCSYLPETLGGkKPNDGIKPNGIIHWVDANNCLDAEVRIYDRLF 477
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG-NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754269803 478 NDENPANADRIEDVLNPDSLqVIKNAKVERSLESVKAEERFQFNRVGYFIADlKDCSNDTLVFNRIVTLRN 548
Cdd:PRK05347 481 TVPNPAAGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRD 549
glnS TIGR00440
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ...
31-548 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: 690.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803   31 TRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKMYE 110
Cdd:TIGR00440   3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  111 LAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINLRDP 190
Cdd:TIGR00440  83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  191 ALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLNLNYTIT 270
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  271 SKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLRKNVVLDP 350
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  351 IRVSIKDMPDHH--LDVPNHPQEPEFGRREITISSQIFIERDDFVFKLEKDMKKLSPNGRVRLLNGYVIECQEVITDTNG 428
Cdd:TIGR00440 323 VEVVIENLSDEYelATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAAG 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  429 EVIELKCSYLPETLgGKKPNDGIKPNGIIHWVDANNCLDAEVRIYDRLFNDENPANADRIEDVLNPDSLqVIKNAKVERS 508
Cdd:TIGR00440 403 KITTIFCTYDNKTL-GKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL-VIKQGFMEHS 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 754269803  509 LESVKAEERFQFNRVGYFIADLKDCSNDTLVFNRIVTLRN 548
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKD 520
GlnRS_core cd00807
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ...
29-343 1.11e-140

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: 405.87  E-value: 1.11e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQpRFASEYFDKM 108
Cdd:cd00807    2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV-TYASDYFDQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYVcdlsaeeirayrgtlkepgknspyrersitenlelfeemkngkfaegsktlrakidmssgninlr 188
Cdd:cd00807   81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 189 dpalyrikfshHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSiKPQQIEFSRLNLNYT 268
Cdd:cd00807   96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTYT 163
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803 269 ITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLR 343
Cdd:cd00807  164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
29-338 5.58e-138

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: 402.08  E-value: 5.58e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803   29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKM 108
Cdd:pfam00749   2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  109 YELAILLIKKGKAYVCDLSAEEIRAYRGTLkePGKNSPYRERSITENLELF-EEMKNGKFAEGSKTLRAKIDMSSgNINL 187
Cdd:pfam00749  82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  188 RDPALYRIKFS---HHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLN 264
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803  265 LNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSV-LEDAVRDDLN 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKsLEAFDRKKLD 313
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
27-531 1.57e-121

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: 365.66  E-value: 1.57e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  27 SSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFD 106
Cdd:COG0008    3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 107 KMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPY----RERSITENlelfEEMKngkfAEG-SKTLRAKI--- 178
Cdd:COG0008   83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGePPVLRFKIpee 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 179 -----DMSSG-----NINLRDPALYRikfshhpKTGdkwciYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEE 248
Cdd:COG0008  155 gvvfdDLVRGeitfpNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 249 TEFSIkPqqiEFSRLNLNY----TITSKRKlkylvdnKLVngwddprmpTIKGYRRRGYTPESIRNFCEMIGISKQDS-- 322
Cdd:COG0008  223 LGWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqe 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 323 VIDVSVLEDAVrdDLNKsVLRKNVVLDPIRV------SIKDMPDHHLD---VPNHPQE--PEFGRREITIS--------- 382
Cdd:COG0008  283 IFSLEELIEAF--DLDR-VSRSPAVFDPVKLvwlngpYIRALDDEELAellAPELPEAgiREDLERLVPLVreraktlse 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 383 -----SQIFIERDDfvfklEKDMKKLSPNGRVRllngyviecqEVITDTnGEVIELKCSYLPETLggkkpndgikpNGII 457
Cdd:COG0008  360 laelaRFFFIERED-----EKAAKKRLAPEEVR----------KVLKAA-LEVLEAVETWDPETV-----------KGTI 412
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754269803 458 HWVDAnnclDAEVRiyDRLFndenpANADRIedvlnpdslqVIKNAKVERSL-ESVKA--EERFqFNRVGYFIADLK 531
Cdd:COG0008  413 HWVSA----EAGVK--DGLL-----FMPLRV----------ALTGRTVEPSLfDVLELlgKERV-FERLGYAIDKLA 467
 
Name Accession Description Interval E-value
PRK05347 PRK05347
glutaminyl-tRNA synthetase; Provisional
1-548 0e+00

glutaminyl-tRNA synthetase; Provisional


Pssm-ID: 235424 [Multi-domain]  Cd Length: 554  Bit Score: 1053.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803   1 MTSEIKVNKTNFIKNIIKKDLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYI 80
Cdd:PRK05347   2 MMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  81 NAIQEDVEWLGFKWENQPRFASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFE 160
Cdd:PRK05347  82 DSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 161 EMKNGKFAEGSKTLRAKIDMSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRP 240
Cdd:PRK05347 162 RMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 241 FYDWVIEETEFSIKPQQIEFSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQ 320
Cdd:PRK05347 242 LYDWVLDNLPIPPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQ 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 321 DSVIDVSVLEDAVRDDLNKSVLRKNVVLDPIRVSIKDMPDHH---LDVPNHPQEPEFGRREITISSQIFIERDDFVFKLE 397
Cdd:PRK05347 322 DSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQveeLEAPNHPEDPEMGTREVPFSRELYIEREDFMEEPP 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 398 KDMKKLSPNGRVRLLNGYVIECQEVITDTNGEVIELKCSYLPETLGGkKPNDGIKPNGIIHWVDANNCLDAEVRIYDRLF 477
Cdd:PRK05347 402 KKYFRLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSG-NPADGRKVKGTIHWVSAAHAVPAEVRLYDRLF 480
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754269803 478 NDENPANADRIEDVLNPDSLqVIKNAKVERSLESVKAEERFQFNRVGYFIADlKDCSNDTLVFNRIVTLRN 548
Cdd:PRK05347 481 TVPNPAAGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCAD-KDSTPGKLVFNRTVGLRD 549
PRK14703 PRK14703
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
11-548 0e+00

glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional


Pssm-ID: 237793 [Multi-domain]  Cd Length: 771  Bit Score: 785.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  11 NFIKNIIKKDLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWL 90
Cdd:PRK14703  14 NFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  91 GFKWENQPRFASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFEEMKNGKFAEG 170
Cdd:PRK14703  94 GFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 171 SKTLRAKIDMSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEET- 249
Cdd:PRK14703 174 AHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLg 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 250 EFSIKPQQIEFSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVL 329
Cdd:PRK14703 254 PWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVL 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 330 EDAVRDDLNKSVLRKNVVLDPIRVSIKDMPDHH---LDVPNHPQE-PEFGRREITISSQIFIERDDFVFKLEKDMKKLSP 405
Cdd:PRK14703 334 EFAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKveeLDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTP 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 406 NGRVRLLNGYVIECQEVITDTNGEVIELKCSYLPETLGGKKPndGIKPNGIIHWVDANNCLDAEVRIYDRLFNDENPANA 485
Cdd:PRK14703 414 GREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT--GRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEAA 491
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803 486 DR--IEDvLNPDSLQVIKNaKVERSLESVKAEERFQFNRVGYFIADLKDCSNDTLVFNRIVTLRN 548
Cdd:PRK14703 492 DEdfLEF-LNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKD 554
glnS TIGR00440
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ...
31-548 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: 690.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803   31 TRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKMYE 110
Cdd:TIGR00440   3 TRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDELYR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  111 LAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINLRDP 190
Cdd:TIGR00440  83 YAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMRDP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  191 ALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLNLNYTIT 270
Cdd:TIGR00440 163 VAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPRPAQYEFSRLNLEGTVL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  271 SKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLRKNVVLDP 350
Cdd:TIGR00440 243 SKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVIDP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  351 IRVSIKDMPDHH--LDVPNHPQEPEFGRREITISSQIFIERDDFVFKLEKDMKKLSPNGRVRLLNGYVIECQEVITDTNG 428
Cdd:TIGR00440 323 VEVVIENLSDEYelATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAAG 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  429 EVIELKCSYLPETLgGKKPNDGIKPNGIIHWVDANNCLDAEVRIYDRLFNDENPANADRIEDVLNPDSLqVIKNAKVERS 508
Cdd:TIGR00440 403 KITTIFCTYDNKTL-GKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL-VIKQGFMEHS 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 754269803  509 LESVKAEERFQFNRVGYFIADLKDCSNDTLVFNRIVTLRN 548
Cdd:TIGR00440 481 LGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKD 520
PLN02859 PLN02859
glutamine-tRNA ligase
29-547 0e+00

glutamine-tRNA ligase


Pssm-ID: 178450 [Multi-domain]  Cd Length: 788  Bit Score: 543.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGfkWEN-QPRFASEYFDK 107
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WEPfKITYTSDYFQE 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 108 MYELAILLIKKGKAYVCDLSAEEIRAYRgtlkEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINL 187
Cdd:PLN02859 343 LYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNM 418
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 188 RDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFsIKPQQIEFSRLNLNY 267
Cdd:PLN02859 419 YDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGL-YQPYVWEYSRLNVTN 497
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 268 TITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQD-SVIDVSVLEDAVRDDLNKSVLRKNV 346
Cdd:PLN02859 498 TVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDnSLIRMDRLEHHIREELNKTAPRTMV 577
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 347 VLDPIRVSIKDMPDHHLD------VPNHPQEPEFGRREITISSQIFIERDDFVFKLEKDMKKLSPNGRVRLLNGYVIECQ 420
Cdd:PLN02859 578 VLHPLKVVITNLESGEVIeldakrWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFPIKCT 657
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 421 EVI-TDTNGEVIELKCSYLPEtlggKKpndgIKPNGIIHWVDAN----NCLDAEVRIYDRLFNDENPANADRIEDVLNPD 495
Cdd:PLN02859 658 DVVlADDNETVVEIRAEYDPE----KK----TKPKGVLHWVAEPspgvEPLKVEVRLFDKLFLSENPAELEDWLEDLNPQ 729
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 754269803 496 SLQVIKNAKVERSLESVKAEERFQFNRVGYFIADlKDCSNDTLVFNRIVTLR 547
Cdd:PLN02859 730 SKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVD-KDSTPEKLVFNRTVTLK 780
PTZ00437 PTZ00437
glutaminyl-tRNA synthetase; Provisional
32-547 2.66e-158

glutaminyl-tRNA synthetase; Provisional


Pssm-ID: 240418 [Multi-domain]  Cd Length: 574  Bit Score: 463.69  E-value: 2.66e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  32 RFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFK--WENqprFASEYFDKMY 109
Cdd:PTZ00437  55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKpdWVT---FSSDYFDQLH 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 110 ELAILLIKKGKAYVCDLSAEEIRAYRgtlkEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINLRD 189
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 190 PALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFsIKPQQIEFSRLNLNYTI 269
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNL-WRPHVWEFSRLNVTGSL 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 270 TSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLRKNVVLD 349
Cdd:PTZ00437 287 LSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVID 366
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 350 PIRVSIKDMP-DHHLDVPNHPQEPEFGRREITISSQIFIERDDfvFKLEKDMKK---LSPNGRVRLL--NGYVIeCQEVI 423
Cdd:PTZ00437 367 PIKVVVDNWKgEREFECPNHPRKPELGSRKVMFTDTFYVDRSD--FRTEDNNSKfygLAPGPRVVGLkySGNVV-CKGFE 443
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 424 TDTNGE--VIELKCSYLPETlggkkpndgiKPNGIIHWVDANNCLDAEVRIYDRLFNDENPANADRIEDVLNPDSlQVIK 501
Cdd:PTZ00437 444 VDAAGQpsVIHVDIDFERKD----------KPKTNISWVSATACTPVEVRLYNALLKDDRAAIDPEFLKFIDEDS-EVVS 512
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 754269803 502 NAKVERSLESVKAEERFQFNRVGYFIADlKDCSNDTLVFNRIVTLR 547
Cdd:PTZ00437 513 HGYAEKGIENAKHFESVQAERFGYFVVD-PDTRPDHLVMNRVLGLR 557
GlnRS_core cd00807
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ...
29-343 1.11e-140

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: 405.87  E-value: 1.11e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQpRFASEYFDKM 108
Cdd:cd00807    2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV-TYASDYFDQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYVcdlsaeeirayrgtlkepgknspyrersitenlelfeemkngkfaegsktlrakidmssgninlr 188
Cdd:cd00807   81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 189 dpalyrikfshHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSiKPQQIEFSRLNLNYT 268
Cdd:cd00807   96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLY-RPHQWEFSRLNLTYT 163
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803 269 ITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLR 343
Cdd:cd00807  164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
29-338 5.58e-138

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: 402.08  E-value: 5.58e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803   29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKM 108
Cdd:pfam00749   2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  109 YELAILLIKKGKAYVCDLSAEEIRAYRGTLkePGKNSPYRERSITENLELF-EEMKNGKFAEGSKTLRAKIDMSSgNINL 187
Cdd:pfam00749  82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  188 RDPALYRIKFS---HHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLN 264
Cdd:pfam00749 159 RDPVRGRIKFTpqeIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLN 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803  265 LNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSV-LEDAVRDDLN 338
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKsLEAFDRKKLD 313
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
27-531 1.57e-121

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: 365.66  E-value: 1.57e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  27 SSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFD 106
Cdd:COG0008    3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 107 KMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPY----RERSITENlelfEEMKngkfAEG-SKTLRAKI--- 178
Cdd:COG0008   83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGePPVLRFKIpee 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 179 -----DMSSG-----NINLRDPALYRikfshhpKTGdkwciYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEE 248
Cdd:COG0008  155 gvvfdDLVRGeitfpNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 249 TEFSIkPqqiEFSRLNLNY----TITSKRKlkylvdnKLVngwddprmpTIKGYRRRGYTPESIRNFCEMIGISKQDS-- 322
Cdd:COG0008  223 LGWEP-P---EFAHLPLILgpdgTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKSDDqe 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 323 VIDVSVLEDAVrdDLNKsVLRKNVVLDPIRV------SIKDMPDHHLD---VPNHPQE--PEFGRREITIS--------- 382
Cdd:COG0008  283 IFSLEELIEAF--DLDR-VSRSPAVFDPVKLvwlngpYIRALDDEELAellAPELPEAgiREDLERLVPLVreraktlse 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 383 -----SQIFIERDDfvfklEKDMKKLSPNGRVRllngyviecqEVITDTnGEVIELKCSYLPETLggkkpndgikpNGII 457
Cdd:COG0008  360 laelaRFFFIERED-----EKAAKKRLAPEEVR----------KVLKAA-LEVLEAVETWDPETV-----------KGTI 412
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754269803 458 HWVDAnnclDAEVRiyDRLFndenpANADRIedvlnpdslqVIKNAKVERSL-ESVKA--EERFqFNRVGYFIADLK 531
Cdd:COG0008  413 HWVSA----EAGVK--DGLL-----FMPLRV----------ALTGRTVEPSLfDVLELlgKERV-FERLGYAIDKLA 467
gltX_arch TIGR00463
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ...
1-540 2.60e-103

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: 321.77  E-value: 2.60e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803    1 MTSEIKVNKTNFIKniikkDLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYI 80
Cdd:TIGR00463  71 LDIKKKEKKRKGLR-----ELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAY 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803   81 NAIQEDVEWLGFKWEnQPRFASEYFDKMYELAILLIKKGKAYVCDLSAEEIRayrgTLKEPGKNSPYRERSITENLELFE 160
Cdd:TIGR00463 146 DMILEDLEWLGVKWD-EVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFR----ELRNRGEACHCRDRSVEENLERWE 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  161 EMKNGKFAEGSKTLRAKIDMSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQD--Q 238
Cdd:TIGR00463 221 EMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDnrR 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  239 RPFYDWVIEETEFsikPQQIEFSRLNLNY--TITSKRKLKYLVDNKLVnGWDDPRMPTIKGYRRRGYTPESIRNFCEMIG 316
Cdd:TIGR00463 301 KQEYIYRYFGWEP---PEFIHWGRLKIDDvrALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIG 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  317 ISKQDSVIDVSVLEDAVRDDLNKSVLRKNVVLDPIRVSIKDMPDHHLDV-PNHPQEPEFGRREITISSQIFIERDDFVFK 395
Cdd:TIGR00463 377 VKINDVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRVErPLHPDHPEIGERVLILRGEIYVPKDDLEEG 456
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  396 LEKdmkklspngrVRLLNGyvieCQEVITDTNGEVIELkcsylpETLGGKKpndgiKPNGIIHWVDANNCLDAevriydr 475
Cdd:TIGR00463 457 VEP----------VRLMDA----VNVIYSKKELRYHSE------GLEGARK-----LGKSIIHWLPAKDAVKV------- 504
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754269803  476 lfndenpanadrieDVLNPDSLqvIKNAKVERSLESVKAEERFQFNRVGYFIADLKDcsNDTLVF 540
Cdd:TIGR00463 505 --------------KVIMPDAS--IVEGVIEADASELEVGDVVQFERFGFARLDSAD--KDGMVF 551
PLN02907 PLN02907
glutamate-tRNA ligase
20-529 5.96e-99

glutamate-tRNA ligase


Pssm-ID: 215492 [Multi-domain]  Cd Length: 722  Bit Score: 315.13  E-value: 5.96e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  20 DLETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWEnQPR 99
Cdd:PLN02907 205 DLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVT 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 100 FASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTlkepGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKID 179
Cdd:PLN02907 284 YTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLD 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 180 MSSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEetEFSIKPQQI- 258
Cdd:PLN02907 360 MQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILE--DMGLRKVHIw 437
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 259 EFSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKqdsviDVSVLEdavRDDL- 337
Cdd:PLN02907 438 EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASK-----NLNLME---WDKLw 509
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 338 --NKSVL-----RKNVVLDPIRV--SIKDMPDHHL--DVPNHPQEPEFGRREITISSQIFIERDDFVfklekdmkKLSPN 406
Cdd:PLN02907 510 tiNKKIIdpvcpRHTAVLKEGRVllTLTDGPETPFvrIIPRHKKYEGAGKKATTFTNRIWLDYADAE--------AISEG 581
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 407 GRVRLLN-GYVIeCQEVITDTNGEVIELKCSYLPEtlgGKKPNDGIKpngiIHWV-DANNCLDAEVRIYDRLFNDENPAN 484
Cdd:PLN02907 582 EEVTLMDwGNAI-IKEITKDEGGAVTALSGELHLE---GSVKTTKLK----LTWLpDTNELVPLSLVEFDYLITKKKLEE 653
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 754269803 485 ADRIEDVLNPDSlQVIKNAKVERSLESVKAEERFQFNRVGYFIAD 529
Cdd:PLN02907 654 DDNFLDVLNPCT-KKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
PTZ00402 PTZ00402
glutamyl-tRNA synthetase; Provisional
29-529 4.98e-94

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 240404 [Multi-domain]  Cd Length: 601  Bit Score: 299.18  E-value: 4.98e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKM 108
Cdd:PTZ00402  53 VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDLM 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYvCDLSA-EEIRAYRGTlkepGKNSPYRERSITENLELFEEMKNGKfAEGSKT-LRAKIDMSSGNIN 186
Cdd:PTZ00402 133 YEKAEELIKKGLAY-CDKTPrEEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNENKA 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 187 LRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSiKPQQIEFSRLNLN 266
Cdd:PTZ00402 207 MRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIR-KPIVEDFSRLNME 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 267 YTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSVLRKNV 346
Cdd:PTZ00402 286 YSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTV 365
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 347 VLDPIRVSIKDMPDHHLDV---PNHPQEPEFGRREITISSQIFIERDDFVFKLEKDMKKLSPNGrvrllNGYVIECQEvi 423
Cdd:PTZ00402 366 VSNTLKVRCTVEGQIHLEAcekLLHKKVPDMGEKTYYKSDVIFLDAEDVALLKEGDEVTLMDWG-----NAYIKNIRR-- 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 424 TDTNGEVIELKCSYLPEtlggkkpNDGIKPNGIIHWV-DANNCLDAEVRIYDRLFNDENPANADRIEDVLNPDSlQVIKN 502
Cdd:PTZ00402 439 SGEDALITDADIVLHLE-------GDVKKTKFKLTWVpESPKAEVMELNEYDHLLTKKKPDPEESIDDIIAPVT-KYTQE 510
                        490       500
                 ....*....|....*....|....*..
gi 754269803 503 AKVERSLESVKAEERFQFNRVGYFIAD 529
Cdd:PTZ00402 511 VYGEEALSVLKKGDIIQLERRGYYIVD 537
gltX PRK04156
glutamyl-tRNA synthetase; Provisional
31-525 1.12e-93

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 235229 [Multi-domain]  Cd Length: 567  Bit Score: 297.15  E-value: 1.12e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  31 TRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPD--KEDIEYINAIQEDVEWLGFKWeNQPRFASEYFDKM 108
Cdd:PRK04156 104 MRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKW-DEVVIQSDRLEIY 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGKAYVCDLSAEEIRAyrgtLKEPGKNSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDMSSGNINLR 188
Cdd:PRK04156 183 YEYARKLIEMGGAYVCTCDPEEFKE----LRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVR 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 189 DPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQD----QRPFYD---WVIEETefsikpqqIEFS 261
Cdd:PRK04156 259 DWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYDyfgWEYPET--------IHYG 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 262 RLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKSV 341
Cdd:PRK04156 331 RLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIA 410
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 342 LRKNVVLDPIRVSIKDMPDHHLDVPNHPQEPEFGRREITISSQIFIERDDFVfklekdmkklSPNGRVRLLNGYVIECQE 421
Cdd:PRK04156 411 NRYFFVRDPVELEIEGAEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLE----------AEGKMVRLMDLFNVEITG 480
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 422 VITDtngevielKCSYLPETLggkkpnDGIKPNG--IIHWVDANNCLDAEVRIYDRlfndenpanadriedvlnpdslqV 499
Cdd:PRK04156 481 VSVD--------KARYHSDDL------EEARKNKapIIQWVPEDESVPVRVLKPDG-----------------------G 523
                        490       500
                 ....*....|....*....|....*.
gi 754269803 500 IKNAKVERSLESVKAEERFQFNRVGY 525
Cdd:PRK04156 524 DIEGLAEPDVADLEVDDIVQFERFGF 549
PLN03233 PLN03233
putative glutamate-tRNA ligase; Provisional
21-529 3.78e-90

putative glutamate-tRNA ligase; Provisional


Pssm-ID: 178772 [Multi-domain]  Cd Length: 523  Bit Score: 286.52  E-value: 3.78e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  21 LETNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKwENQPRF 100
Cdd:PLN03233   4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 101 ASEYFDKMYELAILLIKKGKAYVCDLSAEEIRAYRGTLKEpgknSPYRERSITENLELFEEMKNGKFAEGSKTLRAKIDM 180
Cdd:PLN03233  83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 181 SSGNINLRDPALYRIKFSHHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSiKPQQIEF 260
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR-RPRIHAF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 261 SRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVLEDAVRDDLNKS 340
Cdd:PLN03233 238 ARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 341 VLRKNVV--LDPIRVSIKDMPD--HHLDVPN--HPQEPEFGRREITISSQIFIERddfvfkleKDMKKLSPNGRVRLLNG 414
Cdd:PLN03233 318 AKRFMAIdkADHTALTVTNADEeaDFAFSETdcHPKDPGFGKRAMRICDEVLLEK--------ADTEDIQLGEDIVLLRW 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 415 YVIECQEVITDTNGEVIelkcsylpetlggkkPNDGIK-PNGIIHWV-DANNCLDAEVRIYDRLFNDENPANADRIEDVL 492
Cdd:PLN03233 390 GVIEISKIDGDLEGHFI---------------PDGDFKaAKKKISWIaDVSDNIPVVLSEFDNLIIKEKLEEDDKFEDFI 454
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 754269803 493 NPDSL---QVIKNAkverSLESVKAEERFQFNRVGYFIAD 529
Cdd:PLN03233 455 NPDTLaetDVIGDA----GLKTLKEHDIIQLERRGFYRVD 490
GlxRS_core cd00418
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ...
29-350 1.47e-64

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: 210.02  E-value: 1.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDKM 108
Cdd:cd00418    2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 109 YELAILLIKKGkayvcdlsaeeirayrgtlkepgknspyrersitenlelfeemkngkfaegsktlrakidmssgninlr 188
Cdd:cd00418   82 RAYAEELIKKG--------------------------------------------------------------------- 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 189 dpalyrikfshhpktgdkwcIYPMYTFAHPLEDAIEEITHSLCTLEFQDQRPFYDWVIEETEFSIkPQQIEFSRLNLNY- 267
Cdd:cd00418   93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEP-PRFYHFPRLLLEDg 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 268 TITSKRKLKylvdnklvngwddprmPTIKGYRRRGYTPESIRNFCEMIGISKQDSViDVSVLEDAVRDDLNKSVLRKNVV 347
Cdd:cd00418  152 TKLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGH-ELFTLEEMIAAFSVERVNSADAT 214

                 ...
gi 754269803 348 LDP 350
Cdd:cd00418  215 FDW 217
tRNA-synt_1c_C pfam03950
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ...
347-529 1.21e-58

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: 192.49  E-value: 1.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  347 VLDPIRVSIKDMPDHH---LDVPNHPQEPEFGRREITISSQIFIERDDFvfklekdmKKLSPNGRVRLLNGYVIECQEVI 423
Cdd:pfam03950   7 VLDPVKVVIENYPEGQeetAEVPNHPKNPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNIKVTEVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  424 TDTNGEVIELKCSYLPETLGGKKpndgiKPNG-IIHWVDANNCLDAEVRIYDRLFNDENPANadrieDVLNPDSLQVIKN 502
Cdd:pfam03950  79 KDEDGNVTELHCTYDGDDLGGAR-----KVKGkIIHWVSASDAVPAEVRLYDRLFKDEDDAD-----FLLNPDSLKVLTE 148
                         170       180
                  ....*....|....*....|....*..
gi 754269803  503 AKVERSLESVKAEERFQFNRVGYFIAD 529
Cdd:pfam03950 149 GLAEPALANLKPGDIVQFERIGYFRVD 175
GluRS_non_core cd09287
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ...
29-329 2.66e-45

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: 159.44  E-value: 2.66e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  29 ILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPD--KEDIEYINAIQEDVEWLGFKWEnQPRFASEYFD 106
Cdd:cd09287    2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 107 KMYELAILLIKKGKAYVcdlsaeeirayrgtlkepgknspyrersitenlelfeemkngkfaegsktlrakidmssgnin 186
Cdd:cd09287   81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 187 lrdpalyrikfshHPKTGDKWCIYPMYTFAHPLEDAIEEITHSLCTLEFQD----QRPFYD---WvieetefsIKPQQIE 259
Cdd:cd09287   98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEyfgW--------EYPETIH 156
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 260 FSRLNLNYTITSKRKLKYLVDNKLVNGWDDPRMPTIKGYRRRGYTPESIRNFCEMIGISKQDSVIDVSVL 329
Cdd:cd09287  157 WGRLKIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENL 226
PRK05710 PRK05710
tRNA glutamyl-Q(34) synthetase GluQRS;
31-142 1.20e-15

tRNA glutamyl-Q(34) synthetase GluQRS;


Pssm-ID: 235573  Cd Length: 299  Bit Score: 77.58  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  31 TRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYFDkMYE 110
Cdd:PRK05710   8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD-AYR 86
                         90       100       110
                 ....*....|....*....|....*....|...
gi 754269803 111 LAI-LLIKKGKAYVCDLSAEEIRAYRGTLKEPG 142
Cdd:PRK05710  87 AALdRLRAQGLVYPCFCSRKEIAAAAPAPPDGG 119
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
28-340 1.64e-13

catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173905 [Multi-domain]  Cd Length: 239  Bit Score: 70.31  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  28 SILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFASEYfdk 107
Cdd:cd00808    1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPY--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 108 myelaillikkgkayvcdlsaeeirayrgtlkepgknSPYRErsiTENLELFEEmkngkfaegsktlrakidmssgninl 187
Cdd:cd00808   78 -------------------------------------GPYRQ---SERLEIYRK-------------------------- 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 188 rdpALYRIKfshhpKTGDKwciYPMYTFAHPLEDAIEEITHslctlefqdqrpfydwVIE-ETEFSIKPQQI-------- 258
Cdd:cd00808   92 ---YAEKLL-----EKGDG---FPTYHLANVVDDHLMGITH----------------VIRgEEHLSSTPKQIllyealgw 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 259 ---EFSRLNLnytIT-------SKRKLKYLVDnklvngwddprmptikGYRRRGYTPESIRNFCEMIGISKQDSViDVSV 328
Cdd:cd00808  145 eppKFAHLPL---ILnpdgkklSKRKGDTSIS----------------DYREEGYLPEALLNYLALLGWSPPDGE-EFFT 204
                        330
                 ....*....|....*.
gi 754269803 329 LEDAVR----DDLNKS 340
Cdd:cd00808  205 LEELIElfdlERVSKS 220
PLN02627 PLN02627
glutamyl-tRNA synthetase
23-230 1.20e-11

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 67.07  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803  23 TNKVSSILTRFPPEPNGYLHIGHAKSICLNFGIAQEFDGKCNLRFDDTNPDKEDIEYINAIQEDVEWLGFKWENQPRFAS 102
Cdd:PLN02627  40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGG 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 103 EY-------FDKMY-ELAILLIKKGKAYVCDLSAEEIRAYRGTLKEPGKNSPYRERSITENLELFEEMKngkfAEGSK-T 173
Cdd:PLN02627 120 EYgpyrqseRNAIYkQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAEL----AKGTPyT 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754269803 174 LRAKIDmSSGNINLRDpaLYRIKFSHHPKT-GDkWCIY-----PMYTFAHPLEDAIEEITHSL 230
Cdd:PLN02627 196 YRFRVP-KEGSVKIDD--LIRGEVSWNTDTlGD-FVLLrsngqPVYNFCVAVDDATMGITHVI 254
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
31-90 4.41e-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: 60.96  E-value: 4.41e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754269803  31 TRFPPEPNGYLHIGHAKSICLNFGIAQE-----FDGKCNLRFDDTNPDKED-------------IEYINAIQEDVEWL 90
Cdd:cd00802    2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLIGDpankkgenakafvERWIERIKEDVEYM 79
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
31-97 6.06e-10

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: 56.39  E-value: 6.06e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754269803  31 TRFPPEPnGYLHIGHAKSICLNFGIAqefdGKCNLRFDDTNPDK------EDIEYINAIQEDVEWLGFKWENQ 97
Cdd:cd02156    2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQN 69
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
217-274 1.05e-04

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: 41.76  E-value: 1.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 754269803 217 HPLEDAIEEIT--HSLCTLEFQDQRPFYDWVIEETEFSIKPQQIEFSRLNLNYTITSKRK 274
Cdd:cd02156   46 HELEERKESIEedISVCGEDFQQNRELYRWVKDNITLPVDPEQVELPRLNLETTVMSKRK 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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