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Conserved domains on  [gi|492174676|ref|WP_005770152|]
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elongation factor P--(R)-beta-lysine ligase [Coxiella burnetii]

Protein Classification

EF-P lysine aminoacylase GenX( domain architecture ID 11455190)

EF-P lysine aminoacylase GenX catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EpmA COG2269
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ...
 10-314 0e+00

Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 441870 [Multi-domain]  Cd Length: 309  Bit Score: 511.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  10 ASIENQRLRAQLLRDIRQFFAERKVMEVETPILSQHTVTDIHIDSFQTTYL-NGKEKQHYYLQTSPEYAMKRLLSAGSGP 88
Cdd:COG2269    1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIgPDGGGRPLYLHTSPEFAMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  89 IYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQ---SKKASRITYEELFLKHLGINPHQISLHQ 165
Cdd:COG2269   81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGaagFAPAERLSYQEAFLRYLGIDPLTADLDE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 166 LQSLANQFSLENSTEyNDRNTLLQFLFSECLEPKIGFDAPLFVYHFPATQAALSKINPQDPNVALRFEVYIQGMECANGF 245
Cdd:COG2269  161 LAAAAAAAGLRVADD-DDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELANGF 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492174676 246 EELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVI 314
Cdd:COG2269  240 HELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVL 308
 
Name Accession Description Interval E-value
EpmA COG2269
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ...
 10-314 0e+00

Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441870 [Multi-domain]  Cd Length: 309  Bit Score: 511.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  10 ASIENQRLRAQLLRDIRQFFAERKVMEVETPILSQHTVTDIHIDSFQTTYL-NGKEKQHYYLQTSPEYAMKRLLSAGSGP 88
Cdd:COG2269    1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIgPDGGGRPLYLHTSPEFAMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  89 IYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQ---SKKASRITYEELFLKHLGINPHQISLHQ 165
Cdd:COG2269   81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGaagFAPAERLSYQEAFLRYLGIDPLTADLDE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 166 LQSLANQFSLENSTEyNDRNTLLQFLFSECLEPKIGFDAPLFVYHFPATQAALSKINPQDPNVALRFEVYIQGMECANGF 245
Cdd:COG2269  161 LAAAAAAAGLRVADD-DDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELANGF 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492174676 246 EELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVI 314
Cdd:COG2269  240 HELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVL 308
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 28-314 2.79e-173

EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]


Pssm-ID: 273090 [Multi-domain]  Cd Length: 290  Bit Score: 481.67  E-value: 2.79e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   28 FFAERKVMEVETPILSQHTVTDIHIDSFQTTYLN-GKEKQHYYLQTSPEYAMKRLLSAGSGPIYQICKAFRNGESGSQHN 106
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGpDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  107 PEFSMLEWYRPDFSCHDLMDEMDELLQFILQ--SKKASRITYEELFLKHLGINPHQISLHQLQSLANQFSLENStEYNDR 184
Cdd:TIGR00462  81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGIRAS-EEDDR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  185 NTLLQFLFSECLEPKIGFDAPLFVYHFPATQAALSKINPQDPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTK 264
Cdd:TIGR00462 160 DDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADNAL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 492174676  265 RNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVI 314
Cdd:TIGR00462 240 RKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
PRK09350 PRK09350
elongation factor P--(R)-beta-lysine ligase;
11-313 4.90e-154

elongation factor P--(R)-beta-lysine ligase;


Pssm-ID: 236474 [Multi-domain]  Cd Length: 306  Bit Score: 433.59  E-value: 4.90e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  11 SIENQRLRAQLLRDIRQFFAERKVMEVETPILSQHTVTDIHIDSFQTTYLN--GKEKQHYYLQTSPEYAMKRLLSAGSGP 88
Cdd:PRK09350   1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGpgASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  89 IYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQSKKASRITYEELFLKHLGINPHQISLHQLQS 168
Cdd:PRK09350  81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 169 LANQFSLENST-EYNDRNTLLQFLFSECLEPKIGFDAPLFVYHFPATQAALSKINPQDPNVALRFEVYIQGMECANGFEE 247
Cdd:PRK09350 161 VAAKLGLSNIAdEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492174676 248 LTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDV 313
Cdd:PRK09350 241 LTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 16-317 8.60e-60

Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238398 [Multi-domain]  Cd Length: 329  Bit Score: 194.34  E-value: 8.60e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPILSQ-------------HTVTDIHIdsfqttylngkekqhyYLQTSPEYAMKRLL 82
Cdd:cd00775    9 IVRSKIISYIRKFLDDRGFLEVETPMLQPiaggaaarpfithHNALDMDL----------------YLRIAPELYLKRLI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  83 SAGSGPIYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQ-----------------SKKASRIT 145
Cdd:cd00775   73 VGGFERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVT 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 146 YEELFLKHLGINPHQISLHQLQSLANQFSLENSTEYNDRNT---LLQFLFSECLEPKigFDAPLFVYHFPATQAALSKIN 222
Cdd:cd00775  153 MVDALKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEKPRTlgkLLDKLFEEFVEPT--LIQPTFIIDHPVEISPLAKRH 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 223 PQDPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIM 302
Cdd:cd00775  231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310

                        330
                 ....*....|....*
gi 492174676 303 IKAERKCIDDVINFP 317
Cdd:cd00775  311 LLTDSNSIRDVILFP 325
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
13-317 3.37e-48

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 163.89  E-value: 3.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   13 ENQRLRAQLLRDIRQFFAERKVMEVETPILSQHT---------VTDIHIDSFqttylngkekqhYYLQTSPEYAMKRLLS 83
Cdd:pfam00152  20 ANLKLRSKIIKAIRNFLDENGFLEVETPILTKSAtpegardflVPSRALGKF------------YALPQSPQLYKQLLMV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   84 AGSGPIYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQSKKASRITYEELFLKHLGINPHQISL 163
Cdd:pfam00152  88 AGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLKKPFPRITY 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  164 HQLQSLANQFSLENSTEYNDRNTlLQFLFSECLEPkiGFDAPLFVYHFPATQAALSK-INPQDPNVALRFEVYIQGMECA 242
Cdd:pfam00152 168 AEAIEKLNGKDVEELGYGSDKPD-LRFLLELVIDK--NKFNPLWVTDFPAEHHPFTMpKDEDDPALAEAFDLVLNGVEIG 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492174676  243 NGFEELTNADEQRQRFLNDNTKRNQQNRPsiniDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVINFP 317
Cdd:pfam00152 245 GGSIRIHDPELQEERFEEQGLDPEEAEEK----FGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFP 315
 
Name Accession Description Interval E-value
EpmA COG2269
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ...
 10-314 0e+00

Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441870 [Multi-domain]  Cd Length: 309  Bit Score: 511.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  10 ASIENQRLRAQLLRDIRQFFAERKVMEVETPILSQHTVTDIHIDSFQTTYL-NGKEKQHYYLQTSPEYAMKRLLSAGSGP 88
Cdd:COG2269    1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIgPDGGGRPLYLHTSPEFAMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  89 IYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQ---SKKASRITYEELFLKHLGINPHQISLHQ 165
Cdd:COG2269   81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGaagFAPAERLSYQEAFLRYLGIDPLTADLDE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 166 LQSLANQFSLENSTEyNDRNTLLQFLFSECLEPKIGFDAPLFVYHFPATQAALSKINPQDPNVALRFEVYIQGMECANGF 245
Cdd:COG2269  161 LAAAAAAAGLRVADD-DDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELANGF 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492174676 246 EELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVI 314
Cdd:COG2269  240 HELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVL 308
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 28-314 2.79e-173

EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]


Pssm-ID: 273090 [Multi-domain]  Cd Length: 290  Bit Score: 481.67  E-value: 2.79e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   28 FFAERKVMEVETPILSQHTVTDIHIDSFQTTYLN-GKEKQHYYLQTSPEYAMKRLLSAGSGPIYQICKAFRNGESGSQHN 106
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGpDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  107 PEFSMLEWYRPDFSCHDLMDEMDELLQFILQ--SKKASRITYEELFLKHLGINPHQISLHQLQSLANQFSLENStEYNDR 184
Cdd:TIGR00462  81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGIRAS-EEDDR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  185 NTLLQFLFSECLEPKIGFDAPLFVYHFPATQAALSKINPQDPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTK 264
Cdd:TIGR00462 160 DDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADNAL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 492174676  265 RNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVI 314
Cdd:TIGR00462 240 RKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVL 289
PRK09350 PRK09350
elongation factor P--(R)-beta-lysine ligase;
11-313 4.90e-154

elongation factor P--(R)-beta-lysine ligase;


Pssm-ID: 236474 [Multi-domain]  Cd Length: 306  Bit Score: 433.59  E-value: 4.90e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  11 SIENQRLRAQLLRDIRQFFAERKVMEVETPILSQHTVTDIHIDSFQTTYLN--GKEKQHYYLQTSPEYAMKRLLSAGSGP 88
Cdd:PRK09350   1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGpgASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  89 IYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQSKKASRITYEELFLKHLGINPHQISLHQLQS 168
Cdd:PRK09350  81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 169 LANQFSLENST-EYNDRNTLLQFLFSECLEPKIGFDAPLFVYHFPATQAALSKINPQDPNVALRFEVYIQGMECANGFEE 247
Cdd:PRK09350 161 VAAKLGLSNIAdEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492174676 248 LTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDV 313
Cdd:PRK09350 241 LTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 16-317 8.60e-60

Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238398 [Multi-domain]  Cd Length: 329  Bit Score: 194.34  E-value: 8.60e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPILSQ-------------HTVTDIHIdsfqttylngkekqhyYLQTSPEYAMKRLL 82
Cdd:cd00775    9 IVRSKIISYIRKFLDDRGFLEVETPMLQPiaggaaarpfithHNALDMDL----------------YLRIAPELYLKRLI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  83 SAGSGPIYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQ-----------------SKKASRIT 145
Cdd:cd00775   73 VGGFERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVT 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 146 YEELFLKHLGINPHQISLHQLQSLANQFSLENSTEYNDRNT---LLQFLFSECLEPKigFDAPLFVYHFPATQAALSKIN 222
Cdd:cd00775  153 MVDALKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEKPRTlgkLLDKLFEEFVEPT--LIQPTFIIDHPVEISPLAKRH 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 223 PQDPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIM 302
Cdd:cd00775  231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310

                        330
                 ....*....|....*
gi 492174676 303 IKAERKCIDDVINFP 317
Cdd:cd00775  311 LLTDSNSIRDVILFP 325
LysU COG1190
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
 16-317 4.47e-59

Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440803 [Multi-domain]  Cd Length: 495  Bit Score: 196.79  E-value: 4.47e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPILsqHT----------VTdiHIDSFqttylngkeKQHYYLQTSPEYAMKRLLSAG 85
Cdd:COG1190  175 RKRSKIIRAIRRFLDERGFLEVETPML--QPiaggaaarpfIT--HHNAL---------DMDLYLRIAPELYLKRLIVGG 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  86 SGPIYQICKAFRN-GESgSQHNPEFSMLEWYRP--DFscHDLMDEMDELLQFILQ-----------------SKKASRIT 145
Cdd:COG1190  242 FERVFEIGRNFRNeGID-TTHNPEFTMLELYQAyaDY--NDMMDLTEELIREAAEavlgttkvtyqgqeidlSPPWRRIT 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 146 YEELFLKHLGINPHQI-SLHQLQSLANQFSLENSTEYNdRNTLLQFLFSECLEPKIgfDAPLFVYHFPATQAALSKINPQ 224
Cdd:COG1190  319 MVEAIKEATGIDVTPLtDDEELRALAKELGIEVDPGWG-RGKLIDELFEELVEPKL--IQPTFVTDYPVEVSPLAKRHRD 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 225 DPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIK 304
Cdd:COG1190  396 DPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLL 475

                        330
                 ....*....|...
gi 492174676 305 AERKCIDDVINFP 317
Cdd:COG1190  476 TDSPSIRDVILFP 488
lysS_bact TIGR00499
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ...
 18-317 1.27e-58

lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the lysyl-tRNA synthetases that are class II amino-acyl tRNA synthetases. It includes all eukaryotic and most bacterial examples of the enzyme, but not archaeal or spirochete forms. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273107 [Multi-domain]  Cd Length: 493  Bit Score: 195.66  E-value: 1.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   18 RAQLLRDIRQFFAERKVMEVETPILsQHTVTDIHIDSFQTTYlnGKEKQHYYLQTSPEYAMKRLLSAGSGPIYQICKAFR 97
Cdd:TIGR00499 175 RSKIIKAIRRFLDDRGFIEVETPML-QSIPGGANAKPFITHH--NALDMDLYLRIAPELYLKRLIVGGLEKVYEIGRVFR 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   98 NGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQ-----------------SKKASRITYEELFLKHLGINPHQ 160
Cdd:TIGR00499 252 NEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKellgtfiinyndleidlKPPWKRITMVDALEMVTGIDFDI 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  161 I-SLHQLQSLANQFSLENSTEYNDRNTLLQFLFSECLEPKIgfDAPLFVYHFPATQAALSKINPQDPNVALRFEVYIQGM 239
Cdd:TIGR00499 332 LkDDETAKALAKEHGIEVAEDSLTLGHILNKFFEQFLEHTL--IQPTFITHYPAEISPLAKRDPSNPEFTERFELFIAGK 409

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492174676  240 ECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVINFP 317
Cdd:TIGR00499 410 EIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIRDVLLFP 487
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 16-317 3.13e-57

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 192.23  E-value: 3.13e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPILsqHT----------VTdiHIDSFqttylngkeKQHYYLQTSPEYAMKRLLSAG 85
Cdd:PRK00484 173 RKRSKIISAIRRFLDNRGFLEVETPML--QPiaggaaarpfIT--HHNAL---------DIDLYLRIAPELYLKRLIVGG 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  86 SGPIYQICKAFRN-GESgSQHNPEFSMLEWYRP--DFscHDLMDEMDELLQFILQ-----------------SKKASRIT 145
Cdd:PRK00484 240 FERVYEIGRNFRNeGID-TRHNPEFTMLEFYQAyaDY--NDMMDLTEELIRHLAQavlgttkvtyqgteidfGPPFKRLT 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 146 YEELFLKHLGINPHQISLHQLQSLANQFSLENSTEYNdRNTLLQFLFSECLEPKIgfDAPLFVYHFPATQAALSKINPQD 225
Cdd:PRK00484 317 MVDAIKEYTGVDFDDMTDEEARALAKELGIEVEKSWG-LGKLINELFEEFVEPKL--IQPTFITDYPVEISPLAKRHRED 393

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 226 PNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIMIKA 305
Cdd:PRK00484 394 PGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLT 473

                        330
                 ....*....|..
gi 492174676 306 ERKCIDDVINFP 317
Cdd:PRK00484 474 DSPSIRDVILFP 485
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
13-317 3.37e-48

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 163.89  E-value: 3.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   13 ENQRLRAQLLRDIRQFFAERKVMEVETPILSQHT---------VTDIHIDSFqttylngkekqhYYLQTSPEYAMKRLLS 83
Cdd:pfam00152  20 ANLKLRSKIIKAIRNFLDENGFLEVETPILTKSAtpegardflVPSRALGKF------------YALPQSPQLYKQLLMV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   84 AGSGPIYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQSKKASRITYEELFLKHLGINPHQISL 163
Cdd:pfam00152  88 AGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLKKPFPRITY 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  164 HQLQSLANQFSLENSTEYNDRNTlLQFLFSECLEPkiGFDAPLFVYHFPATQAALSK-INPQDPNVALRFEVYIQGMECA 242
Cdd:pfam00152 168 AEAIEKLNGKDVEELGYGSDKPD-LRFLLELVIDK--NKFNPLWVTDFPAEHHPFTMpKDEDDPALAEAFDLVLNGVEIG 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492174676  243 NGFEELTNADEQRQRFLNDNTKRNQQNRPsiniDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVINFP 317
Cdd:pfam00152 245 GGSIRIHDPELQEERFEEQGLDPEEAEEK----FGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFP 315
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
 16-321 1.50e-40

Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.


Pssm-ID: 238358 [Multi-domain]  Cd Length: 269  Bit Score: 142.62  E-value: 1.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPILsQHTVTDIHIDSFQTTYlNGKEKQhYYLQTSPEYAMKRLLSAGSGPIYQICKA 95
Cdd:cd00669    2 KVRSKIIKAIRDFMDDRGFLEVETPML-QKITGGAGARPFLVKY-NALGLD-YYLRISPQLFKKRLMVGGLDRVFEINRN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  96 FRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQfilqskkasrityeELFLKHLGINPHQISLHQLQslanqFSL 175
Cdd:cd00669   79 FRNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVR--------------HLAREVLGVTAVTYGFELED-----FGL 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 176 EnsteyndrntLLQFLFSECLEpKIGfdAPLFVYHFPA-TQAALSKINPQDPNVALRFEVYIQGMECANGFEELTNADEQ 254
Cdd:cd00669  140 P----------FPRLTYREALE-RYG--QPLFLTDYPAeMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLHDPDIQ 206

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492174676 255 RQRFLNDNTKRNQQnrpsINIDERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVINFPWERA 321
Cdd:cd00669  207 AEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
PLN02502 PLN02502
lysyl-tRNA synthetase
 16-317 3.40e-39

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 145.13  E-value: 3.40e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPILsqhtvtdihidsfQT-----------TYLNGKEKQhYYLQTSPEYAMKRLLSA 84
Cdd:PLN02502 230 RTRAKIISYIRRFLDDRGFLEVETPML-------------NMiaggaaarpfvTHHNDLNMD-LYLRIATELHLKRLVVG 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  85 GSGPIYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQSKKAS-----------------RITYE 147
Cdd:PLN02502 296 GFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSykikyhgieidftppfrRISMI 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 148 ELFLKHLGINphqISLHQLQSLANQFSLENSTEYNDR----NT---LLQFLFSECLEPKIgfDAPLFVYHFPATQAALSK 220
Cdd:PLN02502 376 SLVEEATGID---FPADLKSDEANAYLIAACEKFDVKcpppQTtgrLLNELFEEFLEETL--VQPTFVLDHPVEMSPLAK 450

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 221 INPQDPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRL 300
Cdd:PLN02502 451 PHRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRL 530

                        330
                 ....*....|....*..
gi 492174676 301 IMIKAERKCIDDVINFP 317
Cdd:PLN02502 531 VMLLTDSASIRDVIAFP 547
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
 12-320 9.42e-37

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 139.40  E-value: 9.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  12 IENQRLRAQLLRDIRQFFAERKVMEVETPILsqHTV-TDIHIDSFQTTYlnGKEKQHYYLQTSPEYAMKRLLSAGSGPIY 90
Cdd:PTZ00385 230 IETIKKRHVMLQALRDYFNERNFVEVETPVL--HTVaSGANAKSFVTHH--NANAMDLFLRVAPELHLKQCIVGGMERIY 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  91 QICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELlqFILQSKKASRITYEELFLKHLGINPHQISL---HQLQ 167
Cdd:PTZ00385 306 EIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDI--FRQLAMRVNGTTVVQIYPENAHGNPVTVDLgkpFRRV 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 168 SLANQFSLENSTEY---NDRNT----------LLQ---------------------FLFSECLEPKIGFDAPLFVyhfpa 213
Cdd:PTZ00385 384 SVYDEIQRMSGVEFpppNELNTpkgiaymsvvMLRyniplppvrtaakmfeklidfFITDRVVEPTFVMDHPLFM----- 458

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 214 tqAALSKINPQDPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGV 293
Cdd:PTZ00385 459 --SPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGW 536

                        330       340
                 ....*....|....*....|....*..
gi 492174676 294 AVGLDRLIMIKAERKCIDDVINFPWER 320
Cdd:PTZ00385 537 GMGIDRALMLLTNSSNIRDGIIFPLLR 563
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 16-320 1.22e-36

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 137.50  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPIL-------------SQHTVTDIHIdsfqttylngkekqhyYLQTSPEYAMKRLL 82
Cdd:PRK12445 185 VVRSKILAAIRQFMVARGFMEVETPMMqvipggasarpfiTHHNALDLDM----------------YLRIAPELYLKRLV 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  83 SAGSGPIYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELLQFILQS-----------------KKASRIT 145
Cdd:PRK12445 249 VGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEvlgttkvtygehvfdfgKPFEKLT 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 146 YEELFLKHlgiNPhQISLHQLQSLANQFSLENSTEYNDRNT-----LLQFLFSECLEPKIgfDAPLFVYHFPATQAALSK 220
Cdd:PRK12445 329 MREAIKKY---RP-ETDMADLDNFDAAKALAESIGITVEKSwglgrIVTEIFDEVAEAHL--IQPTFITEYPAEVSPLAR 402

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 221 INPQDPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRL 300
Cdd:PRK12445 403 RNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRM 482

                        330       340
                 ....*....|....*....|
gi 492174676 301 IMIKAERKCIDDVINFPWER 320
Cdd:PRK12445 483 IMLFTNSHTIRDVILFPAMR 502
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
16-317 5.56e-34

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 132.01  E-value: 5.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   16 RLRAQLLRDIRQFFAERKVMEVETPILSQhtvtdIH----IDSFqTTYLNGKEkQHYYLQTSPEYAMKRLLSAGSGPIYQ 91
Cdd:PRK02983  771 RARSAVVRAVRETLVARGFLEVETPILQQ-----VHgganARPF-VTHINAYD-MDLYLRIAPELYLKRLCVGGVERVFE 843

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676   92 ICKAFRNGESGSQHNPEFSMLEWYRPdfscHDLMDEMDELLQFILQSkKASRITYEELFLKH------------------ 153
Cdd:PRK02983  844 LGRNFRNEGVDATHNPEFTLLEAYQA----HADYDTMRDLTRELIQN-AAQAAHGAPVVMRPdgdgvlepvdisgpwpvv 918

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  154 ---------LG--INPHqISLHQLQSLANQFSLENSTEYnDRNTLLQFLFSECLEPKIGFdaPLFVYHFPATQAALSKIN 222
Cdd:PRK02983  919 tvhdavseaLGeeIDPD-TPLAELRKLCDAAGIPYRTDW-DAGAVVLELYEHLVEDRTTF--PTFYTDFPTSVSPLTRPH 994

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  223 PQDPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVGLDRLIM 302
Cdd:PRK02983  995 RSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVM 1074

                         330
                  ....*....|....*
gi 492174676  303 IKAERKcIDDVINFP 317
Cdd:PRK02983 1075 LLTGRS-IRETLPFP 1088
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 18-320 3.81e-27

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 111.26  E-value: 3.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  18 RAQLLRDIRQFFAERKVMEVETPIL-------------SQHTVTDIHIdsfqttylngkekqhyYLQTSPEYAMKRLLSA 84
Cdd:PTZ00417 256 RTKIINYLRNFLNDRGFIEVETPTMnlvagganarpfiTHHNDLDLDL----------------YLRIATELPLKMLIVG 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  85 GSGPIYQICKAFRNGESGSQHNPEFSMLEWYRPDFSCHDLMDEMDELL-QFILQSKKASRITY-------EELFLKHLGI 156
Cdd:PTZ00417 320 GIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFsQLVMHLFGTYKILYnkdgpekDPIEIDFTPP 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 157 NPHQISLHQLQSLAN-----------------QFSLENSTEYNDRNT---LLQFLFSECLEPKIGfDAPLFVYHFPATQA 216
Cdd:PTZ00417 400 YPKVSIVEELEKLTNtkleqpfdspetinkmiNLIKENKIEMPNPPTaakLLDQLASHFIENKYP-NKPFFIIEHPQIMS 478

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 217 ALSKINPQDPNVALRFEVYIQGMECANGFEELTNADEQRQRFLNDNTKRNQQNRPSINIDERFLAALIHGLPPCAGVAVG 296
Cdd:PTZ00417 479 PLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLG 558

                        330       340
                 ....*....|....*....|....
gi 492174676 297 LDRLIMIKAERKCIDDVINFPWER 320
Cdd:PTZ00417 559 IDRITMFLTNKNCIKDVILFPTMR 582
AspRS_core cd00777
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ...
 16-317 8.60e-16

Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.


Pssm-ID: 238400 [Multi-domain]  Cd Length: 280  Bit Score: 76.07  E-value: 8.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPILSQHT--------V-TDIHIDSFqttylngkekqhYYLQTSPEYAMKRLLSAGS 86
Cdd:cd00777    2 RLRSRVIKAIRNFLDEQGFVEIETPILTKSTpegardflVpSRLHPGKF------------YALPQSPQLFKQLLMVSGF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  87 GPIYQICKAFRNGESGSQHNPEFSMLewyrpDF-----SCHDLMDEMDELLQFILQ-------SKKASRITYEELFLKHl 154
Cdd:cd00777   70 DRYFQIARCFRDEDLRADRQPEFTQI-----DIemsfvDQEDIMSLIEGLLKYVFKevlgvelTTPFPRMTYAEAMERY- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 155 GINPHQIslhqlqslaNQFSLensTEYNDRNTLLQflfseclepkigfdaplFVYH-FPATQAALSKINPQDPN--VALR 231
Cdd:cd00777  144 GFKFLWI---------VDFPL---FEWDEEEGRLV-----------------SAHHpFTAPKEEDLDLLEKDPEdaRAQA 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 232 FEVYIQGMECANGFEELTNADEQRQRFlndntkrNQQNRPSINIDERF---LAALIHGLPPCAGVAVGLDRLIMIKAERK 308
Cdd:cd00777  195 YDLVLNGVELGGGSIRIHDPDIQEKVF-------EILGLSEEEAEEKFgflLEAFKYGAPPHGGIALGLDRLVMLLTGSE 267


                 ....*....
gi 492174676 309 CIDDVINFP 317
Cdd:cd00777  268 SIRDVIAFP 276
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 16-317 3.13e-13

Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238399 [Multi-domain]  Cd Length: 322  Bit Score: 69.13  E-value: 3.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPILSQhTVTDIHIDSFQTTYLngkeKQHYYLQTSPE-YamKRLLSAGSGPIYQICK 94
Cdd:cd00776   25 RIRSEVLRAFREFLRENGFTEVHTPKITS-TDTEGGAELFKVSYF----GKPAYLAQSPQlY--KEMLIAALERVYEIGP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  95 AFRNGESGS-QHNPEFSMLEW---YRPDFscHDLMDEMDELLQFILQSKKASRITYEELF------LKHLGINPHQISLH 164
Cdd:cd00776   98 VFRAEKSNTrRHLSEFWMLEAemaFIEDY--NEVMDLIEELIKYIFKRVLERCAKELELVnqlnreLLKPLEPFPRITYD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 165 QLQSLANQFSLENSTEYNDRntllqflFSECLEPKIG---FDAPLFVYHFPATQAAL-SKINPQDPNVALRFEVYIQG-M 239
Cdd:cd00776  176 EAIELLREKGVEEEVKWGED-------LSTEHERLLGeivKGDPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGvG 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492174676 240 ECANGFEELTNADEQRQRFlndntKRNQQNRPSInidERFLAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVINFP 317
Cdd:cd00776  249 EIVGGSQRIHDYDELEERI-----KEHGLDPESF---EWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 17-116 2.89e-07

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


Pssm-ID: 238391 [Multi-domain]  Cd Length: 211  Bit Score: 50.19  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  17 LRAQLLRDIRQFFAERKVMEVETPILSQHTV--TDIHIDSFQTTYLNGKEKQhYYLQTSPEYAMKRLLSAG--SGP--IY 90
Cdd:cd00768    1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLleKAGHEPKDLLPVGAENEED-LYLRPTLEPGLVRLFVSHirKLPlrLA 79

                         90       100
                 ....*....|....*....|....*...
gi 492174676  91 QICKAFRNGESGSQ--HNPEFSMLEWYR 116
Cdd:cd00768   80 EIGPAFRNEGGRRGlrRVREFTQLEGEV 107
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 16-317 1.22e-06

Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439788 [Multi-domain]  Cd Length: 430  Bit Score: 49.66  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  16 RLRAQLLRDIRQFFAERKVMEVETPILsqhTVTD-------IHIDSFqttylnGKEKqhyYLQTSPE-YamKRLLSAGSG 87
Cdd:COG0017  131 RIRSELARAIREFFQERGFVEVHTPII---TASAtegggelFPVDYF------GKEA---YLTQSGQlY--KEALAMALE 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  88 PIYQICKAFRNGESG-SQHNPEFSMLEwyrPDFSCHDLMDEMD---ELLQFILQS--KKAS------------------- 142
Cdd:COG0017  197 KVYTFGPTFRAEKSNtRRHLAEFWMIE---PEMAFADLEDVMDlaeEMLKYIIKYvlENCPeeleflgrdverlekvpes 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 143 ---RITYEEL--FLKHLGINPHQ---ISLHQLQSLANQFslensteyndrntllqflfseclepkigFDAPLFVYHFPAT 214
Cdd:COG0017  274 pfpRITYTEAieILKKSGEKVEWgddLGTEHERYLGEEF----------------------------FKKPVFVTDYPKE 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676 215 QAAL-SKINPQDPNVALRFEVYIQGM-ECANGFEELTNADEQRQRFlndntkrNQQNrpsINID--ERFLAALIHGLPPC 290
Cdd:COG0017  326 IKAFyMKPNPDDPKTVAAFDLLAPGIgEIIGGSQREHRYDVLVERI-------KEKG---LDPEdyEWYLDLRRYGSVPH 395

                        330       340
                 ....*....|....*....|....*..
gi 492174676 291 AGVAVGLDRLIMIKAERKCIDDVINFP 317
Cdd:COG0017  396 AGFGLGLERLVMWLTGLENIREVIPFP 422
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 275-317 2.08e-06

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 48.91  E-value: 2.08e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 492174676 275 IDERF---LAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVINFP 317
Cdd:PRK00476 511 AEEKFgflLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 275-317 5.61e-06

Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 47.69  E-value: 5.61e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 492174676 275 IDERF---LAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVINFP 317
Cdd:COG0173  510 AEEKFgflLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
PLN02903 PLN02903
aminoacyl-tRNA ligase
 280-317 7.53e-06

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 47.48  E-value: 7.53e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 492174676 280 LAALIHGLPPCAGVAVGLDRLIMIKAERKCIDDVINFP 317
Cdd:PLN02903 582 LEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFP 619
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 13-113 1.86e-05

bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 46.13  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  13 ENQRLRAQLLRDIRQFFAERKVMEVETPILSQHTVTDIHiDSFQTTYLNGKEkqHYYLQTSPEYAMKRLLSAGSGPIYQI 92
Cdd:PRK12820 154 DHLAKRHRIIKCARDFLDSRGFLEIETPILTKSTPEGAR-DYLVPSRIHPKE--FYALPQSPQLFKQLLMIAGFERYFQL 230

                         90       100
                 ....*....|....*....|.
gi 492174676  93 CKAFRNGESGSQHNPEFSMLE 113
Cdd:PRK12820 231 ARCFRDEDLRPNRQPEFTQLD 251
pylS PRK09537
pyrrolysine--tRNA(Pyl) ligase;
19-157 5.42e-05

pyrrolysine--tRNA(Pyl) ligase;


Pssm-ID: 236555 [Multi-domain]  Cd Length: 417  Bit Score: 44.45  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  19 AQLLRDIRQFFAERKVMEVETPIL-SQHTVTDIHIDSfqTTYLNgkeKQHYYLQTS----PEYA------MKRLLSAGSG 87
Cdd:PRK09537 207 GKLERDITKFFVDRGFLEIKSPILiPAEYIERMGIDN--DTELS---KQIFRVDKNfclrPMLApglynyLRKLDRILPD 281

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492174676  88 P--IYQICKAFRNGESGSQHNPEFSMLEWYRPDFSC--HDLMDEMDEllqfilqskkasrityeelFLKHLGIN 157
Cdd:PRK09537 282 PikIFEIGPCYRKESDGKEHLEEFTMVNFCQMGSGCtrENLENIIDD-------------------FLKHLGID 336
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 20-132 2.36e-04

Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer.


Pssm-ID: 238277 [Multi-domain]  Cd Length: 218  Bit Score: 41.76  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492174676  20 QLLRDIRQFFA-----ERKVMEVETP--------ILSQHTVTDIHiDSFqttYLNGKEKQHYYLQTSPEYAmkRLLSAGS 86
Cdd:cd00496    5 KVIEEIEDIFVsmgftEVEGPEVETDfynfdalnIPQDHPARDMQ-DTF---YINDPARLLLRTHTSAVQA--RALAKLK 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 492174676  87 GPIYQIC--KAFRNGESGSQHNPEFSMLE--WYRPDFSCHDLMDEMDELL 132
Cdd:cd00496   79 PPIRIFSigRVYRNDEIDATHLPEFHQIEglVVDKGLTFADLKGTLEEFA 128
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 13-42 1.11e-03

Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 40.37  E-value: 1.11e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 492174676  13 ENQRLRAQLLRDIRQFFAERKVMEVETPIL 42
Cdd:COG0173  140 KNLILRHKVTKAIRNYLDENGFLEIETPIL 169
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 13-43 4.50e-03

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 38.51  E-value: 4.50e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 492174676  13 ENQRLRAQLLRDIRQFFAERKVMEVETPILS 43
Cdd:PRK00476 139 KNLKLRSKVTSAIRNFLDDNGFLEIETPILT 169
 
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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