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Conserved domains on  [gi|1738963691|emb|VAT82027|]
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translation elongation factor P Lys34:lysine transferase [Klebsiella pneumoniae]

Protein Classification

EF-P lysine aminoacylase GenX( domain architecture ID 11483997)

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
PRK09350 PRK09350
elongation factor P--(R)-beta-lysine ligase;
12-317 0e+00

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


:

Pssm-ID: 236474 [Multi-domain]  Cd Length: 306  Bit Score: 648.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  12 PIPNLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGLNLYLMTSPEYHMKRLLAAGCGP 91
Cdd:PRK09350    1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  92 VFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLECQPAESLSYQQAFQRHLEIDPLSADKAQLRE 171
Cdd:PRK09350   81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 172 VAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350  161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1738963691 252 LTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEV 317
Cdd:PRK09350  241 LTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
 
Name Accession Description Interval E-value
PRK09350 PRK09350
elongation factor P--(R)-beta-lysine ligase;
12-317 0e+00

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


Pssm-ID: 236474 [Multi-domain]  Cd Length: 306  Bit Score: 648.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  12 PIPNLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGLNLYLMTSPEYHMKRLLAAGCGP 91
Cdd:PRK09350    1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  92 VFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLECQPAESLSYQQAFQRHLEIDPLSADKAQLRE 171
Cdd:PRK09350   81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 172 VAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350  161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1738963691 252 LTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEV 317
Cdd:PRK09350  241 LTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
EpmA COG2269
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ...
 11-319 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: 557.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  11 APIPNLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGhSQGLNLYLMTSPEYHMKRLLAAGCG 90
Cdd:COG2269     1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPD-GGGRPLYLHTSPEFAMKRLLAAGSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  91 PVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEC---QPAESLSYQQAFQRHLEIDPLSADKA 167
Cdd:COG2269    80 PIYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAagfAPAERLSYQEAFLRYLGIDPLTADLD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 168 QLREVAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPEDHRVAERFEVYYKGIELAN 247
Cdd:COG2269   160 ELAAAAAAAGLR--VADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELAN 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738963691 248 GFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIA 319
Cdd:COG2269   238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 29-319 5.23e-180

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: 498.61  E-value: 5.23e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  29 FFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGhSQGLNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHH 108
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPD-GQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 109 NPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE--CQPAESLSYQQAFQRHLEIDPLSADKAQLREVAAKLDLsnIADTEE 186
Cdd:TIGR00462  80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGI--RASEED 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 187 DRDTLLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPEDHRVAERFEVYYKGIELANGFHELTDAHEQRLRFEQDN 266
Cdd:TIGR00462 158 DRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1738963691 267 RKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIA 319
Cdd:TIGR00462 238 ALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVLA 290
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 16-320 2.52e-67

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: 213.99  E-value: 2.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  16 LLKRAAVMAEIRRFFTDRGVLEVETPCMSQ----ATVTdihlfPFETrfvgpgHSQGL--NLYLMTSPEYHMKRLLAAGC 89
Cdd:cd00775     8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPiaggAAAR-----PFIT------HHNALdmDLYLRIAPELYLKRLIVGGF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  90 GPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE-----------------CQPAESLSYQQA 152
Cdd:cd00775    77 ERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVTMVDA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 153 FQRHLEIDPLSADKAQLREVAAKLDLSnIADTEEDRDTLLQLL---FTMGVEPHIGKdrPTFIYHFPATQASLAQISPED 229
Cdd:cd00775   157 LKEKTGIDFPELDLEQPEELAKLLAKL-IKEKIEKPRTLGKLLdklFEEFVEPTLIQ--PTFIIDHPVEISPLAKRHRSN 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 230 HRVAERFEVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLAL 309
Cdd:cd00775   234 PGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLT 313

                         330
                  ....*....|.
gi 1738963691 310 GAESIGEVIAF 320
Cdd:cd00775   314 DSNSIRDVILF 324
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
15-320 1.29e-51

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 173.14  E-value: 1.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  15 NLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATVtdihlfPFETR-FVGPGHSQGLNLYLMTSPEYHMKRLLAAGCGPVF 93
Cdd:pfam00152  21 NLKLRSKIIKAIRNFLDENGFLEVETPILTKSAT------PEGARdFLVPSRALGKFYALPQSPQLYKQLLMVAGFDRVF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  94 QLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEcqpaESLSYQQAFQRHLEID-PLSADKAQLREV 172
Cdd:pfam00152  95 QIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFK----EVEGIAKELEGGTLLDlKKPFPRITYAEA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 173 AAKLDLSNIADTEEDRDTlLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPED-HRVAERFEVYYKGIELANGFHE 251
Cdd:pfam00152 171 IEKLNGKDVEELGYGSDK-PDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDdPALAEAFDLVLNGVEIGGGSIR 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1738963691 252 LTDAHEQRLRFEQDNRKRAArglpQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIAF 320
Cdd:pfam00152 250 IHDPELQEERFEEQGLDPEE----AEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAF 314
 
Name Accession Description Interval E-value
PRK09350 PRK09350
elongation factor P--(R)-beta-lysine ligase;
12-317 0e+00

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


Pssm-ID: 236474 [Multi-domain]  Cd Length: 306  Bit Score: 648.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  12 PIPNLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGLNLYLMTSPEYHMKRLLAAGCGP 91
Cdd:PRK09350    1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  92 VFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLECQPAESLSYQQAFQRHLEIDPLSADKAQLRE 171
Cdd:PRK09350   81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 172 VAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350  161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1738963691 252 LTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEV 317
Cdd:PRK09350  241 LTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
EpmA COG2269
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ...
 11-319 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: 557.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  11 APIPNLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGhSQGLNLYLMTSPEYHMKRLLAAGCG 90
Cdd:COG2269     1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPD-GGGRPLYLHTSPEFAMKRLLAAGSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  91 PVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEC---QPAESLSYQQAFQRHLEIDPLSADKA 167
Cdd:COG2269    80 PIYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAagfAPAERLSYQEAFLRYLGIDPLTADLD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 168 QLREVAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPEDHRVAERFEVYYKGIELAN 247
Cdd:COG2269   160 ELAAAAAAAGLR--VADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELAN 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738963691 248 GFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIA 319
Cdd:COG2269   238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 29-319 5.23e-180

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: 498.61  E-value: 5.23e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  29 FFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGhSQGLNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHH 108
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPD-GQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 109 NPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE--CQPAESLSYQQAFQRHLEIDPLSADKAQLREVAAKLDLsnIADTEE 186
Cdd:TIGR00462  80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGI--RASEED 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 187 DRDTLLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPEDHRVAERFEVYYKGIELANGFHELTDAHEQRLRFEQDN 266
Cdd:TIGR00462 158 DRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1738963691 267 RKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIA 319
Cdd:TIGR00462 238 ALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVLA 290
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 16-320 2.52e-67

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: 213.99  E-value: 2.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  16 LLKRAAVMAEIRRFFTDRGVLEVETPCMSQ----ATVTdihlfPFETrfvgpgHSQGL--NLYLMTSPEYHMKRLLAAGC 89
Cdd:cd00775     8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPiaggAAAR-----PFIT------HHNALdmDLYLRIAPELYLKRLIVGGF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  90 GPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE-----------------CQPAESLSYQQA 152
Cdd:cd00775    77 ERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVTMVDA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 153 FQRHLEIDPLSADKAQLREVAAKLDLSnIADTEEDRDTLLQLL---FTMGVEPHIGKdrPTFIYHFPATQASLAQISPED 229
Cdd:cd00775   157 LKEKTGIDFPELDLEQPEELAKLLAKL-IKEKIEKPRTLGKLLdklFEEFVEPTLIQ--PTFIIDHPVEISPLAKRHRSN 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 230 HRVAERFEVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLAL 309
Cdd:cd00775   234 PGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLT 313

                         330
                  ....*....|.
gi 1738963691 310 GAESIGEVIAF 320
Cdd:cd00775   314 DSNSIRDVILF 324
LysU COG1190
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
 16-320 1.57e-65

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: 214.13  E-value: 1.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  16 LLKRAAVMAEIRRFFTDRGVLEVETPcMSQ-----ATVTdihlfPFETrfvgpgHSQGLN--LYLMTSPEYHMKRLLAAG 88
Cdd:COG1190   174 FRKRSKIIRAIRRFLDERGFLEVETP-MLQpiaggAAAR-----PFIT------HHNALDmdLYLRIAPELYLKRLIVGG 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  89 CGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQV---------LECQ--------PAESLSYQQ 151
Cdd:COG1190   242 FERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAaeavlgttkVTYQgqeidlspPWRRITMVE 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 152 AFQRHLEIDPLS-ADKAQLREVAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIgkDRPTFIYHFPATQASLAQISPEDH 230
Cdd:COG1190   322 AIKEATGIDVTPlTDDEELRALAKELGIE--VDPGWGRGKLIDELFEELVEPKL--IQPTFVTDYPVEVSPLAKRHRDDP 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 231 RVAERFEVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALG 310
Cdd:COG1190   398 GLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTD 477

                         330
                  ....*....|
gi 1738963691 311 AESIGEVIAF 320
Cdd:COG1190   478 SPSIRDVILF 487
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 17-320 2.57e-64

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 210.72  E-value: 2.57e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  17 LKRAAVMAEIRRFFTDRGVLEVETPcMSQ-----ATVTdihlfPFETrfvgpgHSQGLN--LYLMTSPEYHMKRLLAAGC 89
Cdd:PRK00484  173 RKRSKIISAIRRFLDNRGFLEVETP-MLQpiaggAAAR-----PFIT------HHNALDidLYLRIAPELYLKRLIVGGF 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  90 GPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE-----------------CQPAESLSYQQA 152
Cdd:PRK00484  241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQavlgttkvtyqgteidfGPPFKRLTMVDA 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 153 FQRHLEIDPLSADKAQLREVAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIgkDRPTFIYHFPATQASLAQISPEDHRV 232
Cdd:PRK00484  321 IKEYTGVDFDDMTDEEARALAKELGIE--VEKSWGLGKLINELFEEFVEPKL--IQPTFITDYPVEISPLAKRHREDPGL 396

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 233 AERFEVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAE 312
Cdd:PRK00484  397 TERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSP 476


                  ....*...
gi 1738963691 313 SIGEVIAF 320
Cdd:PRK00484  477 SIRDVILF 484
lysS_bact TIGR00499
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ...
 16-320 1.10e-60

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: 201.44  E-value: 1.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  16 LLKRAAVMAEIRRFFTDRGVLEVETPCMsQATVTDIHLFPFETrfvgpgHSQGL--NLYLMTSPEYHMKRLLAAGCGPVF 93
Cdd:TIGR00499 172 FLKRSKIIKAIRRFLDDRGFIEVETPML-QSIPGGANAKPFIT------HHNALdmDLYLRIAPELYLKRLIVGGLEKVY 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  94 QLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEC-----------------QPAESLSYQQAFQRH 156
Cdd:TIGR00499 245 EIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKEllgtfiinyndleidlkPPWKRITMVDALEMV 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 157 LEIDPLSADKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKdrPTFIYHFPATQASLAQISPEDHRVAERF 236
Cdd:TIGR00499 325 TGIDFDILKDDETAKALAKEHGIEVAEDSLTLGHILNKFFEQFLEHTLIQ--PTFITHYPAEISPLAKRDPSNPEFTERF 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 237 EVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGE 316
Cdd:TIGR00499 403 ELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIRD 482


                  ....
gi 1738963691 317 VIAF 320
Cdd:TIGR00499 483 VLLF 486
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
15-320 1.29e-51

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 173.14  E-value: 1.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  15 NLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATVtdihlfPFETR-FVGPGHSQGLNLYLMTSPEYHMKRLLAAGCGPVF 93
Cdd:pfam00152  21 NLKLRSKIIKAIRNFLDENGFLEVETPILTKSAT------PEGARdFLVPSRALGKFYALPQSPQLYKQLLMVAGFDRVF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  94 QLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEcqpaESLSYQQAFQRHLEID-PLSADKAQLREV 172
Cdd:pfam00152  95 QIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFK----EVEGIAKELEGGTLLDlKKPFPRITYAEA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 173 AAKLDLSNIADTEEDRDTlLQLLFTMGVEPHIGKDRPTFIYHFPATQASLAQISPED-HRVAERFEVYYKGIELANGFHE 251
Cdd:pfam00152 171 IEKLNGKDVEELGYGSDK-PDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDEDdPALAEAFDLVLNGVEIGGGSIR 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1738963691 252 LTDAHEQRLRFEQDNRKRAArglpQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIAF 320
Cdd:pfam00152 250 IHDPELQEERFEEQGLDPEE----AEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAF 314
PLN02502 PLN02502
lysyl-tRNA synthetase
 18-320 4.37e-50

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 174.79  E-value: 4.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  18 KRAAVMAEIRRFFTDRGVLEVETPCM-SQATVTDIHlfPFETRfvgpgH-SQGLNLYLMTSPEYHMKRLLAAGCGPVFQL 95
Cdd:PLN02502  231 TRAKIISYIRRFLDDRGFLEVETPMLnMIAGGAAAR--PFVTH-----HnDLNMDLYLRIATELHLKRLVVGGFERVYEI 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  96 CRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQ-VLECQPAESLSYQQafqrhLEID---PLS-ADKAQLR 170
Cdd:PLN02502  304 GRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGmVKELTGSYKIKYHG-----IEIDftpPFRrISMISLV 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 171 EVAAKLDLSNIADTEEDRDT--------------------LLQLLFTMGVEPHIGKdrPTFIYHFPATQASLAQispeDH 230
Cdd:PLN02502  379 EEATGIDFPADLKSDEANAYliaacekfdvkcpppqttgrLLNELFEEFLEETLVQ--PTFVLDHPVEMSPLAK----PH 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 231 R----VAERFEVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVM 306
Cdd:PLN02502  453 RskpgLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVM 532

                         330
                  ....*....|....
gi 1738963691 307 LALGAESIGEVIAF 320
Cdd:PLN02502  533 LLTDSASIRDVIAF 546
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
15-320 3.46e-45

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 164.75  E-value: 3.46e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691   15 NLLKRAAVMAEIRRFFTDRGVLEVETPCMSQatvtdIH----LFPFETRFvgpgHSQGLNLYLMTSPEYHMKRLLAAGCG 90
Cdd:PRK02983   769 LLRARSAVVRAVRETLVARGFLEVETPILQQ-----VHgganARPFVTHI----NAYDMDLYLRIAPELYLKRLCVGGVE 839

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691   91 PVFQLCRSFRNEEMGRHHNPEFTMLEWYRPC--YDMYR-----LINEV---------------DDLLQQVLECQPAESLS 148
Cdd:PRK02983   840 RVFELGRNFRNEGVDATHNPEFTLLEAYQAHadYDTMRdltreLIQNAaqaahgapvvmrpdgDGVLEPVDISGPWPVVT 919

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  149 YQQAFQRHL--EIDPlSADKAQLREVAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIgkDRPTFIYHFPATQASLAQIS 226
Cdd:PRK02983   920 VHDAVSEALgeEIDP-DTPLAELRKLCDAAGIP--YRTDWDAGAVVLELYEHLVEDRT--TFPTFYTDFPTSVSPLTRPH 994

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  227 PEDHRVAERFEVYYKGIELANGFHELTDAHEQRLRFEQDNRKrAARGLPQ-QPIDNNLLAALEAGLPDCSGVALGVDRVV 305
Cdd:PRK02983   995 RSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLL-AAGGDPEaMELDEDFLQALEYAMPPTGGLGMGVDRLV 1073

                          330
                   ....*....|....*
gi 1738963691  306 MLALGAeSIGEVIAF 320
Cdd:PRK02983  1074 MLLTGR-SIRETLPF 1087
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
 19-325 1.79e-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: 1.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  19 RAAVMAEIRRFFTDRGVLEVETPcMSQATVTDIHLFPFETRFVGPGHsqglNLYLMTSPEYHMKRLLAAGCGPVFQLCRS 98
Cdd:cd00669     4 RSKIIKAIRDFMDDRGFLEVETP-MLQKITGGAGARPFLVKYNALGL----DYYLRISPQLFKKRLMVGGLDRVFEINRN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  99 FRNEEMGRHHNPEFTMLEWYRPCYDMYRLI--NE--VDDLLQQVLEcqpaeslSYQQAFQRHLEIDPLSADKAQLREVAA 174
Cdd:cd00669    79 FRNEDLRARHQPEFTMMDLEMAFADYEDVIelTErlVRHLAREVLG-------VTAVTYGFELEDFGLPFPRLTYREALE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 175 KLdlsniadteedrdtllqllftmgvephigkDRPTFIYHFPATQAS-LAQISPEDHRVAERFEVYYKGIELANGFHELT 253
Cdd:cd00669   152 RY------------------------------GQPLFLTDYPAEMHSpLASPHDVNPEIADAFDLFINGVEVGNGSSRLH 201

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738963691 254 DAHEQRLRFEQDNRKRAArglpQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIAFTVDRA 325
Cdd:cd00669   202 DPDIQAEVFQEQGINKEA----GMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 19-324 2.42e-40

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 147.52  E-value: 2.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  19 RAAVMAEIRRFFTDRGVLEVETPCMsQATVTDIHLFPFETRFvgpgHSQGLNLYLMTSPEYHMKRLLAAGCGPVFQLCRS 98
Cdd:PRK12445  187 RSKILAAIRQFMVARGFMEVETPMM-QVIPGGASARPFITHH----NALDLDMYLRIAPELYLKRLVVGGFERVFEINRN 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  99 FRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLL----QQVLEC-------------QPAESLSYQQAFQRH----- 156
Cdd:PRK12445  262 FRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFrtlaQEVLGTtkvtygehvfdfgKPFEKLTMREAIKKYrpetd 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 157 -LEIDPLSADKAQLREVAAKLDLSniadteEDRDTLLQLLFTMGVEPHIgkDRPTFIYHFPATQASLAQISPEDHRVAER 235
Cdd:PRK12445  342 mADLDNFDAAKALAESIGITVEKS------WGLGRIVTEIFDEVAEAHL--IQPTFITEYPAEVSPLARRNDVNPEITDR 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 236 FEVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVMLALGAESIG 315
Cdd:PRK12445  414 FEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIR 493


                  ....*....
gi 1738963691 316 EVIAFTVDR 324
Cdd:PRK12445  494 DVILFPAMR 502
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
 13-324 7.97e-36

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 136.70  E-value: 7.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  13 IPNLLKRAAVMAEIRRFFTDRGVLEVETPCMsQATVTDIHLFPFETRFvgpgHSQGLNLYLMTSPEYHMKRLLAAGCGPV 92
Cdd:PTZ00385  230 IETIKKRHVMLQALRDYFNERNFVEVETPVL-HTVASGANAKSFVTHH----NANAMDLFLRVAPELHLKQCIVGGMERI 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  93 FQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQ---------VLECQPAES---------------LS 148
Cdd:PTZ00385  305 YEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQlamrvngttVVQIYPENAhgnpvtvdlgkpfrrVS 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 149 YQQAFQRH--LEIDP---LSADK--AQLREVAAKLD--LSNIADTEEDRDTLLQLLFTMGVEphigkdRPTFIYHFPATQ 219
Cdd:PTZ00385  385 VYDEIQRMsgVEFPPpneLNTPKgiAYMSVVMLRYNipLPPVRTAAKMFEKLIDFFITDRVV------EPTFVMDHPLFM 458

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 220 ASLAQISPEDHRVAERFEVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVAL 299
Cdd:PTZ00385  459 SPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGM 538

                         330       340
                  ....*....|....*....|....*
gi 1738963691 300 GVDRVVMLALGAESIGEVIAFTVDR 324
Cdd:PTZ00385  539 GIDRALMLLTNSSNIRDGIIFPLLR 563
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 16-324 2.13e-30

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 120.89  E-value: 2.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  16 LLKRAAVMAEIRRFFTDRGVLEVETPCMSqATVTDIHLFPFETRFvgpgHSQGLNLYLMTSPEYHMKRLLAAGCGPVFQL 95
Cdd:PTZ00417  253 FITRTKIINYLRNFLNDRGFIEVETPTMN-LVAGGANARPFITHH----NDLDLDLYLRIATELPLKMLIVGGIDKVYEI 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  96 CRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQ-VLECQPAESLSYQQAFQrhlEIDPLSAD------KAQ 168
Cdd:PTZ00417  328 GKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQlVMHLFGTYKILYNKDGP---EKDPIEIDftppypKVS 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 169 LREVAAKLD---LSNIADTEEDRDTLLQLLFTMGVE----PHIGK---------------DRPTFIYHFPATQASLAQIS 226
Cdd:PTZ00417  405 IVEELEKLTntkLEQPFDSPETINKMINLIKENKIEmpnpPTAAKlldqlashfienkypNKPFFIIEHPQIMSPLAKYH 484

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 227 PEDHRVAERFEVYYKGIELANGFHELTDAHEQRLRFEQDNRKRAARGLPQQPIDNNLLAALEAGLPDCSGVALGVDRVVM 306
Cdd:PTZ00417  485 RSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITM 564

                         330
                  ....*....|....*...
gi 1738963691 307 LALGAESIGEVIAFTVDR 324
Cdd:PTZ00417  565 FLTNKNCIKDVILFPTMR 582
AspRS_core cd00777
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ...
 16-320 1.11e-15

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: 75.69  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  16 LLKRAAVMAEIRRFFTDRGVLEVETPCMSQATvtdihlfPFETR-FVGPGHSQGLNLY-LMTSPEYHMKRLLAAGCGPVF 93
Cdd:cd00777     1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKST-------PEGARdFLVPSRLHPGKFYaLPQSPQLFKQLLMVSGFDRYF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  94 QLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE-------CQPAESLSYQQAFQR-----HLEID- 160
Cdd:cd00777    74 QIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKevlgvelTTPFPRMTYAEAMERygfkfLWIVDf 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 161 PLSADkaqlrevaakldlsniaDTEEDRDTLLQLLFTMgvePHiGKDRPTFiyhfpatqaslaQISPEDHRvAERFEVYY 240
Cdd:cd00777   154 PLFEW-----------------DEEEGRLVSAHHPFTA---PK-EEDLDLL------------EKDPEDAR-AQAYDLVL 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 241 KGIELANGFHELTDAHEQRLRFEQdnrkraaRGLPQQPIDNN---LLAALEAGLPDCSGVALGVDRVVMLALGAESIGEV 317
Cdd:cd00777   200 NGVELGGGSIRIHDPDIQEKVFEI-------LGLSEEEAEEKfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDV 272


                  ...
gi 1738963691 318 IAF 320
Cdd:cd00777   273 IAF 275
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 15-325 1.23e-10

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


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 62.31  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  15 NLLKRAAVMAEIRRFFTDRGVLEVETPCMSQATvtdihlfPFETR-FVGPGHSQGLNLY-LMTSPEYHMKRLLAAGCGPV 92
Cdd:PRK12820  155 HLAKRHRIIKCARDFLDSRGFLEIETPILTKST-------PEGARdYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERY 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  93 FQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEC------QPAESLSY----------------- 149
Cdd:PRK12820  228 FQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFAIggialpRPFPRMPYaeamdttgsdrpdlrfd 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 150 ------------------QQAFQRHLEI---------DPLSADKAQ------------------LREVAAKLDlSNIAD- 183
Cdd:PRK12820  308 lkfadatdifentrygifKQILQRGGRIkginikgqsEKLSKNVLQneyakeiapsfgakgmtwMRAEAGGLD-SNIVQf 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 184 -TEEDRDTLLQL-------LFTMGVEP--------------HIGkDR----------PTFIYHFPATQASLAQISPEDHR 231
Cdd:PRK12820  387 fSADEKEALKRRfhaedgdVIIMIADAscaivlsalgqlrlHLA-DRlglipegvfhPLWITDFPLFEATDDGGVTSSHH 465

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 232 V---------------------AERFEVYYKGIELANGFHELTDAHEQRLRFeqdnrkrAARGLPQQPIDNN---LLAAL 287
Cdd:PRK12820  466 PftapdredfdpgdieelldlrSRAYDLVVNGEELGGGSIRINDKDIQLRIF-------AALGLSEEDIEDKfgfFLRAF 538

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1738963691 288 EAGLPDCSGVALGVDRVVMLALGAESIGEVIAFTVDRA 325
Cdd:PRK12820  539 DFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPKNRS 576
PLN02903 PLN02903
aminoacyl-tRNA ligase
 15-181 4.06e-09

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 57.49  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  15 NLLKRAAVMAEIRRFFTDR-GVLEVETPCMSQATVTDIHLFPFETRfVGPGhsqglNLY-LMTSPEYHMKRLLAAGCGPV 92
Cdd:PLN02903  202 NLRLRHRVVKLIRRYLEDVhGFVEIETPILSRSTPEGARDYLVPSR-VQPG-----TFYaLPQSPQLFKQMLMVSGFDRY 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  93 FQLCRSFRNEEMGRHHNPEFTMLEW---YRPCYDMYRLiNEvdDLLQQVLE-------CQPAESLSYQQAFQRHleidpl 162
Cdd:PLN02903  276 YQIARCFRDEDLRADRQPEFTQLDMelaFTPLEDMLKL-NE--DLIRQVFKeikgvqlPNPFPRLTYAEAMSKY------ 346

                         170
                  ....*....|....*....
gi 1738963691 163 SADKAQLREVAAKLDLSNI 181
Cdd:PLN02903  347 GSDKPDLRYGLELVDVSDV 365
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 19-209 7.35e-09

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: 55.20  E-value: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  19 RAAVMAEIRRFFTDRGVLEVETPCMSQATV--TDIHLFPfetRFVGPGHSQGLNLYLMTSPEYHMKRLLAAGCGP----V 92
Cdd:cd00768     2 RSKIEQKLRRFMAELGFQEVETPIVEREPLleKAGHEPK---DLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKlplrL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  93 FQLCRSFRNEEMGRH--HNPEFTMLEWYRPC------YDMYRLINEVDDLLQQ--------VLECQPAESLSYQQAFQRH 156
Cdd:cd00768    79 AEIGPAFRNEGGRRGlrRVREFTQLEGEVFGedgeeaSEFEELIELTEELLRAlgikldivFVEKTPGEFSPGGAGPGFE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1738963691 157 LEIDPLSADKAQLREVAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKDRP 209
Cdd:cd00768   159 IEVDHPEGRGLEIGSGGYRQDEQARAADLYFLDEALEYRYPPTIGFGLGLERL 211
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 283-320 3.11e-07

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 51.61  E-value: 3.11e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1738963691 283 LLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIAF 320
Cdd:PRK00476  518 LLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAF 555
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 283-320 3.80e-07

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: 51.54  E-value: 3.80e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1738963691 283 LLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIAF 320
Cdd:COG0173   517 LLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
PRK06462 PRK06462
asparagine synthetase A; Reviewed
 26-320 3.73e-05

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 45.01  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691  26 IRRFFTDRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGLNLYLMTSPEYHmKRLLAAGCGPVFQLCRSFRNEE-- 103
Cdd:PRK06462   40 TREFLDGRGFVEVLPPIISPSTDPLMGLGSDLPVKQISIDFYGVEYYLADSMILH-KQLALRMLGKIFYLSPNFRLEPvd 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 104 --MGRHHNpEFTMLEW---YRPCYDMYRLINE-VDDLLQQVLECQPAESLSYQQ---AFQRHLEIDPLS-ADKAQLREVA 173
Cdd:PRK06462  119 kdTGRHLY-EFTQLDIeieGADLDEVMDLIEDlIKYLVKELLEEHEDELEFFGRdlpHLKRPFKRITHKeAVEILNEEGC 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963691 174 AKLDLSNIADTEEdrdTLLQLLFtmgvephigkDRPTFIYHFPATQASLAQ-ISPEDHRVAERFEVYYkgielANGFHEL 252
Cdd:PRK06462  198 RGIDLEELGSEGE---KSLSEHF----------EEPFWIIDIPKGSREFYDrEDPERPGVLRNYDLLL-----PEGYGEA 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1738963691 253 TDAHEQRLRFEQDNRKRAARGLPQQPIDnNLLAALEAGLPDCSGVALGVDRVVMLALGAESIGEVIAF 320
Cdd:PRK06462  260 VSGGEREYEYEEIVERIREHGVDPEKYK-WYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPF 326
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 15-47 1.10e-04

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 43.90  E-value: 1.10e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1738963691  15 NLLKRAAVMAEIRRFFTDRGVLEVETPCMSQAT 47
Cdd:PRK00476  140 NLKLRSKVTSAIRNFLDDNGFLEIETPILTKST 172
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 15-41 2.05e-04

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: 43.06  E-value: 2.05e-04
                          10        20
                  ....*....|....*....|....*..
gi 1738963691  15 NLLKRAAVMAEIRRFFTDRGVLEVETP 41
Cdd:COG0173   141 NLILRHKVTKAIRNYLDENGFLEIETP 167
 
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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