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Conserved domains on  [gi|495162709|ref|WP_007887508|]
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MULTISPECIES: elongation factor P--(R)-beta-lysine ligase [Cronobacter]

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: 653.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  12 SIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGP 91
Cdd:PRK09350   1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  92 VYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLECQPAETISYQQAFQRHLEIDPLSADKTQLRE 171
Cdd:PRK09350  81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 172 VAAKLDLSNIADTEEDRDTLLQLLFSMGVEPHIGKDRPVFVYHFPASQAALAQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350 161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495162709 252 LTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEV 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: 653.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  12 SIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGP 91
Cdd:PRK09350   1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  92 VYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLECQPAETISYQQAFQRHLEIDPLSADKTQLRE 171
Cdd:PRK09350  81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 172 VAAKLDLSNIADTEEDRDTLLQLLFSMGVEPHIGKDRPVFVYHFPASQAALAQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350 161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495162709 252 LTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEV 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: 560.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  11 ASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGhSQGINLYLMTSPEYHMKRLLAAGCG 90
Cdd:COG2269    1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPD-GGGRPLYLHTSPEFAMKRLLAAGSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  91 PVYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLEC---QPAETISYQQAFQRHLEIDPLSADKT 167
Cdd:COG2269   80 PIYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAagfAPAERLSYQEAFLRYLGIDPLTADLD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 168 QLREVAAKLDLSniADTEEDRDTLLQLLFSMGVEPHIGKDRPVFVYHFPASQAALAQISTEDHRVAERFEVYYKGIELAN 247
Cdd:COG2269  160 ELAAAAAAAGLR--VADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELAN 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495162709 248 GFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIA 319
Cdd:COG2269  238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 29-319 5.12e-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: 499.00  E-value: 5.12e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   29 FFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGhSQGINLYLMTSPEYHMKRLLAAGCGPVYQLCRSFRNEEMGRHH 108
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPD-GQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  109 NPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLE--CQPAETISYQQAFQRHLEIDPLSADKTQLREVAAKLDLsnIADTEE 186
Cdd:TIGR00462  80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGI--RASEED 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  187 DRDTLLQLLFSMGVEPHIGKDRPVFVYHFPASQAALAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDN 266
Cdd:TIGR00462 158 DRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 495162709  267 RKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIA 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 3.44e-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: 213.60  E-value: 3.44e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  16 LLKRAAIMAEIRRFFADRGVLEVETPCMSQ----ATVTdihlfPFETrfvgpgH--SQGINLYLMTSPEYHMKRLLAAGC 89
Cdd:cd00775    8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPiaggAAAR-----PFIT------HhnALDMDLYLRIAPELYLKRLIVGGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  90 GPVYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLE-----------------CQPAETISYQQA 152
Cdd:cd00775   77 ERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVTMVDA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 153 FQRHLEIDPLSADKTQLREVAAKLDLSnIADTEEDRDTLLQLL---FSMGVEPHIGKdrPVFVYHFPASQAALAQISTED 229
Cdd:cd00775  157 LKEKTGIDFPELDLEQPEELAKLLAKL-IKEKIEKPRTLGKLLdklFEEFVEPTLIQ--PTFIIDHPVEISPLAKRHRSN 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 230 HRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLAL 309
Cdd:cd00775  234 PGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLT 313

                        330
                 ....*....|.
gi 495162709 310 GAESLAEVIAF 320
Cdd:cd00775  314 DSNSIRDVILF 324
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
15-320 2.26e-52

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 175.06  E-value: 2.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVtdihlfPFETR-FVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVY 93
Cdd:pfam00152  21 NLKLRSKIIKAIRNFLDENGFLEVETPILTKSAT------PEGARdFLVPSRALGKFYALPQSPQLYKQLLMVAGFDRVF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   94 QLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLEcqpaETISYQQAFQRHLEID-PLSADKTQLREV 172
Cdd:pfam00152  95 QIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFK----EVEGIAKELEGGTLLDlKKPFPRITYAEA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  173 AAKLDLSNIADTEEDRDTlLQLLFSMGVEPHIGKDRPVFVYHFPASQAAL-AQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:pfam00152 171 IEKLNGKDVEELGYGSDK-PDLRFLLELVIDKNKFNPLWVTDFPAEHHPFtMPKDEDDPALAEAFDLVLNGVEIGGGSIR 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495162709  252 LTDAREQQQRFEQDNRKRLQrglpQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIAF 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: 653.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  12 SIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGP 91
Cdd:PRK09350   1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  92 VYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLECQPAETISYQQAFQRHLEIDPLSADKTQLRE 171
Cdd:PRK09350  81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 172 VAAKLDLSNIADTEEDRDTLLQLLFSMGVEPHIGKDRPVFVYHFPASQAALAQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350 161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495162709 252 LTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEV 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: 560.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  11 ASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGhSQGINLYLMTSPEYHMKRLLAAGCG 90
Cdd:COG2269    1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPD-GGGRPLYLHTSPEFAMKRLLAAGSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  91 PVYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLEC---QPAETISYQQAFQRHLEIDPLSADKT 167
Cdd:COG2269   80 PIYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAagfAPAERLSYQEAFLRYLGIDPLTADLD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 168 QLREVAAKLDLSniADTEEDRDTLLQLLFSMGVEPHIGKDRPVFVYHFPASQAALAQISTEDHRVAERFEVYYKGIELAN 247
Cdd:COG2269  160 ELAAAAAAAGLR--VADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELAN 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495162709 248 GFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIA 319
Cdd:COG2269  238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 29-319 5.12e-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: 499.00  E-value: 5.12e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   29 FFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGhSQGINLYLMTSPEYHMKRLLAAGCGPVYQLCRSFRNEEMGRHH 108
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPD-GQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  109 NPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLE--CQPAETISYQQAFQRHLEIDPLSADKTQLREVAAKLDLsnIADTEE 186
Cdd:TIGR00462  80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGI--RASEED 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  187 DRDTLLQLLFSMGVEPHIGKDRPVFVYHFPASQAALAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDN 266
Cdd:TIGR00462 158 DRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 495162709  267 RKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIA 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 3.44e-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: 213.60  E-value: 3.44e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  16 LLKRAAIMAEIRRFFADRGVLEVETPCMSQ----ATVTdihlfPFETrfvgpgH--SQGINLYLMTSPEYHMKRLLAAGC 89
Cdd:cd00775    8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPiaggAAAR-----PFIT------HhnALDMDLYLRIAPELYLKRLIVGGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  90 GPVYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLE-----------------CQPAETISYQQA 152
Cdd:cd00775   77 ERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVTMVDA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 153 FQRHLEIDPLSADKTQLREVAAKLDLSnIADTEEDRDTLLQLL---FSMGVEPHIGKdrPVFVYHFPASQAALAQISTED 229
Cdd:cd00775  157 LKEKTGIDFPELDLEQPEELAKLLAKL-IKEKIEKPRTLGKLLdklFEEFVEPTLIQ--PTFIIDHPVEISPLAKRHRSN 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 230 HRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLAL 309
Cdd:cd00775  234 PGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLT 313

                        330
                 ....*....|.
gi 495162709 310 GAESLAEVIAF 320
Cdd:cd00775  314 DSNSIRDVILF 324
LysU COG1190
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
 16-320 2.24e-64

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: 211.05  E-value: 2.24e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  16 LLKRAAIMAEIRRFFADRGVLEVETPcMSQ-----ATVTdihlfPFETrfvgpgHSQ--GINLYLMTSPEYHMKRLLAAG 88
Cdd:COG1190  174 FRKRSKIIRAIRRFLDERGFLEVETP-MLQpiaggAAAR-----PFIT------HHNalDMDLYLRIAPELYLKRLIVGG 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  89 CGPVYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQV---------LECQ--------PAETISYQQ 151
Cdd:COG1190  242 FERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAaeavlgttkVTYQgqeidlspPWRRITMVE 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 152 AFQRHLEIDPLS-ADKTQLREVAAKLDLSniADTEEDRDTLLQLLFSMGVEPHIgkDRPVFVYHFPASQAALAQISTEDH 230
Cdd:COG1190  322 AIKEATGIDVTPlTDDEELRALAKELGIE--VDPGWGRGKLIDELFEELVEPKL--IQPTFVTDYPVEVSPLAKRHRDDP 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 231 RVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALG 310
Cdd:COG1190  398 GLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTD 477

                        330
                 ....*....|
gi 495162709 311 AESLAEVIAF 320
Cdd:COG1190  478 SPSIRDVILF 487
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 17-320 2.49e-63

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 208.02  E-value: 2.49e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  17 LKRAAIMAEIRRFFADRGVLEVETPcMSQ-----ATVTdihlfPFETrfvgpgHSQ--GINLYLMTSPEYHMKRLLAAGC 89
Cdd:PRK00484 173 RKRSKIISAIRRFLDNRGFLEVETP-MLQpiaggAAAR-----PFIT------HHNalDIDLYLRIAPELYLKRLIVGGF 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  90 GPVYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLE-----------------CQPAETISYQQA 152
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQavlgttkvtyqgteidfGPPFKRLTMVDA 320

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 153 FQRHLEIDPLSADKTQLREVAAKLDLSniADTEEDRDTLLQLLFSMGVEPHIgkDRPVFVYHFPASQAALAQISTEDHRV 232
Cdd:PRK00484 321 IKEYTGVDFDDMTDEEARALAKELGIE--VEKSWGLGKLINELFEEFVEPKL--IQPTFITDYPVEISPLAKRHREDPGL 396

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 233 AERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAE 312
Cdd:PRK00484 397 TERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSP 476


                 ....*...
gi 495162709 313 SLAEVIAF 320
Cdd:PRK00484 477 SIRDVILF 484
lysS_bact TIGR00499
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ...
 16-320 4.05e-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: 199.90  E-value: 4.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   16 LLKRAAIMAEIRRFFADRGVLEVETPCMsQATVTDIHLFPFETrfvgpgHSQ--GINLYLMTSPEYHMKRLLAAGCGPVY 93
Cdd:TIGR00499 172 FLKRSKIIKAIRRFLDDRGFIEVETPML-QSIPGGANAKPFIT------HHNalDMDLYLRIAPELYLKRLIVGGLEKVY 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   94 QLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLEC-----------------QPAETISYQQAFQRH 156
Cdd:TIGR00499 245 EIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKEllgtfiinyndleidlkPPWKRITMVDALEMV 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  157 LEIDPLSADKTQLREVAAKLDLSNIADTEEDRDTLLQLLFSMGVEPHIGKdrPVFVYHFPASQAALAQISTEDHRVAERF 236
Cdd:TIGR00499 325 TGIDFDILKDDETAKALAKEHGIEVAEDSLTLGHILNKFFEQFLEHTLIQ--PTFITHYPAEISPLAKRDPSNPEFTERF 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  237 EVYYKGIELANGFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAE 316
Cdd:TIGR00499 403 ELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIRD 482


                  ....
gi 495162709  317 VIAF 320
Cdd:TIGR00499 483 VLLF 486
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
15-320 2.26e-52

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 175.06  E-value: 2.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVtdihlfPFETR-FVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVY 93
Cdd:pfam00152  21 NLKLRSKIIKAIRNFLDENGFLEVETPILTKSAT------PEGARdFLVPSRALGKFYALPQSPQLYKQLLMVAGFDRVF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   94 QLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLEcqpaETISYQQAFQRHLEID-PLSADKTQLREV 172
Cdd:pfam00152  95 QIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFK----EVEGIAKELEGGTLLDlKKPFPRITYAEA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  173 AAKLDLSNIADTEEDRDTlLQLLFSMGVEPHIGKDRPVFVYHFPASQAAL-AQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:pfam00152 171 IEKLNGKDVEELGYGSDK-PDLRFLLELVIDKNKFNPLWVTDFPAEHHPFtMPKDEDDPALAEAFDLVLNGVEIGGGSIR 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495162709  252 LTDAREQQQRFEQDNRKRLQrglpQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIAF 320
Cdd:pfam00152 250 IHDPELQEERFEEQGLDPEE----AEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAF 314
PLN02502 PLN02502
lysyl-tRNA synthetase
 18-320 3.35e-49

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 172.10  E-value: 3.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  18 KRAAIMAEIRRFFADRGVLEVETPCM-SQATVTDIHlfPFETRfvgpgH-SQGINLYLMTSPEYHMKRLLAAGCGPVYQL 95
Cdd:PLN02502 231 TRAKIISYIRRFLDDRGFLEVETPMLnMIAGGAAAR--PFVTH-----HnDLNMDLYLRIATELHLKRLVVGGFERVYEI 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  96 CRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQ-VLECQPAETISYQQafqrhLEID---PLS-ADKTQLR 170
Cdd:PLN02502 304 GRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGmVKELTGSYKIKYHG-----IEIDftpPFRrISMISLV 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 171 EVAAKLDLSNIADTEEDRDT--------------------LLQLLFSMGVEPHIGKdrPVFVYHFPASQAALAQisteDH 230
Cdd:PLN02502 379 EEATGIDFPADLKSDEANAYliaacekfdvkcpppqttgrLLNELFEEFLEETLVQ--PTFVLDHPVEMSPLAK----PH 452

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 231 R----VAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIM 306
Cdd:PLN02502 453 RskpgLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVM 532

                        330
                 ....*....|....
gi 495162709 307 LALGAESLAEVIAF 320
Cdd:PLN02502 533 LLTDSASIRDVIAF 546
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
15-320 1.45e-40

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 151.27  E-value: 1.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQatvtdIH----LFPFETRfvgpghsqgIN-----LYLMTSPEYHMKRLL 85
Cdd:PRK02983  769 LLRARSAVVRAVRETLVARGFLEVETPILQQ-----VHgganARPFVTH---------INaydmdLYLRIAPELYLKRLC 834

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   86 AAGCGPVYQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDmYRLMNEV-----------------------DDLLQQVLECQ 142
Cdd:PRK02983  835 VGGVERVFELGRNFRNEGVDATHNPEFTLLEAYQAHAD-YDTMRDLtreliqnaaqaahgapvvmrpdgDGVLEPVDISG 913

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  143 PAETISYQQAFQRHL--EIDPlSADKTQLREVAAKLDLSniADTEEDRDTLLQLLFSMGVEPHIgkDRPVFVYHFPASQA 220
Cdd:PRK02983  914 PWPVVTVHDAVSEALgeEIDP-DTPLAELRKLCDAAGIP--YRTDWDAGAVVLELYEHLVEDRT--TFPTFYTDFPTSVS 988

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  221 ALAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRLQrGLPQ-QPVDYNLLEALKVGLPDCSGVAL 299
Cdd:PRK02983  989 PLTRPHRSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAG-GDPEaMELDEDFLQALEYAMPPTGGLGM 1067

                         330       340
                  ....*....|....*....|.
gi 495162709  300 GVDRLIMLALGAeSLAEVIAF 320
Cdd:PRK02983 1068 GVDRLVMLLTGR-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 1.56e-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: 1.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  19 RAAIMAEIRRFFADRGVLEVETPcMSQATVTDIHLFPFETRFVGPGHsqgiNLYLMTSPEYHMKRLLAAGCGPVYQLCRS 98
Cdd:cd00669    4 RSKIIKAIRDFMDDRGFLEVETP-MLQKITGGAGARPFLVKYNALGL----DYYLRISPQLFKKRLMVGGLDRVFEINRN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  99 FRNEEMGRHHNPEFTMLEWYRPHYDMYRLM--NE--VDDLLQQVLEcqpaetiSYQQAFQRHLEIDPLSADKTQLREVAA 174
Cdd:cd00669   79 FRNEDLRARHQPEFTMMDLEMAFADYEDVIelTErlVRHLAREVLG-------VTAVTYGFELEDFGLPFPRLTYREALE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 175 KLdlsniadteedrdtllqllfsmgvephigkDRPVFVYHFPA-SQAALAQISTEDHRVAERFEVYYKGIELANGFHELT 253
Cdd:cd00669  152 RY------------------------------GQPLFLTDYPAeMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLH 201

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495162709 254 DAREQQQRF-EQDNRKRLQRglpqqPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIAFTVDRA 325
Cdd:cd00669  202 DPDIQAEVFqEQGINKEAGM-----EYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 19-324 9.39e-37

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 137.89  E-value: 9.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  19 RAAIMAEIRRFFADRGVLEVETPCMsQATVTDIHLFPFETRFvgpgHSQGINLYLMTSPEYHMKRLLAAGCGPVYQLCRS 98
Cdd:PRK12445 187 RSKILAAIRQFMVARGFMEVETPMM-QVIPGGASARPFITHH----NALDLDMYLRIAPELYLKRLVVGGFERVFEINRN 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  99 FRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLL----QQVLEC-------------QPAETISYQQAFQRHL-EID 160
Cdd:PRK12445 262 FRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFrtlaQEVLGTtkvtygehvfdfgKPFEKLTMREAIKKYRpETD 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 161 PLSADKTQlrevAAKLDLSNIADTEEDRDTLLQL---LFSMGVEPHIgkDRPVFVYHFPASQAALAQISTEDHRVAERFE 237
Cdd:PRK12445 342 MADLDNFD----AAKALAESIGITVEKSWGLGRIvteIFDEVAEAHL--IQPTFITEYPAEVSPLARRNDVNPEITDRFE 415

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 238 VYYKGIELANGFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIMLALGAESLAEV 317
Cdd:PRK12445 416 FFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDV 495


                 ....*..
gi 495162709 318 IAFTVDR 324
Cdd:PRK12445 496 ILFPAMR 502
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
 13-324 3.15e-35

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 135.16  E-value: 3.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  13 IPNLLKRAAIMAEIRRFFADRGVLEVETPCMsQATVTDIHLFPFETRFvgpgHSQGINLYLMTSPEYHMKRLLAAGCGPV 92
Cdd:PTZ00385 230 IETIKKRHVMLQALRDYFNERNFVEVETPVL-HTVASGANAKSFVTHH----NANAMDLFLRVAPELHLKQCIVGGMERI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  93 YQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQ---------VLECQPAE------TISYQQAFQR-- 155
Cdd:PTZ00385 305 YEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQlamrvngttVVQIYPENahgnpvTVDLGKPFRRvs 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 156 -HLEIDPLSA------------------DKTQLREvaaKLDLSNIADTEEDRDTLLQLLF-SMGVEPHIGKDRPVFVyhf 215
Cdd:PTZ00385 385 vYDEIQRMSGvefpppnelntpkgiaymSVVMLRY---NIPLPPVRTAAKMFEKLIDFFItDRVVEPTFVMDHPLFM--- 458

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 216 pasqAALAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCS 295
Cdd:PTZ00385 459 ----SPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTA 534

                        330       340
                 ....*....|....*....|....*....
gi 495162709 296 GVALGVDRLIMLALGAESLAEVIAFTVDR 324
Cdd:PTZ00385 535 GWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 16-324 8.18e-30

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 119.34  E-value: 8.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  16 LLKRAAIMAEIRRFFADRGVLEVETPCMSqATVTDIHLFPFETRFvgpgHSQGINLYLMTSPEYHMKRLLAAGCGPVYQL 95
Cdd:PTZ00417 253 FITRTKIINYLRNFLNDRGFIEVETPTMN-LVAGGANARPFITHH----NDLDLDLYLRIATELPLKMLIVGGIDKVYEI 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  96 CRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQ-VLECQPAETISYQQAFQrhlEIDPLSAD------KTQ 168
Cdd:PTZ00417 328 GKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQlVMHLFGTYKILYNKDGP---EKDPIEIDftppypKVS 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 169 LREVAAKLD---LSNIADTEEDRDTLLQLLFSMGVE----PHIGK---------------DRPVFVYHFPASQAALAQIS 226
Cdd:PTZ00417 405 IVEELEKLTntkLEQPFDSPETINKMINLIKENKIEmpnpPTAAKlldqlashfienkypNKPFFIIEHPQIMSPLAKYH 484

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 227 TEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRLQRGLPQQPVDYNLLEALKVGLPDCSGVALGVDRLIM 306
Cdd:PTZ00417 485 RSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITM 564

                        330
                 ....*....|....*...
gi 495162709 307 LALGAESLAEVIAFTVDR 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 3.76e-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: 77.23  E-value: 3.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  16 LLKRAAIMAEIRRFFADRGVLEVETPCMSQATvtdihlfPFETR-FVGPGHSQGINLY-LMTSPEYHMKRLLAAGCGPVY 93
Cdd:cd00777    1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKST-------PEGARdFLVPSRLHPGKFYaLPQSPQLFKQLLMVSGFDRYF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  94 QLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLE-------CQPAETISYQQAFQRHleidplsadk 166
Cdd:cd00777   74 QIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKevlgvelTTPFPRMTYAEAMERY---------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 167 tqlrevaaKLDLSNIADteedrdtllqllFSMgVEPHIGKDRPVFVYH-FPASQA---ALAQISTEDHRvAERFEVYYKG 242
Cdd:cd00777  144 --------GFKFLWIVD------------FPL-FEWDEEEGRLVSAHHpFTAPKEedlDLLEKDPEDAR-AQAYDLVLNG 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 243 IELANGFHELTDAREQQQRFEQdnrkrlqRGLPQQPVDYN---LLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIA 319
Cdd:cd00777  202 VELGGGSIRIHDPDIQEKVFEI-------LGLSEEEAEEKfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIA 274


                 .
gi 495162709 320 F 320
Cdd:cd00777  275 F 275
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 19-320 6.80e-16

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: 76.84  E-value: 6.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  19 RAAIMAEIRRFFADRGVLEVETPCM------SQATVTDIHLFPFETrfvgpghsqginlYLMTSPEYHmKRLLAAGCGPV 92
Cdd:cd00776   27 RSEVLRAFREFLRENGFTEVHTPKItstdteGGAELFKVSYFGKPA-------------YLAQSPQLY-KEMLIAALERV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  93 YQLCRSFRNEE--MGRHHNpEFTMLEW---YRPHYDmyRLMNEVDDLLQQV---LECQPAETISYQQAFQRHLEIDP--- 161
Cdd:cd00776   93 YEIGPVFRAEKsnTRRHLS-EFWMLEAemaFIEDYN--EVMDLIEELIKYIfkrVLERCAKELELVNQLNRELLKPLepf 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 162 ----------LSADKTQLREVAAKLDLSniadTEEDRDtLLQLLfsmgvephigKDRPVFVYHFPASQAAL-AQISTEDH 230
Cdd:cd00776  170 pritydeaieLLREKGVEEEVKWGEDLS----TEHERL-LGEIV----------KGDPVFVTDYPKEIKPFyMKPDDDNP 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 231 RVAERFEVYYKGI-ELANGFHELTDAREQQQRFEqdnrkrlQRGLPQQPVDYnLLEALKVGLPDCSGVALGVDRLIMLAL 309
Cdd:cd00776  235 ETVESFDLLMPGVgEIVGGSQRIHDYDELEERIK-------EHGLDPESFEW-YLDLRKYGMPPHGGFGLGLERLVMWLL 306

                        330
                 ....*....|.
gi 495162709 310 GAESLAEVIAF 320
Cdd:cd00776  307 GLDNIREAILF 317
PLN02903 PLN02903
aminoacyl-tRNA ligase
 15-181 4.62e-10

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 60.57  E-value: 4.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  15 NLLKRAAIMAEIRRFFADR-GVLEVETPCMSQATVTDIHLFPFETRfVGPGhsqgiNLY-LMTSPEYHMKRLLAAGCGPV 92
Cdd:PLN02903 202 NLRLRHRVVKLIRRYLEDVhGFVEIETPILSRSTPEGARDYLVPSR-VQPG-----TFYaLPQSPQLFKQMLMVSGFDRY 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  93 YQLCRSFRNEEMGRHHNPEFTMLEW---YRPHYDMYRLMnevDDLLQQVLE-------CQPAETISYQQAFQRHleidpl 162
Cdd:PLN02903 276 YQIARCFRDEDLRADRQPEFTQLDMelaFTPLEDMLKLN---EDLIRQVFKeikgvqlPNPFPRLTYAEAMSKY------ 346

                        170
                 ....*....|....*....
gi 495162709 163 SADKTQLREVAAKLDLSNI 181
Cdd:PLN02903 347 GSDKPDLRYGLELVDVSDV 365
PRK06462 PRK06462
asparagine synthetase A; Reviewed
 5-320 1.01e-09

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 58.88  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709   5 ATWQPSASIPNLLK-RAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHmKR 83
Cdd:PRK06462  18 WKHISSEKYRKVLKvQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLGSDLPVKQISIDFYGVEYYLADSMILH-KQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  84 LLAAGCGPVYQLCRSFRNEE----MGRHHNpEFTMLEWYRPHYDMYRLMNEVDDLL----QQVLECQPAETISYQQ---A 152
Cdd:PRK06462  97 LALRMLGKIFYLSPNFRLEPvdkdTGRHLY-EFTQLDIEIEGADLDEVMDLIEDLIkylvKELLEEHEDELEFFGRdlpH 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 153 FQRHLEIDPLS-ADKTQLREVAAKLDLSNIADTEEDrdtllqlLFSMgvepHIGKdrPVFVYHFPASQAALAQISTEDHR 231
Cdd:PRK06462 176 LKRPFKRITHKeAVEILNEEGCRGIDLEELGSEGEK-------SLSE----HFEE--PFWIIDIPKGSREFYDREDPERP 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 232 -VAERFEVYYkgielANGFHELTDAREQQQRFEQDNRKRLQRGL-PQQPVDYnlLEALKVGLPDCSGVALGVDRLIMLAL 309
Cdd:PRK06462 243 gVLRNYDLLL-----PEGYGEAVSGGEREYEYEEIVERIREHGVdPEKYKWY--LEMAKEGPLPSAGFGIGVERLTRYIC 315

                        330
                 ....*....|.
gi 495162709 310 GAESLAEVIAF 320
Cdd:PRK06462 316 GLRHIREVQPF 326
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 19-121 5.13e-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: 55.59  E-value: 5.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  19 RAAIMAEIRRFFADRGVLEVETPCMSQATV--TDIHLFPfetRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGP----V 92
Cdd:cd00768    2 RSKIEQKLRRFMAELGFQEVETPIVEREPLleKAGHEPK---DLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKlplrL 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495162709  93 YQLCRSFRNEEMGRH--HNPEFTMLEWYRPH 121
Cdd:cd00768   79 AEIGPAFRNEGGRRGlrRVREFTQLEGEVFG 109
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 15-170 1.56e-08

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


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 55.76  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQATvtdihlfPFETR-FVGPGHSQGINLY-LMTSPEYHMKRLLAAGCGPV 92
Cdd:PRK12820 155 HLAKRHRIIKCARDFLDSRGFLEIETPILTKST-------PEGARdYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERY 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  93 YQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLEC------QPAETISYQQAfqrhleIDPLSADK 166
Cdd:PRK12820 228 FQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFAIggialpRPFPRMPYAEA------MDTTGSDR 301


                 ....
gi 495162709 167 TQLR 170
Cdd:PRK12820 302 PDLR 305
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 283-320 2.25e-08

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 55.07  E-value: 2.25e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 495162709 283 LLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIAF 320
Cdd:PRK00476 518 LLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAF 555
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 283-320 3.67e-08

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: 54.62  E-value: 3.67e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 495162709 283 LLEALKVGLPDCSGVALGVDRLIMLALGAESLAEVIAF 320
Cdd:COG0173  517 LLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
PTZ00425 PTZ00425
asparagine-tRNA ligase; Provisional
 85-320 2.41e-06

asparagine-tRNA ligase; Provisional


Pssm-ID: 240414 [Multi-domain]  Cd Length: 586  Bit Score: 48.87  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709  85 LAAGCGPVYQLCRSFR--NEEMGRHHnPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLECQPAETISYQQAFQRHLEIDPL 162
Cdd:PTZ00425 339 LCSSMGDVYTFGPTFRaeNSHTSRHL-AEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNFDDIYYFEENVETGLI 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 163 SADKTQLREVAAKLDLSNIADTEEDRDTLLQLLFSMGVEPHIGKDR---------PVFVYHFPASQAALAQISTEDHRVA 233
Cdd:PTZ00425 418 SRLKNILDEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERfvaeqifkkPVIVYNYPKDLKAFYMKLNEDQKTV 497

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162709 234 ERFEVYYKGI-ELANGfheltdareqQQRfeQDNRKRLQRGLPQQPVD------YNLLEalKVGLPDCSGVALGVDRLIM 306
Cdd:PTZ00425 498 AAMDVLVPKIgEVIGG----------SQR--EDNLERLDKMIKEKKLNmesywwYRQLR--KFGSHPHAGFGLGFERLIM 563

                        250
                 ....*....|....
gi 495162709 307 LALGAESLAEVIAF 320
Cdd:PTZ00425 564 LVTGVDNIKDTIPF 577
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 15-47 2.25e-04

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 42.75  E-value: 2.25e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 495162709  15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQAT 47
Cdd:PRK00476 140 NLKLRSKVTSAIRNFLDDNGFLEIETPILTKST 172
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 15-41 6.40e-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: 41.52  E-value: 6.40e-04
                         10        20
                 ....*....|....*....|....*..
gi 495162709  15 NLLKRAAIMAEIRRFFADRGVLEVETP 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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