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Conserved domains on  [gi|90111694|ref|NP_418579|]
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EF-P-lysine lysyltransferase [Escherichia coli str. K-12 substr. MG1655]

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: 655.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   12 SIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGP 91
Cdd:PRK09350   1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   92 VFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLRE 171
Cdd:PRK09350  81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  172 VAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350 161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111694  252 LTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEV 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: 655.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   12 SIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGP 91
Cdd:PRK09350   1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   92 VFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLRE 171
Cdd:PRK09350  81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  172 VAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350 161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111694  252 LTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEV 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 90111694  11 ASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGhSQGMNLWLMTSPEYHMKRLLVAGCG 90
Cdd:COG2269   1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPD-GGGRPLYLHTSPEFAMKRLLAAGSG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  91 PVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDC---PAAESLSYQQAFLRYLEIDPLSADKT 167
Cdd:COG2269  80 PIYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAagfAPAERLSYQEAFLRYLGIDPLTADLD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 168 QLREVAAKLDLSnvADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELAN 247
Cdd:COG2269 160 ELAAAAAAAGLR--VADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELAN 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111694 248 GFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIA 319
Cdd:COG2269 238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 29-319 2.45e-178

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: 494.38  E-value: 2.45e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    29 FFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGhSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYH 108
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPD-GQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   109 NPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD--CPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLsnVADTEE 186
Cdd:TIGR00462  80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGI--RASEED 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   187 DRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDN 266
Cdd:TIGR00462 158 DRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 90111694   267 RKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIA 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 2.94e-70

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: 221.30  E-value: 2.94e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  16 LLKRAAIMAEIRRFFADRGVLEVETPCMSQ----ATVTdihlvPFETrfvgpgH--SQGMNLWLMTSPEYHMKRLLVAGC 89
Cdd:cd00775   8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPiaggAAAR-----PFIT------HhnALDMDLYLRIAPELYLKRLIVGGF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  90 GPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD-----------------CPAAESLSYQQA 152
Cdd:cd00775  77 ERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVTMVDA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 153 FLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDT--LLQLLFTFGVEPNIgkEKPTFVYHFPASQASLAQISTEDH 230
Cdd:cd00775 157 LKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEKPRTLgkLLDKLFEEFVEPTL--IQPTFIIDHPVEISPLAKRHRSNP 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 231 RVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALG 310
Cdd:cd00775 235 GLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTD 314

                       330
                ....*....|
gi 90111694 311 AETLAEVIAF 320
Cdd:cd00775 315 SNSIRDVILF 324
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
15-320 3.79e-53

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 176.99  E-value: 3.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVtdihlvPFETR-FVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVF 93
Cdd:pfam00152  21 NLKLRSKIIKAIRNFLDENGFLEVETPILTKSAT------PEGARdFLVPSRALGKFYALPQSPQLYKQLLMVAGFDRVF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    94 QLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDcpaaESLSYQQAFLRYLEID-PLSADKTQLREV 172
Cdd:pfam00152  95 QIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFK----EVEGIAKELEGGTLLDlKKPFPRITYAEA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   173 AAKLDLSNVADTEEDRDTL-LQLLFTFGVEPNigKEKPTFVYHFPASQASL-AQISTEDHRVAERFEVYYKGIELANGFH 250
Cdd:pfam00152 171 IEKLNGKDVEELGYGSDKPdLRFLLELVIDKN--KFNPLWVTDFPAEHHPFtMPKDEDDPALAEAFDLVLNGVEIGGGSI 248

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   251 ELTDAREQQQRFEQDNRKRAArglpQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAF 320
Cdd:pfam00152 249 RIHDPELQEERFEEQGLDPEE----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: 655.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   12 SIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGP 91
Cdd:PRK09350   1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   92 VFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLRE 171
Cdd:PRK09350  81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  172 VAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350 161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111694  252 LTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEV 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 90111694  11 ASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGhSQGMNLWLMTSPEYHMKRLLVAGCG 90
Cdd:COG2269   1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPD-GGGRPLYLHTSPEFAMKRLLAAGSG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  91 PVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDC---PAAESLSYQQAFLRYLEIDPLSADKT 167
Cdd:COG2269  80 PIYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAagfAPAERLSYQEAFLRYLGIDPLTADLD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 168 QLREVAAKLDLSnvADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELAN 247
Cdd:COG2269 160 ELAAAAAAAGLR--VADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELAN 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111694 248 GFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIA 319
Cdd:COG2269 238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 29-319 2.45e-178

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: 494.38  E-value: 2.45e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    29 FFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGhSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYH 108
Cdd:TIGR00462   1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPD-GQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   109 NPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD--CPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLsnVADTEE 186
Cdd:TIGR00462  80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGI--RASEED 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   187 DRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDN 266
Cdd:TIGR00462 158 DRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 90111694   267 RKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIA 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 2.94e-70

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: 221.30  E-value: 2.94e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  16 LLKRAAIMAEIRRFFADRGVLEVETPCMSQ----ATVTdihlvPFETrfvgpgH--SQGMNLWLMTSPEYHMKRLLVAGC 89
Cdd:cd00775   8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPiaggAAAR-----PFIT------HhnALDMDLYLRIAPELYLKRLIVGGF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  90 GPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD-----------------CPAAESLSYQQA 152
Cdd:cd00775  77 ERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVTMVDA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 153 FLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDT--LLQLLFTFGVEPNIgkEKPTFVYHFPASQASLAQISTEDH 230
Cdd:cd00775 157 LKEKTGIDFPELDLEQPEELAKLLAKLIKEKIEKPRTLgkLLDKLFEEFVEPTL--IQPTFIIDHPVEISPLAKRHRSNP 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 231 RVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALG 310
Cdd:cd00775 235 GLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTD 314

                       330
                ....*....|
gi 90111694 311 AETLAEVIAF 320
Cdd:cd00775 315 SNSIRDVILF 324
LysU COG1190
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
 16-320 2.52e-69

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: 223.76  E-value: 2.52e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  16 LLKRAAIMAEIRRFFADRGVLEVETPCMsqatvtdiHLV-------PFETrfvgpgHSQ--GMNLWLMTSPEYHMKRLLV 86
Cdd:COG1190 174 FRKRSKIIRAIRRFLDERGFLEVETPML--------QPIaggaaarPFIT------HHNalDMDLYLRIAPELYLKRLIV 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  87 AGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDcpAA-------------------ESL 147
Cdd:COG1190 240 GGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAE--AVlgttkvtyqgqeidlsppwRRI 317

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 148 SYQQAFLRYLEIDPLS-ADKTQLREVAAKLDLSnvADTEEDRDTLLQLLFTFGVEPNIgkEKPTFVYHFPASQASLAQIS 226
Cdd:COG1190 318 TMVEAIKEATGIDVTPlTDDEELRALAKELGIE--VDPGWGRGKLIDELFEELVEPKL--IQPTFVTDYPVEVSPLAKRH 393

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 227 TEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVM 306
Cdd:COG1190 394 RDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVM 473

                       330
                ....*....|....
gi 90111694 307 LALGAETLAEVIAF 320
Cdd:COG1190 474 LLTDSPSIRDVILF 487
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 17-320 6.20e-68

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 220.35  E-value: 6.20e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   17 LKRAAIMAEIRRFFADRGVLEVETPCMsqatvtdiHLV-------PFETrfvgpgHSQ--GMNLWLMTSPEYHMKRLLVA 87
Cdd:PRK00484 173 RKRSKIISAIRRFLDNRGFLEVETPML--------QPIaggaaarPFIT------HHNalDIDLYLRIAPELYLKRLIVG 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   88 GCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDcpAA-------------------ESLS 148
Cdd:PRK00484 239 GFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQ--AVlgttkvtyqgteidfgppfKRLT 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  149 YQQAFLRYLEIDPLSADKTQLREVAAKLDLsnVADTEEDRDTLLQLLFTFGVEPNIgkEKPTFVYHFPASQASLAQISTE 228
Cdd:PRK00484 317 MVDAIKEYTGVDFDDMTDEEARALAKELGI--EVEKSWGLGKLINELFEEFVEPKL--IQPTFITDYPVEISPLAKRHRE 392

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  229 DHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLA 308
Cdd:PRK00484 393 DPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLL 472

                        330
                 ....*....|..
gi 90111694  309 LGAETLAEVIAF 320
Cdd:PRK00484 473 TDSPSIRDVILF 484
lysS_bact TIGR00499
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ...
 16-320 3.71e-61

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: 202.60  E-value: 3.71e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    16 LLKRAAIMAEIRRFFADRGVLEVETPCMsQATVTDIHLVPFETrfvgpgHSQ--GMNLWLMTSPEYHMKRLLVAGCGPVF 93
Cdd:TIGR00499 172 FLKRSKIIKAIRRFLDDRGFIEVETPML-QSIPGGANAKPFIT------HHNalDMDLYLRIAPELYLKRLIVGGLEKVY 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    94 QLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVldcpaAESLSYQQAF-LRYLEIDPlsadKTQLREV 172
Cdd:TIGR00499 245 EIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFL-----AKELLGTFIInYNDLEIDL----KPPWKRI 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   173 ----AAKLDLSNVADTEEDRDTLLQLLFTFGV---EPNIGKEK----------------PTFVYHFPASQASLAQISTED 229
Cdd:TIGR00499 316 tmvdALEMVTGIDFDILKDDETAKALAKEHGIevaEDSLTLGHilnkffeqflehtliqPTFITHYPAEISPLAKRDPSN 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   230 HRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLAL 309
Cdd:TIGR00499 396 PEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLT 475

                         330
                  ....*....|.
gi 90111694   310 GAETLAEVIAF 320
Cdd:TIGR00499 476 DAPSIRDVLLF 486
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
15-320 3.79e-53

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


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 176.99  E-value: 3.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVtdihlvPFETR-FVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVF 93
Cdd:pfam00152  21 NLKLRSKIIKAIRNFLDENGFLEVETPILTKSAT------PEGARdFLVPSRALGKFYALPQSPQLYKQLLMVAGFDRVF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    94 QLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDcpaaESLSYQQAFLRYLEID-PLSADKTQLREV 172
Cdd:pfam00152  95 QIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFK----EVEGIAKELEGGTLLDlKKPFPRITYAEA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   173 AAKLDLSNVADTEEDRDTL-LQLLFTFGVEPNigKEKPTFVYHFPASQASL-AQISTEDHRVAERFEVYYKGIELANGFH 250
Cdd:pfam00152 171 IEKLNGKDVEELGYGSDKPdLRFLLELVIDKN--KFNPLWVTDFPAEHHPFtMPKDEDDPALAEAFDLVLNGVEIGGGSI 248

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   251 ELTDAREQQQRFEQDNRKRAArglpQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAF 320
Cdd:pfam00152 249 RIHDPELQEERFEEQGLDPEE----AEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAF 314
PLN02502 PLN02502
lysyl-tRNA synthetase
 18-322 7.10e-50

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 174.02  E-value: 7.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   18 KRAAIMAEIRRFFADRGVLEVETPCM-SQATVTDIHlvPFETRfvgpgH-SQGMNLWLMTSPEYHMKRLLVAGCGPVFQL 95
Cdd:PLN02502 231 TRAKIISYIRRFLDDRGFLEVETPMLnMIAGGAAAR--PFVTH-----HnDLNMDLYLRIATELHLKRLVVGGFERVYEI 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   96 CRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQ-VLDCPAAESLSYQQaflryLEID---PLS-ADKTQLR 170
Cdd:PLN02502 304 GRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGmVKELTGSYKIKYHG-----IEIDftpPFRrISMISLV 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  171 EVAAKLDLSNVADTEEDRDTLLQLLFTFGVE----PNIGK----------EK----PTFVYHFPASQASLAQisteDHR- 231
Cdd:PLN02502 379 EEATGIDFPADLKSDEANAYLIAACEKFDVKcpppQTTGRllnelfeeflEEtlvqPTFVLDHPVEMSPLAK----PHRs 454

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  232 ---VAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLA 308
Cdd:PLN02502 455 kpgLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLL 534

                        330
                 ....*....|....
gi 90111694  309 LGAETLAEVIAFSV 322
Cdd:PLN02502 535 TDSASIRDVIAFPA 548
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
15-320 1.07e-45

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 165.91  E-value: 1.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQatvtdIH----LVPFETRFvgpgHSQGMNLWLMTSPEYHMKRLLVAGCG 90
Cdd:PRK02983  769 LLRARSAVVRAVRETLVARGFLEVETPILQQ-----VHgganARPFVTHI----NAYDMDLYLRIAPELYLKRLCVGGVE 839

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    91 PVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDmYRLMNEV-DDLLQ---------QVLDCPAAESLSYQ---------- 150
Cdd:PRK02983  840 RVFELGRNFRNEGVDATHNPEFTLLEAYQAHAD-YDTMRDLtRELIQnaaqaahgaPVVMRPDGDGVLEPvdisgpwpvv 918

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   151 ---QAFLRYL--EIDPlSADKTQLREVAAKLDLSnvADTEEDRDTLLQLLFTFGVEPNIgkEKPTFVYHFPASQASLAQI 225
Cdd:PRK02983  919 tvhDAVSEALgeEIDP-DTPLAELRKLCDAAGIP--YRTDWDAGAVVLELYEHLVEDRT--TFPTFYTDFPTSVSPLTRP 993

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   226 STEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKrAARGLPQ-HPIDQNLIEALKVGMPDCSGVALGVDRL 304
Cdd:PRK02983  994 HRSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLL-AAGGDPEaMELDEDFLQALEYAMPPTGGLGMGVDRL 1072

                         330
                  ....*....|....*.
gi 90111694   305 VMLALGAeTLAEVIAF 320
Cdd:PRK02983 1073 VMLLTGR-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 2.54e-41

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: 144.93  E-value: 2.54e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  19 RAAIMAEIRRFFADRGVLEVETPcMSQATVTDIHLVPFETRFVGPGHsqgmNLWLMTSPEYHMKRLLVAGCGPVFQLCRS 98
Cdd:cd00669   4 RSKIIKAIRDFMDDRGFLEVETP-MLQKITGGAGARPFLVKYNALGL----DYYLRISPQLFKKRLMVGGLDRVFEINRN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  99 FRNEEMGRYHNPEFTMLEWYRPHYDMYRLMnevdDLLQQVLDCPAAESL-SYQQAFLRYLEIDPLSADKTQLREVAAKLd 177
Cdd:cd00669  79 FRNEDLRARHQPEFTMMDLEMAFADYEDVI----ELTERLVRHLAREVLgVTAVTYGFELEDFGLPFPRLTYREALERY- 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 178 lsnvadteedrdtllqllftfgvepnigkEKPTFVYHFPASQAS-LAQISTEDHRVAERFEVYYKGIELANGFHELTDAR 256
Cdd:cd00669 154 -----------------------------GQPLFLTDYPAEMHSpLASPHDVNPEIADAFDLFINGVEVGNGSSRLHDPD 204

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111694 257 EQQQRFEQDNRKRAArglpQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA 325
Cdd:cd00669 205 IQAEVFQEQGINKEA----GMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 19-324 1.55e-37

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 139.81  E-value: 1.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   19 RAAIMAEIRRFFADRGVLEVETPCMsQATVTDIHLVPFETRFvgpgHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRS 98
Cdd:PRK12445 187 RSKILAAIRQFMVARGFMEVETPMM-QVIPGGASARPFITHH----NALDLDMYLRIAPELYLKRLVVGGFERVFEINRN 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   99 FRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL----QQVLDCPAA-------------ESLSYQQAFLRYL-EID 160
Cdd:PRK12445 262 FRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFrtlaQEVLGTTKVtygehvfdfgkpfEKLTMREAIKKYRpETD 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  161 PLSADKTQlrevAAKLDLSNVADTEEDRDTLLQL---LFTFGVEPNIgkEKPTFVYHFPASQASLAQISTEDHRVAERFE 237
Cdd:PRK12445 342 MADLDNFD----AAKALAESIGITVEKSWGLGRIvteIFDEVAEAHL--IQPTFITEYPAEVSPLARRNDVNPEITDRFE 415

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  238 VYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEV 317
Cdd:PRK12445 416 FFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDV 495


                 ....*..
gi 90111694  318 IAFSVDR 324
Cdd:PRK12445 496 ILFPAMR 502
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
 13-324 1.05e-36

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 139.40  E-value: 1.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   13 IPNLLKRAAIMAEIRRFFADRGVLEVETPCMsQATVTDIHLVPFETRFvgpgHSQGMNLWLMTSPEYHMKRLLVAGCGPV 92
Cdd:PTZ00385 230 IETIKKRHVMLQALRDYFNERNFVEVETPVL-HTVASGANAKSFVTHH----NANAMDLFLRVAPELHLKQCIVGGMERI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   93 FQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQV-----------LDCPAAESLSYQ----QAFLR-- 155
Cdd:PTZ00385 305 YEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLamrvngttvvqIYPENAHGNPVTvdlgKPFRRvs 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  156 -YLEIDPLSA------------------DKTQLREvaaKLDLSNVADTEEDRDTLLQLLFTFGVEpnigkeKPTFVYHFP 216
Cdd:PTZ00385 385 vYDEIQRMSGvefpppnelntpkgiaymSVVMLRY---NIPLPPVRTAAKMFEKLIDFFITDRVV------EPTFVMDHP 455

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  217 ASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSG 296
Cdd:PTZ00385 456 LFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAG 535

                        330       340
                 ....*....|....*....|....*...
gi 90111694  297 VALGVDRLVMLALGAETLAEVIAFSVDR 324
Cdd:PTZ00385 536 WGMGIDRALMLLTNSSNIRDGIIFPLLR 563
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 16-324 1.29e-28

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 115.88  E-value: 1.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   16 LLKRAAIMAEIRRFFADRGVLEVETPCMSqATVTDIHLVPFETRFvgpgHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQL 95
Cdd:PTZ00417 253 FITRTKIINYLRNFLNDRGFIEVETPTMN-LVAGGANARPFITHH----NDLDLDLYLRIATELPLKMLIVGGIDKVYEI 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   96 CRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQ-VLDCPAAESLSYQQaflRYLEIDPLSAD------KTQ 168
Cdd:PTZ00417 328 GKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQlVMHLFGTYKILYNK---DGPEKDPIEIDftppypKVS 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  169 LREVAAKLD---LSNVADTEEDRDTLLQLLFTFGVE----PNIGK---------------EKPTFVYHFPASQASLAQIS 226
Cdd:PTZ00417 405 IVEELEKLTntkLEQPFDSPETINKMINLIKENKIEmpnpPTAAKlldqlashfienkypNKPFFIIEHPQIMSPLAKYH 484

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  227 TEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVM 306
Cdd:PTZ00417 485 RSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITM 564

                        330
                 ....*....|....*...
gi 90111694  307 LALGAETLAEVIAFSVDR 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 2.94e-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: 74.53  E-value: 2.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  16 LLKRAAIMAEIRRFFADRGVLEVETPCMSQAT---VTDiHLVPfeTRfVGPGHSQGmnlwLMTSPEYHMKRLLVAGCGPV 92
Cdd:cd00777   1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTpegARD-FLVP--SR-LHPGKFYA----LPQSPQLFKQLLMVSGFDRY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  93 FQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESL-------SYQQAFLRYleidplsad 165
Cdd:cd00777  73 FQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELttpfprmTYAEAMERY--------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 166 ktqlrevaaKLDLSNVADTEedrdtllqlLFtfgvEPNIGKEKPTFVYH-FPASQAS---LAQISTEDHRvAERFEVYYK 241
Cdd:cd00777 144 ---------GFKFLWIVDFP---------LF----EWDEEEGRLVSAHHpFTAPKEEdldLLEKDPEDAR-AQAYDLVLN 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 242 GIELANGFHELTDAREQQQRFEQdnrkraaRGLPQHPIDQN---LIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVI 318
Cdd:cd00777 201 GVELGGGSIRIHDPDIQEKVFEI-------LGLSEEEAEEKfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVI 273


                ..
gi 90111694 319 AF 320
Cdd:cd00777 274 AF 275
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 19-320 4.03e-15

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: 74.91  E-value: 4.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  19 RAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHsqgmnlwLMTSPEYHmKRLLVAGCGPVFQLCRS 98
Cdd:cd00776  27 RSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAY-------LAQSPQLY-KEMLIAALERVYEIGPV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  99 FRNEEMG-RYHNPEFTMLEW---YRPHYDmyRLMNEVDDLLQQVL-----DCPAAESLSYQQAF-----------LRYLE 158
Cdd:cd00776  99 FRAEKSNtRRHLSEFWMLEAemaFIEDYN--EVMDLIEELIKYIFkrvleRCAKELELVNQLNRellkplepfprITYDE 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 159 IDPLSADKTQLREVAAKLDLSnvadTEEDRDtLLQLLFTfgvepnigkeKPTFVYHFPASQ-ASLAQISTEDHRVAERFE 237
Cdd:cd00776 177 AIELLREKGVEEEVKWGEDLS----TEHERL-LGEIVKG----------DPVFVTDYPKEIkPFYMKPDDDNPETVESFD 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 238 VYYKGI-ELANGFHELTDAREQQQRFEQdnrkraaRGLPQHPIDQNLiEALKVGMPDCSGVALGVDRLVMLALGAETLAE 316
Cdd:cd00776 242 LLMPGVgEIVGGSQRIHDYDELEERIKE-------HGLDPESFEWYL-DLRKYGMPPHGGFGLGLERLVMWLLGLDNIRE 313


                ....
gi 90111694 317 VIAF 320
Cdd:cd00776 314 AILF 317
PLN02903 PLN02903
aminoacyl-tRNA ligase
 15-183 1.51e-10

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 62.11  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   15 NLLKRAAIMAEIRRFFADR-GVLEVETPCMSQAT---VTDiHLVPfeTRfVGPGHSQGmnlwLMTSPEYHMKRLLVAGCG 90
Cdd:PLN02903 202 NLRLRHRVVKLIRRYLEDVhGFVEIETPILSRSTpegARD-YLVP--SR-VQPGTFYA----LPQSPQLFKQMLMVSGFD 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   91 PVFQLCRSFRNEEMGRYHNPEFTMLEW---YRPHYDMYRLMnevDDLLQQV------LDCPAA-ESLSYQQAFLRYleid 160
Cdd:PLN02903 274 RYYQIARCFRDEDLRADRQPEFTQLDMelaFTPLEDMLKLN---EDLIRQVfkeikgVQLPNPfPRLTYAEAMSKY---- 346

                        170       180
                 ....*....|....*....|...
gi 90111694  161 plSADKTQLRevaAKLDLSNVAD 183
Cdd:PLN02903 347 --GSDKPDLR---YGLELVDVSD 364
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 15-116 1.30e-08

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


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 56.15  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQATvtdihlvPFETR-FVGPGHSQGMNLW-LMTSPEYHMKRLLVAGCGPV 92
Cdd:PRK12820 155 HLAKRHRIIKCARDFLDSRGFLEIETPILTKST-------PEGARdYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERY 227

                         90       100
                 ....*....|....*....|....
gi 90111694   93 FQLCRSFRNEEMGRYHNPEFTMLE 116
Cdd:PRK12820 228 FQLARCFRDEDLRPNRQPEFTQLD 251
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 283-320 6.71e-08

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 53.92  E-value: 6.71e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 90111694  283 LIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAF 320
Cdd:PRK00476 518 LLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAF 555
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 283-320 9.37e-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: 53.46  E-value: 9.37e-08
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 90111694 283 LIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAF 320
Cdd:COG0173 517 LLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 19-121 1.76e-07

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


Pssm-ID: 238391 [Multi-domain]  Cd Length: 211  Bit Score: 50.96  E-value: 1.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  19 RAAIMAEIRRFFADRGVLEVETPCMSQATV--TDIHlvpFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGP----V 92
Cdd:cd00768   2 RSKIEQKLRRFMAELGFQEVETPIVEREPLleKAGH---EPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKlplrL 78

                        90       100       110
                ....*....|....*....|....*....|.
gi 90111694  93 FQLCRSFRNEEMGRY--HNPEFTMLEWYRPH 121
Cdd:cd00768  79 AEIGPAFRNEGGRRGlrRVREFTQLEGEVFG 109
PRK06462 PRK06462
asparagine synthetase A; Reviewed
 5-320 4.25e-06

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 47.71  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694    5 ASWQPSASIPNLLK-RAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHmKR 83
Cdd:PRK06462  18 WKHISSEKYRKVLKvQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLGSDLPVKQISIDFYGVEYYLADSMILH-KQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   84 LLVAGCGPVFQLCRSFRNEE----MGRyHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDcpaaESLSYQQAFLRYLEI 159
Cdd:PRK06462  97 LALRMLGKIFYLSPNFRLEPvdkdTGR-HLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVK----ELLEEHEDELEFFGR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  160 DpLSADKTQLREVaakldlsnvadTEEDRDTLLQLLFTFG-VEPNIGKE----------KPTFVYHFPASQASLAQISTE 228
Cdd:PRK06462 172 D-LPHLKRPFKRI-----------THKEAVEILNEEGCRGiDLEELGSEgekslsehfeEPFWIIDIPKGSREFYDREDP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  229 DHR-VAERFEVYYkgielANGFHELTDAREQQQRFEQDNRKRAARGL-PQHPidQNLIEALKVGMPDCSGVALGVDRLVM 306
Cdd:PRK06462 240 ERPgVLRNYDLLL-----PEGYGEAVSGGEREYEYEEIVERIREHGVdPEKY--KWYLEMAKEGPLPSAGFGIGVERLTR 312

                        330
                 ....*....|....
gi 90111694  307 LALGAETLAEVIAF 320
Cdd:PRK06462 313 YICGLRHIREVQPF 326
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
 211-324 1.73e-05

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 45.95  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  211 FVYHFPAS-QASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEqdnrkraARGLpqHPID-QNLIEALK 288
Cdd:PRK05159 326 FITDYPSEkRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIK-------EKGL--NPESfEFYLEAFK 396

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 90111694  289 VGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDR 324
Cdd:PRK05159 397 YGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDR 432
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 19-320 1.69e-04

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


Pssm-ID: 439788 [Multi-domain]  Cd Length: 430  Bit Score: 43.12  E-value: 1.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  19 RAAIMAEIRRFFADRGVLEVETP------CMSQATVtdihlvpFETRFVG-PGH-SQgmnlwlmtSPEYHmKRLLVAGCG 90
Cdd:COG0017 133 RSELARAIREFFQERGFVEVHTPiitasaTEGGGEL-------FPVDYFGkEAYlTQ--------SGQLY-KEALAMALE 196

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  91 PVFQLCRSFRNEEMG-RYHNPEFTMLE----WYRpHYDMYRLMNE-VDDLLQQVLD-CPAAeslsyqqafLRYLEIDPLS 163
Cdd:COG0017 197 KVYTFGPTFRAEKSNtRRHLAEFWMIEpemaFAD-LEDVMDLAEEmLKYIIKYVLEnCPEE---------LEFLGRDVER 266

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 164 adktqlrevaakldLSNVADTEEDR---DTLLQLLFTFGVEPNIG---------------KEKPTFVYHFPAS-QASLAQ 224
Cdd:COG0017 267 --------------LEKVPESPFPRityTEAIEILKKSGEKVEWGddlgteherylgeefFKKPVFVTDYPKEiKAFYMK 332

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694 225 ISTEDHRVAERFEVYYKGI-ELANGFHELTDAREQQQRFEQdnrkraaRGLPQHPIDQNLiEALKVGMPDCSGVALGVDR 303
Cdd:COG0017 333 PNPDDPKTVAAFDLLAPGIgEIIGGSQREHRYDVLVERIKE-------KGLDPEDYEWYL-DLRRYGSVPHAGFGLGLER 404

                       330
                ....*....|....*..
gi 90111694 304 LVMLALGAETLAEVIAF 320
Cdd:COG0017 405 LVMWLTGLENIREVIPF 421
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 15-47 2.12e-04

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 42.75  E-value: 2.12e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 90111694   15 NLLKRAAIMAEIRRFFADRGVLEVETPCMSQAT 47
Cdd:PRK00476 140 NLKLRSKVTSAIRNFLDDNGFLEIETPILTKST 172
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 15-41 6.12e-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: 6.12e-04
                        10        20
                ....*....|....*....|....*..
gi 90111694  15 NLLKRAAIMAEIRRFFADRGVLEVETP 41
Cdd:COG0173 141 NLILRHKVTKAIRNYLDENGFLEIETP 167
PTZ00425 PTZ00425
asparagine-tRNA ligase; Provisional
 85-320 1.33e-03

asparagine-tRNA ligase; Provisional


Pssm-ID: 240414 [Multi-domain]  Cd Length: 586  Bit Score: 40.39  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694   85 LVAGCGPVFQLCRSFR--NEEMGRyHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPL 162
Cdd:PTZ00425 339 LCSSMGDVYTFGPTFRaeNSHTSR-HLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNFDDIYYFEENVETGLI 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  163 SADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKE---------KPTFVYHFPASQASLAQISTEDHRVA 233
Cdd:PTZ00425 418 SRLKNILDEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHErfvaeqifkKPVIVYNYPKDLKAFYMKLNEDQKTV 497

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111694  234 ERFEVYYKGI-ELANGFH-----ELTDAREQQQRFEQDNR--KRAARGLPQHPidqnliealkvgmpdCSGVALGVDRLV 305
Cdd:PTZ00425 498 AAMDVLVPKIgEVIGGSQrednlERLDKMIKEKKLNMESYwwYRQLRKFGSHP---------------HAGFGLGFERLI 562

                        250
                 ....*....|....*
gi 90111694  306 MLALGAETLAEVIAF 320
Cdd:PTZ00425 563 MLVTGVDNIKDTIPF 577
 
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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