|
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: 646.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 12 SIPNLLKRAAIMAEIRRFFSDRGVLEVETPCMSQATVTDIHMFPFQTRFVGPGYSQGMDLYLMTSPEYHMKRLLAAGCGP 91
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 92 VFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLECQPAESLSYQQAFLRHLELDPLSADKTQLRE 171
Cdd:PRK09350 81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 172 AAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKDRPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350 161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695766826 252 LTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEV 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: 557.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 11 ASIPNLLKRAAIMAEIRRFFSDRGVLEVETPCMSQATVTDIHMFPFQTRFVGPGySQGMDLYLMTSPEYHMKRLLAAGCG 90
Cdd:COG2269 1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPD-GGGRPLYLHTSPEFAMKRLLAAGSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 91 PVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEC---QPAESLSYQQAFLRHLELDPLSADKT 167
Cdd:COG2269 80 PIYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAagfAPAERLSYQEAFLRYLGIDPLTADLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 168 QLREAAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIGKDRPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELAN 247
Cdd:COG2269 160 ELAAAAAAAGLR--VADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELAN 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695766826 248 GFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEVIA 319
Cdd:COG2269 238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
29-319 |
2.56e-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: 2.56e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 29 FFSDRGVLEVETPCMSQATVTDIHMFPFQTRFVGPGySQGMDLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHH 108
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPD-GQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 109 NPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE--CQPAESLSYQQAFLRHLELDPLSADKTQLREAAAKLDLsnIADTEE 186
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGI--RASEED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 187 DRDTLLQLLFTMGVEPHIGKDRPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDN 266
Cdd:TIGR00462 158 DRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 695766826 267 RKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEVIA 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 |
3.31e-66 |
|
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: 210.90 E-value: 3.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 16 LLKRAAIMAEIRRFFSDRGVLEVETPCMSQ----ATVTdihmfPFQTRFvgpgYSQGMDLYLMTSPEYHMKRLLAAGCGP 91
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPiaggAAAR-----PFITHH----NALDMDLYLRIAPELYLKRLIVGGFER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 92 VFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE-----------------CQPAESLSYQQAFL 154
Cdd:cd00775 79 VYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVTMVDALK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 155 RHLELDPLSADKTQLREAAAKLDLSnIADTEEDRDTLLQLL---FTMGVEPHIGKdrPTFVYHFPASQASLAQISTEDHR 231
Cdd:cd00775 159 EKTGIDFPELDLEQPEELAKLLAKL-IKEKIEKPRTLGKLLdklFEEFVEPTLIQ--PTFIIDHPVEISPLAKRHRSNPG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 232 VAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGA 311
Cdd:cd00775 236 LTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDS 315
|
....*....
gi 695766826 312 ESISEVIAF 320
Cdd:cd00775 316 NSIRDVILF 324
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
15-320 |
5.22e-53 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 176.60 E-value: 5.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 15 NLLKRAAIMAEIRRFFSDRGVLEVETPCMSQATV----TDihmFPFQTRFVGPGYsqgmdlYLMTSPEYHMKRLLAAGCG 90
Cdd:pfam00152 21 NLKLRSKIIKAIRNFLDENGFLEVETPILTKSATpegaRD---FLVPSRALGKFY------ALPQSPQLYKQLLMVAGFD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 91 PVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEcqpaESLSYQQAFLRHLELD-PLSADKTQL 169
Cdd:pfam00152 92 RVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFK----EVEGIAKELEGGTLLDlKKPFPRITY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 170 REAAAKLDLSNIADTEEDRDTlLQLLFTMGVEPHIGKDRPTFVYHFPASQASL-AQISTEDHRVAERFEVYYKGIELANG 248
Cdd:pfam00152 168 AEAIEKLNGKDVEELGYGSDK-PDLRFLLELVIDKNKFNPLWVTDFPAEHHPFtMPKDEDDPALAEAFDLVLNGVEIGGG 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695766826 249 FHELTDAREQQQRFEQDNRKRAArglpQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEVIAF 320
Cdd:pfam00152 247 SIRIHDPELQEERFEEQGLDPEE----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: 646.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 12 SIPNLLKRAAIMAEIRRFFSDRGVLEVETPCMSQATVTDIHMFPFQTRFVGPGYSQGMDLYLMTSPEYHMKRLLAAGCGP 91
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 92 VFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLECQPAESLSYQQAFLRHLELDPLSADKTQLRE 171
Cdd:PRK09350 81 IFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCEPAESLSYQQAFLRYLGIDPLSADKTQLRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 172 AAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKDRPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHE 251
Cdd:PRK09350 161 VAAKLGLSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695766826 252 LTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEV 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: 557.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 11 ASIPNLLKRAAIMAEIRRFFSDRGVLEVETPCMSQATVTDIHMFPFQTRFVGPGySQGMDLYLMTSPEYHMKRLLAAGCG 90
Cdd:COG2269 1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPD-GGGRPLYLHTSPEFAMKRLLAAGSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 91 PVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEC---QPAESLSYQQAFLRHLELDPLSADKT 167
Cdd:COG2269 80 PIYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAagfAPAERLSYQEAFLRYLGIDPLTADLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 168 QLREAAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIGKDRPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELAN 247
Cdd:COG2269 160 ELAAAAAAAGLR--VADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELAN 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695766826 248 GFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEVIA 319
Cdd:COG2269 238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
29-319 |
2.56e-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: 2.56e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 29 FFSDRGVLEVETPCMSQATVTDIHMFPFQTRFVGPGySQGMDLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHH 108
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPD-GQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 109 NPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE--CQPAESLSYQQAFLRHLELDPLSADKTQLREAAAKLDLsnIADTEE 186
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLGdpFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGI--RASEED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 187 DRDTLLQLLFTMGVEPHIGKDRPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDN 266
Cdd:TIGR00462 158 DRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 695766826 267 RKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEVIA 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 |
3.31e-66 |
|
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: 210.90 E-value: 3.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 16 LLKRAAIMAEIRRFFSDRGVLEVETPCMSQ----ATVTdihmfPFQTRFvgpgYSQGMDLYLMTSPEYHMKRLLAAGCGP 91
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPiaggAAAR-----PFITHH----NALDMDLYLRIAPELYLKRLIVGGFER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 92 VFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE-----------------CQPAESLSYQQAFL 154
Cdd:cd00775 79 VYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKkingktkieyggkeldfTPPFKRVTMVDALK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 155 RHLELDPLSADKTQLREAAAKLDLSnIADTEEDRDTLLQLL---FTMGVEPHIGKdrPTFVYHFPASQASLAQISTEDHR 231
Cdd:cd00775 159 EKTGIDFPELDLEQPEELAKLLAKL-IKEKIEKPRTLGKLLdklFEEFVEPTLIQ--PTFIIDHPVEISPLAKRHRSNPG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 232 VAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGA 311
Cdd:cd00775 236 LTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDS 315
|
....*....
gi 695766826 312 ESISEVIAF 320
Cdd:cd00775 316 NSIRDVILF 324
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
16-320 |
1.77e-62 |
|
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: 206.04 E-value: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 16 LLKRAAIMAEIRRFFSDRGVLEVETPcMSQ-----ATVTdihmfPFQTrfvgpgYSQ--GMDLYLMTSPEYHMKRLLAAG 88
Cdd:COG1190 174 FRKRSKIIRAIRRFLDERGFLEVETP-MLQpiaggAAAR-----PFIT------HHNalDMDLYLRIAPELYLKRLIVGG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 89 CGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQV---------LECQ--------PAESLSYQQ 151
Cdd:COG1190 242 FERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAaeavlgttkVTYQgqeidlspPWRRITMVE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 152 AFLRHLELDPLS-ADKTQLREAAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIgkDRPTFVYHFPASQASLAQISTEDH 230
Cdd:COG1190 322 AIKEATGIDVTPlTDDEELRALAKELGIE--VDPGWGRGKLIDELFEELVEPKL--IQPTFVTDYPVEVSPLAKRHRDDP 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 231 RVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALG 310
Cdd:COG1190 398 GLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTD 477
|
330
....*....|
gi 695766826 311 AESISEVIAF 320
Cdd:COG1190 478 SPSIRDVILF 487
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
17-320 |
9.07e-62 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 204.17 E-value: 9.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 17 LKRAAIMAEIRRFFSDRGVLEVETPcMSQ-----ATVTdihmfPFQTRFvgpgYSQGMDLYLMTSPEYHMKRLLAAGCGP 91
Cdd:PRK00484 173 RKRSKIISAIRRFLDNRGFLEVETP-MLQpiaggAAAR-----PFITHH----NALDIDLYLRIAPELYLKRLIVGGFER 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 92 VFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE-----------------CQPAESLSYQQAFL 154
Cdd:PRK00484 243 VYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQavlgttkvtyqgteidfGPPFKRLTMVDAIK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 155 RHLELDPLSADKTQLREAAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIgkDRPTFVYHFPASQASLAQISTEDHRVAE 234
Cdd:PRK00484 323 EYTGVDFDDMTDEEARALAKELGIE--VEKSWGLGKLINELFEEFVEPKL--IQPTFITDYPVEISPLAKRHREDPGLTE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 235 RFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESI 314
Cdd:PRK00484 399 RFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSI 478
|
....*.
gi 695766826 315 SEVIAF 320
Cdd:PRK00484 479 RDVILF 484
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
16-320 |
4.25e-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: 4.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 16 LLKRAAIMAEIRRFFSDRGVLEVETPCMsQATVTDIHMFPFQTRFvgpgYSQGMDLYLMTSPEYHMKRLLAAGCGPVFQL 95
Cdd:TIGR00499 172 FLKRSKIIKAIRRFLDDRGFIEVETPML-QSIPGGANAKPFITHH----NALDMDLYLRIAPELYLKRLIVGGLEKVYEI 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 96 CRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEC-----------------QPAESLSYQQAFLRHLE 158
Cdd:TIGR00499 247 GRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKEllgtfiinyndleidlkPPWKRITMVDALEMVTG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 159 LDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKdrPTFVYHFPASQASLAQISTEDHRVAERFEV 238
Cdd:TIGR00499 327 IDFDILKDDETAKALAKEHGIEVAEDSLTLGHILNKFFEQFLEHTLIQ--PTFITHYPAEISPLAKRDPSNPEFTERFEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 239 YYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEVI 318
Cdd:TIGR00499 405 FIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIRDVL 484
|
..
gi 695766826 319 AF 320
Cdd:TIGR00499 485 LF 486
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
15-320 |
5.22e-53 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 176.60 E-value: 5.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 15 NLLKRAAIMAEIRRFFSDRGVLEVETPCMSQATV----TDihmFPFQTRFVGPGYsqgmdlYLMTSPEYHMKRLLAAGCG 90
Cdd:pfam00152 21 NLKLRSKIIKAIRNFLDENGFLEVETPILTKSATpegaRD---FLVPSRALGKFY------ALPQSPQLYKQLLMVAGFD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 91 PVFQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEcqpaESLSYQQAFLRHLELD-PLSADKTQL 169
Cdd:pfam00152 92 RVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFK----EVEGIAKELEGGTLLDlKKPFPRITY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 170 REAAAKLDLSNIADTEEDRDTlLQLLFTMGVEPHIGKDRPTFVYHFPASQASL-AQISTEDHRVAERFEVYYKGIELANG 248
Cdd:pfam00152 168 AEAIEKLNGKDVEELGYGSDK-PDLRFLLELVIDKNKFNPLWVTDFPAEHHPFtMPKDEDDPALAEAFDLVLNGVEIGGG 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695766826 249 FHELTDAREQQQRFEQDNRKRAArglpQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEVIAF 320
Cdd:pfam00152 247 SIRIHDPELQEERFEEQGLDPEE----AEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAF 314
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
18-320 |
1.86e-48 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 170.17 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 18 KRAAIMAEIRRFFSDRGVLEVETPCM-SQATVTDIHmfPFQTRFvgpgYSQGMDLYLMTSPEYHMKRLLAAGCGPVFQLC 96
Cdd:PLN02502 231 TRAKIISYIRRFLDDRGFLEVETPMLnMIAGGAAAR--PFVTHH----NDLNMDLYLRIATELHLKRLVVGGFERVYEIG 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 97 RSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQ-VLECQPAESLSYQ-------QAFLRhleldplsADKTQ 168
Cdd:PLN02502 305 RQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGmVKELTGSYKIKYHgieidftPPFRR--------ISMIS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 169 LREAAAKLDLSNIADTEEDRDT--------------------LLQLLFTMGVEPHIGKdrPTFVYHFPASQASLAQiste 228
Cdd:PLN02502 377 LVEEATGIDFPADLKSDEANAYliaacekfdvkcpppqttgrLLNELFEEFLEETLVQ--PTFVLDHPVEMSPLAK---- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 229 DHR----VAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRV 304
Cdd:PLN02502 451 PHRskpgLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRL 530
|
330
....*....|....*.
gi 695766826 305 VMLALGAESISEVIAF 320
Cdd:PLN02502 531 VMLLTDSASIRDVIAF 546
|
|
| 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 |
1.29e-42 |
|
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: 148.01 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 19 RAAIMAEIRRFFSDRGVLEVETPcMSQATVTDIHMFPFQTrfvgPGYSQGMDLYLMTSPEYHMKRLLAAGCGPVFQLCRS 98
Cdd:cd00669 4 RSKIIKAIRDFMDDRGFLEVETP-MLQKITGGAGARPFLV----KYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 99 FRNEEMGRHHNPEFTMLEWYRPCYDMYRLI--NE--VDDLLQQVLEcqpaeslSYQQAFLRHLELDPLSADKTQLREAAA 174
Cdd:cd00669 79 FRNEDLRARHQPEFTMMDLEMAFADYEDVIelTErlVRHLAREVLG-------VTAVTYGFELEDFGLPFPRLTYREALE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 175 KLdlsniadteedrdtllqllftmgvephigkDRPTFVYHFPASQAS-LAQISTEDHRVAERFEVYYKGIELANGFHELT 253
Cdd:cd00669 152 RY------------------------------GQPLFLTDYPAEMHSpLASPHDVNPEIADAFDLFINGVEVGNGSSRLH 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695766826 254 DAREQQQRFEQDNRKRAArglpQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEVIAFTVDRA 325
Cdd:cd00669 202 DPDIQAEVFQEQGINKEA----GMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
15-320 |
1.76e-42 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 156.66 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 15 NLLKRAAIMAEIRRFFSDRGVLEVETPCMSQatvtdIH----MFPFQTRFvgPGYsqGMDLYLMTSPEYHMKRLLAAGCG 90
Cdd:PRK02983 769 LLRARSAVVRAVRETLVARGFLEVETPILQQ-----VHgganARPFVTHI--NAY--DMDLYLRIAPELYLKRLCVGGVE 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 91 PVFQLCRSFRNEEMGRHHNPEFTMLEWYRPC--YDMYR-----LINEV---------------DDLLQQVLECQPAESLS 148
Cdd:PRK02983 840 RVFELGRNFRNEGVDATHNPEFTLLEAYQAHadYDTMRdltreLIQNAaqaahgapvvmrpdgDGVLEPVDISGPWPVVT 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 149 YQQAFLRHL--ELDPlSADKTQLREAAAKLDLSniADTEEDRDTLLQLLFTMGVEPHIgkDRPTFVYHFPASQASLAQIS 226
Cdd:PRK02983 920 VHDAVSEALgeEIDP-DTPLAELRKLCDAAGIP--YRTDWDAGAVVLELYEHLVEDRT--TFPTFYTDFPTSVSPLTRPH 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 227 TEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKrAARGLPQ-QPIDRNLLDALAAGLPDCSGVALGVDRVV 305
Cdd:PRK02983 995 RSDPGLAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLL-AAGGDPEaMELDEDFLQALEYAMPPTGGLGMGVDRLV 1073
|
330
....*....|....*
gi 695766826 306 MLALGAeSISEVIAF 320
Cdd:PRK02983 1074 MLLTGR-SIRETLPF 1087
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
19-324 |
1.28e-39 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 145.59 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 19 RAAIMAEIRRFFSDRGVLEVETPCMsQATVTDIHMFPFQTRFvgpgYSQGMDLYLMTSPEYHMKRLLAAGCGPVFQLCRS 98
Cdd:PRK12445 187 RSKILAAIRQFMVARGFMEVETPMM-QVIPGGASARPFITHH----NALDLDMYLRIAPELYLKRLVVGGFERVFEINRN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 99 FRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLL----QQVLEC-------------QPAESLSYQQAFLRHL-ELD 160
Cdd:PRK12445 262 FRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFrtlaQEVLGTtkvtygehvfdfgKPFEKLTMREAIKKYRpETD 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 161 PLSADKTQlreaAAKLDLSNIADTEEDRDTLLQL---LFTMGVEPHIgkDRPTFVYHFPASQASLAQISTEDHRVAERFE 237
Cdd:PRK12445 342 MADLDNFD----AAKALAESIGITVEKSWGLGRIvteIFDEVAEAHL--IQPTFITEYPAEVSPLARRNDVNPEITDRFE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 238 VYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVMLALGAESISEV 317
Cdd:PRK12445 416 FFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDV 495
|
....*..
gi 695766826 318 IAFTVDR 324
Cdd:PRK12445 496 ILFPAMR 502
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
13-324 |
3.91e-36 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 137.47 E-value: 3.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 13 IPNLLKRAAIMAEIRRFFSDRGVLEVETPCMsQATVTDIHMFPFQTRFvgpgYSQGMDLYLMTSPEYHMKRLLAAGCGPV 92
Cdd:PTZ00385 230 IETIKKRHVMLQALRDYFNERNFVEVETPVL-HTVASGANAKSFVTHH----NANAMDLFLRVAPELHLKQCIVGGMERI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 93 FQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQ---------VLECQPAES------LSYQQAFLR-- 155
Cdd:PTZ00385 305 YEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQlamrvngttVVQIYPENAhgnpvtVDLGKPFRRvs 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 156 ---------HLELDP---LSADKTQLREAAAKL----DLSNIADTEEDRDTLLQLLFTMGVEphigkdRPTFVYHFPASQ 219
Cdd:PTZ00385 385 vydeiqrmsGVEFPPpneLNTPKGIAYMSVVMLryniPLPPVRTAAKMFEKLIDFFITDRVV------EPTFVMDHPLFM 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 220 ASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVAL 299
Cdd:PTZ00385 459 SPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGM 538
|
330 340
....*....|....*....|....*
gi 695766826 300 GVDRVVMLALGAESISEVIAFTVDR 324
Cdd:PTZ00385 539 GIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
16-324 |
3.92e-30 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 120.11 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 16 LLKRAAIMAEIRRFFSDRGVLEVETPCMSqATVTDIHMFPFQTRFvgpgYSQGMDLYLMTSPEYHMKRLLAAGCGPVFQL 95
Cdd:PTZ00417 253 FITRTKIINYLRNFLNDRGFIEVETPTMN-LVAGGANARPFITHH----NDLDLDLYLRIATELPLKMLIVGGIDKVYEI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 96 CRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQ-VLECQPAESLSYQQaflRHLELDPLSAD------KTQ 168
Cdd:PTZ00417 328 GKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQlVMHLFGTYKILYNK---DGPEKDPIEIDftppypKVS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 169 LREAAAKLD---LSNIADTEEDRDTLLQLLFTMGVE----PHIGK---------------DRPTFVYHFPASQASLAQIS 226
Cdd:PTZ00417 405 IVEELEKLTntkLEQPFDSPETINKMINLIKENKIEmpnpPTAAKlldqlashfienkypNKPFFIIEHPQIMSPLAKYH 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 227 TEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDRNLLDALAAGLPDCSGVALGVDRVVM 306
Cdd:PTZ00417 485 RSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITM 564
|
330
....*....|....*...
gi 695766826 307 LALGAESISEVIAFTVDR 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 |
7.66e-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: 73.38 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 16 LLKRAAIMAEIRRFFSDRGVLEVETPCMSQATVTDIHMFPFQTRfVGPG--YSqgmdlyLMTSPEYHMKRLLAAGCGPVF 93
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSR-LHPGkfYA------LPQSPQLFKQLLMVSGFDRYF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 94 QLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLE-------CQPAESLSYQQAFLRH---------- 156
Cdd:cd00777 74 QIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKevlgvelTTPFPRMTYAEAMERYgfkflwivdf 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 157 --LELDPlsadktqlreaaakldlsniadtEEDRDTLLQLLFTMgvePHiGKDRPTFvyhfpasqaslaQISTEDHRvAE 234
Cdd:cd00777 154 plFEWDE-----------------------EEGRLVSAHHPFTA---PK-EEDLDLL------------EKDPEDAR-AQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 235 RFEVYYKGIELANGFHELTDAREQQQRFEQdnrkraaRGLPQQPIDRN---LLDALAAGLPDCSGVALGVDRVVMLALGA 311
Cdd:cd00777 194 AYDLVLNGVELGGGSIRIHDPDIQEKVFEI-------LGLSEEEAEEKfgfLLEAFKYGAPPHGGIALGLDRLVMLLTGS 266
|
....*....
gi 695766826 312 ESISEVIAF 320
Cdd:cd00777 267 ESIRDVIAF 275
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
15-325 |
7.78e-11 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 63.08 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 15 NLLKRAAIMAEIRRFFSDRGVLEVETPCMSQATvtdihmfPFQTR-FVGPGYSQGMDLY-LMTSPEYHMKRLLAAGCGPV 92
Cdd:PRK12820 155 HLAKRHRIIKCARDFLDSRGFLEIETPILTKST-------PEGARdYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 93 FQLCRSFRNEEMGRHHNPEFTMLEWYRPCYDMYRLINEVDDLLQQVLEC------QPAESLSYQQAF------------- 153
Cdd:PRK12820 228 FQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFAIggialpRPFPRMPYAEAMdttgsdrpdlrfd 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 154 LRHLEL-------------------------------DPLSADKTQ------------------LREAAAKLDlSNIAD- 183
Cdd:PRK12820 308 LKFADAtdifentrygifkqilqrggrikginikgqsEKLSKNVLQneyakeiapsfgakgmtwMRAEAGGLD-SNIVQf 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 184 -TEEDRDTLLQL-------LFTMGVEP--------------HIGkDR----------PTFVYHFPASQASLAQISTEDHR 231
Cdd:PRK12820 387 fSADEKEALKRRfhaedgdVIIMIADAscaivlsalgqlrlHLA-DRlglipegvfhPLWITDFPLFEATDDGGVTSSHH 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 232 V---------------------AERFEVYYKGIELANGFHELTDAREQQQRFeqdnrkrAARGLPQQPIDRN---LLDAL 287
Cdd:PRK12820 466 PftapdredfdpgdieelldlrSRAYDLVVNGEELGGGSIRINDKDIQLRIF-------AALGLSEEDIEDKfgfFLRAF 538
|
410 420 430
....*....|....*....|....*....|....*...
gi 695766826 288 AAGLPDCSGVALGVDRVVMLALGAESISEVIAFTVDRA 325
Cdd:PRK12820 539 DFAAPPHGGIALGLDRVVSMILQTPSIREVIAFPKNRS 576
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
19-119 |
1.79e-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: 56.74 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 19 RAAIMAEIRRFFSDRGVLEVETPCMSQATV--TDIHMFPfqtRFVGPGYSQGMDLYLMTSPEYHMKRLLAAGCGP----V 92
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLleKAGHEPK---DLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKlplrL 78
|
90 100
....*....|....*....|....*....
gi 695766826 93 FQLCRSFRNEEMGRH--HNPEFTMLEWYR 119
Cdd:cd00768 79 AEIGPAFRNEGGRRGlrRVREFTQLEGEV 107
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
15-181 |
1.93e-09 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 58.65 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 15 NLLKRAAIMAEIRRFFSDR-GVLEVETPCMSQATVTDIHMFPFQTRfVGPGysqgmDLY-LMTSPEYHMKRLLAAGCGPV 92
Cdd:PLN02903 202 NLRLRHRVVKLIRRYLEDVhGFVEIETPILSRSTPEGARDYLVPSR-VQPG-----TFYaLPQSPQLFKQMLMVSGFDRY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 93 FQLCRSFRNEEMGRHHNPEFTMLEW---YRPCYDMYRLiNEvdDLLQQVLE-------CQPAESLSYQQAflrhleLDPL 162
Cdd:PLN02903 276 YQIARCFRDEDLRADRQPEFTQLDMelaFTPLEDMLKL-NE--DLIRQVFKeikgvqlPNPFPRLTYAEA------MSKY 346
|
170
....*....|....*....
gi 695766826 163 SADKTQLREAAAKLDLSNI 181
Cdd:PLN02903 347 GSDKPDLRYGLELVDVSDV 365
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
283-320 |
4.53e-08 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 54.30 E-value: 4.53e-08
10 20 30
....*....|....*....|....*....|....*...
gi 695766826 283 LLDALAAGLPDCSGVALGVDRVVMLALGAESISEVIAF 320
Cdd:PRK00476 518 LLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAF 555
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
283-320 |
8.42e-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: 8.42e-08
10 20 30
....*....|....*....|....*....|....*...
gi 695766826 283 LLDALAAGLPDCSGVALGVDRVVMLALGAESISEVIAF 320
Cdd:COG0173 517 LLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
5-320 |
1.26e-05 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 46.17 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 5 ATWQPSASIPNLLK-RAAIMAEIRRFFSDRGVLEVETPCMSQAT------VTDIHMFPFQTRFvgpgYsqGMDLYLMTSP 77
Cdd:PRK06462 18 WKHISSEKYRKVLKvQSSILRYTREFLDGRGFVEVLPPIISPSTdplmglGSDLPVKQISIDF----Y--GVEYYLADSM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 78 EYHmKRLLAAGCGPVFQLCRSFRNEE----MGRHHNpEFTMLEW---YRPCYDMYRLINE-VDDLLQQVLECQPAEsLSY 149
Cdd:PRK06462 92 ILH-KQLALRMLGKIFYLSPNFRLEPvdkdTGRHLY-EFTQLDIeieGADLDEVMDLIEDlIKYLVKELLEEHEDE-LEF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 150 QQAFLRHLE-----LDPLSADKTQLREAAAKLDLSNIADTEEdrdTLLQLLFtmgvephigkDRPTFVYHFPASQASLAQ 224
Cdd:PRK06462 169 FGRDLPHLKrpfkrITHKEAVEILNEEGCRGIDLEELGSEGE---KSLSEHF----------EEPFWIIDIPKGSREFYD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766826 225 ISTEDHR-VAERFEVYYkgielANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIdRNLLDALAAGLPDCSGVALGVDR 303
Cdd:PRK06462 236 REDPERPgVLRNYDLLL-----PEGYGEAVSGGEREYEYEEIVERIREHGVDPEKY-KWYLEMAKEGPLPSAGFGIGVER 309
|
330
....*....|....*..
gi 695766826 304 VVMLALGAESISEVIAF 320
Cdd:PRK06462 310 LTRYICGLRHIREVQPF 326
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
15-47 |
1.71e-04 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 43.13 E-value: 1.71e-04
10 20 30
....*....|....*....|....*....|...
gi 695766826 15 NLLKRAAIMAEIRRFFSDRGVLEVETPCMSQAT 47
Cdd:PRK00476 140 NLKLRSKVTSAIRNFLDDNGFLEIETPILTKST 172
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
15-41 |
3.30e-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: 42.29 E-value: 3.30e-04
10 20
....*....|....*....|....*..
gi 695766826 15 NLLKRAAIMAEIRRFFSDRGVLEVETP 41
Cdd:COG0173 141 NLILRHKVTKAIRNYLDENGFLEIETP 167
|
|
| |
