|
Name |
Accession |
Description |
Interval |
E-value |
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
31-328 |
1.98e-161 |
|
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: 452.64 E-value: 1.98e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVHLQAFRTERIGVDGVVTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSARHA 110
Cdd:COG2269 19 FFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKVFRNGERGRRHN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 111 AEFTMLEWYRPGSSMTDLIAETMELLCSVLPPVVSsggvitriEEPEILTVAEAFTRYTGADVL-ATADNAPALSEAAGV 189
Cdd:COG2269 99 PEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGF--------APAERLSYQEAFLRYLGIDPLtADLDELAAAAAAAGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 190 RLREGEGWEDLFFRLLLDRIEPHLGRERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELANAFVELTDAEEQRR 269
Cdd:COG2269 171 RVADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELANGFHELTDAAEQRR 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 644460963 270 RFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQW 328
Cdd:COG2269 251 RFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
31-328 |
5.15e-159 |
|
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: 445.84 E-value: 5.15e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVHLQAFRTERIGVDGVVTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSARHA 110
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 111 AEFTMLEWYRPGSSMTDLIAETMELLCSVLPpvvssggviTRIEEPEILTVAEAFTRYTGADVL-ATADNAPALSEAAGV 189
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------DPFAPAERLSYQEAFLRYAGIDPLtASLAELQAAAAAHGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 190 RLREGEGWEDLFFRLLLDRIEPHLGRERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELANAFVELTDAEEQRR 269
Cdd:TIGR00462 152 RASEEDDRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRR 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 644460963 270 RFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQW 328
Cdd:TIGR00462 232 RFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
31-326 |
7.55e-109 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 319.57 E-value: 7.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVHLQAFRTERIG---VDGVvtPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSA 107
Cdd:PRK09350 18 FFADRGVLEVETPILSQATVTDIHLVPFETRFVGpgaSQGK--TLWLMTSPEYHMKRLLAAGSGPIFQICKSFRNEEAGR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 108 RHAAEFTMLEWYRPGSSMTDLIAETMELLCSVLppvvssggvitRIEEPEILTVAEAFTRYTGADVLaTADNApALSEAA 187
Cdd:PRK09350 96 YHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVL-----------DCEPAESLSYQQAFLRYLGIDPL-SADKT-QLREVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 188 -----GVRLREGEGWEDLFFRLLLDRIEPHLGRERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELANAFVELT 262
Cdd:PRK09350 163 aklglSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHELT 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644460963 263 DAEEQRRRFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:PRK09350 243 DAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
31-326 |
4.56e-56 |
|
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: 185.10 E-value: 4.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVhLQAFRTERIGVDgvvTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNgEG-SARH 109
Cdd:cd00775 21 FLDDRGFLEVETPMLQPIAGGAA-ARPFITHHNALD---MDLYLRIAPELYLKRLIVGGFERVYEIGRNFRN-EGiDLTH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 110 AAEFTMLEWYRPGSSMTDLIAETMELLCSVLPPVvsSGGVITRIEEPEI--------LTVAEAFTRYTGADVLATADNAP 181
Cdd:cd00775 96 NPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKI--NGKTKIEYGGKELdftppfkrVTMVDALKEKTGIDFPELDLEQP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 182 -----ALSEAAGVRLREGEGWEDLFFRLLLDRIEPHLgrERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELAN 256
Cdd:cd00775 174 eelakLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTL--IQPTFIIDHPVEISPLAKRHRSNPGLTERFELFICGKEIAN 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 257 AFVELTDAEEQRRRFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:cd00775 252 AYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDV 321
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
31-330 |
4.61e-47 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 161.19 E-value: 4.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEvhlqafrteriGVDGVVTPLWLHT-------SPEFAMKRLLVAGAGPIFQMARVWRNg 103
Cdd:pfam00152 35 FLDENGFLEVETPILTKSATPE-----------GARDFLVPSRALGkfyalpqSPQLYKQLLMVAGFDRVFQIARCFRD- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 104 EGS-ARHAAEFTMLEWYRPGSSMTDLIAETMELLCSVLPPVVSSGGVITRIEEPEI------LTVAEAFTRYTGADVlat 176
Cdd:pfam00152 103 EDLrTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLkkpfprITYAEAIEKLNGKDV--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 177 adnapalseaagVRLREGEGWEDLFFRLLLDRIEphlGRERPTFLTHWPVAQAALARP-CPNDPRVAERFELFVCGIELA 255
Cdd:pfam00152 180 ------------EELGYGSDKPDLRFLLELVIDK---NKFNPLWVTDFPAEHHPFTMPkDEDDPALAEAFDLVLNGVEIG 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644460963 256 NAFVELTDAEEQRRRFlidrsRRQALG-GQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQWLP 330
Cdd:pfam00152 245 GGSIRIHDPELQEERF-----EEQGLDpEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFP 315
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
31-328 |
1.98e-161 |
|
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: 452.64 E-value: 1.98e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVHLQAFRTERIGVDGVVTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSARHA 110
Cdd:COG2269 19 FFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKVFRNGERGRRHN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 111 AEFTMLEWYRPGSSMTDLIAETMELLCSVLPPVVSsggvitriEEPEILTVAEAFTRYTGADVL-ATADNAPALSEAAGV 189
Cdd:COG2269 99 PEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAGF--------APAERLSYQEAFLRYLGIDPLtADLDELAAAAAAAGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 190 RLREGEGWEDLFFRLLLDRIEPHLGRERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELANAFVELTDAEEQRR 269
Cdd:COG2269 171 RVADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARISPDDPRVAERFELYACGVELANGFHELTDAAEQRR 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 644460963 270 RFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQW 328
Cdd:COG2269 251 RFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
31-328 |
5.15e-159 |
|
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: 445.84 E-value: 5.15e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVHLQAFRTERIGVDGVVTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSARHA 110
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 111 AEFTMLEWYRPGSSMTDLIAETMELLCSVLPpvvssggviTRIEEPEILTVAEAFTRYTGADVL-ATADNAPALSEAAGV 189
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLG---------DPFAPAERLSYQEAFLRYAGIDPLtASLAELQAAAAAHGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 190 RLREGEGWEDLFFRLLLDRIEPHLGRERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELANAFVELTDAEEQRR 269
Cdd:TIGR00462 152 RASEEDDRDDLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPRVAERFELYIKGLELANGFHELTDAAEQRR 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 644460963 270 RFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQW 328
Cdd:TIGR00462 232 RFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
31-326 |
7.55e-109 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 319.57 E-value: 7.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVHLQAFRTERIG---VDGVvtPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSA 107
Cdd:PRK09350 18 FFADRGVLEVETPILSQATVTDIHLVPFETRFVGpgaSQGK--TLWLMTSPEYHMKRLLAAGSGPIFQICKSFRNEEAGR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 108 RHAAEFTMLEWYRPGSSMTDLIAETMELLCSVLppvvssggvitRIEEPEILTVAEAFTRYTGADVLaTADNApALSEAA 187
Cdd:PRK09350 96 YHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVL-----------DCEPAESLSYQQAFLRYLGIDPL-SADKT-QLREVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 188 -----GVRLREGEGWEDLFFRLLLDRIEPHLGRERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELANAFVELT 262
Cdd:PRK09350 163 aklglSNIADEEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHELT 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644460963 263 DAEEQRRRFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:PRK09350 243 DAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
31-326 |
1.91e-59 |
|
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440803 [Multi-domain] Cd Length: 495 Bit Score: 198.33 E-value: 1.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPcaVLAPGE--------EVHLQAFrterigvDgvvTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRN 102
Cdd:COG1190 187 FLDERGFLEVETP--MLQPIAggaaarpfITHHNAL-------D---MDLYLRIAPELYLKRLIVGGFERVFEIGRNFRN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 103 gEG-SARHAAEFTMLEWYRPGSSMTDLIAETMELLCSVL-----PPVVSSGGVITRIEEP-EILTVAEAFTRYTGADV-- 173
Cdd:COG1190 255 -EGiDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAeavlgTTKVTYQGQEIDLSPPwRRITMVEAIKEATGIDVtp 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 174 LATADNAPALSEAAGVRLREGEGWEDLFFRLLLDRIEPHLgrERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIE 253
Cdd:COG1190 334 LTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKL--IQPTFVTDYPVEVSPLAKRHRDDPGLTERFELFIAGRE 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644460963 254 LANAFVELTDAEEQRRRFLiDRSRRQALG-GQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:COG1190 412 IANAFSELNDPIDQRERFE-EQLELKAAGdDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDV 484
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
31-326 |
4.95e-59 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 197.23 E-value: 4.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPcaVLAP---GEE-----VHLQAFrterigvDgvvTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRN 102
Cdd:PRK00484 185 FLDNRGFLEVETP--MLQPiagGAAarpfiTHHNAL-------D---IDLYLRIAPELYLKRLIVGGFERVYEIGRNFRN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 103 gEG-SARHAAEFTMLEWYRPGSSMTDLIAETMELLCSVL-----PPVVSSGGVITRIEEP-EILTVAEAFTRYTGADVLA 175
Cdd:PRK00484 253 -EGiDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAqavlgTTKVTYQGTEIDFGPPfKRLTMVDAIKEYTGVDFDD 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 176 -TADNAPALSEAAGVRLREGEGWEDL---FFRLLldrIEPHLgrERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCG 251
Cdd:PRK00484 332 mTDEEARALAKELGIEVEKSWGLGKLineLFEEF---VEPKL--IQPTFITDYPVEISPLAKRHREDPGLTERFELFIGG 406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644460963 252 IELANAFVELTDAEEQRRRFLiDRSRRQALGGQ-TWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:PRK00484 407 REIANAFSELNDPIDQRERFE-AQVEAKEAGDDeAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDV 481
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
31-326 |
4.56e-56 |
|
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: 185.10 E-value: 4.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVhLQAFRTERIGVDgvvTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNgEG-SARH 109
Cdd:cd00775 21 FLDDRGFLEVETPMLQPIAGGAA-ARPFITHHNALD---MDLYLRIAPELYLKRLIVGGFERVYEIGRNFRN-EGiDLTH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 110 AAEFTMLEWYRPGSSMTDLIAETMELLCSVLPPVvsSGGVITRIEEPEI--------LTVAEAFTRYTGADVLATADNAP 181
Cdd:cd00775 96 NPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKI--NGKTKIEYGGKELdftppfkrVTMVDALKEKTGIDFPELDLEQP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 182 -----ALSEAAGVRLREGEGWEDLFFRLLLDRIEPHLgrERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELAN 256
Cdd:cd00775 174 eelakLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTL--IQPTFIIDHPVEISPLAKRHRSNPGLTERFELFICGKEIAN 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 257 AFVELTDAEEQRRRFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:cd00775 252 AYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDV 321
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
31-330 |
3.90e-55 |
|
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: 187.19 E-value: 3.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEeVHLQAFRTERIGVDGvvtPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNgEG-SARH 109
Cdd:TIGR00499 185 FLDDRGFIEVETPMLQSIPGG-ANAKPFITHHNALDM---DLYLRIAPELYLKRLIVGGLEKVYEIGRVFRN-EGvDTTH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 110 AAEFTMLEWYRPGSSMTDLIAETMELLCSVLPPVVSSGGVITRIEE-----P-EILTVAEAFTRYTGA--DVLATADNAP 181
Cdd:TIGR00499 260 NPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYNDLEidlkpPwKRITMVDALEMVTGIdfDILKDDETAK 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 182 ALSEAAGVRLREGEgwedLFFRLLLDRIEPHLGRER---PTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELANAF 258
Cdd:TIGR00499 340 ALAKEHGIEVAEDS----LTLGHILNKFFEQFLEHTliqPTFITHYPAEISPLAKRDPSNPEFTERFELFIAGKEIANAY 415
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644460963 259 VELTDAEEQRRRFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQWLP 330
Cdd:TIGR00499 416 SELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIRDVLLFP 487
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
31-330 |
4.61e-47 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 161.19 E-value: 4.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEvhlqafrteriGVDGVVTPLWLHT-------SPEFAMKRLLVAGAGPIFQMARVWRNg 103
Cdd:pfam00152 35 FLDENGFLEVETPILTKSATPE-----------GARDFLVPSRALGkfyalpqSPQLYKQLLMVAGFDRVFQIARCFRD- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 104 EGS-ARHAAEFTMLEWYRPGSSMTDLIAETMELLCSVLPPVVSSGGVITRIEEPEI------LTVAEAFTRYTGADVlat 176
Cdd:pfam00152 103 EDLrTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGTLLDLkkpfprITYAEAIEKLNGKDV--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 177 adnapalseaagVRLREGEGWEDLFFRLLLDRIEphlGRERPTFLTHWPVAQAALARP-CPNDPRVAERFELFVCGIELA 255
Cdd:pfam00152 180 ------------EELGYGSDKPDLRFLLELVIDK---NKFNPLWVTDFPAEHHPFTMPkDEDDPALAEAFDLVLNGVEIG 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644460963 256 NAFVELTDAEEQRRRFlidrsRRQALG-GQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQWLP 330
Cdd:pfam00152 245 GGSIRIHDPELQEERF-----EEQGLDpEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFP 315
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
31-326 |
1.03e-42 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 154.76 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVhLQAFRTER--IGVDgvvtpLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNgEG-SA 107
Cdd:PLN02502 242 FLDDRGFLEVETPMLNMIAGGAA-ARPFVTHHndLNMD-----LYLRIATELHLKRLVVGGFERVYEIGRQFRN-EGiST 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 108 RHAAEFTMLEWYRPGSSMTDLIAETMELLCSVLPPV-----VSSGGVITRIEEPeiltvaeaFTRYTGADVLATA----D 178
Cdd:PLN02502 315 RHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELtgsykIKYHGIEIDFTPP--------FRRISMISLVEEAtgidF 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 179 NAPALSEAAGVRLREGEGWEDLFFRL------LLDRIEPHLGRER---PTFLTHWPVAQAALARPCPNDPRVAERFELFV 249
Cdd:PLN02502 387 PADLKSDEANAYLIAACEKFDVKCPPpqttgrLLNELFEEFLEETlvqPTFVLDHPVEMSPLAKPHRSKPGLTERFELFI 466
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644460963 250 CGIELANAFVELTDAEEQRRRFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:PLN02502 467 NGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDV 543
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
31-320 |
1.68e-42 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 157.05 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPcaVLAPgeeVHLQA----FRTERIGVDgvvTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNgEG- 105
Cdd:PRK02983 783 TLVARGFLEVETP--ILQQ---VHGGAnarpFVTHINAYD---MDLYLRIAPELYLKRLCVGGVERVFELGRNFRN-EGv 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 106 SARHAAEFTMLEWYRPGSSMTDLIAETMELLCS----------VLPPVVSSGGVITRIEEP-EILTVAEAFTRYTGADVL 174
Cdd:PRK02983 854 DATHNPEFTLLEAYQAHADYDTMRDLTRELIQNaaqaahgapvVMRPDGDGVLEPVDISGPwPVVTVHDAVSEALGEEID 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 175 ATADNAP--ALSEAAGVRLREGEGWEDLFFRLLLDRIEPHLgrERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGI 252
Cdd:PRK02983 934 PDTPLAElrKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRT--TFPTFYTDFPTSVSPLTRPHRSDPGLAERWDLVAWGV 1011
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644460963 253 ELANAFVELTDAEEQRRRfLIDRSRRQALGG-QTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGA 320
Cdd:PRK02983 1012 ELGTAYSELTDPVEQRRR-LTEQSLLAAGGDpEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLTGR 1079
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
31-330 |
1.21e-41 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 151.37 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEeVHLQAFRTERIGVDgvvTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSARHA 110
Cdd:PRK12445 197 FMVARGFMEVETPMMQVIPGG-ASARPFITHHNALD---LDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 111 AEFTMLEWYRPGSSMTDLIAETMELLCSVLPPV-----VSSGGVITRIEEP-EILTVAEAFTRYTGADVLATADN---AP 181
Cdd:PRK12445 273 PEFTMMELYMAYADYHDLIELTESLFRTLAQEVlgttkVTYGEHVFDFGKPfEKLTMREAIKKYRPETDMADLDNfdaAK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 182 ALSEAAGVRLREGEGWEDLFFRLLLDRIEPHLgrERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGIELANAFVEL 261
Cdd:PRK12445 353 ALAESIGITVEKSWGLGRIVTEIFDEVAEAHL--IQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSEL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644460963 262 TDAEEQRRRFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQWLP 330
Cdd:PRK12445 431 NDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
31-324 |
4.49e-33 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 129.00 E-value: 4.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCA-VLAPGeeVHLQAFRTERigvDGVVTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSARH 109
Cdd:PTZ00385 246 YFNERNFVEVETPVLhTVASG--ANAKSFVTHH---NANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSH 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 110 AAEFTMLEWYRPGSSMTDLIAETMELLCSVlpPVVSSGGVITRIE------EPEILTVAEAFTRYTGADVLATAD----- 178
Cdd:PTZ00385 321 NPEFTSCEFYAAYHTYEDLMPMTEDIFRQL--AMRVNGTTVVQIYpenahgNPVTVDLGKPFRRVSVYDEIQRMSgvefp 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 179 -----NAP-ALSEAAGVRLR----------EGEGWEDLFFRLLLDRIEphlgreRPTFLTHWPVAQAALARPCPNDPRVA 242
Cdd:PTZ00385 399 ppnelNTPkGIAYMSVVMLRyniplppvrtAAKMFEKLIDFFITDRVV------EPTFVMDHPLFMSPLAKEQVSRPGLA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 243 ERFELFVCGIELANAFVELTDAEEQRRRF---LIDrsrRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASG 319
Cdd:PTZ00385 473 ERFELFVNGIEYCNAYSELNDPHEQYHRFqqqLVD---RQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTN 549
|
....*
gi 644460963 320 ADRIQ 324
Cdd:PTZ00385 550 SSNIR 554
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
31-330 |
6.87e-33 |
|
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: 122.97 E-value: 6.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETP-CAVLAPGEEVHLQAFRTERIGVDgvvtpLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSARH 109
Cdd:cd00669 14 FMDDRGFLEVETPmLQKITGGAGARPFLVKYNALGLD-----YYLRISPQLFKKRLMVGGLDRVFEINRNFRNEDLRARH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 110 AAEFTMLEWYrpgssmtdliaetmellcsvlppvvssggvITRIEEPEILTVAEAFTRYTGADVLATAdnapalseaAGV 189
Cdd:cd00669 89 QPEFTMMDLE------------------------------MAFADYEDVIELTERLVRHLAREVLGVT---------AVT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 190 RLREGEGWEDLFFRLLLDRIEPHLGRerPTFLTHWPV-AQAALARPCPNDPRVAERFELFVCGIELANAFVELTDAEEQR 268
Cdd:cd00669 130 YGFELEDFGLPFPRLTYREALERYGQ--PLFLTDYPAeMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLHDPDIQA 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644460963 269 RRFLiDRSRRQALGGQTwplDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQWLP 330
Cdd:cd00669 208 EVFQ-EQGINKEAGMEY---FEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFP 265
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
31-330 |
4.33e-25 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 105.86 E-value: 4.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEeVHLQAFRTERIGVDgvvTPLWLHTSPEFAMKRLLVAGAGPIFQMARVWRNGEGSARHA 110
Cdd:PTZ00417 266 FLNDRGFIEVETPTMNLVAGG-ANARPFITHHNDLD---LDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 111 AEFTMLEWYRPGSSMTDLIAETMELLCSVLPPVVSSGGVITRIEEPE-------------ILTVAEAFTRYTGADVLATA 177
Cdd:PTZ00417 342 PEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDGPEkdpieidftppypKVSIVEELEKLTNTKLEQPF 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 178 DNAPALSEAAG-VRLREGEGWEDLFFRLLLDRIEPHLGR----ERPTFLTHWPVAQAALARPCPNDPRVAERFELFVCGI 252
Cdd:PTZ00417 422 DSPETINKMINlIKENKIEMPNPPTAAKLLDQLASHFIEnkypNKPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGK 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644460963 253 ELANAFVELTDAEEQRRRFLIDRSRRQALGGQTWPLDEDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQWLP 330
Cdd:PTZ00417 502 EVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
31-330 |
7.05e-08 |
|
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: 53.34 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAP---GEEVhlqaFRTERIGvdgvvTPLWLHTSPEFaMKRLLVAGAGPIFQMARVWRnGEGS- 106
Cdd:cd00776 37 FLRENGFTEVHTPKITSTDtegGAEL----FKVSYFG-----KPAYLAQSPQL-YKEMLIAALERVYEIGPVFR-AEKSn 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 107 -ARHAAEFTMLEwyrpgSSMTdlIAETMELLCSVLPPVVSSggVITRIEE-------------PEILTVAEAFTRYT--- 169
Cdd:cd00776 106 tRRHLSEFWMLE-----AEMA--FIEDYNEVMDLIEELIKY--IFKRVLErcakelelvnqlnRELLKPLEPFPRITyde 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 170 GADVLATADNAPALSeaAGVRL-REGEgwedlffRLLLDRIephlgRERPTFLTHWPVAQAAL-ARPCPNDPRVAERFEL 247
Cdd:cd00776 177 AIELLREKGVEEEVK--WGEDLsTEHE-------RLLGEIV-----KGDPVFVTDYPKEIKPFyMKPDDDNPETVESFDL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 248 FVCGIElanafvELT-------DAEEQRRRFlidrsrrQALGGQTWPLdEDFLAALAFGMPQAAGIAMGFDRLAMLASGA 320
Cdd:cd00776 243 LMPGVG------EIVggsqrihDYDELEERI-------KEHGLDPESF-EWYLDLRKYGMPPHGGFGLGLERLVMWLLGL 308
|
330
....*....|
gi 644460963 321 DRIQQVQWLP 330
Cdd:cd00776 309 DNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
242-326 |
1.18e-05 |
|
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: 46.03 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 242 AERFELFVCGIELANAFVELTDAEEQRRRF---LIDRSRRQALGGQtwpldedFLAALAFGMPQAAGIAMGFDRLAMLAS 318
Cdd:cd00777 192 AQAYDLVLNGVELGGGSIRIHDPDIQEKVFeilGLSEEEAEEKFGF-------LLEAFKYGAPPHGGIALGLDRLVMLLT 264
|
....*...
gi 644460963 319 GADRIQQV 326
Cdd:cd00777 265 GSESIRDV 272
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
31-136 |
3.18e-05 |
|
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: 44.42 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 31 FFEARSYLEVETPCAVLAPGEEVHLQAFRTERIGVDGVVTPLWLHTSPEFAMKRLLVAG--AGP--IFQMARVWRNGEGS 106
Cdd:cd00768 12 FMAELGFQEVETPIVEREPLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHirKLPlrLAEIGPAFRNEGGR 91
|
90 100 110
....*....|....*....|....*....|..
gi 644460963 107 A--RHAAEFTMLEWYRPGssMTDLIAETMELL 136
Cdd:cd00768 92 RglRRVREFTQLEGEVFG--EDGEEASEFEEL 121
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
220-326 |
6.71e-05 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 44.41 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 220 FLTHWPVAqaalARP-----CPNDPRVAERFELFVCGIELAnafvelTDAE-EQRRRFLIDRSRRQALGgqtwPldEDF- 292
Cdd:PRK05159 326 FITDYPSE----KRPfytmpDEDDPEISKSFDLLFRGLEIT------SGGQrIHRYDMLVESIKEKGLN----P--ESFe 389
|
90 100 110
....*....|....*....|....*....|....*.
gi 644460963 293 --LAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:PRK05159 390 fyLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREA 425
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
263-326 |
1.52e-04 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 43.52 E-value: 1.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644460963 263 DAEEQRRRFlidrsrrqalGGqtwpldedFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:PRK00476 507 SEEEAEEKF----------GF--------LLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDV 552
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
108-326 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 108 RHAAEFTMLEwyrPGSSMTDLiAETMELLCSVLPPVVSSggVIT-RIEEPEIL---------TVAEAFTRYTGADVLAta 177
Cdd:COG0017 214 RHLAEFWMIE---PEMAFADL-EDVMDLAEEMLKYIIKY--VLEnCPEELEFLgrdverlekVPESPFPRITYTEAIE-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 178 dnapaLSEAAGVRLREGE--GWEDLffRLLLDRIEphlgrERPTFLTHWPVAQAAL-ARPCPNDPRVAERFELFVCGI-E 253
Cdd:COG0017 286 -----ILKKSGEKVEWGDdlGTEHE--RYLGEEFF-----KKPVFVTDYPKEIKAFyMKPNPDDPKTVAAFDLLAPGIgE 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644460963 254 LAnafvelTDAE-EQRRRFLIDRSRRQALggqtwPLD--EDFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:COG0017 354 II------GGSQrEHRYDVLVERIKEKGL-----DPEdyEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREV 418
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
263-326 |
3.32e-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: 3.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644460963 263 DAEEQRRRFlidrsrrqalGGqtwpldedFLAALAFGMPQAAGIAMGFDRLAMLASGADRIQQV 326
Cdd:COG0173 506 SEEEAEEKF----------GF--------LLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDV 551
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
293-330 |
1.76e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 40.16 E-value: 1.76e-03
10 20 30
....*....|....*....|....*....|....*...
gi 644460963 293 LAALAFGMPQAAGIAMGFDRLAMLASGADRIQQVQWLP 330
Cdd:PLN02903 582 LEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFP 619
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
245-331 |
8.55e-03 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 38.04 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644460963 245 FELFVCGIELANAFVELTDAEEQRRRFlidrsrrQALGGQTWPLDEDF---LAALAFGMPQAAGIAMGFDRLAMLASGAD 321
Cdd:PRK12820 491 YDLVVNGEELGGGSIRINDKDIQLRIF-------AALGLSEEDIEDKFgffLRAFDFAAPPHGGIALGLDRVVSMILQTP 563
|
90
....*....|
gi 644460963 322 RIQQVQWLPE 331
Cdd:PRK12820 564 SIREVIAFPK 573
|
|
| |
