|
Name |
Accession |
Description |
Interval |
E-value |
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
9-318 |
1.47e-153 |
|
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: 432.61 E-value: 1.47e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 9 AEIATLRERARLMAEVRAFFAERGVWEVETPVLGHGGSTDVHLASLCCEAVTPAG-RERLWLQTSPEFHMKRLLAAGSGA 87
Cdd:COG2269 1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPDGgGRPLYLHTSPEFAMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 88 IFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVLP-FDPGPLRRRRYRELFREHLGLDPFREPLDA 166
Cdd:COG2269 81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGaAGFAPAERLSYQEAFLRYLGIDPLTADLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 167 LRRRAAETGGLDMATASRDDCLDLLISLSIEPHLGRDGIDVVVDYPASQAALARRHqdpEDGEWVASRFEVYRHGLELAN 246
Cdd:COG2269 161 LAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARIS---PDDPRVAERFELYACGVELAN 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515332313 247 GYDELTDAAEQRARFEEDNAARRAAGLDEVDVDERLLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMA 318
Cdd:COG2269 238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
27-318 |
4.21e-142 |
|
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: 402.70 E-value: 4.21e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 27 FFAERGVWEVETPVLGHGGSTDVHLASLCCEAVTPAG-RERLWLQTSPEFHMKRLLAAGSGAIFQIARSFRDGEVGGRHN 105
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPDGqGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 106 LEFSMLEWYRPGLDLDGLIAETDALIRRVLPFDPGPLRRRRYRELFREHLGLDPFREPLDALRRRAAETGGLDMATASRD 185
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLGDPFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGIRASEEDDRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 186 DCLDLLISLSIEPHLGRDGIDVVVDYPASQAALARRHQDPEDgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEDN 265
Cdd:TIGR00462 161 DLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPR---VAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 515332313 266 AARRAAGLDEVDVDERLLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMA 318
Cdd:TIGR00462 238 ALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
11-316 |
2.56e-116 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 338.06 E-value: 2.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 11 IATLRERARLMAEVRAFFAERGVWEVETPVLGHGGSTDVHLASLCCEAVTP--AGRERLWLQTSPEFHMKRLLAAGSGAI 88
Cdd:PRK09350 2 IPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPgaSQGKTLWLMTSPEYHMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 89 FQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVLpfDPGPLRRRRYRELFREHLGLDPFREPLDALR 168
Cdd:PRK09350 82 FQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVL--DCEPAESLSYQQAFLRYLGIDPLSADKTQLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 169 RRAAETGGLDMATAS--RDDCLDLLISLSIEPHLGRDGIDVVVDYPASQAALARrhQDPEDGEwVASRFEVYRHGLELAN 246
Cdd:PRK09350 160 EVAAKLGLSNIADEEedRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAK--ISTEDHR-VAERFEVYFKGIELAN 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 247 GYDELTDAAEQRARFEEDNAARRAAGLDEVDVDERLLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEV 316
Cdd:PRK09350 237 GFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
13-323 |
1.20e-41 |
|
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: 147.35 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 13 TLRERARLMAEVRAFFAERGVWEVETPVLG-------------HGGSTDVHLaslcceavtpagrerlWLQTSPEFHMKR 79
Cdd:cd00775 7 TFIVRSKIISYIRKFLDDRGFLEVETPMLQpiaggaaarpfitHHNALDMDL----------------YLRIAPELYLKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 80 LLAAGSGAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRV----------------LPFDPgPLR 143
Cdd:cd00775 71 LIVGGFERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLvkkingktkieyggkeLDFTP-PFK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 144 RRRYRELFREHLGLDpFRE-----PLDALRRRAAETGGLDMATASRDDCLDLLISLSIEPHLgrdgID--VVVDYPASQA 216
Cdd:cd00775 150 RVTMVDALKEKTGID-FPEldleqPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTL----IQptFIIDHPVEIS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 217 ALARRH-QDPEdgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEdNAARRAAGLDE-VDVDERLLAALEAGMPAGS 294
Cdd:cd00775 225 PLAKRHrSNPG----LTERFELFICGKEIANAYTELNDPFDQRERFEE-QAKQKEAGDDEaMMMDEDFVTALEYGMPPTG 299
|
330 340
....*....|....*....|....*....
gi 515332313 295 GVALGLDRLFQLAQGRASVAEVMAFATPR 323
Cdd:cd00775 300 GLGIGIDRLVMLLTDSNSIRDVILFPAMR 328
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
12-323 |
4.39e-39 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 140.01 E-value: 4.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 12 ATLRERARLMAEVRAFFAERGVWEVETPVLGH----GGSTDvhlaslcceAVTPAGRERLW--LQTSPEFHMKRLLAAGS 85
Cdd:pfam00152 20 ANLKLRSKIIKAIRNFLDENGFLEVETPILTKsatpEGARD---------FLVPSRALGKFyaLPQSPQLYKQLLMVAGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 86 GAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVlpFDPGPLRRRRYRELFREHLGlDPF-REPL 164
Cdd:pfam00152 91 DRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEI--FKEVEGIAKELEGGTLLDLK-KPFpRITY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 165 DALRRRAAETGGLDMATASRDDCLDLLISLSIEPHlgRDGIDVVVDYPASQAALARRHqdPEDGEWVASRFEVYRHGLEL 244
Cdd:pfam00152 168 AEAIEKLNGKDVEELGYGSDKPDLRFLLELVIDKN--KFNPLWVTDFPAEHHPFTMPK--DEDDPALAEAFDLVLNGVEI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 245 ANGYDELTDAAEQRARFEEdnaarraAGLDEVDVDER---LLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMAFat 321
Cdd:pfam00152 244 GGGSIRIHDPELQEERFEE-------QGLDPEEAEEKfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAF-- 314
|
..
gi 515332313 322 PR 323
Cdd:pfam00152 315 PK 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
9-318 |
1.47e-153 |
|
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: 432.61 E-value: 1.47e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 9 AEIATLRERARLMAEVRAFFAERGVWEVETPVLGHGGSTDVHLASLCCEAVTPAG-RERLWLQTSPEFHMKRLLAAGSGA 87
Cdd:COG2269 1 ASREALRARARLLAAIRAFFAERGVLEVETPALSVAPGTDPHLDSFATEFIGPDGgGRPLYLHTSPEFAMKRLLAAGSGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 88 IFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVLP-FDPGPLRRRRYRELFREHLGLDPFREPLDA 166
Cdd:COG2269 81 IYQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGaAGFAPAERLSYQEAFLRYLGIDPLTADLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 167 LRRRAAETGGLDMATASRDDCLDLLISLSIEPHLGRDGIDVVVDYPASQAALARRHqdpEDGEWVASRFEVYRHGLELAN 246
Cdd:COG2269 161 LAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQLGRDRPTFLYDYPASQAALARIS---PDDPRVAERFELYACGVELAN 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515332313 247 GYDELTDAAEQRARFEEDNAARRAAGLDEVDVDERLLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMA 318
Cdd:COG2269 238 GFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALGAERIDDVLA 309
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
27-318 |
4.21e-142 |
|
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: 402.70 E-value: 4.21e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 27 FFAERGVWEVETPVLGHGGSTDVHLASLCCEAVTPAG-RERLWLQTSPEFHMKRLLAAGSGAIFQIARSFRDGEVGGRHN 105
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPVTDPHLDAFATEFVGPDGqGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 106 LEFSMLEWYRPGLDLDGLIAETDALIRRVLPFDPGPLRRRRYRELFREHLGLDPFREPLDALRRRAAETGGLDMATASRD 185
Cdd:TIGR00462 81 PEFTMLEWYRPGFDYHDLMDEVEALLQELLGDPFAPAERLSYQEAFLRYAGIDPLTASLAELQAAAAAHGIRASEEDDRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 186 DCLDLLISLSIEPHLGRDGIDVVVDYPASQAALARRHQDPEDgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEDN 265
Cdd:TIGR00462 161 DLLDLLFSEKVEPHLGFGRPTFLYDYPASQAALARISPDDPR---VAERFELYIKGLELANGFHELTDAAEQRRRFEADN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 515332313 266 AARRAAGLDEVDVDERLLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMA 318
Cdd:TIGR00462 238 ALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
11-316 |
2.56e-116 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 338.06 E-value: 2.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 11 IATLRERARLMAEVRAFFAERGVWEVETPVLGHGGSTDVHLASLCCEAVTP--AGRERLWLQTSPEFHMKRLLAAGSGAI 88
Cdd:PRK09350 2 IPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHLVPFETRFVGPgaSQGKTLWLMTSPEYHMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 89 FQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVLpfDPGPLRRRRYRELFREHLGLDPFREPLDALR 168
Cdd:PRK09350 82 FQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVL--DCEPAESLSYQQAFLRYLGIDPLSADKTQLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 169 RRAAETGGLDMATAS--RDDCLDLLISLSIEPHLGRDGIDVVVDYPASQAALARrhQDPEDGEwVASRFEVYRHGLELAN 246
Cdd:PRK09350 160 EVAAKLGLSNIADEEedRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQAALAK--ISTEDHR-VAERFEVYFKGIELAN 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 247 GYDELTDAAEQRARFEEDNAARRAAGLDEVDVDERLLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEV 316
Cdd:PRK09350 237 GFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
13-323 |
1.20e-41 |
|
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: 147.35 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 13 TLRERARLMAEVRAFFAERGVWEVETPVLG-------------HGGSTDVHLaslcceavtpagrerlWLQTSPEFHMKR 79
Cdd:cd00775 7 TFIVRSKIISYIRKFLDDRGFLEVETPMLQpiaggaaarpfitHHNALDMDL----------------YLRIAPELYLKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 80 LLAAGSGAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRV----------------LPFDPgPLR 143
Cdd:cd00775 71 LIVGGFERVYEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLvkkingktkieyggkeLDFTP-PFK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 144 RRRYRELFREHLGLDpFRE-----PLDALRRRAAETGGLDMATASRDDCLDLLISLSIEPHLgrdgID--VVVDYPASQA 216
Cdd:cd00775 150 RVTMVDALKEKTGID-FPEldleqPEELAKLLAKLIKEKIEKPRTLGKLLDKLFEEFVEPTL----IQptFIIDHPVEIS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 217 ALARRH-QDPEdgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEdNAARRAAGLDE-VDVDERLLAALEAGMPAGS 294
Cdd:cd00775 225 PLAKRHrSNPG----LTERFELFICGKEIANAYTELNDPFDQRERFEE-QAKQKEAGDDEaMMMDEDFVTALEYGMPPTG 299
|
330 340
....*....|....*....|....*....
gi 515332313 295 GVALGLDRLFQLAQGRASVAEVMAFATPR 323
Cdd:cd00775 300 GLGIGIDRLVMLLTDSNSIRDVILFPAMR 328
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
13-319 |
3.70e-40 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 146.77 E-value: 3.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 13 TLRERARLMAEVRAFFAERGVWEVETPVLG--HGGS------TdvHLASLCCEavtpagrerLWLQTSPEFHMKRLLAAG 84
Cdd:PRK00484 171 TFRKRSKIISAIRRFLDNRGFLEVETPMLQpiAGGAaarpfiT--HHNALDID---------LYLRIAPELYLKRLIVGG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 85 SGAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRV---------LPFDP------GPLRRRRYRE 149
Cdd:PRK00484 240 FERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLaqavlgttkVTYQGteidfgPPFKRLTMVD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 150 LFREHLGLDPFREPLDALRRRAAETGGLDMATASRDDCLDLLISLSIEPHLgrdgID--VVVDYPASQAALARRH-QDPE 226
Cdd:PRK00484 320 AIKEYTGVDFDDMTDEEARALAKELGIEVEKSWGLGKLINELFEEFVEPKL----IQptFITDYPVEISPLAKRHrEDPG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 227 dgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEdNAARRAAGLDE-VDVDERLLAALEAGMPAGSGVALGLDRLFQ 305
Cdd:PRK00484 396 ----LTERFELFIGGREIANAFSELNDPIDQRERFEA-QVEAKEAGDDEaMFMDEDFLRALEYGMPPTGGLGIGIDRLVM 470
|
330
....*....|....
gi 515332313 306 LAQGRASVAEVMAF 319
Cdd:PRK00484 471 LLTDSPSIRDVILF 484
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
12-323 |
4.39e-39 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 140.01 E-value: 4.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 12 ATLRERARLMAEVRAFFAERGVWEVETPVLGH----GGSTDvhlaslcceAVTPAGRERLW--LQTSPEFHMKRLLAAGS 85
Cdd:pfam00152 20 ANLKLRSKIIKAIRNFLDENGFLEVETPILTKsatpEGARD---------FLVPSRALGKFyaLPQSPQLYKQLLMVAGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 86 GAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVlpFDPGPLRRRRYRELFREHLGlDPF-REPL 164
Cdd:pfam00152 91 DRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEI--FKEVEGIAKELEGGTLLDLK-KPFpRITY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 165 DALRRRAAETGGLDMATASRDDCLDLLISLSIEPHlgRDGIDVVVDYPASQAALARRHqdPEDGEWVASRFEVYRHGLEL 244
Cdd:pfam00152 168 AEAIEKLNGKDVEELGYGSDKPDLRFLLELVIDKN--KFNPLWVTDFPAEHHPFTMPK--DEDDPALAEAFDLVLNGVEI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 245 ANGYDELTDAAEQRARFEEdnaarraAGLDEVDVDER---LLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMAFat 321
Cdd:pfam00152 244 GGGSIRIHDPELQEERFEE-------QGLDPEEAEEKfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAF-- 314
|
..
gi 515332313 322 PR 323
Cdd:pfam00152 315 PK 316
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
13-319 |
2.22e-37 |
|
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: 139.40 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 13 TLRERARLMAEVRAFFAERGVWEVETPVL--GHGGS------TdvHLASLCCEavtpagrerLWLQTSPEFHMKRLLAAG 84
Cdd:COG1190 173 TFRKRSKIIRAIRRFLDERGFLEVETPMLqpIAGGAaarpfiT--HHNALDMD---------LYLRIAPELYLKRLIVGG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 85 SGAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRV---------LPFDP------GPLRRRRYRE 149
Cdd:COG1190 242 FERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAaeavlgttkVTYQGqeidlsPPWRRITMVE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 150 LFREHLGLDPFR-EPLDALRRRAAETGGLDMATASRDDCLDLLISLSIEPHLgrdgID--VVVDYPASQAALARRH-QDP 225
Cdd:COG1190 322 AIKEATGIDVTPlTDDEELRALAKELGIEVDPGWGRGKLIDELFEELVEPKL----IQptFVTDYPVEVSPLAKRHrDDP 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 226 EdgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEdNAARRAAGLDEV-DVDERLLAALEAGMPAGSGVALGLDRLF 304
Cdd:COG1190 398 G----LTERFELFIAGREIANAFSELNDPIDQRERFEE-QLELKAAGDDEAmPMDEDFLRALEYGMPPTGGLGIGIDRLV 472
|
330
....*....|....*
gi 515332313 305 QLAQGRASVAEVMAF 319
Cdd:COG1190 473 MLLTDSPSIRDVILF 487
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
13-319 |
1.04e-33 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 129.73 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 13 TLRERARLMAEVRAFFAERGVWEVETPVLGH--GGST----DVHLASLcceavtpagRERLWLQTSPEFHMKRLLAAGSG 86
Cdd:PLN02502 228 IFRTRAKIISYIRRFLDDRGFLEVETPMLNMiaGGAAarpfVTHHNDL---------NMDLYLRIATELHLKRLVVGGFE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 87 AIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVLP----------------FDPgPLRRRRYREL 150
Cdd:PLN02502 299 RVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKeltgsykikyhgieidFTP-PFRRISMISL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 151 FREHLGLDpFREPLD-----ALRRRAAETGGLDM---ATASRddCLDLLISLSIEPHLGRDGIdvVVDYPASQAALARRH 222
Cdd:PLN02502 378 VEEATGID-FPADLKsdeanAYLIAACEKFDVKCpppQTTGR--LLNELFEEFLEETLVQPTF--VLDHPVEMSPLAKPH 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 223 QDPEDgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEdNAARRAAGLDE-VDVDERLLAALEAGMPAGSGVALGLD 301
Cdd:PLN02502 453 RSKPG---LTERFELFINGRELANAFSELTDPVDQRERFEE-QVKQHNAGDDEaMALDEDFCTALEYGLPPTGGWGLGID 528
|
330
....*....|....*...
gi 515332313 302 RLFQLAQGRASVAEVMAF 319
Cdd:PLN02502 529 RLVMLLTDSASIRDVIAF 546
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
13-323 |
1.47e-30 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 120.55 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 13 TLRERARLMAEVRAFFAERGVWEVETPVLG--HGGSTD----VHLASLCCEavtpagrerLWLQTSPEFHMKRLLAAGSG 86
Cdd:PRK12445 183 TFVVRSKILAAIRQFMVARGFMEVETPMMQviPGGASArpfiTHHNALDLD---------MYLRIAPELYLKRLVVGGFE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 87 AIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVLPFDPGPLRRRRYRELFRehlgldpFREPLDA 166
Cdd:PRK12445 254 RVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFD-------FGKPFEK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 167 LRRRAA------ETGGLDMATASRDDCLDLLISLSIEPH--LGRDGIDV--------------VVDYPASQAALARRHQ- 223
Cdd:PRK12445 327 LTMREAikkyrpETDMADLDNFDAAKALAESIGITVEKSwgLGRIVTEIfdevaeahliqptfITEYPAEVSPLARRNDv 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 224 DPEdgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEDNAARRAAGLDEVDVDERLLAALEAGMPAGSGVALGLDRL 303
Cdd:PRK12445 407 NPE----ITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRM 482
|
330 340
....*....|....*....|
gi 515332313 304 FQLAQGRASVAEVMAFATPR 323
Cdd:PRK12445 483 IMLFTNSHTIRDVILFPAMR 502
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
14-319 |
9.05e-28 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 113.91 E-value: 9.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 14 LRERARLMAEVRAFFAERGVWEVETPVLG--HGGSTdvhlaslcceaVTP------AGRERLWLQTSPEFHMKRLLAAGS 85
Cdd:PRK02983 770 LRARSAVVRAVRETLVARGFLEVETPILQqvHGGAN-----------ARPfvthinAYDMDLYLRIAPELYLKRLCVGGV 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 86 GAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVLPFDPG-PLRRRRYRELFREHLGLD---PFR 161
Cdd:PRK02983 839 ERVFELGRNFRNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGaPVVMRPDGDGVLEPVDISgpwPVV 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 162 EPLDALRRRAAETggLDMATaSRDDCLDLLISLSIEPHLGRDGIDVV------------------VDYPASQAALARRH- 222
Cdd:PRK02983 919 TVHDAVSEALGEE--IDPDT-PLAELRKLCDAAGIPYRTDWDAGAVVlelyehlvedrttfptfyTDFPTSVSPLTRPHr 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 223 QDPEdgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEDnaARRAAGLDE--VDVDERLLAALEAGMPAGSGVALGL 300
Cdd:PRK02983 996 SDPG----LAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQ--SLLAAGGDPeaMELDEDFLQALEYAMPPTGGLGMGV 1069
|
330
....*....|....*....
gi 515332313 301 DRLFQLAQGRaSVAEVMAF 319
Cdd:PRK02983 1070 DRLVMLLTGR-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 ... |
14-324 |
1.54e-27 |
|
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: 108.33 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 14 LRERARLMAEVRAFFAERGVWEVETPVL----GHGGSTDVHLASLCCEavtpagrERLWLQTSPEFHMKRLLAAGSGAIF 89
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLqkitGGAGARPFLVKYNALG-------LDYYLRISPQLFKKRLMVGGLDRVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 90 QIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVLpfdpgplrrrryrelfrehlgldpfrepldalrR 169
Cdd:cd00669 74 EINRNFRNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLA---------------------------------R 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 170 RAAETGGLDMATASRDDCLDLLiSLSIEPHLGRDGIDV-VVDYPA-SQAALARRH-QDPEdgewVASRFEVYRHGLELAN 246
Cdd:cd00669 121 EVLGVTAVTYGFELEDFGLPFP-RLTYREALERYGQPLfLTDYPAeMHSPLASPHdVNPE----IADAFDLFINGVEVGN 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515332313 247 GYDELTDAAEQRARFEEDNAARRAagldEVDVDERLLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMAFATPRA 324
Cdd:cd00669 196 GSSRLHDPDIQAEVFQEQGINKEA----GMEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
11-323 |
4.10e-24 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 102.80 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 11 IATLRERARLMAEVRAFFAERGVWEVETPVLgHGGSTDVHLASLCCEAvtPAGRERLWLQTSPEFHMKRLLAAGSGAIFQ 90
Cdd:PTZ00385 230 IETIKKRHVMLQALRDYFNERNFVEVETPVL-HTVASGANAKSFVTHH--NANAMDLFLRVAPELHLKQCIVGGMERIYE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 91 IARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETD---------------------------------ALIRRVLPF 137
Cdd:PTZ00385 307 IGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEdifrqlamrvngttvvqiypenahgnpvtvdlgKPFRRVSVY 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 138 D----------PGPLRRRRYRELFREHLGLDPFREPLDALRrraaetggldmaTASR--DDCLDLLISLSI-EPHLgrdg 204
Cdd:PTZ00385 387 DeiqrmsgvefPPPNELNTPKGIAYMSVVMLRYNIPLPPVR------------TAAKmfEKLIDFFITDRVvEPTF---- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 205 idvVVDYPASQAALARRHQDPEDgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEDNAARRAAGLDEVDVDERLLA 284
Cdd:PTZ00385 451 ---VMDHPLFMSPLAKEQVSRPG---LAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLK 524
|
330 340 350
....*....|....*....|....*....|....*....
gi 515332313 285 ALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMAFATPR 323
Cdd:PTZ00385 525 SLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
12-323 |
5.66e-17 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 81.60 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 12 ATLRERARLMAEVRAFFAERGVWEVETPVLG--HGGSTD----VHLASLCCEavtpagrerLWLQTSPEFHMKRLLAAGS 85
Cdd:PTZ00417 251 STFITRTKIINYLRNFLNDRGFIEVETPTMNlvAGGANArpfiTHHNDLDLD---------LYLRIATELPLKMLIVGGI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 86 GAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVL-------------------PFD-----PGP 141
Cdd:PTZ00417 322 DKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVmhlfgtykilynkdgpekdPIEidftpPYP 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 142 LRRRRYRELFREHLGLD-PFREP------LDALRRRAAETGglDMATASRddCLDLLISLSIEPHLGRDGIdVVVDYPAS 214
Cdd:PTZ00417 402 KVSIVEELEKLTNTKLEqPFDSPetinkmINLIKENKIEMP--NPPTAAK--LLDQLASHFIENKYPNKPF-FIIEHPQI 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 215 QAALARRHQDPEDgewVASRFEVYRHGLELANGYDELTDAAEQRARFEEDNAARRAAGLDEVDVDERLLAALEAGMPAGS 294
Cdd:PTZ00417 477 MSPLAKYHRSKPG---LTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTG 553
|
330 340
....*....|....*....|....*....
gi 515332313 295 GVALGLDRLFQLAQGRASVAEVMAFATPR 323
Cdd:PTZ00417 554 GLGLGIDRITMFLTNKNCIKDVILFPTMR 582
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
14-319 |
5.92e-09 |
|
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: 56.04 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 14 LRERARLMAEVRAFFAERGVWEVETPVLGhggstdvhlaslcceAVTPAG-RE-----RLW------LQTSPEFHMKRLL 81
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILT---------------KSTPEGaRDflvpsRLHpgkfyaLPQSPQLFKQLLM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 82 AAGSGAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVLPFDPGPLRRRryrelfrehlgldPF- 160
Cdd:cd00777 66 VSGFDRYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELTT-------------PFp 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 161 REPL-DALRR---------------RAAETGGLDMA----TASRDDCLDLLislsiephlgrdgidvvvdypasqaalar 220
Cdd:cd00777 133 RMTYaEAMERygfkflwivdfplfeWDEEEGRLVSAhhpfTAPKEEDLDLL----------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 221 rHQDPEDGewVASRFEVYRHGLELANGYDELTDAAEQRARFEednaarrAAGLDEVDVDER---LLAALEAGMPAGSGVA 297
Cdd:cd00777 184 -EKDPEDA--RAQAYDLVLNGVELGGGSIRIHDPDIQEKVFE-------ILGLSEEEAEEKfgfLLEAFKYGAPPHGGIA 253
|
330 340
....*....|....*....|..
gi 515332313 298 LGLDRLFQLAQGRASVAEVMAF 319
Cdd:cd00777 254 LGLDRLVMLLTGSESIRDVIAF 275
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
3-135 |
2.64e-06 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 48.83 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 3 IDWRPTAEIATLRERARLMAEVRAFFAERGVWEVETPVLGHG---GSTDVHLASlcceAVTPagRERLWLQTSPEFHMKR 79
Cdd:PRK12820 145 LDIRRPAMQDHLAKRHRIIKCARDFLDSRGFLEIETPILTKStpeGARDYLVPS----RIHP--KEFYALPQSPQLFKQL 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 515332313 80 LLAAGSGAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRVL 135
Cdd:PRK12820 219 LMIAGFERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARMF 274
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
17-139 |
1.75e-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: 45.19 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 17 RARLMAEVRAFFAERGVWEVETPVLGH---GGSTDVHLASLccEAVTPAGRERLWLQTSPEFHMKRLLAAGSGA----IF 89
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEReplLEKAGHEPKDL--LPVGAENEEDLYLRPTLEPGLVRLFVSHIRKlplrLA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 515332313 90 QIARSFRDGE--VGGRHNLEFSMLEWY---RPGLDLDG---LIAETDALIRRVLPFDP 139
Cdd:cd00768 80 EIGPAFRNEGgrRGLRRVREFTQLEGEvfgEDGEEASEfeeLIELTEELLRALGIKLD 137
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
269-319 |
1.75e-04 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 43.13 E-value: 1.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 515332313 269 RAAGLDEVDVDER---LLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMAF 319
Cdd:PRK00476 502 EILGISEEEAEEKfgfLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAF 555
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
235-324 |
2.69e-04 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 42.67 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 235 FEVYRHGLELANGYDELTDAAEQRARFeednaarRAAGLDEVDVDERL---LAALEAGMPAGSGVALGLDRLFQLAQGRA 311
Cdd:PRK12820 491 YDLVVNGEELGGGSIRINDKDIQLRIF-------AALGLSEEDIEDKFgffLRAFDFAAPPHGGIALGLDRVVSMILQTP 563
|
90
....*....|...
gi 515332313 312 SVAEVMAFATPRA 324
Cdd:PRK12820 564 SIREVIAFPKNRS 576
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
269-319 |
2.85e-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: 2.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 515332313 269 RAAGLDEVDVDER---LLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMAF 319
Cdd:COG0173 501 ELLGISEEEAEEKfgfLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
3-134 |
3.76e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 42.08 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 3 IDWRPTAEIATLRERARLMAEVRAFFAER-GVWEVETPVLGHG---GSTDVHLASlcceAVTPAgrERLWLQTSPEFHMK 78
Cdd:PLN02903 192 LDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEIETPILSRStpeGARDYLVPS----RVQPG--TFYALPQSPQLFKQ 265
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 515332313 79 RLLAAGSGAIFQIARSFRDGEVGGRHNLEFSMLEWYRPGLDLDGLIAETDALIRRV 134
Cdd:PLN02903 266 MLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQV 321
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
208-323 |
6.14e-04 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 41.33 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 208 VVDYPASqaalAR---RHQDPEDGEWVASrFE-VYRhGLELANG------YDELTDAAEQRarfeednaarraaGLDeVD 277
Cdd:PRK05159 327 ITDYPSE----KRpfyTMPDEDDPEISKS-FDlLFR-GLEITSGgqrihrYDMLVESIKEK-------------GLN-PE 386
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 515332313 278 VDERLLAALEAGMPAGSGVALGLDRLFQLAQGRASVAEVMAFatPR 323
Cdd:PRK05159 387 SFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLF--PR 430
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
12-323 |
7.63e-04 |
|
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: 40.63 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 12 ATLRERARLMAEVRAFFAERGVWEVETPVLGhggSTDvhlaslcCEAVTPAGR-----ERLWLQTSPEFHmKRLLAAGSG 86
Cdd:cd00776 22 AIFRIRSEVLRAFREFLRENGFTEVHTPKIT---STD-------TEGGAELFKvsyfgKPAYLAQSPQLY-KEMLIAALE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 87 AIFQIARSFRDGEVGG-RHNLEFSMLEwyrPGL----DLDGLIAETDALIRRV---LPFDPGPLRRRRYRELFREHLGLD 158
Cdd:cd00776 91 RVYEIGPVFRAEKSNTrRHLSEFWMLE---AEMafieDYNEVMDLIEELIKYIfkrVLERCAKELELVNQLNRELLKPLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 159 PF-----REPLDALRRRAAETG---GLDMATASrddcldllislsiEPHLG---RDGIDVVVDYPASQAALARRhQDPED 227
Cdd:cd00776 168 PFprityDEAIELLREKGVEEEvkwGEDLSTEH-------------ERLLGeivKGDPVFVTDYPKEIKPFYMK-PDDDN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 228 GEWVASrFEV-YRHGLELANG------YDELTDAAEQRarfeednaarraaGLDEVDVdERLLAALEAGMPAGSGVALGL 300
Cdd:cd00776 234 PETVES-FDLlMPGVGEIVGGsqrihdYDELEERIKEH-------------GLDPESF-EWYLDLRKYGMPPHGGFGLGL 298
|
330 340
....*....|....*....|...
gi 515332313 301 DRLFQLAQGRASVAEVMAFatPR 323
Cdd:cd00776 299 ERLVMWLLGLDNIREAILF--PR 319
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
13-97 |
8.35e-03 |
|
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: 37.67 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515332313 13 TLRERARLMAEVRAFFAERGVWEVETPVLGhggstdvhlASlcceavTPAG-RE-----RLW------LQTSPE-FhmKR 79
Cdd:COG0173 141 NLILRHKVTKAIRNYLDENGFLEIETPILT---------KS------TPEGaRDylvpsRVHpgkfyaLPQSPQlF--KQ 203
|
90
....*....|....*....
gi 515332313 80 LL-AAGSGAIFQIARSFRD 97
Cdd:COG0173 204 LLmVSGFDRYFQIARCFRD 222
|
|
| |
