|
Name |
Accession |
Description |
Interval |
E-value |
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
2-400 |
1.71e-106 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 324.37 E-value: 1.71e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEedvvkKIVEG-----GAEKL--------------------TLKSNGTPVEWIE 56
Cdd:COG0143 108 RLYDNGDIYKGEYEGWYCPECERFLPD-----RYVEGtcpkcGAEDAygdqcencgatleptelinpRSAISGAPPELRE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 57 EENYMFRLSEFREKVAEWInRENIVVHPSKYKSLA------LTSLEMSEDLSisrsrsrlsWGIPVPNDPTQTIYVWLDA 130
Cdd:COG0143 183 EEHYFFRLSKYQDRLLEWI-EENPDIQPEVRNEVLswlkegLQDLSISRDFD---------WGIPVPGDPGKVFYVWFDA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 131 LVNYLTVT-GFPNAQ-------SVWP----PTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSL 198
Cdd:COG0143 253 LIGYISATkGYADDRglpedfeKYWPapdtELVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAHGFLTVEGEKMSKSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 199 GNVVNPSEAITKFTAEGLRYFLLKHGNPSYDCSFNWNSCLQTINSDLVNNVGNLLNRST--VEKiNKEGMYPKM-EIEDI 275
Cdd:COG0143 333 GNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLsmIHK-YFDGKVPEPgELTEA 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 276 EAEIRENAKKLMEMVEEsrencvdLYDEMSYFKIIENLMLTMKEANRLFQSSQPW---KEIDEKRLKSLLFVTYDTIRVV 352
Cdd:COG0143 412 DEELLAEAEAALEEVAE-------AMEAFEFRKALEEIMALARAANKYIDETAPWklaKDEDPERLATVLYTLLEALRIL 484
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 71992781 353 TILLQPITPKMAEFCLNRLGVPKNERNLENSRFGSYSGGKLGAERGVF 400
Cdd:COG0143 485 AILLKPFLPETAEKILEQLGLEGDELTWEDAGWPLPAGHKIGKPEPLF 532
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
2-401 |
1.18e-102 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 313.36 E-value: 1.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEEDVVKKiveggaeKLTLKSNGTPVEWIEEENYMFRLSEFREKVAEWI------ 75
Cdd:PRK11893 108 RLLANGDIYLGKYEGWYCVRCEEFYTESELIED-------GYRCPPTGAPVEWVEEESYFFRLSKYQDKLLELYeanpdf 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 76 ----NRENIVVHPSKYK----SLALTSLEmsedlsisrsrsrlsWGIPVPNDPTQTIYVWLDALVNYLTVTGFPNAQSV- 146
Cdd:PRK11893 181 iqpaSRRNEVISFVKSGlkdlSISRTNFD---------------WGIPVPGDPKHVIYVWFDALTNYLTALGYPDDEELl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 147 -------WPPTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYF 219
Cdd:PRK11893 246 aelfnkyWPADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 220 LLKH---GNPSydcSFNWNSCLQTINSDLVNNVGNLLNRsTVEKINK--EGMYPKMEIEDIEAEirenakKLMEMVEESR 294
Cdd:PRK11893 326 LLREipfGQDG---DFSREAFINRINADLANDLGNLAQR-TLSMIAKnfDGKVPEPGALTEADE------ALLEAAAALL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 295 ENCVDLYDEMSYFKIIENLMLTMKEANRLFQSSQPWKEI--DEKRLKSLLFVTYDTIRVVTILLQPITPKMAEFCLNRLG 372
Cdd:PRK11893 396 ERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAktDPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLG 475
|
410 420 430
....*....|....*....|....*....|.
gi 71992781 373 VPKNE-RNLENSRFGSYSGGK-LGAERGVFI 401
Cdd:PRK11893 476 VEEDEnRDFAALSWGRLAPGTtLPKPEPIFP 506
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
2-375 |
4.33e-91 |
|
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273058 [Multi-domain] Cd Length: 530 Bit Score: 284.27 E-value: 4.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEEDVVKKIVEGGAE--------------------KLTLKSNGTPVEWIEEENYM 61
Cdd:TIGR00398 106 KLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEdargdhcevcgrhlepteliNPRCKICGAKPELRDSEHYF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 62 FRLSEFREKVAEWInrenivvhpskykSLALTSLEMSEDLSISRSR-------------SRLSWGIPVPNDPTQTIYVWL 128
Cdd:TIGR00398 186 FRLSAFEKELEEWI-------------RKNPESGSPASNVKNKAQNwlkgglkdlaitrDLVYWGIPVPNDPNKVVYVWF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 129 DALVNYLTVTGF-----PNAQSVWP-----PTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSL 198
Cdd:TIGR00398 253 DALIGYISSLGIlsgdtEDWKKWWNndedaELIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFSHGYLTVEGGKMSKSL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 199 GNVVNPSEAITKFTAEGLRYFLLKHGNPSYDCSFNWNSCLQTINSDLVNNVGNLLNRsTVEKINKegmYPKMEIEDIEaE 278
Cdd:TIGR00398 333 GNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNR-TLGFIKK---YFNGVLPSED-I 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 279 IRENAKKLMEMVEESRENCVDLYDEMSYFKIIENLMLTMKEANRLFQSSQPWK-EIDEKRLKSLLFVTYDTIRVVTILLQ 357
Cdd:TIGR00398 408 TDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWElFKQSPRLKELLAVCSMLIRVLSILLY 487
|
410
....*....|....*...
gi 71992781 358 PITPKMAEFCLNRLGVPK 375
Cdd:TIGR00398 488 PIMPKLSEKILKFLNFEL 505
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
1-232 |
2.02e-78 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 244.75 E-value: 2.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 1 MKIQDNGYIYKSTYSGYYSITDECFIPEedvvkkiveggaekltlksngtpveWIEEENYMFRLSEFREKVAEWINRENI 80
Cdd:cd00814 106 KKLYENGYIYEGEYEGLYCVSCERFLPE-------------------------WREEEHYFFRLSKFQDRLLEWLEKNPD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 81 VVHPSKYKSLALTSLE-------MSEDLSIsrsrsrlsWGIPVPNDPTQTIYVWLDALVNYLTVTGFPNAQ--------S 145
Cdd:cd00814 161 FIWPENARNEVLSWLKeglkdlsITRDLFD--------WGIPVPLDPGKVIYVWFDALIGYISATGYYNEEwgnswwwkD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 146 VWPPTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGN 225
Cdd:cd00814 233 GWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERP 312
|
....*..
gi 71992781 226 PSYDCSF 232
Cdd:cd00814 313 EGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
2-256 |
1.12e-75 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 240.27 E-value: 1.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEEDVVKKIVEGGAEKLT--------------------LKSNGTPVEWIEEENYM 61
Cdd:pfam09334 106 KLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARgdqcencgrhleptelinpkCVICGTTPEVKETEHYF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 62 FRLSEFREKVAEWINRENiVVHPSKYKSLALTSLEM-------SEDlsisrsrsrLSWGIPVPNDPTQTIYVWLDALVNY 134
Cdd:pfam09334 186 FDLSKFQDKLREWIEENN-PEWPENVKNMVLEWLKEglkdraiSRD---------LDWGIPVPGAEGKVFYVWLDAPIGY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 135 LTVTGFP-----NAQSVWP-----PTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSLGNVVNP 204
Cdd:pfam09334 256 ISATKELsgneeKWKEWWPndpdtELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHGYLTYEGGKMSKSRGNVVWP 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 71992781 205 SEAITKFTAEGLRYFLLKHGNPSYDCSFNWNSCLQTINSDLVNNVGNLLNRS 256
Cdd:pfam09334 336 SEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
2-400 |
1.71e-106 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 324.37 E-value: 1.71e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEedvvkKIVEG-----GAEKL--------------------TLKSNGTPVEWIE 56
Cdd:COG0143 108 RLYDNGDIYKGEYEGWYCPECERFLPD-----RYVEGtcpkcGAEDAygdqcencgatleptelinpRSAISGAPPELRE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 57 EENYMFRLSEFREKVAEWInRENIVVHPSKYKSLA------LTSLEMSEDLSisrsrsrlsWGIPVPNDPTQTIYVWLDA 130
Cdd:COG0143 183 EEHYFFRLSKYQDRLLEWI-EENPDIQPEVRNEVLswlkegLQDLSISRDFD---------WGIPVPGDPGKVFYVWFDA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 131 LVNYLTVT-GFPNAQ-------SVWP----PTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSL 198
Cdd:COG0143 253 LIGYISATkGYADDRglpedfeKYWPapdtELVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAHGFLTVEGEKMSKSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 199 GNVVNPSEAITKFTAEGLRYFLLKHGNPSYDCSFNWNSCLQTINSDLVNNVGNLLNRST--VEKiNKEGMYPKM-EIEDI 275
Cdd:COG0143 333 GNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLsmIHK-YFDGKVPEPgELTEA 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 276 EAEIRENAKKLMEMVEEsrencvdLYDEMSYFKIIENLMLTMKEANRLFQSSQPW---KEIDEKRLKSLLFVTYDTIRVV 352
Cdd:COG0143 412 DEELLAEAEAALEEVAE-------AMEAFEFRKALEEIMALARAANKYIDETAPWklaKDEDPERLATVLYTLLEALRIL 484
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 71992781 353 TILLQPITPKMAEFCLNRLGVPKNERNLENSRFGSYSGGKLGAERGVF 400
Cdd:COG0143 485 AILLKPFLPETAEKILEQLGLEGDELTWEDAGWPLPAGHKIGKPEPLF 532
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
2-401 |
1.18e-102 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 313.36 E-value: 1.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEEDVVKKiveggaeKLTLKSNGTPVEWIEEENYMFRLSEFREKVAEWI------ 75
Cdd:PRK11893 108 RLLANGDIYLGKYEGWYCVRCEEFYTESELIED-------GYRCPPTGAPVEWVEEESYFFRLSKYQDKLLELYeanpdf 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 76 ----NRENIVVHPSKYK----SLALTSLEmsedlsisrsrsrlsWGIPVPNDPTQTIYVWLDALVNYLTVTGFPNAQSV- 146
Cdd:PRK11893 181 iqpaSRRNEVISFVKSGlkdlSISRTNFD---------------WGIPVPGDPKHVIYVWFDALTNYLTALGYPDDEELl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 147 -------WPPTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYF 219
Cdd:PRK11893 246 aelfnkyWPADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 220 LLKH---GNPSydcSFNWNSCLQTINSDLVNNVGNLLNRsTVEKINK--EGMYPKMEIEDIEAEirenakKLMEMVEESR 294
Cdd:PRK11893 326 LLREipfGQDG---DFSREAFINRINADLANDLGNLAQR-TLSMIAKnfDGKVPEPGALTEADE------ALLEAAAALL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 295 ENCVDLYDEMSYFKIIENLMLTMKEANRLFQSSQPWKEI--DEKRLKSLLFVTYDTIRVVTILLQPITPKMAEFCLNRLG 372
Cdd:PRK11893 396 ERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAktDPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLG 475
|
410 420 430
....*....|....*....|....*....|.
gi 71992781 373 VPKNE-RNLENSRFGSYSGGK-LGAERGVFI 401
Cdd:PRK11893 476 VEEDEnRDFAALSWGRLAPGTtLPKPEPIFP 506
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
2-381 |
3.23e-95 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 298.25 E-value: 3.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEedvvKKIVEGGaekltlKS--NGTPVEWIEEENYMFRLSEFREKVAEWINREN 79
Cdd:PRK12267 111 KLYEQGDIYKGEYEGWYCVSCETFFTE----SQLVDGG------KCpdCGREVELVKEESYFFRMSKYQDRLLEYYEENP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 80 IVVHPSKYK---------------SLALTSLEmsedlsisrsrsrlsWGIPVPNDPTQTIYVWLDALVNYLTVTGFP--- 141
Cdd:PRK12267 181 DFIQPESRKneminnfikpgledlSISRTSFD---------------WGIPVPFDPKHVVYVWIDALLNYITALGYGsdd 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 142 --NAQSVWPPTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYF 219
Cdd:PRK12267 246 deLFKKFWPADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 220 LLKH---GNpsyDCSFNWNSCLQTINSDLVNNVGNLLNRsTVEKINK--EG-MYPKMEIEDIEAEIRENAKKLMEMVEEs 293
Cdd:PRK12267 326 LLREvpfGS---DGDFSPEALVERINSDLANDLGNLLNR-TVAMINKyfDGeIPAPGNVTEFDEELIALAEETLKNYEE- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 294 rencvdLYDEMSYFKIIENLMLTMKEANRLFQSSQPW---KEIDEK-RLKSLLFVTYDTIRVVTILLQPITPKMAEFCLN 369
Cdd:PRK12267 401 ------LMEELQFSRALEEVWKLISRANKYIDETAPWvlaKDEGKKeRLATVMYHLAESLRKVAVLLSPFMPETSKKIFE 474
|
410
....*....|..
gi 71992781 370 RLGVPKNERNLE 381
Cdd:PRK12267 475 QLGLEEELTSWE 486
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
2-375 |
4.33e-91 |
|
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273058 [Multi-domain] Cd Length: 530 Bit Score: 284.27 E-value: 4.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEEDVVKKIVEGGAE--------------------KLTLKSNGTPVEWIEEENYM 61
Cdd:TIGR00398 106 KLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEdargdhcevcgrhlepteliNPRCKICGAKPELRDSEHYF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 62 FRLSEFREKVAEWInrenivvhpskykSLALTSLEMSEDLSISRSR-------------SRLSWGIPVPNDPTQTIYVWL 128
Cdd:TIGR00398 186 FRLSAFEKELEEWI-------------RKNPESGSPASNVKNKAQNwlkgglkdlaitrDLVYWGIPVPNDPNKVVYVWF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 129 DALVNYLTVTGF-----PNAQSVWP-----PTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSL 198
Cdd:TIGR00398 253 DALIGYISSLGIlsgdtEDWKKWWNndedaELIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFSHGYLTVEGGKMSKSL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 199 GNVVNPSEAITKFTAEGLRYFLLKHGNPSYDCSFNWNSCLQTINSDLVNNVGNLLNRsTVEKINKegmYPKMEIEDIEaE 278
Cdd:TIGR00398 333 GNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNR-TLGFIKK---YFNGVLPSED-I 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 279 IRENAKKLMEMVEESRENCVDLYDEMSYFKIIENLMLTMKEANRLFQSSQPWK-EIDEKRLKSLLFVTYDTIRVVTILLQ 357
Cdd:TIGR00398 408 TDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWElFKQSPRLKELLAVCSMLIRVLSILLY 487
|
410
....*....|....*...
gi 71992781 358 PITPKMAEFCLNRLGVPK 375
Cdd:TIGR00398 488 PIMPKLSEKILKFLNFEL 505
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
1-232 |
2.02e-78 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 244.75 E-value: 2.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 1 MKIQDNGYIYKSTYSGYYSITDECFIPEedvvkkiveggaekltlksngtpveWIEEENYMFRLSEFREKVAEWINRENI 80
Cdd:cd00814 106 KKLYENGYIYEGEYEGLYCVSCERFLPE-------------------------WREEEHYFFRLSKFQDRLLEWLEKNPD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 81 VVHPSKYKSLALTSLE-------MSEDLSIsrsrsrlsWGIPVPNDPTQTIYVWLDALVNYLTVTGFPNAQ--------S 145
Cdd:cd00814 161 FIWPENARNEVLSWLKeglkdlsITRDLFD--------WGIPVPLDPGKVIYVWFDALIGYISATGYYNEEwgnswwwkD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 146 VWPPTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGN 225
Cdd:cd00814 233 GWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERP 312
|
....*..
gi 71992781 226 PSYDCSF 232
Cdd:cd00814 313 EGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
2-256 |
1.12e-75 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 240.27 E-value: 1.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEEDVVKKIVEGGAEKLT--------------------LKSNGTPVEWIEEENYM 61
Cdd:pfam09334 106 KLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARgdqcencgrhleptelinpkCVICGTTPEVKETEHYF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 62 FRLSEFREKVAEWINRENiVVHPSKYKSLALTSLEM-------SEDlsisrsrsrLSWGIPVPNDPTQTIYVWLDALVNY 134
Cdd:pfam09334 186 FDLSKFQDKLREWIEENN-PEWPENVKNMVLEWLKEglkdraiSRD---------LDWGIPVPGAEGKVFYVWLDAPIGY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 135 LTVTGFP-----NAQSVWP-----PTCQVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSLGNVVNP 204
Cdd:pfam09334 256 ISATKELsgneeKWKEWWPndpdtELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHGYLTYEGGKMSKSRGNVVWP 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 71992781 205 SEAITKFTAEGLRYFLLKHGNPSYDCSFNWNSCLQTINSDLVNNVGNLLNRS 256
Cdd:pfam09334 336 SEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
6-405 |
8.52e-54 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 188.38 E-value: 8.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 6 NGYIYKSTYSGYYSITDEcfipeedvvkkivEGGAEKLTLKSNGTPVEWI-----EEENYMFRLSEFREKVAEWINRENI 80
Cdd:PLN02224 180 NGDIYRADYEGLYCVNCE-------------EYKDEKELLENNCCPVHQMpcvarKEDNYFFALSKYQKPLEDILAQNPR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 81 VVHPSkYKSLALTSLEMSEDLSISRSRSRLSWGIPVPNDPTQTIYVWLDALVNYLTVTGFPNAQSV--------WPPTCQ 152
Cdd:PLN02224 247 FVQPS-YRLNEVQSWIKSGLRDFSISRALVDWGIPVPDDDKQTIYVWFDALLGYISALTEDNKQQNletavsfgWPASLH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 153 VIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGNPSYDCSF 232
Cdd:PLN02224 326 LIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFGNDGDY 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 233 NWNSCLQTINSDLVNNVGNLLNRsTVEKINKEGMYPKMEIEDIEAEIRENAKKLMEMVEESRENcvdlYDEMSYFKIIEN 312
Cdd:PLN02224 406 SEDRFIKIVNAHLANTIGNLLNR-TLGLLKKNCESTLVEDSTVAAEGVPLKDTVEKLVEKAQTN----YENLSLSSACEA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 313 LMLTMKEANRLFQSSQPW-----KEIDEKRLKSLLFVTYDTIRVVTILLQPITPKMAEFCLNRLGVPKNERN---LENSR 384
Cdd:PLN02224 481 VLEIGNAGNTYMDQRAPWflfkqGGVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQLGYSEDQFNsitWSDTK 560
|
410 420
....*....|....*....|.
gi 71992781 385 FGSYSGGKLGAERGVFIDRIQ 405
Cdd:PLN02224 561 WGGLKGGQVMEQASPVFARIE 581
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
2-374 |
1.71e-52 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 185.74 E-value: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSITDECFIPEedvvkKIVEG-----GAEK---------------LTLK------SNGTPVEWi 55
Cdd:PRK00133 109 KLKENGYIYEKTIEQLYDPEKGMFLPD-----RFVKGtcpkcGAEDqygdncevcgatyspTELInpksaiSGATPVLK- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 56 EEENYMFRLSEFREKVAEWINRENiVVHPSKYKSLA------LTSLEMSEDLSisrsrsrlsW-GIPVPNDPTQTIYVWL 128
Cdd:PRK00133 183 ESEHFFFKLPRFEEFLKEWITRSG-ELQPNVANKMKewleegLQDWDISRDAP---------YfGFEIPGAPGKVFYVWL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 129 DALVNYLTVT-------GFPNAQSVWP--PTC---QVIGKDITKFHLYYWPAFLMAAGLSLPQKVFIHGHWLIDNVKMSK 196
Cdd:PRK00133 253 DAPIGYISSTknlcdkrGGLDWDEYWKkdSDTelyHFIGKDIIYFHTLFWPAMLEGAGYRLPTNVFAHGFLTVEGAKMSK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 197 SLGNVVNPSEAITKFTAEGLRYFLLKHGNPSY-DCSFNWNSCLQTINSDLVNNVGNLLNRSTVeKINK--EGmypKMEIE 273
Cdd:PRK00133 333 SRGTFIWARTYLDHLDPDYLRYYLAAKLPETIdDLDFNWEDFQQRVNSELVGKVVNFASRTAG-FINKrfDG---KLPDA 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 274 DIEAEIRENAKKLMEMVEEsrencvdLYDEMSYFKIIENLMLTMKEANRLFQSSQPWKEI--DEKRLKSLLFVTYDTIRV 351
Cdd:PRK00133 409 LADPELLEEFEAAAEKIAE-------AYEAREFRKALREIMALADFANKYVDDNEPWKLAkqDGERLQAVCSVGLNLFRA 481
|
410 420
....*....|....*....|...
gi 71992781 352 VTILLQPITPKMAEFCLNRLGVP 374
Cdd:PRK00133 482 LAIYLKPVLPELAERAEAFLNLE 504
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
55-221 |
8.60e-31 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 119.83 E-value: 8.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 55 IEEENYMFRLSEFREKVAEWINRENIVvhPSKYKSlalTSLEMSEDLSISRSRSRLSWGIPVPNDptqTIYVWLDALVNY 134
Cdd:cd00668 137 RITEQWFFDMPKFKEKLLKALRRGKIV--PEHVKN---RMEAWLESLLDWAISRQRYWGTPLPED---VFDVWFDSGIGP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 135 LTVTGFPNAQSV----WPPTCQVIGKDITKFHLYYWPAFLMAAGLSLPQK-VFIHGHWLI-DNVKMSKSLGNVVNPSEAI 208
Cdd:cd00668 209 LGSLGYPEEKEWfkdsYPADWHLIGKDILRGWANFWITMLVALFGEIPPKnLLVHGFVLDeGGQKMSKSKGNVIDPSDVV 288
|
170
....*....|...
gi 71992781 209 TKFTAEGLRYFLL 221
Cdd:cd00668 289 EKYGADALRYYLT 301
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
241-365 |
5.40e-21 |
|
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA synthetases (MetRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon (CAU). MetRS catalyzes the transfer of methionine to the 3'-end of its tRNA.
Pssm-ID: 153411 [Multi-domain] Cd Length: 129 Bit Score: 87.93 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 241 INSDLVNNVGNLLNRsTVEKINK--EGMYPKMEIEDIEAEirenakKLMEMVEESRENCVDLYDEMSYFKIIENLMLTMK 318
Cdd:cd07957 1 INSELANNLGNLVNR-TLNMASKyfGGVVPEFGGLTEEDE------ELLEEAEELLEEVAEAMEELEFRKALEEIMELAR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 71992781 319 EANRLFQSSQPW---KEIDEKRLKSLLFVTYDTIRVVTILLQPITPKMAE 365
Cdd:cd07957 74 AANKYIDETAPWklaKEEDPERLATVLYVLLELLRILAILLSPFMPETAE 123
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
112-374 |
2.94e-19 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 90.22 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 112 WGIPVPND--PTQTIYVWLDALVNYLTVTG--FPNAQSVW--PPTC---QVIGKDITKFHLYYWPAFLMAAG--LSLPQK 180
Cdd:PLN02610 256 WGVPVPLEkyKDKVFYVWFDAPIGYVSITAcyTPEWEKWWknPENVelyQFMGKDNVPFHTVMFPSTLLGTGenWTMMKT 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 181 VFIHGHWLIDNVKMSKSLGNVVNPSEAI-TKFTAEGLRYFLLKHGNPSYDCSFNWNSCLQTINSDLVNNVGNLLNR--ST 257
Cdd:PLN02610 336 ISVTEYLNYEGGKFSKSKGVGVFGNDAKdTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNFINRvlSF 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 258 VEKINKEGmYPKMEIEDIEAEIRENAKKLMEMVEESRENCVdlyDEMSYFKIIENLMLTM---KEANRLFQSSQPWKEID 334
Cdd:PLN02610 416 IAKPPGAG-YGSVIPDAPGAESHPLTKKLAEKVGKLVEQYV---EAMEKVKLKQGLKTAMsisSEGNAYLQESQFWKLYK 491
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 71992781 335 EKRLKSLLFV--TYDTIRVVTILLQPITPKMAEFCLNRLGVP 374
Cdd:PLN02610 492 EDKPSCAIVVktSVGLVYLLACLLEPFMPSFSKEVLKQLNLP 533
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
155-234 |
2.11e-11 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 64.58 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 155 GKDITKFHLYY---WPAFLMAAGLSL---PQKVFIHGHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGNPsy 228
Cdd:cd00812 231 GKEHAPNHLLYsrfNHKALFDEGLVTdepPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAPP-- 308
|
....*.
gi 71992781 229 DCSFNW 234
Cdd:cd00812 309 DADFDW 314
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
49-372 |
3.45e-11 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 65.08 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 49 GTPVEWIEEENYMFRLSEFREKVAEWINRENIVVHPSKYKSLALTSLEMSEDLSISRSRSrlsWG--IPV---------- 116
Cdd:TIGR00422 347 GTVVEPLLSKQWFVKVEKLADKALEAAEEGEIKFVPKRMEKRYLNWLRNIKDWCISRQLI---WGhrIPVwyckecgevy 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 117 -------PNDPTQTIYV------------WLDALVNYLTVTGFPN----AQSVWPPTCQVIGKDItkfhLYYWPAFLMAA 173
Cdd:TIGR00422 424 vakeeplPDDKTNTGPSveleqdtdvldtWFSSSLWPFSTLGWPDetkdLKKFYPTDLLVTGYDI----IFFWVARMIFR 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 174 GLSL----PQK-VFIHGhwLI---DNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGNPSYDCSFNWnsclqtinsDL 245
Cdd:TIGR00422 500 SLALtgqvPFKeVYIHG--LVrdeQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDW---------KR 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 246 VNNVGNLLNR----STVEKINKEGM----YPKMEIEDIEAEIREnakKLMEMVEESRENcVDLYDEMSYFKIIENLMLTM 317
Cdd:TIGR00422 569 VESARNFLNKlwnaSRFVLMNLSDDlelsGGEEKLSLADRWILS---KLNRTIKEVRKA-LDKYRFAEAAKALYEFIWND 644
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 71992781 318 KEANRLFQSSQPWKEIDEKRLKSLLFVTYDTIRVVTILLQPITPKMAEFCLNRLG 372
Cdd:TIGR00422 645 FCDWYIELVKYRLYNGNEAEKKAARDTLYYVLDKALRLLHPFMPFITEEIWQHFK 699
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
180-223 |
2.77e-10 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 59.51 E-value: 2.77e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 71992781 180 KVFIH-GHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLKH 223
Cdd:cd00672 160 RYWLHtGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSS 204
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
127-232 |
1.44e-09 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 59.18 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 127 WLDALVNYLTVTGFPNAQSV----WPPTCQVIGKDItkfhLYYWPAFLMAAGLSLPQK-----VFIHGhwLI---DNVKM 194
Cdd:cd00817 271 WFSSSLWPFSTLGWPEETKDlkkfYPTSLLVTGHDI----IFFWVARMIMRGLKLTGKlpfkeVYLHG--LVrdeDGRKM 344
|
90 100 110
....*....|....*....|....*....|....*...
gi 71992781 195 SKSLGNVVNPSEAITKFTAEGLRYFLLKHGNPSYDCSF 232
Cdd:cd00817 345 SKSLGNVIDPLDVIDGYGADALRFTLASAATQGRDINL 382
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
180-221 |
6.61e-09 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 57.42 E-value: 6.61e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 71992781 180 KVFIHGHWL-IDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLL 221
Cdd:COG0215 251 RYWMHNGFLtVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLL 293
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
171-221 |
9.99e-08 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 53.14 E-value: 9.99e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 71992781 171 MAAGLSLPQKVFIH-GHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLL 221
Cdd:pfam01406 230 EAAFDKQLANYWLHnGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLL 281
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
153-221 |
1.05e-07 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 53.96 E-value: 1.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71992781 153 VIGKDItkfhLYYWPAFLMAAGLSL----P-QKVFIHGhwLI---DNVKMSKSLGNVVNPSEAITKFTAEGLRYFLL 221
Cdd:PRK05729 478 VTGFDI----IFFWVARMIMMGLHFtgqvPfKDVYIHG--LVrdeQGRKMSKSKGNVIDPLDLIDKYGADALRFTLA 548
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
182-329 |
1.76e-07 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 53.11 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 182 FIH-GHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLKHgnpSYDCSFNWN--SCLQTINSDLV-----NNVGNLL 253
Cdd:PTZ00399 303 FLHsGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLH---KWDKPMNYSdeSMDEAIEKDKVffnffANVKIKL 379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71992781 254 NRSTVEKINKEGmypkmeiedieaeirENAKKLMEMVEESRENcVD--LYDEMSYFKIIENLMLTMKEAN-RLFQSSQP 329
Cdd:PTZ00399 380 RESELTSPQKWT---------------QHDFELNELFEETKSA-VHaaLLDNFDTPEALQALQKLISATNtYLNSGEQP 442
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
180-221 |
8.14e-07 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 51.21 E-value: 8.14e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 71992781 180 KVFIHGhwLI---DNVKMSKSLGNVVNPSEAITKFTAEGLRYFLL 221
Cdd:COG0525 508 DVYIHG--LVrdeQGRKMSKSKGNVIDPLDLIDKYGADALRFTLA 550
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
2-221 |
1.55e-06 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 49.54 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 2 KIQDNGYIYKSTYSGYYSI----TDECFIPEEDVVKKIveggaekltLKSNGTpVEWIEEENYMfRLSEFREKVAEW-IN 76
Cdd:cd00818 127 QLHEKGLLYRGYKVVPWPLiyraTPQWFIRVTKIKDRL---------LEANDK-VNWIPEWVKN-RFGNWLENRRDWcIS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 77 RenivvhpSKYkslaltslemsedlsisrsrsrlsWGIPVPndptqtiyVWLDALVNYLTVTGFPNAQSVW-----PPTC 151
Cdd:cd00818 196 R-------QRY------------------------WGTPIP--------VWYCEDCGEVLVRRVPDVLDVWfdsgsMPYA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 152 QVIGKDITKFHLYYWPAFLMAAGL--------SL-----------PQK-VFIHGHWLI-DNVKMSKSLGNVVNPSEAITK 210
Cdd:cd00818 237 QLHYPFENEDFEELFPADFILEGSdqtrgwfySLlllstalfgkaPYKnVIVHGFVLDeDGRKMSKSLGNYVDPQEVVDK 316
|
250
....*....|.
gi 71992781 211 FTAEGLRYFLL 221
Cdd:cd00818 317 YGADALRLWVA 327
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
155-235 |
1.62e-06 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 50.19 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 155 GKDITKFHLYYwpAFLMAAGL--SLPQK-VFIHGHWL-IDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLkHGNPSYDC 230
Cdd:PRK13208 493 GHDIIRTWLFY--TILRAYLLtgKLPWKnIMISGMVLdPDGKKMSKSKGNVVTPEELLEKYGADAVRYWAA-SARLGSDT 569
|
....*
gi 71992781 231 SFNWN 235
Cdd:PRK13208 570 PFDEK 574
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
127-225 |
3.19e-06 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 49.51 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 127 WLDALVNYLTVTGFPNA----QSVWPPTCQVIGKDItkfhLYYWPAFLMAAGLSLP-----QKVFIHGhwLIDNV---KM 194
Cdd:PLN02381 583 WFSSGLFPLSVLGWPDDtddlKAFYPTSVLETGHDI----LFFWVARMVMMGMQLGgdvpfRKVYLHP--MIRDAhgrKM 656
|
90 100 110
....*....|....*....|....*....|.
gi 71992781 195 SKSLGNVVNPSEAITKFTAEGLrYFLLKHGN 225
Cdd:PLN02381 657 SKSLGNVIDPLEVINGISLEGL-HKRLEEGN 686
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
193-235 |
3.88e-06 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 49.31 E-value: 3.88e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 71992781 193 KMSKSLGNVVNPSEAITKFTAEGLRYFLLKHgNPSYDCSFNWN 235
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASS-DYWGDLRFSDE 644
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
127-220 |
2.01e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 46.86 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 127 WLDALVNYLTVTGFPNA-----QSVWPPTCQVIGKDItkfhLYYWPAFLMAAGLSLPQKV---FIHGHWLIDNV---KMS 195
Cdd:PLN02943 510 WFSSALWPFSTLGWPDVsaedfKKFYPTTVLETGHDI----LFFWVARMVMMGIEFTGTVpfsYVYLHGLIRDSqgrKMS 585
|
90 100
....*....|....*....|....*
gi 71992781 196 KSLGNVVNPSEAITKFTAEGLRYFL 220
Cdd:PLN02943 586 KTLGNVIDPLDTIKEFGTDALRFTL 610
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
155-221 |
2.22e-05 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 46.63 E-value: 2.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992781 155 GKDITKFHLYYWPAFLMAAGLSLPQK-VFIHGhwLI---DNVKMSKSLGNVVNPSEAITKFTAEGLRYFLL 221
Cdd:pfam00133 523 GSDQTRGWFYRMIMLSTALTGSVPFKnVLVHG--LVrdeQGRKMSKSLGNVIDPLDVIDKYGADALRLWLA 591
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
193-372 |
5.10e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 45.58 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 193 KMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGnPSYDcsfnwnscLQTINSDLVNNVGNLLNRS---TVEKINKEGMYPK 269
Cdd:PLN02563 723 KMSKSRGNVVNPDDVVSEYGADSLRLYEMFMG-PLRD--------SKTWSTSGVEGVHRFLGRTwrlVVGAPLPDGSFRD 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 270 MEIEDIEAEIRENAKKLMEMVEESRENCvdlyDEMSYFKIIENLMLTMKEANRlfqssqpWkeidEKRLKSLlfvtydtI 349
Cdd:PLN02563 794 GTVVTDEEPSLEQLRLLHKCIAKVTEEI----ESTRFNTAISAMMEFTNAAYK-------W----DKVPREA-------I 851
|
170 180
....*....|....*....|...
gi 71992781 350 RVVTILLQPITPKMAEFCLNRLG 372
Cdd:PLN02563 852 EPFVLLLSPYAPHLAEELWFRLG 874
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
177-365 |
5.39e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 45.63 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 177 LPQKVFIHGHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGNPSYDcsFNWnsclqtiNSDLVNNVGNLLNRs 256
Cdd:PRK12300 561 WPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQD--ADW-------REKEVESVRRQLER- 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 257 tvekinkegMYPKM-EIEDIEAEIRENA------KKLMEMVEESRENcvdlYDEMSYFKIIENLMLTMKEANRLFQSSQP 329
Cdd:PRK12300 631 ---------FYELAkELIEIGGEEELRFidkwllSRLNRIIKETTEA----MESFQTRDAVQEAFYELLNDLRWYLRRVG 697
|
170 180 190
....*....|....*....|....*....|....*.
gi 71992781 330 wkEIDEKRLKSLlfvtydtIRVVTILLQPITPKMAE 365
Cdd:PRK12300 698 --EANNKVLREV-------LEIWIRLLAPFTPHLAE 724
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
193-372 |
8.11e-05 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 45.04 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 193 KMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGNPsyDCSFNWNsclqtiNSDlVNNVGNLLNR--STVEKINKEGMYPKM 270
Cdd:COG0495 589 KMSKSKGNVVDPDEIIEKYGADTLRLFEMFAGPP--ERDLEWS------DSG-VEGAYRFLNRvwRLVVDEAEALKLDVA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 271 EIEDIEAEIRenaKKLMEMVEESRENcvdlYDEMSYFKIIENLMLTMKEANRLFQSSQPWKEidekrlksllfVTYDTIR 350
Cdd:COG0495 660 DLSEADKELR---RALHKTIKKVTED----IERLRFNTAIAALMELVNALYKAKDSGEADRA-----------VLREALE 721
|
170 180
....*....|....*....|..
gi 71992781 351 VVTILLQPITPKMAEFCLNRLG 372
Cdd:COG0495 722 TLVLLLAPFAPHIAEELWERLG 743
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
153-232 |
7.05e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 41.98 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 153 VIGKDITKFHL----YYWPAflMAAGLSLPQKVFIHGHWLIDNVKMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGNPSY 228
Cdd:PLN02959 676 VSGKDLIQNHLtfaiYNHTA--IWAEEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALADAGDGVD 753
|
....
gi 71992781 229 DCSF 232
Cdd:PLN02959 754 DANF 757
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
141-220 |
9.28e-04 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 41.52 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 141 PNAQSVWPPTCQVIGKDItkfhLYYWPAFLMAAGLSLPQKVFIHGHWLIDNV------KMSKSLGNVVNPSEAITKFTAE 214
Cdd:PRK14900 484 DTLRTFYPTSVMETGHDI----IFFWVARMMMMGLHFMGEVPFRTVYLHPMVrdekgqKMSKTKGNVIDPLVITEQYGAD 559
|
....*.
gi 71992781 215 GLRYFL 220
Cdd:PRK14900 560 ALRFTL 565
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
193-232 |
9.39e-04 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 41.16 E-value: 9.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 71992781 193 KMSKSLGNVVNPSEAITKFTAEGLRYFLLKHGNPSYDCSF 232
Cdd:cd00674 275 KMSSSKGNVITPSDWLEVAPPEVLRYLYARRKNPEKHIGF 314
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
135-216 |
8.38e-03 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 38.45 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992781 135 LTVTGFPNA----QSVWPPTCQVIGKDItkfhLYYWPAFLMAAGLSLPQK-----VFIHGhwLI---DNVKMSKSLGNVV 202
Cdd:PTZ00419 521 FSTLGWPDQtddlQRFFPTSLLETGSDI----LFFWVARMVMMSLHLTDKlpfktVFLHA--MVrdsQGEKMSKSKGNVI 594
|
90
....*....|....
gi 71992781 203 NPSEAITKFTAEGL 216
Cdd:PTZ00419 595 DPLEVIEGISLQDL 608
|
|
| |
