|
Name |
Accession |
Description |
Interval |
E-value |
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
1-550 |
0e+00 |
|
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: 696.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 1 MKVLVTAAWPYVNSVPHLGNLIgSILSADVFARYARLRyGKEnVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYDR 80
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLR-GHD-VLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 81 HLFlNVWKISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPDRFVKGTCPYCGFEDARGDQCDN 158
Cdd:COG0143 78 ELF-EKLGISFDNFIRTTSPEHKELVQEIFQRLYDngDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 159 CGKLLTPSLLVNPKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWISSSNEMPDNVKSVALSWVGEGLKPRSITRDNKWGI 238
Cdd:COG0143 157 CGATLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPDIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 239 PAPfeGAQDKSIYVWFEALLGYISAVIEYFERKGDQEKWKEYWFGPNIKSYYFIGKDNIPFHAVILPAMLMASeeEYHLP 318
Cdd:COG0143 237 PVP--GDPGKVFYVWFDALIGYISATKGYADDRGLPEDFEKYWPAPDTELVHFIGKDIIRFHAIIWPAMLMAA--GLPLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 319 DVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGNYVNRVLS 398
Cdd:COG0143 313 KKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 399 MVNRYYSGIVPEfkIDILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDLYKSGKEIEL 478
Cdd:COG0143 393 MIHKYFDGKVPE--PGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPERL 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497676884 479 KNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLNMgNIENEKWDVASTLsVNPGHKIGKVNVLFKKLEPEFE 550
Cdd:COG0143 471 ATVLYTLLEALRILAILLKPFLPETAEKILEQLGL-EGDELTWEDAGWP-LPAGHKIGKPEPLFPRIEDEQI 540
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
3-396 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 587.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 3 VLVTAAWPYVNSVPHLGNLIgSILSADVFARYARLRygKENVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYDRHL 82
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLY-SYIPADIFARYLRLR--GYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHRED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 83 FLNvWKISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPDRFVKGTCPYCGFEDARGDQCDNCG 160
Cdd:pfam09334 78 FKK-FNISFDDYGRTTSERHHELVQEFFLKLYEngYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 161 KLLTPSLLVNPKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWISSSN-EMPDNVKSVALSWVGEGLKPRSITRDNKWGIP 239
Cdd:pfam09334 157 RHLEPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNpEWPENVKNMVLEWLKEGLKDRAISRDLDWGIP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 240 APfeGAQDKSIYVWFEALLGYISAVIEYFerkGDQEKWKEYW-FGPNIKSYYFIGKDNIPFHAVILPAMLMAseEEYHLP 318
Cdd:pfam09334 237 VP--GAEGKVFYVWLDAPIGYISATKELS---GNEEKWKEWWpNDPDTELVHFIGKDIIYFHTIFWPAMLLG--AGYRLP 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497676884 319 DVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGNYVNRV 396
Cdd:pfam09334 310 TTVFAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
1-569 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 567.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 1 MKVLVTAAWPYVNSVPHLGNLIGSIlSADVFARYARLRygKENVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAH-EYD 79
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVEYI-QADIWVRYQRMR--GHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHaEHK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 80 RHL--FLnvwkISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPDRFVKGTCPYCGFEDARGDQ 155
Cdd:PRK00133 79 RDFagFG----ISFDNYGSTHSEENRELAQEIYLKLKEngYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 156 CDNCGKLLTPSLLVNPKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWISSSNEMPDNVKSVALSWVGEGLKPRSITRDNK 235
Cdd:PRK00133 155 CEVCGATYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRSGELQPNVANKMKEWLEEGLQDWDISRDAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 236 W-GIPAPfeGAQDKSIYVWFEALLGYISAVIEYFERKGDqEKWKEYWF-GPNIKSYYFIGKDNIPFHAVILPAMLMASee 313
Cdd:PRK00133 235 YfGFEIP--GAPGKVFYVWLDAPIGYISSTKNLCDKRGG-LDWDEYWKkDSDTELYHFIGKDIIYFHTLFWPAMLEGA-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 314 EYHLPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPE-EKDTNFTWRETVRIVNTELNDDIGNY 392
Cdd:PRK00133 310 GYRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPEtIDDLDFNWEDFQQRVNSELVGKVVNF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 393 VNRVLSMVNRYYSGIVPefkidiLDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDLYKS 472
Cdd:PRK00133 390 ASRTAGFINKRFDGKLP------DALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 473 GKEiELKNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLNMgniENEKWDVASTLSVnpGHKIGKVNVLFKKLEPEfesK 552
Cdd:PRK00133 464 DGE-RLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNL---EELTWDDAQQPLA--GHPINKFKILFTRIEDK---Q 534
|
570
....*....|....*..
gi 497676884 553 IKDKLEKIRKDIEKIRP 569
Cdd:PRK00133 535 IEALIEASKEAAAAKAA 551
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
3-546 |
4.31e-175 |
|
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: 505.76 E-value: 4.31e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 3 VLVTAAWPYVNSVPHLGNLIgSILSADVFARYARLRygKENVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYdrhl 82
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLR--GYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 83 FLNVWK---ISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPDRFVKGTCPYCGFEDARGDQCD 157
Cdd:TIGR00398 74 FKDDWKwlnISFDRFIRTTDEEHKEIVQKIFQKLKEngYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 158 NCGKLLTPSLLVNPKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWI---SSSNEMPDNVKSVALSWVGEGLKPRSITRDN 234
Cdd:TIGR00398 154 VCGRHLEPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIrknPESGSPASNVKNKAQNWLKGGLKDLAITRDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 235 K-WGIPAPFEgaQDKSIYVWFEALLGYISAVIEyfeRKGDQEKWKEYWF-GPNIKSYYFIGKDNIPFHAVILPAMLMASe 312
Cdd:TIGR00398 234 VyWGIPVPND--PNKVVYVWFDALIGYISSLGI---LSGDTEDWKKWWNnDEDAELIHFIGKDIVRFHTIYWPAMLMGL- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 313 eEYHLPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGNY 392
Cdd:TIGR00398 308 -GLPLPTQVFSHGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 393 VNRVLSMVNRYYSGIVPefKIDILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDLYKS 472
Cdd:TIGR00398 387 LNRTLGFIKKYFNGVLP--SEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQ 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497676884 473 GKeiELKNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLnmgNIENEKWDVASTLSvnpGHKIGKVNVLFKKLE 546
Cdd:TIGR00398 465 SP--RLKELLAVCSMLIRVLSILLYPIMPKLSEKILKFL---NFELEWDFKLKLLE---GHKLNKAEPLFSKIE 530
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
2-372 |
3.58e-144 |
|
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: 418.86 E-value: 3.58e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 2 KVLVTAAWPYVNSVPHLGNLIGSILsADVFARYARLRYgkENVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYDRH 81
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRG--YDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 82 LFLNvWKISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPdrfvkgtcpycgfedargdqcdnc 159
Cdd:cd00814 78 LFKW-LNISFDYFIRTTSPRHKEIVQEFFKKLYEngYIYEGEYEGLYCVSCERFLP------------------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 160 gklltpsllvnpkcsicgktpVFKKTKHWFFDLSEFNDKIRGWISSSNE--MPDNVKSVALSWVGEGLKPRSITRDN-KW 236
Cdd:cd00814 133 ---------------------EWREEEHYFFRLSKFQDRLLEWLEKNPDfiWPENARNEVLSWLKEGLKDLSITRDLfDW 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 237 GIPAPFegAQDKSIYVWFEALLGYISAVIEYFERKGDQEKWKEYWfgpnIKSYYFIGKDNIPFHAVILPAMLMASEeeYH 316
Cdd:cd00814 192 GIPVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNSWWWKDGW----PELVHFIGKDIIRFHAIYWPAMLLGAG--LP 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 497676884 317 LPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNF 372
Cdd:cd00814 264 LPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
1-550 |
0e+00 |
|
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: 696.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 1 MKVLVTAAWPYVNSVPHLGNLIgSILSADVFARYARLRyGKEnVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYDR 80
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLR-GHD-VLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 81 HLFlNVWKISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPDRFVKGTCPYCGFEDARGDQCDN 158
Cdd:COG0143 78 ELF-EKLGISFDNFIRTTSPEHKELVQEIFQRLYDngDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 159 CGKLLTPSLLVNPKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWISSSNEMPDNVKSVALSWVGEGLKPRSITRDNKWGI 238
Cdd:COG0143 157 CGATLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPDIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 239 PAPfeGAQDKSIYVWFEALLGYISAVIEYFERKGDQEKWKEYWFGPNIKSYYFIGKDNIPFHAVILPAMLMASeeEYHLP 318
Cdd:COG0143 237 PVP--GDPGKVFYVWFDALIGYISATKGYADDRGLPEDFEKYWPAPDTELVHFIGKDIIRFHAIIWPAMLMAA--GLPLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 319 DVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGNYVNRVLS 398
Cdd:COG0143 313 KKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 399 MVNRYYSGIVPEfkIDILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDLYKSGKEIEL 478
Cdd:COG0143 393 MIHKYFDGKVPE--PGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPERL 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497676884 479 KNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLNMgNIENEKWDVASTLsVNPGHKIGKVNVLFKKLEPEFE 550
Cdd:COG0143 471 ATVLYTLLEALRILAILLKPFLPETAEKILEQLGL-EGDELTWEDAGWP-LPAGHKIGKPEPLFPRIEDEQI 540
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
3-396 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 587.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 3 VLVTAAWPYVNSVPHLGNLIgSILSADVFARYARLRygKENVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYDRHL 82
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLY-SYIPADIFARYLRLR--GYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHRED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 83 FLNvWKISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPDRFVKGTCPYCGFEDARGDQCDNCG 160
Cdd:pfam09334 78 FKK-FNISFDDYGRTTSERHHELVQEFFLKLYEngYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 161 KLLTPSLLVNPKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWISSSN-EMPDNVKSVALSWVGEGLKPRSITRDNKWGIP 239
Cdd:pfam09334 157 RHLEPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNpEWPENVKNMVLEWLKEGLKDRAISRDLDWGIP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 240 APfeGAQDKSIYVWFEALLGYISAVIEYFerkGDQEKWKEYW-FGPNIKSYYFIGKDNIPFHAVILPAMLMAseEEYHLP 318
Cdd:pfam09334 237 VP--GAEGKVFYVWLDAPIGYISATKELS---GNEEKWKEWWpNDPDTELVHFIGKDIIYFHTIFWPAMLLG--AGYRLP 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497676884 319 DVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGNYVNRV 396
Cdd:pfam09334 310 TTVFAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
1-569 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 567.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 1 MKVLVTAAWPYVNSVPHLGNLIGSIlSADVFARYARLRygKENVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAH-EYD 79
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVEYI-QADIWVRYQRMR--GHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHaEHK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 80 RHL--FLnvwkISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPDRFVKGTCPYCGFEDARGDQ 155
Cdd:PRK00133 79 RDFagFG----ISFDNYGSTHSEENRELAQEIYLKLKEngYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 156 CDNCGKLLTPSLLVNPKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWISSSNEMPDNVKSVALSWVGEGLKPRSITRDNK 235
Cdd:PRK00133 155 CEVCGATYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRSGELQPNVANKMKEWLEEGLQDWDISRDAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 236 W-GIPAPfeGAQDKSIYVWFEALLGYISAVIEYFERKGDqEKWKEYWF-GPNIKSYYFIGKDNIPFHAVILPAMLMASee 313
Cdd:PRK00133 235 YfGFEIP--GAPGKVFYVWLDAPIGYISSTKNLCDKRGG-LDWDEYWKkDSDTELYHFIGKDIIYFHTLFWPAMLEGA-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 314 EYHLPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPE-EKDTNFTWRETVRIVNTELNDDIGNY 392
Cdd:PRK00133 310 GYRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPEtIDDLDFNWEDFQQRVNSELVGKVVNF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 393 VNRVLSMVNRYYSGIVPefkidiLDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDLYKS 472
Cdd:PRK00133 390 ASRTAGFINKRFDGKLP------DALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 473 GKEiELKNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLNMgniENEKWDVASTLSVnpGHKIGKVNVLFKKLEPEfesK 552
Cdd:PRK00133 464 DGE-RLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNL---EELTWDDAQQPLA--GHPINKFKILFTRIEDK---Q 534
|
570
....*....|....*..
gi 497676884 553 IKDKLEKIRKDIEKIRP 569
Cdd:PRK00133 535 IEALIEASKEAAAAKAA 551
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
3-546 |
4.31e-175 |
|
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: 505.76 E-value: 4.31e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 3 VLVTAAWPYVNSVPHLGNLIgSILSADVFARYARLRygKENVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYdrhl 82
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLR--GYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 83 FLNVWK---ISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPDRFVKGTCPYCGFEDARGDQCD 157
Cdd:TIGR00398 74 FKDDWKwlnISFDRFIRTTDEEHKEIVQKIFQKLKEngYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 158 NCGKLLTPSLLVNPKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWI---SSSNEMPDNVKSVALSWVGEGLKPRSITRDN 234
Cdd:TIGR00398 154 VCGRHLEPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIrknPESGSPASNVKNKAQNWLKGGLKDLAITRDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 235 K-WGIPAPFEgaQDKSIYVWFEALLGYISAVIEyfeRKGDQEKWKEYWF-GPNIKSYYFIGKDNIPFHAVILPAMLMASe 312
Cdd:TIGR00398 234 VyWGIPVPND--PNKVVYVWFDALIGYISSLGI---LSGDTEDWKKWWNnDEDAELIHFIGKDIVRFHTIYWPAMLMGL- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 313 eEYHLPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGNY 392
Cdd:TIGR00398 308 -GLPLPTQVFSHGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 393 VNRVLSMVNRYYSGIVPefKIDILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDLYKS 472
Cdd:TIGR00398 387 LNRTLGFIKKYFNGVLP--SEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQ 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497676884 473 GKeiELKNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLnmgNIENEKWDVASTLSvnpGHKIGKVNVLFKKLE 546
Cdd:TIGR00398 465 SP--RLKELLAVCSMLIRVLSILLYPIMPKLSEKILKFL---NFELEWDFKLKLLE---GHKLNKAEPLFSKIE 530
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
3-548 |
1.21e-152 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 457.70 E-value: 1.21e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 3 VLVTAAWPYVNSVPHLGNLIGSILSADVFARYARLRygKENVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYDRHL 82
Cdd:PLN02610 19 ILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLR--GYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 83 FlNVWKISFDNYTRTESEIHKKFVREFLLKLTKYIKVSEDEI--PYCENDKLYLPDRFVKGTCPY--CGFEDARGDQCDN 158
Cdd:PLN02610 97 Y-DWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMqqLYCDTCQKFLADRLVEGTCPTegCNYDSARGDQCEK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 159 CGKLLTPSLLVNPKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWI---SSSNEMPDNVKSVALSWVGEGLKPRSITRDNK 235
Cdd:PLN02610 176 CGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYInetSVAGGWSQNAIQTTNAWLRDGLKPRCITRDLK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 236 WGIPAPFEGAQDKSIYVWFEALLGYISAVIEYferKGDQEKWkeyWFGP-NIKSYYFIGKDNIPFHAVILPAMLMASEEE 314
Cdd:PLN02610 256 WGVPVPLEKYKDKVFYVWFDAPIGYVSITACY---TPEWEKW---WKNPeNVELYQFMGKDNVPFHTVMFPSTLLGTGEN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 315 YHLPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPEL-MDVEYWRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGNYV 393
Cdd:PLN02610 330 WTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTnIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNFI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 394 NRVLSMV----NRYYSGIVPEFKIDILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDL 469
Cdd:PLN02610 410 NRVLSFIakppGAGYGSVIPDAPGAESHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQFWKL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 470 YKSGKE---IELKNTLYIgtnsVKTIAILLYPLMPSHAQKIYEMLNMG----NIENEKWDVASTLS----VNPGHKIGKV 538
Cdd:PLN02610 490 YKEDKPscaIVVKTSVGL----VYLLACLLEPFMPSFSKEVLKQLNLPpeslSLSDEKGEVARAKRpwelVPAGHKIGTP 565
|
570
....*....|
gi 497676884 539 NVLFKKLEPE 548
Cdd:PLN02610 566 EPLFKELKDE 575
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
2-372 |
3.58e-144 |
|
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: 418.86 E-value: 3.58e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 2 KVLVTAAWPYVNSVPHLGNLIGSILsADVFARYARLRYgkENVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYDRH 81
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRG--YDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 82 LFLNvWKISFDNYTRTESEIHKKFVREFLLKLTK--YIKVSEDEIPYCENDKLYLPdrfvkgtcpycgfedargdqcdnc 159
Cdd:cd00814 78 LFKW-LNISFDYFIRTTSPRHKEIVQEFFKKLYEngYIYEGEYEGLYCVSCERFLP------------------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 160 gklltpsllvnpkcsicgktpVFKKTKHWFFDLSEFNDKIRGWISSSNE--MPDNVKSVALSWVGEGLKPRSITRDN-KW 236
Cdd:cd00814 133 ---------------------EWREEEHYFFRLSKFQDRLLEWLEKNPDfiWPENARNEVLSWLKEGLKDLSITRDLfDW 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 237 GIPAPFegAQDKSIYVWFEALLGYISAVIEYFERKGDQEKWKEYWfgpnIKSYYFIGKDNIPFHAVILPAMLMASEeeYH 316
Cdd:cd00814 192 GIPVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNSWWWKDGW----PELVHFIGKDIIRFHAIYWPAMLLGAG--LP 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 497676884 317 LPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNF 372
Cdd:cd00814 264 LPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
1-548 |
2.31e-120 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 364.97 E-value: 2.31e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 1 MKVLVTAAWPYVNSVPHLGNLiGSILSADVFARYARLRyGKEnVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYDR 80
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHA-YTTLAADVLARFKRLR-GYD-VFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 81 HLfLNVWKISFDNYTRTESEIHKKFVREFLLKLtkyikvsedeipyCENDKLYLpdRFVKGtcPYCgfedargdqcDNCG 160
Cdd:PRK11893 78 RL-WEALNISYDDFIRTTDPRHKEAVQEIFQRL-------------LANGDIYL--GKYEG--WYC----------VRCE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 161 KLLTPSLLVNPK--CSICGKTPVFKKTKHWFFDLSEFNDKIRGWIsssNEMPDNVKSVA-----LSWVGEGLKPRSITRD 233
Cdd:PRK11893 130 EFYTESELIEDGyrCPPTGAPVEWVEEESYFFRLSKYQDKLLELY---EANPDFIQPASrrnevISFVKSGLKDLSISRT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 234 N-KWGIPAPFEGAQdkSIYVWFEALLGYISAVIEYFERKGDQEKWKEYWfgPNikSYYFIGKDNIPFHAVILPAMLMASE 312
Cdd:PRK11893 207 NfDWGIPVPGDPKH--VIYVWFDALTNYLTALGYPDDEELLAELFNKYW--PA--DVHLIGKDILRFHAVYWPAFLMAAG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 313 eeYHLPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGNY 392
Cdd:PRK11893 281 --LPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 393 VNRVLSMVNRYYSGIVPEfkIDILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDLYKS 472
Cdd:PRK11893 359 AQRTLSMIAKNFDGKVPE--PGALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKT 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497676884 473 GKEiELKNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLNMGNIENEKWDVASTLSVNPGHKIGKVNVLFKKLEPE 548
Cdd:PRK11893 437 DPE-RLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEEDENRDFAALSWGRLAPGTTLPKPEPIFPRLEEE 511
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
11-566 |
7.90e-87 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 282.07 E-value: 7.90e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 11 YVNSVPHLGNLIGSILsADVFARYARLRyGKEnVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEydrhLFLNVWK-- 88
Cdd:PRK12267 14 YPNGKPHIGHAYTTIA-ADALARYKRLQ-GYD-VFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISA----GFKELWKkl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 89 -ISFDNYTRTESEIHKKFVREFLLKLtkYikvsedeipycENDKLYlpdrfvKGTcpYCGFedargdQCDNCGKLLTPSL 167
Cdd:PRK12267 87 dISYDKFIRTTDERHKKVVQKIFEKL--Y-----------EQGDIY------KGE--YEGW------YCVSCETFFTESQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 168 LVN-PKCSICGKTPVFKKTKHWFFDLSEFNDKIRGWI----------SSSNEMPDNvksvalsWVGEGLKPRSITRDN-K 235
Cdd:PRK12267 140 LVDgGKCPDCGREVELVKEESYFFRMSKYQDRLLEYYeenpdfiqpeSRKNEMINN-------FIKPGLEDLSISRTSfD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 236 WGIPAPFEGaqDKSIYVWFEALLGYISAvIEYfeRKGDQEKWKEYWfgPNikSYYFIGKDNIPFHAVILPAMLMASEEEy 315
Cdd:PRK12267 213 WGIPVPFDP--KHVVYVWIDALLNYITA-LGY--GSDDDELFKKFW--PA--DVHLVGKDILRFHAIYWPIMLMALGLP- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 316 hLPDVIAATEYLLYEGQKFSKSRkiGVWIDeaPELMDVEY----WRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGN 391
Cdd:PRK12267 283 -LPKKVFAHGWWLMKDGKMSKSK--GNVVD--PEELVDRYgldaLRYYLLREVPFGSDGDFSPEALVERINSDLANDLGN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 392 YVNRVLSMVNRYYSGIVPEFKidILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDLYK 471
Cdd:PRK12267 358 LLNRTVAMINKYFDGEIPAPG--NVTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISRANKYIDETAPWVLAK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 472 S-GKEIELKNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLNMgNIENEKWDVASTLSV-NPGHKIGKVNVLFKKLEPEF 549
Cdd:PRK12267 436 DeGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLGL-EEELTSWESLLEWGGlPAGTKVAKGEPLFPRIDVEE 514
|
570
....*....|....*...
gi 497676884 550 ESK-IKDKLEKIRKDIEK 566
Cdd:PRK12267 515 EIAyIKEQMEGSAPKEPE 532
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
3-568 |
1.30e-48 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 178.75 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 3 VLVTAAWpYVNSVPHLGNLIGSIlSADVFARYARLrYGKEnVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQAHEYDRHL 82
Cdd:PLN02224 72 VLTTPLY-YVNAPPHMGSAYTTI-AADSIARFQRL-LGKK-VIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 83 FLNVwKISFDNYTRTESEIHKKFVREFllkltkYIKVsedeipycendklylpdrFVKGTCPYCGFEdarGDQCDNCGKL 162
Cdd:PLN02224 148 WKDL-DIAYDKFIRTTDPKHEAIVKEF------YARV------------------FANGDIYRADYE---GLYCVNCEEY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 163 LTPSLLVNPKCSICGKTP-VFKKTKHWFFDLSEFNDKIRGWISSSNEM--PDNVKSVALSWVGEGLKPRSITRD-NKWGI 238
Cdd:PLN02224 200 KDEKELLENNCCPVHQMPcVARKEDNYFFALSKYQKPLEDILAQNPRFvqPSYRLNEVQSWIKSGLRDFSISRAlVDWGI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 239 PAPFEGAQdkSIYVWFEALLGYISAVIEYFERKGDQEKWKEYWFGpnikSYYFIGKDNIPFHAVILPAMLMASEEEyhLP 318
Cdd:PLN02224 280 PVPDDDKQ--TIYVWFDALLGYISALTEDNKQQNLETAVSFGWPA----SLHLIGKDILRFHAVYWPAMLMSAGLE--LP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 319 DVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNFTWRETVRIVNTELNDDIGNYVNRVLS 398
Cdd:PLN02224 352 KMVFGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNRTLG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 399 MVNRY-YSGIVPEFKIDI----LDDNDRKIISLINETpkvvgdlFEKGKLKAGTEEMLKFVRECNAYLNMKAPWDLYKSG 473
Cdd:PLN02224 432 LLKKNcESTLVEDSTVAAegvpLKDTVEKLVEKAQTN-------YENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQG 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 474 --KEIELKNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLnmGNIENE----KWDVASTLSVNPGHKIGKVNVLFKKLEP 547
Cdd:PLN02224 505 gvSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQL--GYSEDQfnsiTWSDTKWGGLKGGQVMEQASPVFARIEL 582
|
570 580
....*....|....*....|.
gi 497676884 548 EFESKIKDKLEKIRKDIEKIR 568
Cdd:PLN02224 583 NPEKEEDEKKPKVGKKTGKAK 603
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
381-511 |
2.07e-43 |
|
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: 151.10 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 381 VNTELNDDIGNYVNRVLSMVNRYYSGIVPEFkiDILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAY 460
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEF--GGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKY 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 497676884 461 LNMKAPWDLYKSGKEIELKNTLYIGTNSVKTIAILLYPLMPSHAQKIYEML 511
Cdd:cd07957 79 IDETAPWKLAKEEDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
2-372 |
1.05e-32 |
|
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: 127.53 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 2 KVLVTAAWPYVNSVPHLGNLIGSILsADVFARYARLRyGKEnVLFVSGSDEHGTPIEIEAIKRKVN-------------P 68
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHII-ADFIARYKRMR-GYE-VPFLPGWDTHGLPIELKAERKGGRkkktiwieefredP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 69 KELTDQAHEYDRHLF--LNVWkISFDNYTRTESEIHKKFVREFLLKLtkyikvsedeipycendklylpdrFVKGtcpyc 146
Cdd:cd00668 78 KEFVEEMSGEHKEDFrrLGIS-YDWSDEYITTEPEYSKAVELIFSRL------------------------YEKG----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 147 gfedargdqcdncgklltpsLLVNpkcsicGKTPVfKKTKHWFFDLSEFNDKIRGWISSSNEMPDNVKSVALSWVGEGLK 226
Cdd:cd00668 128 --------------------LIYR------GTHPV-RITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEAWLESLLD 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 227 pRSITRDNKWGIPAPfegaqDKSIYVWFEALLGYISAVIEYFErkgdqEKWKEYWFGpniKSYYFIGKDNIPFHAVILPA 306
Cdd:cd00668 181 -WAISRQRYWGTPLP-----EDVFDVWFDSGIGPLGSLGYPEE-----KEWFKDSYP---ADWHLIGKDILRGWANFWIT 246
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497676884 307 MLMASEEEyHLPDVIAATEYLLYE-GQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDTNF 372
Cdd:cd00668 247 MLVALFGE-IPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYGDDIRL 312
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
2-374 |
2.30e-15 |
|
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: 77.29 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 2 KVLVTAAWPYVNSVPHLGNLIgSILSADVFARYARLRyGKeNVLFVSGSDEHGTPIEIEAIKRKVNPKELTDQaheydrh 81
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVR-TYTIGDIIARYKRMQ-GY-NVLFPMGFDAFGLPAENAAIKIGRDPEDWTEY------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 82 lFLNVWK-------ISFDnYTR---TESEIHKKFVREFLLKLTK--YIKVSEDEIPYCendklylpdrfvkgtcpycgfe 149
Cdd:cd00812 71 -NIKKMKeqlkrmgFSYD-WRReftTCDPEYYKFTQWLFLKLYEkgLAYKKEAPVNWC---------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 150 dargdqcdncgklltpsllvnpkcsicgktpvfKKTKHWFFDLS--EFNDKIRGWISSSNEMPDNVKSVALSWVGeglkp 227
Cdd:cd00812 127 ---------------------------------KLLDQWFLKYSetEWKEKLLKDLEKLDGWPEEVRAMQENWIG----- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 228 rsITRDNKWGIPAPF----EGAQDKSIYvwfeaLLGYISA----VIEYFERKGDQEKwKEYWFGPNIksyYFIGKDNIP- 298
Cdd:cd00812 169 --CSRQRYWGTPIPWtdtmESLSDSTWY-----YARYTDAhnleQPYEGDLEFDREE-FEYWYPVDI---YIGGKEHAPn 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 299 -------FHAVILPAMLMASEEeyhlPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPELMDVEYWRFVLIRLRPEEKDtn 371
Cdd:cd00812 238 hllysrfNHKALFDEGLVTDEP----PKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAPPDAD-- 311
|
...
gi 497676884 372 FTW 374
Cdd:cd00812 312 FDW 314
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
10-278 |
3.23e-07 |
|
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: 52.62 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 10 PYVNSVPHLGNLIGSILSaDVFARYARLRyGKeNVLFVSGSDEHGTPIEIEAIkrkvnpKELTDQAHEydrhlflNVWKI 89
Cdd:cd00818 10 PYANGLPHYGHALNKILK-DIINRYKTMQ-GY-YVPRRPGWDCHGLPIELKVE------KELGISGKK-------DIEKM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 90 SFDNYtrteseihKKFVREFLLkltKYIKVSEDEI-----------PYcendKLYLPDrfvkgtcpycgFEDArgdQCDN 158
Cdd:cd00818 74 GIAEF--------NAKCREFAL---RYVDEQEEQFqrlgvwvdwenPY----KTMDPE-----------YMES---VWWV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 159 CGKLLTPSLLVNpkcsicGKTPV-----FKKTKHWFFDLSEFNDKIRGWISSSNEMPDNVKSVALSWVgEGLKPRSITRD 233
Cdd:cd00818 125 FKQLHEKGLLYR------GYKVVpwpliYRATPQWFIRVTKIKDRLLEANDKVNWIPEWVKNRFGNWL-ENRRDWCISRQ 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 497676884 234 NKWGIPAP-FEGAQDKSIY---------VWFEALLGYiSAVIEY-FERKGDQEKWK 278
Cdd:cd00818 198 RYWGTPIPvWYCEDCGEVLvrrvpdvldVWFDSGSMP-YAQLHYpFENEDFEELFP 252
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
10-89 |
2.16e-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: 47.40 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 10 PYVNSVPHLGNLIGSILSaDVFARYARLRyGKeNVLFVSGSDEHGTPIEIEaIKRKVNPKELTDQaHEYDRHLFLN-VWK 88
Cdd:pfam00133 32 PNATGSLHIGHALAKTLK-DIVIRYKRMK-GY-YVLWVPGWDHHGLPTEQV-VEKKLGIKEKKTR-HKYGREEFREkCRE 106
|
.
gi 497676884 89 I 89
Cdd:pfam00133 107 W 107
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
420-509 |
4.74e-05 |
|
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA synthetases. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 400523 [Multi-domain] Cd Length: 141 Bit Score: 43.55 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 420 DRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRE--CNAYLNMKAPWdLYKSGKEIELKNTLYIgtnSVKTIAILLY 497
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWNdlSDWYLELIKDR-LYGEEPDSRAQTTLYE---VLETLLRLLA 76
|
90
....*....|..
gi 497676884 498 PLMPSHAQKIYE 509
Cdd:pfam08264 77 PFMPFITEELWQ 88
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
185-514 |
1.22e-04 |
|
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: 45.05 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 185 TKHWFFDLSEFNDKIRGWI--SSSNEMPDNVKSVALSWVGEgLKPRSITRDNKWG--IPAPFEgAQDKSIYV-------- 252
Cdd:TIGR00422 355 SKQWFVKVEKLADKALEAAeeGEIKFVPKRMEKRYLNWLRN-IKDWCISRQLIWGhrIPVWYC-KECGEVYVakeeplpd 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 253 --------------------WFEALLGYISaVIEYFERKGDQEKWKE------------YWFGPNI-KSYYFIGKdnIPF 299
Cdd:TIGR00422 433 dktntgpsveleqdtdvldtWFSSSLWPFS-TLGWPDETKDLKKFYPtdllvtgydiifFWVARMIfRSLALTGQ--VPF 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 300 HAVILPAMLMASEeeyhlpdviaateyllyeGQKFSKSRKIGVwideAPELMDVEY----WRFVLIRLRPEEKDTNFTWR 375
Cdd:TIGR00422 510 KEVYIHGLVRDEQ------------------GRKMSKSLGNVI----DPLDVIEKYgadaLRFTLASLVTPGDDINFDWK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 376 E---TVRIVNTELNddignyVNRVLSMVNRYYSGIvpEFKIDILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLK 452
Cdd:TIGR00422 568 RvesARNFLNKLWN------ASRFVLMNLSDDLEL--SGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALYE 639
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497676884 453 FVRE--CNAYLNMKAPwDLYkSGKEIELKNTLYIGTNSVKTIAILLYPLMPSHAQKIYEMLNMG 514
Cdd:TIGR00422 640 FIWNdfCDWYIELVKY-RLY-NGNEAEKKAARDTLYYVLDKALRLLHPFMPFITEEIWQHFKEG 701
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
388-500 |
1.33e-04 |
|
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway.
Pssm-ID: 153408 [Multi-domain] Cd Length: 117 Bit Score: 41.72 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 388 DIGNYVNRVLSMVNRYYSGIVPEFKIDILDDNDRKIISLINETPKVVGDLFEKGKLKAGTEEMLKFVRECNAYLNMKAPW 467
Cdd:cd07375 9 AFLNRLYRLLSFFRKALGGTQPKWDNELLEEADRELLARLQEFIKRTTNALEALDPTTAVQELFKFTNELNWYLDELKPA 88
|
90 100 110
....*....|....*....|....*....|...
gi 497676884 468 DLyksgKEIELKNTLYIGTNSVKTIAILLYPLM 500
Cdd:cd07375 89 LQ----TEELREAVLAVLRAALVVLTKLLAPFT 117
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
279-531 |
1.36e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 41.78 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 279 EYWFGPNIKsyyFIGKDNIP----F----HAVILPamlmaseeEYHLPDVIAATEYLLYEGQKFSKSRKIGVWIDEAPEL 350
Cdd:PRK12300 526 LYWYPVDWR---HSGKDLIPnhltFfifnHVAIFP--------EEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 351 MDVEYWRFVLIRLrpEEKDTNFTWREtvrivntelnddigNYVNRVLSMVNRYYSgIVPEFK----IDILDDNDRKIISL 426
Cdd:PRK12300 595 YGADVVRLYLTSS--AELLQDADWRE--------------KEVESVRRQLERFYE-LAKELIeiggEEELRFIDKWLLSR 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 427 INETpkvvgdlfekgkLKAGTEEMLKF-VREC--NAYLNMKAPWDLYKSGKEIELKNTLYigtNSVKTIAILLYPLMPSH 503
Cdd:PRK12300 658 LNRI------------IKETTEAMESFqTRDAvqEAFYELLNDLRWYLRRVGEANNKVLR---EVLEIWIRLLAPFTPHL 722
|
250 260
....*....|....*....|....*....
gi 497676884 504 AQKIYEMLN-MGNIENEKWDVASTLSVNP 531
Cdd:PRK12300 723 AEELWHKLGgEGFVSLEKWPEPDESKIDE 751
|
|
| Anticodon_3 |
pfam19303 |
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ... |
458-548 |
5.28e-03 |
|
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ligase. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 437135 [Multi-domain] Cd Length: 152 Bit Score: 37.87 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 458 NAYLNMKAPWDLYKSGKE-----IELkntlyiGTNSVKTIAILLYPLMPSHAQKIYEMLNMgniENEKW--DVASTLS-V 529
Cdd:pfam19303 49 NEYLQEAAPWTTFKTDPEaaaaqVRL------ALNLIRLYAVLSAPFIPDAAAAMLAAMGT---DDAAWpdDVAAALTaL 119
|
90
....*....|....*....
gi 497676884 530 NPGHKIGKVNVLFKKLEPE 548
Cdd:pfam19303 120 PAGHAFTVPEVLFAKITDE 138
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
10-88 |
8.22e-03 |
|
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: 39.27 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497676884 10 PYVNSVPHLGNLIGSILSaDVFARYARLRyGKeNVLFVSGSDEHGTPIE--IEAIKRKVNPKEltdqaHEYDRHLFLN-V 86
Cdd:TIGR00422 42 PNVTGSLHIGHALNWSIQ-DIIARYKRMK-GY-NVLWLPGTDHAGIATQvkVEKKLGAEGKTK-----HDLGREEFREkI 113
|
..
gi 497676884 87 WK 88
Cdd:TIGR00422 114 WE 115
|
|
| |
