|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
17-659 |
0e+00 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 863.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 17 RPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQ 96
Cdd:PLN02610 4 EGKSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 97 EICDKYHIIHADIYRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPF--C 174
Cdd:PLN02610 84 EICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 175 GYEEARGDQCDKCGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQFITRSWLRD 254
Cdd:PLN02610 164 NYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 255 GLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSA 334
Cdd:PLN02610 244 GLKPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 335 LGAEDNYTLVSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLN 414
Cdd:PLN02610 324 LGTGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 415 NLGNFINRAGMFVSK----FFGGYVPEMV---LTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQV 487
Cdd:PLN02610 404 NLGNFINRVLSFIAKppgaGYGSVIPDAPgaeSHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 488 NEPWKRIKgseADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSilltnfLCT------------- 554
Cdd:PLN02610 484 SQFWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLS------LSDekgevarakrpwe 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 555 -LPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQQIQALMDEVTKQGNIVRELKAQKADKN 633
Cdd:PLN02610 555 lVPAGHKIGTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAA 634
|
650 660
....*....|....*....|....*.
gi 2462531957 634 EVAAEVAKlLDLKKQLAVAEGKPPEA 659
Cdd:PLN02610 635 EREIDVSR-LDIRVGLIVKAEKHPDA 659
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
30-579 |
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: 651.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 30 RNVLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADI 109
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 110 YRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGK 189
Cdd:COG0143 80 FEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 190 LINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLgRTLPgsDWTPNAQFITRSWLRDGLKPRCITRDLKWGT 269
Cdd:COG0143 160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWI-EENP--DIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 270 PVPleGFEDKVFYVWFDATIGYLSITANYTDQ------WERWWKNPEqVDLYQFMAKDNVPFHSLVFPCSALGAedNYTL 343
Cdd:COG0143 237 PVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAPD-TELVHFIGKDIIRFHAIIWPAMLMAA--GLPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 344 VSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRA 423
Cdd:COG0143 312 PKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 424 GMFVSKFFGGYVPEM-VLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKgsEADRQ 502
Cdd:COG0143 391 LSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAK--DEDPE 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462531957 503 RAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSIllTNFLCTLPAGHQIGTVSPLFQKLENDQIESL 579
Cdd:COG0143 469 RLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTW--EDAGWPLPAGHKIGKPEPLFPRIEDEQIEAL 543
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
32-572 |
0e+00 |
|
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: 587.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 32 VLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYR 111
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 112 WFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLI 191
Cdd:TIGR00398 80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 192 NAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQFITRSWLRDGLKPRCITRDLK-WGTP 270
Cdd:TIGR00398 160 EPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVyWGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 271 VPLEgfEDKVFYVWFDATIGYLS---ITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEdnYTLVSHL 347
Cdd:TIGR00398 240 VPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLG--LPLPTQV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 348 IATEYLNYEDGKFSKSRGVGVFGDMAQDtGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMFV 427
Cdd:TIGR00398 316 FSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 428 SKFFGGYVP-EMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGSEADRQragt 506
Cdd:TIGR00398 395 KKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKE---- 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462531957 507 VTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPppacsiLLTNFLCTLPAGHQIGTVSPLFQKLE 572
Cdd:TIGR00398 471 LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE------LEWDFKLKLLEGHKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
32-423 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 563.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 32 VLITSALPYVNNVPHLGNIIGcVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYR 111
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYS-YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 112 WFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLI 191
Cdd:pfam09334 80 KFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 192 NAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGsdWTPNAQFITRSWLRDGLKPRCITRDLKWGTPV 271
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNPE--WPENVKNMVLEWLKEGLKDRAISRDLDWGIPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 272 PleGFEDKVFYVWFDATIGYLSITANYTDQ---WERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAedNYTLVSHLI 348
Cdd:pfam09334 238 P--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGA--GYRLPTTVF 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462531957 349 ATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRA 423
Cdd:pfam09334 314 AHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
31-399 |
5.58e-174 |
|
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: 498.21 E-value: 5.58e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 31 NVLITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIY 110
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 111 RWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLadrfvegvcpfcgyeeargdqcdkcgkl 190
Cdd:cd00814 80 KWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL---------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 191 inavelkkpqckvcrscPVVQSSQHLFLDLPKLEKRLEEWLGRTlPGSDWTPNAQFITRSWLRDGLKPRCITRDL-KWGT 269
Cdd:cd00814 132 -----------------PEWREEEHYFFRLSKFQDRLLEWLEKN-PDFIWPENARNEVLSWLKEGLKDLSITRDLfDWGI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 270 PVPLegFEDKVFYVWFDATIGYLSITANYTDQWER-WWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAedNYTLVSHLI 348
Cdd:cd00814 194 PVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGA--GLPLPTRIV 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2462531957 349 ATEYLNYEDGKFSKSRGVGVFGDMAQDTGiPADIWRFYLLYIRPEGQDSAF 399
Cdd:cd00814 270 AHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEGKDSDF 319
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
613-665 |
5.64e-17 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 75.07 E-value: 5.64e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462531957 613 DEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKP--PEAPKGKKK 665
Cdd:smart00991 2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDykPGAPPGDTP 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
17-659 |
0e+00 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 863.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 17 RPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQ 96
Cdd:PLN02610 4 EGKSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 97 EICDKYHIIHADIYRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPF--C 174
Cdd:PLN02610 84 EICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 175 GYEEARGDQCDKCGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQFITRSWLRD 254
Cdd:PLN02610 164 NYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 255 GLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSA 334
Cdd:PLN02610 244 GLKPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 335 LGAEDNYTLVSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLN 414
Cdd:PLN02610 324 LGTGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 415 NLGNFINRAGMFVSK----FFGGYVPEMV---LTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQV 487
Cdd:PLN02610 404 NLGNFINRVLSFIAKppgaGYGSVIPDAPgaeSHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 488 NEPWKRIKgseADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSilltnfLCT------------- 554
Cdd:PLN02610 484 SQFWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLS------LSDekgevarakrpwe 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 555 -LPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQQIQALMDEVTKQGNIVRELKAQKADKN 633
Cdd:PLN02610 555 lVPAGHKIGTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAA 634
|
650 660
....*....|....*....|....*.
gi 2462531957 634 EVAAEVAKlLDLKKQLAVAEGKPPEA 659
Cdd:PLN02610 635 EREIDVSR-LDIRVGLIVKAEKHPDA 659
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
30-579 |
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: 651.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 30 RNVLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADI 109
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 110 YRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGK 189
Cdd:COG0143 80 FEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 190 LINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLgRTLPgsDWTPNAQFITRSWLRDGLKPRCITRDLKWGT 269
Cdd:COG0143 160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWI-EENP--DIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 270 PVPleGFEDKVFYVWFDATIGYLSITANYTDQ------WERWWKNPEqVDLYQFMAKDNVPFHSLVFPCSALGAedNYTL 343
Cdd:COG0143 237 PVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAPD-TELVHFIGKDIIRFHAIIWPAMLMAA--GLPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 344 VSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRA 423
Cdd:COG0143 312 PKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 424 GMFVSKFFGGYVPEM-VLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKgsEADRQ 502
Cdd:COG0143 391 LSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAK--DEDPE 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462531957 503 RAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSIllTNFLCTLPAGHQIGTVSPLFQKLENDQIESL 579
Cdd:COG0143 469 RLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTW--EDAGWPLPAGHKIGKPEPLFPRIEDEQIEAL 543
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
30-616 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 642.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 30 RNVLITSALPYVNNVPHLGNIIGcVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADI 109
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVE-YIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 110 YRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGK 189
Cdd:PRK00133 81 FAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 190 LINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLpgsDWTPNAQFITRSWLRDGLKPRCITRDLKW-G 268
Cdd:PRK00133 161 TYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRSG---ELQPNVANKMKEWLEEGLQDWDISRDAPYfG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 269 TPVPleGFEDKVFYVWFDATIGYLSITANYTDQ-----WERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAedNYTL 343
Cdd:PRK00133 238 FEIP--GAPGKVFYVWLDAPIGYISSTKNLCDKrggldWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGA--GYRL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 344 VSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEG-QDSAFSWTDLLLKNNSELLNNLGNFINR 422
Cdd:PRK00133 314 PTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDH-LDPDYLRYYLAAKLPETiDDLDFNWEDFQQRVNSELVGKVVNFASR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 423 AGMFVSKFFGGYVPEMVLTPDdqrLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKgseADRQ 502
Cdd:PRK00133 393 TAGFINKRFDGKLPDALADPE---LLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAK---QDGE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 503 RAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPpacsiLLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQR 582
Cdd:PRK00133 467 RLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEE-----LTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIEA 541
|
570 580 590
....*....|....*....|....*....|....
gi 2462531957 583 FGGGQAKTSPKPAvvetvtTAKPQQIQALMDEVT 616
Cdd:PRK00133 542 SKEAAAAKAAAAA------AAAPLAEEPIAETIS 569
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
32-572 |
0e+00 |
|
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: 587.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 32 VLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYR 111
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 112 WFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLI 191
Cdd:TIGR00398 80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 192 NAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQFITRSWLRDGLKPRCITRDLK-WGTP 270
Cdd:TIGR00398 160 EPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVyWGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 271 VPLEgfEDKVFYVWFDATIGYLS---ITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEdnYTLVSHL 347
Cdd:TIGR00398 240 VPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLG--LPLPTQV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 348 IATEYLNYEDGKFSKSRGVGVFGDMAQDtGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMFV 427
Cdd:TIGR00398 316 FSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 428 SKFFGGYVP-EMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGSEADRQragt 506
Cdd:TIGR00398 395 KKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKE---- 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462531957 507 VTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPppacsiLLTNFLCTLPAGHQIGTVSPLFQKLE 572
Cdd:TIGR00398 471 LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE------LEWDFKLKLLEGHKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
32-423 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 563.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 32 VLITSALPYVNNVPHLGNIIGcVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYR 111
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYS-YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 112 WFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLI 191
Cdd:pfam09334 80 KFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 192 NAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGsdWTPNAQFITRSWLRDGLKPRCITRDLKWGTPV 271
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNPE--WPENVKNMVLEWLKEGLKDRAISRDLDWGIPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 272 PleGFEDKVFYVWFDATIGYLSITANYTDQ---WERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAedNYTLVSHLI 348
Cdd:pfam09334 238 P--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGA--GYRLPTTVF 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462531957 349 ATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRA 423
Cdd:pfam09334 314 AHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
31-399 |
5.58e-174 |
|
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: 498.21 E-value: 5.58e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 31 NVLITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIY 110
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 111 RWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLadrfvegvcpfcgyeeargdqcdkcgkl 190
Cdd:cd00814 80 KWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL---------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 191 inavelkkpqckvcrscPVVQSSQHLFLDLPKLEKRLEEWLGRTlPGSDWTPNAQFITRSWLRDGLKPRCITRDL-KWGT 269
Cdd:cd00814 132 -----------------PEWREEEHYFFRLSKFQDRLLEWLEKN-PDFIWPENARNEVLSWLKEGLKDLSITRDLfDWGI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 270 PVPLegFEDKVFYVWFDATIGYLSITANYTDQWER-WWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAedNYTLVSHLI 348
Cdd:cd00814 194 PVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGA--GLPLPTRIV 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2462531957 349 ATEYLNYEDGKFSKSRGVGVFGDMAQDTGiPADIWRFYLLYIRPEGQDSAF 399
Cdd:cd00814 270 AHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEGKDSDF 319
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
34-572 |
1.06e-98 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 312.20 E-value: 1.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 34 ITSALPYVNNVPHLGNIiGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWF 113
Cdd:PRK11893 5 ITTPIYYPNGKPHIGHA-YTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 114 NISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFV---EGVCPFCGYEeargdqcdkcgkl 190
Cdd:PRK11893 84 NISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELiedGYRCPPTGAP------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 191 inaVELKKpqckvcrscpvVQSsqhLFLDLPKLEKRLEEWLGRtlpgsdwtpNAQFI--------TRSWLRDGLKPRCIT 262
Cdd:PRK11893 151 ---VEWVE-----------EES---YFFRLSKYQDKLLELYEA---------NPDFIqpasrrneVISFVKSGLKDLSIS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 263 R-DLKWGTPVPleGFEDKVFYVWFDATIGYLS------ITANYTDQWERWWknpeQVDLyQFMAKDNVPFHSLVFP--CS 333
Cdd:PRK11893 205 RtNFDWGIPVP--GDPKHVIYVWFDALTNYLTalgypdDEELLAELFNKYW----PADV-HLIGKDILRFHAVYWPafLM 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 334 ALGaednYTLVSHLIATEYLNYEDGKFSKSRG--VGVFgDMAQDTGipADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSE 411
Cdd:PRK11893 278 AAG----LPLPKRVFAHGFLTLDGEKMSKSLGnvIDPF-DLVDEYG--VDAVRYFLLREIPFGQDGDFSREAFINRINAD 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 412 LLNNLGNFINRAGMFVSKFFGGYVPEM-VLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEP 490
Cdd:PRK11893 351 LANDLGNLAQRTLSMIAKNFDGKVPEPgALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAP 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 491 WKRIKgseADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQIGTVSPLFQK 570
Cdd:PRK11893 431 WSLAK---TDPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEEDENRDFAALSWGRLAPGTTLPKPEPIFPR 507
|
..
gi 2462531957 571 LE 572
Cdd:PRK11893 508 LE 509
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
34-599 |
9.95e-88 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 287.47 E-value: 9.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 34 ITSALPYVNNVPHLGN----IIgcvlsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKyhiIHADI 109
Cdd:PRK12267 8 ITTPIYYPNGKPHIGHayttIA-----ADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDE---ISAGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 110 YR-W--FNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARF-----LADrfvEGVCPFCGYEearg 181
Cdd:PRK12267 80 KElWkkLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFftesqLVD---GGKCPDCGRE---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 182 dqcdkcgklinaVELKKpqckvcrscpvvqsSQHLFLDLPKLEKRLEEWLgrtlpgsdwTPNAQFI---------TRSWL 252
Cdd:PRK12267 153 ------------VELVK--------------EESYFFRMSKYQDRLLEYY---------EENPDFIqpesrknemINNFI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 253 RDGLKPRCITRD-LKWGTPVPlegFEDK-VFYVWFDATIGYlsITA-NY----TDQWERWWknPEQVdlyQFMAKDNVPF 325
Cdd:PRK12267 198 KPGLEDLSISRTsFDWGIPVP---FDPKhVVYVWIDALLNY--ITAlGYgsddDELFKKFW--PADV---HLVGKDILRF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 326 HSLVFPC--SALGAEdnytLVSHLIATEYLNYEDGKFSKSRGVGVFG-DMAQDTGIpaDIWRFYLLYIRPEGQDSAFSWT 402
Cdd:PRK12267 268 HAIYWPImlMALGLP----LPKKVFAHGWWLMKDGKMSKSKGNVVDPeELVDRYGL--DALRYYLLREVPFGSDGDFSPE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 403 DLLLKNNSELLNNLGNFINRA-GMfVSKFFGGYVPEM-VLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRH 480
Cdd:PRK12267 342 ALVERINSDLANDLGNLLNRTvAM-INKYFDGEIPAPgNVTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 481 GNQYIQVNEPWKRIKgSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQ 560
Cdd:PRK12267 421 ANKYIDETAPWVLAK-DEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLGLEEELTSWESLLEWGGLPAGTK 499
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2462531957 561 IGTVSPLFQKLENDQ-IESLRQRFGGGQAKTSPKPAVVET 599
Cdd:PRK12267 500 VAKGEPLFPRIDVEEeIAYIKEQMEGSAPKEPEEKEKKPE 539
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
408-537 |
4.36e-47 |
|
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: 162.27 E-value: 4.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 408 NNSELLNNLGNFINRAGMFVSKFFGGYVPEM-VLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQ 486
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFgGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462531957 487 VNEPWKRIKgsEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQL 537
Cdd:cd07957 81 ETAPWKLAK--EEDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
28-602 |
6.65e-39 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 152.18 E-value: 6.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 28 GERNVLiTSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHA 107
Cdd:PLN02224 68 ADTFVL-TTPLYYVNAPPHMGSAY-TTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 108 DIYRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADR-FVEGVCpfcgyeeargdqcdk 186
Cdd:PLN02224 146 TLWKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKeLLENNC--------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 187 cgklinavelkkpqCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRtlpgsdwtpNAQFI--------TRSWLRDGLKP 258
Cdd:PLN02224 211 --------------CPVHQMPCVARKEDNYFFALSKYQKPLEDILAQ---------NPRFVqpsyrlneVQSWIKSGLRD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 259 RCITRDL-KWGTPVPLEgfEDKVFYVWFDATIGYLSITANYTDQwerwwKNPEQVDLY------QFMAKDNVPFHSLVFP 331
Cdd:PLN02224 268 FSISRALvDWGIPVPDD--DKQTIYVWFDALLGYISALTEDNKQ-----QNLETAVSFgwpaslHLIGKDILRFHAVYWP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 332 CSALGAedNYTLVSHLIATEYLNYEDGKFSKSRGVGVFG-DMAQDTGipADIWRFYLLYIRPEGQDSAFSWTDLLLKNNS 410
Cdd:PLN02224 341 AMLMSA--GLELPKMVFGHGFLTKDGMKMGKSLGNTLEPfELVQKFG--PDAVRYFFLREVEFGNDGDYSEDRFIKIVNA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 411 ELLNNLGNFINRA-GMFVSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNE 489
Cdd:PLN02224 417 HLANTIGNLLNRTlGLLKKNCESTLVEDSTVAAEGVPLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNTYMDQRA 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 490 PWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPAC-SILLTNF-LCTLPAGHQIGTVSPL 567
Cdd:PLN02224 497 PWFLFKQGGVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQLGYSEDQFnSITWSDTkWGGLKGGQVMEQASPV 576
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462531957 568 FQKLE-NDQIESLRQRFGGGQAKTSPKPAVVETVTT 602
Cdd:PLN02224 577 FARIElNPEKEEDEKKPKVGKKTGKAKVKVVEQTPT 612
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
33-396 |
1.52e-34 |
|
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: 133.70 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 33 LITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGL-------------TPQEIC 99
Cdd:cd00668 3 YVTTPPPYANGSLHLGHALTHII-ADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 100 DKYHIIHADIYRWFNISFDI--FGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEqlrcehcarfladrfvegvcpfcgye 177
Cdd:cd00668 82 EEMSGEHKEDFRRLGISYDWsdEYITTEPEYSKAVELIFSRLYEKGLIYRGTHP-------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 178 eargdqcdkcgklinavelkkpqckvcrscpvVQSSQHLFLDLPKLEKRLEEWLGRTlpgsDWTPNaQFITR--SWLRDG 255
Cdd:cd00668 136 --------------------------------VRITEQWFFDMPKFKEKLLKALRRG----KIVPE-HVKNRmeAWLESL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 256 LKpRCITRDLKWGTPVPlegfeDKVFYVWFDATIGYLSITANYTDqwERWWKNPEQVDLYqFMAKDNVPFHSLVFPCS-- 333
Cdd:cd00668 179 LD-WAISRQRYWGTPLP-----EDVFDVWFDSGIGPLGSLGYPEE--KEWFKDSYPADWH-LIGKDILRGWANFWITMlv 249
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462531957 334 ALGAEDNYtlvSHLIATEYLNYEDG-KFSKSRG-VGVFGDMAQDTGipADIWRFYLLYIRPEGQD 396
Cdd:cd00668 250 ALFGEIPP---KNLLVHGFVLDEGGqKMSKSKGnVIDPSDVVEKYG--ADALRYYLTSLAPYGDD 309
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
611-655 |
1.03e-19 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 82.52 E-value: 1.03e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2462531957 611 LMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGK 655
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
611-661 |
4.17e-18 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 78.31 E-value: 4.17e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2462531957 611 LMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPK 661
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGA 51
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
613-665 |
5.64e-17 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 75.07 E-value: 5.64e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462531957 613 DEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKP--PEAPKGKKK 665
Cdd:smart00991 2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDykPGAPPGDTP 56
|
|
| Anticodon_3 |
pfam19303 |
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ... |
435-588 |
2.87e-16 |
|
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: 76.39 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 435 VPEM-VLTPDDQRLLAHVTLELQHYHQLLEKVRIRDA---LRSILTIsrhGNQYIQVNEPWKRIKgseADRQRAGTVTGL 510
Cdd:pfam19303 1 VPEGgAYGEAEAALIADLTTRLAAYEGHMEAMEVRKAaaeLRAIWVA---GNEYLQEAAPWTTFK---TDPEAAAAQVRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462531957 511 AVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQIgTVSP-LFQKLENDQIESLRQRFGGGQA 588
Cdd:pfam19303 75 ALNLIRLYAVLSAPFIPDAAAAMLAAMGTDDAAWPDDVAAALTALPAGHAF-TVPEvLFAKITDEQREEWQERFAGTRA 152
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
612-653 |
1.28e-13 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 65.25 E-value: 1.28e-13
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2462531957 612 MDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAE 653
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
217-551 |
2.76e-12 |
|
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: 70.09 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 217 FLDLPKLEKRLEEWLGRTLPgsDWTPNaQFITR--SWLRDgLKPRCITRDLKWGTPVP---------------------- 272
Cdd:TIGR00422 359 FVKVEKLADKALEAAEEGEI--KFVPK-RMEKRylNWLRN-IKDWCISRQLIWGHRIPvwyckecgevyvakeeplpddk 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 273 --------LEGFEDkVFYVWFDATIGYLSITAnytdqwerwWknPEQVDLYqfmaKDNVPFHSLVfpcsaLGAEDNYTLV 344
Cdd:TIGR00422 435 tntgpsveLEQDTD-VLDTWFSSSLWPFSTLG---------W--PDETKDL----KKFYPTDLLV-----TGYDIIFFWV 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 345 SHLI------------ATEYLNY----EDG-KFSKSRGVGVFG-DMAQDTGipADIWRFYLLYIRPEGQDSAFSWTDllL 406
Cdd:TIGR00422 494 ARMIfrslaltgqvpfKEVYIHGlvrdEQGrKMSKSLGNVIDPlDVIEKYG--ADALRFTLASLVTPGDDINFDWKR--V 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 407 KNNSELLNNLGNfinrAGMFVSKFFGGYV----PEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHG- 481
Cdd:TIGR00422 570 ESARNFLNKLWN----ASRFVLMNLSDDLelsgGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALYEFIWNDf 645
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462531957 482 -NQYIQVNEPwkRIKGSEADRQRAGTVTGLAVNIAALlsVMLQPYMPTVSATIqAQlQLPPPACSILLTNF 551
Cdd:TIGR00422 646 cDWYIELVKY--RLYNGNEAEKKAARDTLYYVLDKAL--RLLHPFMPFITEEI-WQ-HFKEGADSIMLQSY 710
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
611-657 |
1.84e-10 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 56.47 E-value: 1.84e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462531957 611 LMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLK---KQLAVAEGKPP 657
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKadyKEATGQDYKPG 50
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
39-399 |
2.61e-10 |
|
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: 62.65 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 39 PYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETK----ALEEGLTPQ--------EIC----DKY 102
Cdd:cd00817 10 PNVTGSLHMGHALNNTI-QDIIARYKRMKGYNVLWPPGTDHAGIATQVVvekkLGIEGKTRHdlgreeflEKCwewkEES 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 103 H--IIHADIYRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVegvcpfcgyeear 180
Cdd:cd00817 89 GgkIREQLKRLGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 181 gdqCDKCGKLInavE-LKKPQckvcrscpvvqssqhLFLDLPKLEKRLEEWLGRTLPgsDWTPNAQFIT-RSWLrDGLKP 258
Cdd:cd00817 156 ---CSRSGDVI---EpLLKPQ---------------WFVKVKDLAKKALEAVKEGDI--KFVPERMEKRyENWL-ENIRD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 259 RCITRDLKWGTPVPlegfedkvfyVWFDATIGYLSITANytdqwerwwkNPEQVDLYQFMAKDNVP-------------- 324
Cdd:cd00817 212 WCISRQLWWGHRIP----------AWYCKDGGHWVVARE----------EDEAIDKAAPEACVPCGgeelkqdedvldtw 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 325 FHSLVFPCSALGAEDN-------------------------YTLVSHLIATE-------YLNY----EDG-KFSKSRGVG 367
Cdd:cd00817 272 FSSSLWPFSTLGWPEEtkdlkkfyptsllvtghdiiffwvaRMIMRGLKLTGklpfkevYLHGlvrdEDGrKMSKSLGNV 351
|
410 420 430
....*....|....*....|....*....|..
gi 2462531957 368 VFGDMAQDtGIPADIWRFYLLYIRPEGQDSAF 399
Cdd:cd00817 352 IDPLDVID-GYGADALRFTLASAATQGRDINL 382
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
34-401 |
6.09e-10 |
|
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: 61.11 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 34 ITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEIcDKYHI--IHADIYR 111
Cdd:cd00812 4 ILVMFPYPSGALHVGHVRTYTI-GDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDW-TEYNIkkMKEQLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 112 wFNISFDiFGR---TTTPQQTKITQDIFQQLLKRGFVLQDtveqlrcEHCARFladrfvegvcpfcgyeeargdqcdkcg 188
Cdd:cd00812 82 -MGFSYD-WRReftTCDPEYYKFTQWLFLKLYEKGLAYKK-------EAPVNW--------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 189 klinavelkkpqCKVCRscpvvqssqHLFLDL------PKLEKRLEEWLGrtlpgsdWTPNAQFITRSWLRdglkprcIT 262
Cdd:cd00812 126 ------------CKLLD---------QWFLKYsetewkEKLLKDLEKLDG-------WPEEVRAMQENWIG-------CS 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 263 RDLKWGTPVPlegFEDkVFYVWFDATIGYLSIT-ANYTDQ--WERWWKNPEQ------VDLYqFMAKDNVP--------F 325
Cdd:cd00812 171 RQRYWGTPIP---WTD-TMESLSDSTWYYARYTdAHNLEQpyEGDLEFDREEfeywypVDIY-IGGKEHAPnhllysrfN 245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462531957 326 HSLVFPCSALGAEdnytLVSHLIATEYLNYEDGKFSKSRGVGV-FGDMAQDTGipADIWRFYLLYIRPegQDSAFSW 401
Cdd:cd00812 246 HKALFDEGLVTDE----PPKGLIVQGMVLLEGEKMSKSKGNVVtPDEAIKKYG--ADAARLYILFAAP--PDADFDW 314
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
610-649 |
3.41e-09 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 52.86 E-value: 3.41e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2462531957 610 ALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQL 649
Cdd:cd00938 2 KLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQL 41
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
606-662 |
3.42e-08 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 56.68 E-value: 3.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462531957 606 QQIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEgKPPEAPKG 662
Cdd:PLN02734 7 DALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALE-KELQAAVG 62
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
46-167 |
2.25e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 54.44 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 46 HLGNIIGCVLSaDVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKyhiihaDIYRW--------FNISF 117
Cdd:PLN02563 127 HVGHPEGYTAT-DILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLK------NIARFrsqlkslgFSYDW 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462531957 118 DIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFV 167
Cdd:PLN02563 200 DREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEV 249
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
39-102 |
2.54e-03 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which 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.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 38.61 E-value: 2.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462531957 39 PYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKY 102
Cdd:cd00802 6 ITPNGYLHIGHLRTIVT-FDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERW 68
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
39-145 |
3.64e-03 |
|
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: 40.47 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462531957 39 PYVNNVPHLGNIIGCVLSaDVFARYSRLRQWNTLYLCGTDEYGTATETK-----ALEEGLTPQ------------EICDK 101
Cdd:pfam00133 32 PNATGSLHIGHALAKTLK-DIVIRYKRMKGYYVLWVPGWDHHGLPTEQVvekklGIKEKKTRHkygreefrekcrEWKME 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462531957 102 YHIIHADIYRWFNISFDiFGR---TTTPQQTKITQDIFQQLLKRGFV 145
Cdd:pfam00133 111 YADEIRKQFRRLGRSID-WDReyfTMDPELEAAVWEVFVRLHDKGLI 156
|
|
| |
