|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
1-515 |
0e+00 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 708.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 1 MEEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFVE 80
Cdd:PLN02610 76 LEENCTPKEICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 81 GVCPF--CGYEEARGDQCDKCGKLINAIELKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLGKTMPGSDWTPNARF 158
Cdd:PLN02610 156 GTCPTegCNYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 159 IIRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFH 238
Cdd:PLN02610 236 TTNAWLRDGLKPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFH 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 239 GLVFPCSALGAEDNYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLI 318
Cdd:PLN02610 316 TVMFPSTLLGTGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQA 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 319 KNNSELLNNLGNFINRAGMFVSK----FFGGCVPEM--VLTHD-DRRLVAHVSWELQRYHQLLEKVRIRDALRSILTISR 391
Cdd:PLN02610 396 KLNSELLNNLGNFINRVLSFIAKppgaGYGSVIPDApgAESHPlTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISS 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 392 HGNQYIQVNEPWKRIKgdeMDRQRAGTVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLP--------EAACRILATSF 463
Cdd:PLN02610 476 EGNAYLQESQFWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPpeslslsdEKGEVARAKRP 552
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1958788508 464 ICTLPAGHRIGTVSPLFQKLENDQIENLRQRFGGGQLEESLELQAKGSPKPA 515
Cdd:PLN02610 553 WELVPAGHKIGTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLA 604
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
2-491 |
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: 563.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFVEG 81
Cdd:COG0143 60 KEGITPQELVDRIHAEFKELFEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 VCPFCGYEEARGDQCDKCGKLINAIELKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLgKTMPgsDWTPNARFIIR 161
Cdd:COG0143 140 TCPKCGAEDAYGDQCENCGATLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWI-EENP--DIQPEVRNEVL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 162 SWLRDGLKPRCITRDLKWGTPVPleGFEDKVFYVWFDATIGYLSITANYTDQ------WERWWKNPEqVDLYQFMAKDNV 235
Cdd:COG0143 217 SWLKEGLQDLSISRDFDWGIPVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAPD-TELVHFIGKDII 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 236 PFHGLVFPCSALGAedNYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTD 315
Cdd:COG0143 294 RFHAIIWPAMLMAA--GLPLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWED 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 316 LLIKNNSELLNNLGNFINRAGMFVSKFFGGCVPEM-VLTHDDRRLVAHVSWELQRYHQLLEKVRIRDALRSILTISRHGN 394
Cdd:COG0143 371 FVARVNSDLANDLGNLASRTLSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAAN 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 395 QYIQVNEPWKRIKgdEMDRQRAGTVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLPEAACRILATSFIctLPAGHRIG 474
Cdd:COG0143 451 KYIDETAPWKLAK--DEDPERLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGWP--LPAGHKIG 526
|
490
....*....|....*..
gi 1958788508 475 TVSPLFQKLENDQIENL 491
Cdd:COG0143 527 KPEPLFPRIEDEQIEAL 543
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
2-484 |
1.36e-169 |
|
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: 492.28 E-value: 1.36e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFVEG 81
Cdd:TIGR00398 58 QEGLTPKELVDKYHEEFKDDWKWLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 VCPFCGYEEARGDQCDKCGKLINAIELKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLGKTMPGSDWTPNARFIIR 161
Cdd:TIGR00398 138 TCPKCGSEDARGDHCEVCGRHLEPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 162 SWLRDGLKPRCITRDLK-WGTPVPLEgfEDKVFYVWFDATIGYLS---ITANYTDQWERWWKNPEQVDLYQFMAKDNVPF 237
Cdd:TIGR00398 218 NWLKGGLKDLAITRDLVyWGIPVPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 238 HGLVFPCSALGAEdnYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDtGIPADIWRFYLLYIRPEGQDSAFSWTDLL 317
Cdd:TIGR00398 296 HTIYWPAMLMGLG--LPLPTQVFSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 318 IKNNSELLNNLGNFINRAGMFVSKFFGGCVP-EMVLTHDDRRLVAHVSWELQRYHQLLEKVRIRDALRSILTISRHGNQY 396
Cdd:TIGR00398 373 ERVNADLANKLGNLLNRTLGFIKKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKY 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 397 IQVNEPWKRIKGDEMDRQragtVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLPeaacriLATSFICTLPAGHRIGTV 476
Cdd:TIGR00398 453 IDENKPWELFKQSPRLKE----LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE------LEWDFKLKLLEGHKLNKA 522
|
....*...
gi 1958788508 477 SPLFQKLE 484
Cdd:TIGR00398 523 EPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
2-335 |
1.26e-163 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 471.77 E-value: 1.26e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFVEG 81
Cdd:pfam09334 58 KEGITPEELVDRYHEIHREDFKKFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 VCPFCGYEEARGDQCDKCGKLINAIELKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLGKTMPGsdWTPNARFIIR 161
Cdd:pfam09334 138 TCPHCGSEDARGDQCENCGRHLEPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNPE--WPENVKNMVL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 162 SWLRDGLKPRCITRDLKWGTPVPleGFEDKVFYVWFDATIGYLSITANYTDQ---WERWWKNPEQVDLYQFMAKDNVPFH 238
Cdd:pfam09334 216 EWLKEGLKDRAISRDLDWGIPVP--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 239 GLVFPCSALGAedNYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLI 318
Cdd:pfam09334 294 TIFWPAMLLGA--GYRLPTTVFAHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVE 370
|
330
....*....|....*..
gi 1958788508 319 KNNSELLNNLGNFINRA 335
Cdd:pfam09334 371 RVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
2-311 |
3.42e-131 |
|
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: 386.12 E-value: 3.42e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLadrfveg 81
Cdd:cd00814 59 EEGVTPQELCDKYHEIFKDLFKWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 vcpfcgyeeargdqcdkcgklinaielkrpqckvcrshPVVKSSKHLFLDLPKLEKRLEDWLgKTMPGSDWTPNARFIIR 161
Cdd:cd00814 132 --------------------------------------PEWREEEHYFFRLSKFQDRLLEWL-EKNPDFIWPENARNEVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 162 SWLRDGLKPRCITRDL-KWGTPVPLegFEDKVFYVWFDATIGYLSITANYTDQWER-WWKNPEQVDLYQFMAKDNVPFHG 239
Cdd:cd00814 173 SWLKEGLKDLSITRDLfDWGIPVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHA 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788508 240 LVFPCSALGAedNYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDTGiPADIWRFYLLYIRPEGQDSAF 311
Cdd:cd00814 251 IYWPAMLLGA--GLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEGKDSDF 319
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
531-575 |
2.29e-18 |
|
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: 78.67 E-value: 2.29e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958788508 531 LVDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 575
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
531-576 |
4.36e-17 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 75.22 E-value: 4.36e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958788508 531 LVDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGKP 576
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKD 46
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
533-575 |
1.21e-15 |
|
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: 71.22 E-value: 1.21e-15
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1958788508 533 DEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 575
Cdd:smart00991 2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQ 44
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
526-582 |
8.74e-07 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 52.05 E-value: 8.74e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788508 526 QDIQVLVDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAEgKPIETPKG 582
Cdd:PLN02734 7 DALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALE-KELQAAVG 62
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
1-515 |
0e+00 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 708.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 1 MEEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFVE 80
Cdd:PLN02610 76 LEENCTPKEICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 81 GVCPF--CGYEEARGDQCDKCGKLINAIELKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLGKTMPGSDWTPNARF 158
Cdd:PLN02610 156 GTCPTegCNYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 159 IIRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFH 238
Cdd:PLN02610 236 TTNAWLRDGLKPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFH 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 239 GLVFPCSALGAEDNYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLI 318
Cdd:PLN02610 316 TVMFPSTLLGTGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQA 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 319 KNNSELLNNLGNFINRAGMFVSK----FFGGCVPEM--VLTHD-DRRLVAHVSWELQRYHQLLEKVRIRDALRSILTISR 391
Cdd:PLN02610 396 KLNSELLNNLGNFINRVLSFIAKppgaGYGSVIPDApgAESHPlTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISS 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 392 HGNQYIQVNEPWKRIKgdeMDRQRAGTVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLP--------EAACRILATSF 463
Cdd:PLN02610 476 EGNAYLQESQFWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPpeslslsdEKGEVARAKRP 552
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1958788508 464 ICTLPAGHRIGTVSPLFQKLENDQIENLRQRFGGGQLEESLELQAKGSPKPA 515
Cdd:PLN02610 553 WELVPAGHKIGTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLA 604
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
2-491 |
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: 563.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFVEG 81
Cdd:COG0143 60 KEGITPQELVDRIHAEFKELFEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 VCPFCGYEEARGDQCDKCGKLINAIELKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLgKTMPgsDWTPNARFIIR 161
Cdd:COG0143 140 TCPKCGAEDAYGDQCENCGATLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWI-EENP--DIQPEVRNEVL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 162 SWLRDGLKPRCITRDLKWGTPVPleGFEDKVFYVWFDATIGYLSITANYTDQ------WERWWKNPEqVDLYQFMAKDNV 235
Cdd:COG0143 217 SWLKEGLQDLSISRDFDWGIPVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAPD-TELVHFIGKDII 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 236 PFHGLVFPCSALGAedNYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTD 315
Cdd:COG0143 294 RFHAIIWPAMLMAA--GLPLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWED 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 316 LLIKNNSELLNNLGNFINRAGMFVSKFFGGCVPEM-VLTHDDRRLVAHVSWELQRYHQLLEKVRIRDALRSILTISRHGN 394
Cdd:COG0143 371 FVARVNSDLANDLGNLASRTLSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAAN 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 395 QYIQVNEPWKRIKgdEMDRQRAGTVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLPEAACRILATSFIctLPAGHRIG 474
Cdd:COG0143 451 KYIDETAPWKLAK--DEDPERLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGWP--LPAGHKIG 526
|
490
....*....|....*..
gi 1958788508 475 TVSPLFQKLENDQIENL 491
Cdd:COG0143 527 KPEPLFPRIEDEQIEAL 543
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
2-523 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 555.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFVEG 81
Cdd:PRK00133 61 KEGITPEELIARYHAEHKRDFAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 VCPFCGYEEARGDQCDKCGKLINAIELKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLGKtmpGSDWTPNARFIIR 161
Cdd:PRK00133 141 TCPKCGAEDQYGDNCEVCGATYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITR---SGELQPNVANKMK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 162 SWLRDGLKPRCITRDLKW-GTPVPleGFEDKVFYVWFDATIGYLSITANYTDQ-----WERWWKNPEQVDLYQFMAKDNV 235
Cdd:PRK00133 218 EWLEEGLQDWDISRDAPYfGFEIP--GAPGKVFYVWLDAPIGYISSTKNLCDKrggldWDEYWKKDSDTELYHFIGKDII 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 236 PFHGLVFPCSALGAedNYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDTgIPADIWRFYLLYIRPEG-QDSAFSWT 314
Cdd:PRK00133 296 YFHTLFWPAMLEGA--GYRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDH-LDPDYLRYYLAAKLPETiDDLDFNWE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 315 DLLIKNNSELLNNLGNFINRAGMFVSKFFGGCVPEMVLthdDRRLVAHVSWELQRYHQLLEKVRIRDALRSILTISRHGN 394
Cdd:PRK00133 373 DFQQRVNSELVGKVVNFASRTAGFINKRFDGKLPDALA---DPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFAN 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 395 QYIQVNEPWKRIKGdemDRQRAGTVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLPEaacriLATSFICTLPAGHRIG 474
Cdd:PRK00133 450 KYVDDNEPWKLAKQ---DGERLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEE-----LTWDDAQQPLAGHPIN 521
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1958788508 475 TVSPLFQKLENDQIENLrqrfgggqLEESLELQAKGSPKPAVVEAVTTA 523
Cdd:PRK00133 522 KFKILFTRIEDKQIEAL--------IEASKEAAAAKAAAAAAAAPLAEE 562
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
2-484 |
1.36e-169 |
|
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: 492.28 E-value: 1.36e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFVEG 81
Cdd:TIGR00398 58 QEGLTPKELVDKYHEEFKDDWKWLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 VCPFCGYEEARGDQCDKCGKLINAIELKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLGKTMPGSDWTPNARFIIR 161
Cdd:TIGR00398 138 TCPKCGSEDARGDHCEVCGRHLEPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 162 SWLRDGLKPRCITRDLK-WGTPVPLEgfEDKVFYVWFDATIGYLS---ITANYTDQWERWWKNPEQVDLYQFMAKDNVPF 237
Cdd:TIGR00398 218 NWLKGGLKDLAITRDLVyWGIPVPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 238 HGLVFPCSALGAEdnYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDtGIPADIWRFYLLYIRPEGQDSAFSWTDLL 317
Cdd:TIGR00398 296 HTIYWPAMLMGLG--LPLPTQVFSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 318 IKNNSELLNNLGNFINRAGMFVSKFFGGCVP-EMVLTHDDRRLVAHVSWELQRYHQLLEKVRIRDALRSILTISRHGNQY 396
Cdd:TIGR00398 373 ERVNADLANKLGNLLNRTLGFIKKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKY 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 397 IQVNEPWKRIKGDEMDRQragtVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLPeaacriLATSFICTLPAGHRIGTV 476
Cdd:TIGR00398 453 IDENKPWELFKQSPRLKE----LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE------LEWDFKLKLLEGHKLNKA 522
|
....*...
gi 1958788508 477 SPLFQKLE 484
Cdd:TIGR00398 523 EPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
2-335 |
1.26e-163 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 471.77 E-value: 1.26e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFVEG 81
Cdd:pfam09334 58 KEGITPEELVDRYHEIHREDFKKFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 VCPFCGYEEARGDQCDKCGKLINAIELKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLGKTMPGsdWTPNARFIIR 161
Cdd:pfam09334 138 TCPHCGSEDARGDQCENCGRHLEPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNPE--WPENVKNMVL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 162 SWLRDGLKPRCITRDLKWGTPVPleGFEDKVFYVWFDATIGYLSITANYTDQ---WERWWKNPEQVDLYQFMAKDNVPFH 238
Cdd:pfam09334 216 EWLKEGLKDRAISRDLDWGIPVP--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 239 GLVFPCSALGAedNYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLI 318
Cdd:pfam09334 294 TIFWPAMLLGA--GYRLPTTVFAHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVE 370
|
330
....*....|....*..
gi 1958788508 319 KNNSELLNNLGNFINRA 335
Cdd:pfam09334 371 RVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
2-311 |
3.42e-131 |
|
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: 386.12 E-value: 3.42e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLadrfveg 81
Cdd:cd00814 59 EEGVTPQELCDKYHEIFKDLFKWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 vcpfcgyeeargdqcdkcgklinaielkrpqckvcrshPVVKSSKHLFLDLPKLEKRLEDWLgKTMPGSDWTPNARFIIR 161
Cdd:cd00814 132 --------------------------------------PEWREEEHYFFRLSKFQDRLLEWL-EKNPDFIWPENARNEVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 162 SWLRDGLKPRCITRDL-KWGTPVPLegFEDKVFYVWFDATIGYLSITANYTDQWER-WWKNPEQVDLYQFMAKDNVPFHG 239
Cdd:cd00814 173 SWLKEGLKDLSITRDLfDWGIPVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHA 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788508 240 LVFPCSALGAedNYTLVKNLIATEYLNYEDGKFSKSRGIGVFGDMAQDTGiPADIWRFYLLYIRPEGQDSAF 311
Cdd:cd00814 251 IYWPAMLLGA--GLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEGKDSDF 319
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
2-484 |
5.48e-76 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 250.18 E-value: 5.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADRFveg 81
Cdd:PRK11893 60 EAGISPQELADRNSAAFKRLWEALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESE--- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 82 vcpfcgyeeargdqcdkcgkLINaielKRPQCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLgKTMPgsDW-TPNARF-I 159
Cdd:PRK11893 137 --------------------LIE----DGYRCPPTGAPVEWVEEESYFFRLSKYQDKLLELY-EANP--DFiQPASRRnE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 160 IRSWLRDGLKPRCITR-DLKWGTPVPleGFEDKVFYVWFDATIGYLS------ITANYTDQWERWWknpeQVDLyQFMAK 232
Cdd:PRK11893 190 VISFVKSGLKDLSISRtNFDWGIPVP--GDPKHVIYVWFDALTNYLTalgypdDEELLAELFNKYW----PADV-HLIGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 233 DNVPFHGLVFP--CSALGaednYTLVKNLIATEYLNYEDGKFSKSRG--IGVFgDMAQDTGipADIWRFYLLYIRPEGQD 308
Cdd:PRK11893 263 DILRFHAVYWPafLMAAG----LPLPKRVFAHGFLTLDGEKMSKSLGnvIDPF-DLVDEYG--VDAVRYFLLREIPFGQD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 309 SAFSWTDLLIKNNSELLNNLGNFINRAGMFVSKFFGGCVPEM-VLTHDDRRLVAHVSWELQRYHQLLEKVRIRDALRSIL 387
Cdd:PRK11893 336 GDFSREAFINRINADLANDLGNLAQRTLSMIAKNFDGKVPEPgALTEADEALLEAAAALLERVRAAMDNLAFDKALEAIL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 388 TISRHGNQYIQVNEPWKRIKGDEmdrQRAGTVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLPEAACRILATSFICTL 467
Cdd:PRK11893 416 ALVRAANKYIDEQAPWSLAKTDP---ERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEEDENRDFAALSWGRL 492
|
490
....*....|....*..
gi 1958788508 468 PAGHRIGTVSPLFQKLE 484
Cdd:PRK11893 493 APGTTLPKPEPIFPRLE 509
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
2-576 |
5.04e-64 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 221.60 E-value: 5.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 2 EEGLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARF-----LAD 76
Cdd:PRK12267 63 KAGKTPQEYVDEISAGFKELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFftesqLVD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 77 rfvEGVCPFCGyeeargdqcdkcgklinaielkrpqckvcrsHPV--VKSSKHlFLDLPKLEKRLEDWLGKtmpgsdwtp 154
Cdd:PRK12267 143 ---GGKCPDCG-------------------------------REVelVKEESY-FFRMSKYQDRLLEYYEE--------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 155 NARFI---------IRSWLRDGLKPRCITRD-LKWGTPVPlegFEDK-VFYVWFDATIGYlsITA-NY----TDQWERWW 218
Cdd:PRK12267 179 NPDFIqpesrknemINNFIKPGLEDLSISRTsFDWGIPVP---FDPKhVVYVWIDALLNY--ITAlGYgsddDELFKKFW 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 219 knPEQVdlyQFMAKDNVPFHGLVFPC--SALGAEdnytLVKNLIATEYLNYEDGKFSKSRGIGVFG-DMAQDTGIpaDIW 295
Cdd:PRK12267 254 --PADV---HLVGKDILRFHAIYWPImlMALGLP----LPKKVFAHGWWLMKDGKMSKSKGNVVDPeELVDRYGL--DAL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 296 RFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNFINRA-GMfVSKFFGGCVPEMVLTHD-DRRLVAHVSWELQRYHQL 373
Cdd:PRK12267 323 RYYLLREVPFGSDGDFSPEALVERINSDLANDLGNLLNRTvAM-INKYFDGEIPAPGNVTEfDEELIALAEETLKNYEEL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 374 LEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKgDEMDRQRAGTVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLPE 453
Cdd:PRK12267 402 MEELQFSRALEEVWKLISRANKYIDETAPWVLAK-DEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLGLEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 454 AACRILATSFICTLPAGHRIGTVSPLFQKLENDqienlrqrfgggqlEESLELQAKGSPKPAVVEAVTTAGSQDIQVLVD 533
Cdd:PRK12267 481 ELTSWESLLEWGGLPAGTKVAKGEPLFPRIDVE--------------EEIAYIKEQMEGSAPKEPEEKEKKPEKPEITID 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1958788508 534 EVTK----QGNIVRELKAQKADknqvaaevaKLldLKKQLALAEGKP 576
Cdd:PRK12267 547 DFDKvelrVAEVLEAEKVEKSD---------KL--LKLQVDLGEEEP 582
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
320-449 |
5.64e-45 |
|
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: 155.34 E-value: 5.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 320 NNSELLNNLGNFINRAGMFVSKFFGGCVPEM-VLTHDDRRLVAHVSWELQRYHQLLEKVRIRDALRSILTISRHGNQYIQ 398
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFgGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958788508 399 VNEPWKRIKgdEMDRQRAGTVTGMAVNIAALLSVMLQPYMPTVSSTIQTQL 449
Cdd:cd07957 81 ETAPWKLAK--EEDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
4-484 |
1.92e-29 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 123.29 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 4 GLTPQEICDKYHAIHVDIYRWFNISFDTFGRTTTPLQTKITQDIFQRLLTRGFVLQDTVEQLRCEQCARFLADR-FVEGV 82
Cdd:PLN02224 130 GRNPPEHCDIISQSYRTLWKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKeLLENN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 83 CpfcgyeeargdqcdkcgklinaielkrpqCKVCRSHPVVKSSKHLFLDLPKLEKRLEDWLGKtmpgsdwtpNARFI--- 159
Cdd:PLN02224 210 C-----------------------------CPVHQMPCVARKEDNYFFALSKYQKPLEDILAQ---------NPRFVqps 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 160 -----IRSWLRDGLKPRCITRDL-KWGTPVPLEgfEDKVFYVWFDATIGYLSITANYTDQwerwwKNPEQVDLY------ 227
Cdd:PLN02224 252 yrlneVQSWIKSGLRDFSISRALvDWGIPVPDD--DKQTIYVWFDALLGYISALTEDNKQ-----QNLETAVSFgwpasl 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 228 QFMAKDNVPFHGLVFPCSALGAedNYTLVKNLIATEYLNYEDGKFSKSRG--IGVFgDMAQDTGipADIWRFYLLYIRPE 305
Cdd:PLN02224 325 HLIGKDILRFHAVYWPAMLMSA--GLELPKMVFGHGFLTKDGMKMGKSLGntLEPF-ELVQKFG--PDAVRYFFLREVEF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 306 GQDSAFSWTDLLIKNNSELLNNLGNFINRAGMFVSKffgGCVPEMVLthdDRRLVAHVSWELQRYHQLLEKVR------- 378
Cdd:PLN02224 400 GNDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLLKK---NCESTLVE---DSTVAAEGVPLKDTVEKLVEKAQtnyenls 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 379 IRDALRSILTISRHGNQYIQVNEPWKRIKGDEMDRQRAGTVTGMAVNIAALLSVMLQPYMPTVSSTIQTQLQLPEAACRI 458
Cdd:PLN02224 474 LSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQLGYSEDQFNS 553
|
490 500
....*....|....*....|....*...
gi 1958788508 459 LATSFI--CTLPAGHRIGTVSPLFQKLE 484
Cdd:PLN02224 554 ITWSDTkwGGLKGGQVMEQASPVFARIE 581
|
|
| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
531-575 |
2.29e-18 |
|
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: 78.67 E-value: 2.29e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958788508 531 LVDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 575
Cdd:cd00939 1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
531-576 |
4.36e-17 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 75.22 E-value: 4.36e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958788508 531 LVDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGKP 576
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKD 46
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
533-575 |
1.21e-15 |
|
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: 71.22 E-value: 1.21e-15
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1958788508 533 DEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 575
Cdd:smart00991 2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQ 44
|
|
| Anticodon_3 |
pfam19303 |
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ... |
358-498 |
3.23e-14 |
|
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: 70.22 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 358 RLVAHVSWELQRYHQLLEKVRIRDA---LRSILTIsrhGNQYIQVNEPWKRIKgdeMDRQRAGTVTGMAVNIAALLSVML 434
Cdd:pfam19303 13 ALIADLTTRLAAYEGHMEAMEVRKAaaeLRAIWVA---GNEYLQEAAPWTTFK---TDPEAAAAQVRLALNLIRLYAVLS 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 435 QPYMPTVSSTIQTQLQL-----PEAACRILATsfictLPAGHRIgTVSP-LFQKLENDQIENLRQRFGGG 498
Cdd:pfam19303 87 APFIPDAAAAMLAAMGTddaawPDDVAAALTA-----LPAGHAF-TVPEvLFAKITDEQREEWQERFAGT 150
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
533-573 |
1.69e-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: 64.87 E-value: 1.69e-13
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958788508 533 DEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAE 573
Cdd:cd01200 2 EKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
117-449 |
8.45e-11 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 65.08 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 117 RSHPVVKS--SKHLFLDLPKLEKRLEDWLGKTMPgsDWTPNaRFIIR--SWLRDgLKPRCITRDLKWGTPVP-------- 184
Cdd:TIGR00422 345 RSGTVVEPllSKQWFVKVEKLADKALEAAEEGEI--KFVPK-RMEKRylNWLRN-IKDWCISRQLIWGHRIPvwyckecg 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 185 ----------------------LEGFEDkVFYVWFDATIGYLSITA--NYTDQWERWWKN---PEQVDLYQFMA------ 231
Cdd:TIGR00422 421 evyvakeeplpddktntgpsveLEQDTD-VLDTWFSSSLWPFSTLGwpDETKDLKKFYPTdllVTGYDIIFFWVarmifr 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 232 ----KDNVPF-----HGLVFPcsalgaednytlvknliateylnyEDG-KFSKSRGIGVFG-DMAQDTGipADIWRFYLL 300
Cdd:TIGR00422 500 slalTGQVPFkevyiHGLVRD------------------------EQGrKMSKSLGNVIDPlDVIEKYG--ADALRFTLA 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 301 YIRPEGQDSAFSWTDLliKNNSELLNNLGNFINRAGMFVSKFFGGCVPEMVLTHDDRRLVAHVSWELQRYHQLLEKVRIR 380
Cdd:TIGR00422 554 SLVTPGDDINFDWKRV--ESARNFLNKLWNASRFVLMNLSDDLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFA 631
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788508 381 DALRSILTISRHG--NQYIQVNEPwkRIKGDEMDRQR-AGTVTGMAVNIAALLsvmLQPYMPTVSSTIQTQL 449
Cdd:TIGR00422 632 EAAKALYEFIWNDfcDWYIELVKY--RLYNGNEAEKKaARDTLYYVLDKALRL---LHPFMPFITEEIWQHF 698
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
531-575 |
1.33e-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: 56.86 E-value: 1.33e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958788508 531 LVDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 575
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQ 45
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
535-569 |
5.46e-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: 52.09 E-value: 5.46e-09
10 20 30
....*....|....*....|....*....|....*
gi 1958788508 535 VTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQL 569
Cdd:cd00938 7 VKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQL 41
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
526-582 |
8.74e-07 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 52.05 E-value: 8.74e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788508 526 QDIQVLVDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLALAEgKPIETPKG 582
Cdd:PLN02734 7 DALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALE-KELQAAVG 62
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
120-318 |
4.09e-04 |
|
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: 42.99 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 120 PVV-KSSKHLFLDLPKLEKRLEDWLGKTMpgsdWTP-NARFIIRSWLRDgLKPRCITRDLKWGTPVPL---EGFEDK--- 191
Cdd:cd00818 144 PLIyRATPQWFIRVTKIKDRLLEANDKVN----WIPeWVKNRFGNWLEN-RRDWCISRQRYWGTPIPVwycEDCGEVlvr 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788508 192 ----VFYVWFD------ATIGYLsitanytdQWERWWKNPEQVDLY-----Q----F--------MAKDNVPFhglvfpc 244
Cdd:cd00818 219 rvpdVLDVWFDsgsmpyAQLHYP--------FENEDFEELFPADFIlegsdQtrgwFysllllstALFGKAPY------- 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788508 245 salgaednytlvKNLIATEYLNYEDG-KFSKSRGIGV--FGDMAQdtgIPADIWRFYLLYirpegqdSAFSWTDLLI 318
Cdd:cd00818 284 ------------KNVIVHGFVLDEDGrKMSKSLGNYVdpQEVVDK---YGADALRLWVAS-------SDVYAEDLRF 338
|
|
| |
