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Conserved domains on  [gi|147905173|ref|NP_001079984|]
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methionine--tRNA ligase, cytoplasmic [Xenopus laevis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02610 super family cl33529
probable methionyl-tRNA synthetase
251-873 0e+00

probable methionyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02610:

Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 853.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 251 RPHPILPVEGEKNVLITSALPYVNNVPHLGNIIGSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQI 330
Cdd:PLN02610   6 KSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 331 CDKYNAIHTAIYQWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPF--CNY 408
Cdd:PLN02610  86 CDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 409 EEARGDQCDKCGKLINAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEQSFSTGDWTSNARFITRSWIRDGL 488
Cdd:PLN02610 166 DSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRDGL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 489 KPRCITRDLKWGTPVPLDGFRDKVFYVWFDAPIGYISITANYTDQWEKWWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLG 568
Cdd:PLN02610 246 KPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLG 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 569 AEDNYTLVNHLVATEYLNYEDGKFSKSRGVGVFGDMAKDTGIPADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSELLNNL 648
Cdd:PLN02610 326 TGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 649 GNFVNRAGMFVQK----FFNGCVPEM---ELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQVNE 721
Cdd:PLN02610 406 GNFINRVLSFIAKppgaGYGSVIPDApgaESHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQ 485
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 722 PWKCIKgnqQEQKRAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPQESKVLTTDFCCC---------LQSGHQI 792
Cdd:PLN02610 486 FWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLSLSDEKGEVarakrpwelVPAGHKI 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 793 GNVSPLFQKLENDQIESLRKRFGGGQVKTESKVSPSQEAP--EQQAPKASGPERVKelmQELEKQGNhvrELKGKKAEKS 870
Cdd:PLN02610 563 GTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKlaKQLKKKALSDGGKK---KQGKKAGG---GGKSKAAAER 636

                 ...
gi 147905173 871 VID 873
Cdd:PLN02610 637 EID 639
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
75-177 1.14e-48

Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


:

Pssm-ID: 198340 [Multi-domain]  Cd Length: 102  Bit Score: 167.29  E-value: 1.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  75 MCDLSNQWLEWEAAELQPALSAALYAHVVQGKKKEDVMATISASLKHLDQSLAGKSSPYLiKDALTVVDIVVWGSIYPLI 154
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79
                         90       100
                 ....*....|....*....|...
gi 147905173 155 VDASNLPEEMASLKRWFQNVSQL 177
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
GST_N_5 pfam18485
Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing ...
1-72 1.16e-24

Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing a thioredoxin fold. This domain found in methionyl-tRNA synthetase (MRS), a multi-tRNA synthetase complex (MSC) component.


:

Pssm-ID: 436537  Cd Length: 74  Bit Score: 97.85  E-value: 1.16e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147905173    1 MKLFVGEGNPQGVKVLAAAALWAQH--VQIDRLQQEEKIVPFMSQPRLPVLDLENGNYLFLSNAICRYFYLSSG 72
Cdd:pfam18485   1 MKLFVSEGNPHCLKVLAAAEATGVKcdVQVQFVNHEEKVVPFLTRPVLPTLELDSGQFLFSPNAICRYLFELSG 74
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
850-904 1.23e-06

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: 46.18  E-value: 1.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 147905173   850 QELEKQGNHVRELKGKKAEKSVIDPEVQKLLALKKELALAEGKSPDPPTQKGKKK 904
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
251-873 0e+00

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 853.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 251 RPHPILPVEGEKNVLITSALPYVNNVPHLGNIIGSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQI 330
Cdd:PLN02610   6 KSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 331 CDKYNAIHTAIYQWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPF--CNY 408
Cdd:PLN02610  86 CDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 409 EEARGDQCDKCGKLINAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEQSFSTGDWTSNARFITRSWIRDGL 488
Cdd:PLN02610 166 DSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRDGL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 489 KPRCITRDLKWGTPVPLDGFRDKVFYVWFDAPIGYISITANYTDQWEKWWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLG 568
Cdd:PLN02610 246 KPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLG 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 569 AEDNYTLVNHLVATEYLNYEDGKFSKSRGVGVFGDMAKDTGIPADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSELLNNL 648
Cdd:PLN02610 326 TGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 649 GNFVNRAGMFVQK----FFNGCVPEM---ELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQVNE 721
Cdd:PLN02610 406 GNFINRVLSFIAKppgaGYGSVIPDApgaESHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQ 485
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 722 PWKCIKgnqQEQKRAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPQESKVLTTDFCCC---------LQSGHQI 792
Cdd:PLN02610 486 FWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLSLSDEKGEVarakrpwelVPAGHKI 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 793 GNVSPLFQKLENDQIESLRKRFGGGQVKTESKVSPSQEAP--EQQAPKASGPERVKelmQELEKQGNhvrELKGKKAEKS 870
Cdd:PLN02610 563 GTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKlaKQLKKKALSDGGKK---KQGKKAGG---GGKSKAAAER 636

                 ...
gi 147905173 871 VID 873
Cdd:PLN02610 637 EID 639
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
262-810 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: 647.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 262 KNVLITSALPYVNNVPHLGNIIgSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAI 341
Cdd:COG0143    1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 342 YQWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPFCNYEEARGDQCDKCGK 421
Cdd:COG0143   80 FEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 422 LINAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEqsfSTGDWTSNARFITRSWIRDGLKPRCITRDLKWGT 501
Cdd:COG0143  160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIE---ENPDIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 502 PVPldGFRDKVFYVWFDAPIGYISITANYTDQ------WEKWWKSPqQVQLYNFMAKDNVPFHSVVFPSCLLGAedNYTL 575
Cdd:COG0143  237 PVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAP-DTELVHFIGKDIIRFHAIIWPAMLMAA--GLPL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 576 VNHLVATEYLNYEDGKFSKSRGVGVFGDMAKDTgIPADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSELLNNLGNFVNRA 655
Cdd:COG0143  312 PKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRT 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 656 GMFVQKFFNGCVPEM-ELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQVNEPWKCIKGNQQEqk 734
Cdd:COG0143  391 LSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPE-- 468
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147905173 735 RAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPQESKVLtTDFCCCLQSGHQIGNVSPLFQKLENDQIESL 810
Cdd:COG0143  469 RLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTW-EDAGWPLPAGHKIGKPEPLFPRIEDEQIEAL 543
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
264-803 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: 592.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  264 VLITSALPYVNNVPHLGNIIgSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAIYQ 343
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  344 WFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPFCNYEEARGDQCDKCGKLI 423
Cdd:TIGR00398  80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  424 NAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEQSFSTGDWTSNARFITRSWIRDGLKPRCITRDLK-WGTP 502
Cdd:TIGR00398 160 EPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVyWGIP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  503 VPLDgfRDKVFYVWFDAPIGYIS---ITANYTDQWEKWWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLGAEdnYTLVNHL 579
Cdd:TIGR00398 240 VPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLG--LPLPTQV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  580 VATEYLNYEDGKFSKSRGVGVFGDMAKDtGIPADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSELLNNLGNFVNRAGMFV 659
Cdd:TIGR00398 316 FSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  660 QKFFNGCVP-EMELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQVNEPWKCIKgnqqEQKRAGT 738
Cdd:TIGR00398 395 KKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFK----QSPRLKE 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147905173  739 VTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPqeskvLTTDFCCCLQSGHQIGNVSPLFQKLE 803
Cdd:TIGR00398 471 LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE-----LEWDFKLKLLEGHKLNKAEPLFSKIE 530
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
264-655 0e+00

tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 563.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  264 VLITSALPYVNNVPHLGNIIgSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAIYQ 343
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLY-SYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  344 WFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPFCNYEEARGDQCDKCGKLI 423
Cdd:pfam09334  80 KFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  424 NAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEQsfSTGDWTSNARFITRSWIRDGLKPRCITRDLKWGTPV 503
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEE--NNPEWPENVKNMVLEWLKEGLKDRAISRDLDWGIPV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  504 PldGFRDKVFYVWFDAPIGYISITANYTDQ---WEKWWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLGAedNYTLVNHLV 580
Cdd:pfam09334 238 P--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGA--GYRLPTTVF 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147905173  581 ATEYLNYEDGKFSKSRGVGVFGDMAKDTgIPADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSELLNNLGNFVNRA 655
Cdd:pfam09334 314 AHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
263-631 2.32e-169

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: 494.74  E-value: 2.32e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 263 NVLITSALPYVNNVPHLGNIIGSVLsADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAIY 342
Cdd:cd00814    1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 343 QWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLadrfvegicpfcnyeeargdqcdkcgkl 422
Cdd:cd00814   80 KWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL---------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 423 inavelkkpqckickqsPVIKSSKHLFLDLPKLEKRLEQWLEQSfSTGDWTSNARFITRSWIRDGLKPRCITRDL-KWGT 501
Cdd:cd00814  132 -----------------PEWREEEHYFFRLSKFQDRLLEWLEKN-PDFIWPENARNEVLSWLKEGLKDLSITRDLfDWGI 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 502 PVPLDgfRDKVFYVWFDAPIGYISITANYTDQWEK-WWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLGAedNYTLVNHLV 580
Cdd:cd00814  194 PVPLD--PGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGA--GLPLPTRIV 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 147905173 581 ATEYLNYEDGKFSKSRGVGVFGDMAKDTGiPADIWRFYLLYVRPEGQDSAF 631
Cdd:cd00814  270 AHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEGKDSDF 319
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
75-177 1.14e-48

Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198340 [Multi-domain]  Cd Length: 102  Bit Score: 167.29  E-value: 1.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  75 MCDLSNQWLEWEAAELQPALSAALYAHVVQGKKKEDVMATISASLKHLDQSLAGKSSPYLiKDALTVVDIVVWGSIYPLI 154
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79
                         90       100
                 ....*....|....*....|...
gi 147905173 155 VDASNLPEEMASLKRWFQNVSQL 177
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
GST_N_5 pfam18485
Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing ...
1-72 1.16e-24

Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing a thioredoxin fold. This domain found in methionyl-tRNA synthetase (MRS), a multi-tRNA synthetase complex (MSC) component.


Pssm-ID: 436537  Cd Length: 74  Bit Score: 97.85  E-value: 1.16e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147905173    1 MKLFVGEGNPQGVKVLAAAALWAQH--VQIDRLQQEEKIVPFMSQPRLPVLDLENGNYLFLSNAICRYFYLSSG 72
Cdd:pfam18485   1 MKLFVSEGNPHCLKVLAAAEATGVKcdVQVQFVNHEEKVVPFLTRPVLPTLELDSGQFLFSPNAICRYLFELSG 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-183 1.86e-11

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 64.15  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173   1 MKLFVGEGNPQGVKVLAAAAL----WaQHVQIDRLQQEEK------IVPFMsqpRLPVLdLENGNYLFLSNAICRYF--- 67
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEkglpY-ELVPVDLAKGEQKspeflaLNPLG---KVPVL-VDDGLVLTESLAILEYLaer 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  68 -----YLSSGHDMCDLSNQWLEWEAAELQPALSAAL--YAHVVQGKKKEDVMATISASLKHLDQSLAGKssPYLIKDALT 140
Cdd:COG0625   77 ypeppLLPADPAARARVRQWLAWADGDLHPALRNLLerLAPEKDPAAIARARAELARLLAVLEARLAGG--PYLAGDRFS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 147905173 141 VVDIVVWGSIYPLivDASNLP-EEMASLKRWFQNVSQLEQCQKA 183
Cdd:COG0625  155 IADIALAPVLRRL--DRLGLDlADYPNLAAWLARLAARPAFQRA 196
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
850-904 1.23e-06

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: 46.18  E-value: 1.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 147905173   850 QELEKQGNHVRELKGKKAEKSVIDPEVQKLLALKKELALAEGKSPDPPTQKGKKK 904
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
2-67 1.05e-04

GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal TRX-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression.


Pssm-ID: 239342 [Multi-domain]  Cd Length: 75  Bit Score: 41.47  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147905173   2 KLFVGEGNPQGVKVLAAAALWAQHVQIDRLQQE--------EKIVPFMsqpRLPVLDLENGNYLFLSNAICRYF 67
Cdd:cd03044    2 TLYTYPGNPRSLKILAAAKYNGLDVEIVDFQPGkenktpefLKKFPLG---KVPAFEGADGFCLFESNAIAYYV 72
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
106-179 9.99e-03

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 36.38  E-value: 9.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147905173  106 KKKEDVMATISASLKHLDQSLAGKSSPYLIKDALTVVDIVVWGSIYPLIV-DASNLPEEMASLKRWFQNVSQLEQ 179
Cdd:pfam14497  22 RRKEFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYpKAPDALDKYPKLKALHERVAARPN 96
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
251-873 0e+00

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 853.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 251 RPHPILPVEGEKNVLITSALPYVNNVPHLGNIIGSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQI 330
Cdd:PLN02610   6 KSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 331 CDKYNAIHTAIYQWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPF--CNY 408
Cdd:PLN02610  86 CDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 409 EEARGDQCDKCGKLINAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEQSFSTGDWTSNARFITRSWIRDGL 488
Cdd:PLN02610 166 DSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRDGL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 489 KPRCITRDLKWGTPVPLDGFRDKVFYVWFDAPIGYISITANYTDQWEKWWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLG 568
Cdd:PLN02610 246 KPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLG 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 569 AEDNYTLVNHLVATEYLNYEDGKFSKSRGVGVFGDMAKDTGIPADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSELLNNL 648
Cdd:PLN02610 326 TGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 649 GNFVNRAGMFVQK----FFNGCVPEM---ELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQVNE 721
Cdd:PLN02610 406 GNFINRVLSFIAKppgaGYGSVIPDApgaESHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQ 485
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 722 PWKCIKgnqQEQKRAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPQESKVLTTDFCCC---------LQSGHQI 792
Cdd:PLN02610 486 FWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLSLSDEKGEVarakrpwelVPAGHKI 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 793 GNVSPLFQKLENDQIESLRKRFGGGQVKTESKVSPSQEAP--EQQAPKASGPERVKelmQELEKQGNhvrELKGKKAEKS 870
Cdd:PLN02610 563 GTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKlaKQLKKKALSDGGKK---KQGKKAGG---GGKSKAAAER 636

                 ...
gi 147905173 871 VID 873
Cdd:PLN02610 637 EID 639
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
262-810 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: 647.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 262 KNVLITSALPYVNNVPHLGNIIgSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAI 341
Cdd:COG0143    1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 342 YQWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPFCNYEEARGDQCDKCGK 421
Cdd:COG0143   80 FEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 422 LINAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEqsfSTGDWTSNARFITRSWIRDGLKPRCITRDLKWGT 501
Cdd:COG0143  160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIE---ENPDIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 502 PVPldGFRDKVFYVWFDAPIGYISITANYTDQ------WEKWWKSPqQVQLYNFMAKDNVPFHSVVFPSCLLGAedNYTL 575
Cdd:COG0143  237 PVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAP-DTELVHFIGKDIIRFHAIIWPAMLMAA--GLPL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 576 VNHLVATEYLNYEDGKFSKSRGVGVFGDMAKDTgIPADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSELLNNLGNFVNRA 655
Cdd:COG0143  312 PKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRT 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 656 GMFVQKFFNGCVPEM-ELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQVNEPWKCIKGNQQEqk 734
Cdd:COG0143  391 LSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPE-- 468
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147905173 735 RAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPQESKVLtTDFCCCLQSGHQIGNVSPLFQKLENDQIESL 810
Cdd:COG0143  469 RLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTW-EDAGWPLPAGHKIGKPEPLFPRIEDEQIEAL 543
metG PRK00133
methionyl-tRNA synthetase; Reviewed
262-847 0e+00

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 646.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 262 KNVLITSALPYVNNVPHLGNIIGsVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAI 341
Cdd:PRK00133   2 RKILVTCALPYANGPIHLGHLVE-YIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 342 YQWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPFCNYEEARGDQCDKCGK 421
Cdd:PRK00133  81 FAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 422 LINAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEQSfstGDWTSNARFITRSWIRDGLKPRCITRDLKW-G 500
Cdd:PRK00133 161 TYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRS---GELQPNVANKMKEWLEEGLQDWDISRDAPYfG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 501 TPVPldGFRDKVFYVWFDAPIGYISITANYTDQ-----WEKWWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLGAedNYTL 575
Cdd:PRK00133 238 FEIP--GAPGKVFYVWLDAPIGYISSTKNLCDKrggldWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGA--GYRL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 576 VNHLVATEYLNYEDGKFSKSRGVGVFGDMAKDTgIPADIWRFYLLYVRPEG-QDSAFSWSDLMLKNNSELLNNLGNFVNR 654
Cdd:PRK00133 314 PTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDH-LDPDYLRYYLAAKLPETiDDLDFNWEDFQQRVNSELVGKVVNFASR 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 655 AGMFVQKFFNGCVPEMEllsEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQVNEPWKCIKgnqQEQK 734
Cdd:PRK00133 393 TAGFINKRFDGKLPDAL---ADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAK---QDGE 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 735 RAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPQeskvLTTDFCCCLQSGHQIGNVSPLFQKLENDQIESLRKrf 814
Cdd:PRK00133 467 RLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEE----LTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIE-- 540
                        570       580       590
                 ....*....|....*....|....*....|...
gi 147905173 815 gggqvktESKVSPSQEAPEQQAPKASGPERVKE 847
Cdd:PRK00133 541 -------ASKEAAAAKAAAAAAAAPLAEEPIAE 566
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
264-803 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: 592.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  264 VLITSALPYVNNVPHLGNIIgSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAIYQ 343
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  344 WFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPFCNYEEARGDQCDKCGKLI 423
Cdd:TIGR00398  80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  424 NAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEQSFSTGDWTSNARFITRSWIRDGLKPRCITRDLK-WGTP 502
Cdd:TIGR00398 160 EPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVyWGIP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  503 VPLDgfRDKVFYVWFDAPIGYIS---ITANYTDQWEKWWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLGAEdnYTLVNHL 579
Cdd:TIGR00398 240 VPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLG--LPLPTQV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  580 VATEYLNYEDGKFSKSRGVGVFGDMAKDtGIPADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSELLNNLGNFVNRAGMFV 659
Cdd:TIGR00398 316 FSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  660 QKFFNGCVP-EMELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQVNEPWKCIKgnqqEQKRAGT 738
Cdd:TIGR00398 395 KKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFK----QSPRLKE 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147905173  739 VTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPqeskvLTTDFCCCLQSGHQIGNVSPLFQKLE 803
Cdd:TIGR00398 471 LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE-----LEWDFKLKLLEGHKLNKAEPLFSKIE 530
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
264-655 0e+00

tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 563.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  264 VLITSALPYVNNVPHLGNIIgSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAIYQ 343
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLY-SYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  344 WFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVEGICPFCNYEEARGDQCDKCGKLI 423
Cdd:pfam09334  80 KFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  424 NAVELKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEQsfSTGDWTSNARFITRSWIRDGLKPRCITRDLKWGTPV 503
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEE--NNPEWPENVKNMVLEWLKEGLKDRAISRDLDWGIPV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  504 PldGFRDKVFYVWFDAPIGYISITANYTDQ---WEKWWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLGAedNYTLVNHLV 580
Cdd:pfam09334 238 P--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGA--GYRLPTTVF 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147905173  581 ATEYLNYEDGKFSKSRGVGVFGDMAKDTgIPADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSELLNNLGNFVNRA 655
Cdd:pfam09334 314 AHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
263-631 2.32e-169

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: 494.74  E-value: 2.32e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 263 NVLITSALPYVNNVPHLGNIIGSVLsADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAIY 342
Cdd:cd00814    1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 343 QWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLadrfvegicpfcnyeeargdqcdkcgkl 422
Cdd:cd00814   80 KWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL---------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 423 inavelkkpqckickqsPVIKSSKHLFLDLPKLEKRLEQWLEQSfSTGDWTSNARFITRSWIRDGLKPRCITRDL-KWGT 501
Cdd:cd00814  132 -----------------PEWREEEHYFFRLSKFQDRLLEWLEKN-PDFIWPENARNEVLSWLKEGLKDLSITRDLfDWGI 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 502 PVPLDgfRDKVFYVWFDAPIGYISITANYTDQWEK-WWKSPQQVQLYNFMAKDNVPFHSVVFPSCLLGAedNYTLVNHLV 580
Cdd:cd00814  194 PVPLD--PGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGA--GLPLPTRIV 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 147905173 581 ATEYLNYEDGKFSKSRGVGVFGDMAKDTGiPADIWRFYLLYVRPEGQDSAF 631
Cdd:cd00814  270 AHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEGKDSDF 319
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
262-803 3.61e-92

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 301.03  E-value: 3.61e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 262 KNVLITSALPYVNNVPHLGNIiGSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIHTAI 341
Cdd:PRK11893   1 KKFYITTPIYYPNGKPHIGHA-YTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 342 YQWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFvegicpfcnyeeargdqcdkcgk 421
Cdd:PRK11893  80 WEALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESE----------------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 422 LINavelKKPQCKICKQSPVIKSSKHLFLDLPKLEKRLEQWLEQsfstgdwtsNARFI--------TRSWIRDGLKPRCI 493
Cdd:PRK11893 137 LIE----DGYRCPPTGAPVEWVEEESYFFRLSKYQDKLLELYEA---------NPDFIqpasrrneVISFVKSGLKDLSI 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 494 TR-DLKWGTPVPLDGfrDKVFYVWFDAPIGYIS------ITANYTDQWEKWWksPQQVqlyNFMAKDNVPFHSVVFPSCL 566
Cdd:PRK11893 204 SRtNFDWGIPVPGDP--KHVIYVWFDALTNYLTalgypdDEELLAELFNKYW--PADV---HLIGKDILRFHAVYWPAFL 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 567 LGAedNYTLVNHLVATEYLNYEDGKFSKSRG--VGVFgDMAKDTGipADIWRFYLLYVRPEGQDSAFSWSDLMLKNNSEL 644
Cdd:PRK11893 277 MAA--GLPLPKRVFAHGFLTLDGEKMSKSLGnvIDPF-DLVDEYG--VDAVRYFLLREIPFGQDGDFSREAFINRINADL 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 645 LNNLGNFVNRAGMFVQKFFNGCVPEM-ELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQVNEPW 723
Cdd:PRK11893 352 ANDLGNLAQRTLSMIAKNFDGKVPEPgALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPW 431
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 724 KCIKgnqQEQKRAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPQESKVLTTDFCC-CLQSGHQIGNVSPLFQKL 802
Cdd:PRK11893 432 SLAK---TDPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEEDENRDFAALSWgRLAPGTTLPKPEPIFPRL 508

                 .
gi 147905173 803 E 803
Cdd:PRK11893 509 E 509
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
261-833 4.99e-80

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 272.06  E-value: 4.99e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 261 EKNVLITSALPYVNNVPHLGN----IIgsvlsADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNA 336
Cdd:PRK12267   3 KKTFYITTPIYYPNGKPHIGHayttIA-----ADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 337 IHTAIYQWFNISFDYFGRTT-TQHQTTIsQDIFHRLLEREFLLTDTVEQLRCEKCQRF-----LADrfvEGICPFCNYEe 410
Cdd:PRK12267  78 GFKELWKKLDISYDKFIRTTdERHKKVV-QKIFEKLYEQGDIYKGEYEGWYCVSCETFftesqLVD---GGKCPDCGRE- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 411 argdqcdkcgklinaVELKKpqckickqspviksSKHLFLDLPKLEKRLEQWLEQsfstgdwtsNARFI---------TR 481
Cdd:PRK12267 153 ---------------VELVK--------------EESYFFRMSKYQDRLLEYYEE---------NPDFIqpesrknemIN 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 482 SWIRDGLKPRCITRD-LKWGTPVPLDGfrDKVFYVWFDAPIGYISiTANY----TDQWEKWWksPQQVQLynfMAKDNVP 556
Cdd:PRK12267 195 NFIKPGLEDLSISRTsFDWGIPVPFDP--KHVVYVWIDALLNYIT-ALGYgsddDELFKKFW--PADVHL---VGKDILR 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 557 FHSVVFPSCL--LGAEdnytLVNHLVATEYLNYEDGKFSKSRGVGVFG-DMAKDTGIpaDIWRFYLLYVRPEGQDSAFSW 633
Cdd:PRK12267 267 FHAIYWPIMLmaLGLP----LPKKVFAHGWWLMKDGKMSKSKGNVVDPeELVDRYGL--DALRYYLLREVPFGSDGDFSP 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 634 SDLMLKNNSELLNNLGNFVNRA-GMfVQKFFNGCVPEMELLSE-DKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISR 711
Cdd:PRK12267 341 EALVERINSDLANDLGNLLNRTvAM-INKYFDGEIPAPGNVTEfDEELIALAEETLKNYEELMEELQFSRALEEVWKLIS 419
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 712 HGNQYIQVNEPWKCIKgNQQEQKRAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQL-LMPQESKVLTTDFCCCLQSGH 790
Cdd:PRK12267 420 RANKYIDETAPWVLAK-DEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLgLEEELTSWESLLEWGGLPAGT 498
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....
gi 147905173 791 QIGNVSPLFQKLENDQ-IESLRKRFGGGQVKTESKVSPSQEAPE 833
Cdd:PRK12267 499 KVAKGEPLFPRIDVEEeIAYIKEQMEGSAPKEPEEKEKKPEKPE 542
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
75-177 1.14e-48

Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198340 [Multi-domain]  Cd Length: 102  Bit Score: 167.29  E-value: 1.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  75 MCDLSNQWLEWEAAELQPALSAALYAHVVQGKKKEDVMATISASLKHLDQSLAGKSSPYLiKDALTVVDIVVWGSIYPLI 154
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79
                         90       100
                 ....*....|....*....|...
gi 147905173 155 VDASNLPEEMASLKRWFQNVSQL 177
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
Anticodon_Ia_Met cd07957
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ...
640-769 1.31e-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: 159.58  E-value: 1.31e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 640 NNSELLNNLGNFVNRAGMFVQKFFNGCVPEME-LLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQ 718
Cdd:cd07957    1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGgLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 147905173 719 VNEPWKCIKGNQQEqkRAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQL 769
Cdd:cd07957   81 ETAPWKLAKEEDPE--RLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
PLN02224 PLN02224
methionine-tRNA ligase
259-832 8.77e-42

methionine-tRNA ligase


Pssm-ID: 177869 [Multi-domain]  Cd Length: 616  Bit Score: 162.58  E-value: 8.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 259 EGEKNVLiTSALPYVNNVPHLGNIIgSVLSADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNAIH 338
Cdd:PLN02224  67 EADTFVL-TTPLYYVNAPPHMGSAY-TTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSY 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 339 TAIYQWFNISFDYFGRTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRfvegicpfcnyeeargdqcdk 418
Cdd:PLN02224 145 RTLWKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEK--------------------- 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 419 cgklinavELKKPQCKICKQSP-VIKSSKHLFLDLPKLEKRLEQWLEQsfstgdwtsNARFI--------TRSWIRDGLK 489
Cdd:PLN02224 204 --------ELLENNCCPVHQMPcVARKEDNYFFALSKYQKPLEDILAQ---------NPRFVqpsyrlneVQSWIKSGLR 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 490 PRCITRDL-KWGTPVPLDGfrDKVFYVWFDAPIGYIS-ITANYTDQWEKWWKSPQQVQLYNFMAKDNVPFHSVVFPSCLL 567
Cdd:PLN02224 267 DFSISRALvDWGIPVPDDD--KQTIYVWFDALLGYISaLTEDNKQQNLETAVSFGWPASLHLIGKDILRFHAVYWPAMLM 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 568 GAedNYTLVNHLVATEYLNYEDGKFSKSRG--------VGVFGdmakdtgipADIWRFYLLYVRPEGQDSAFSWSDLMLK 639
Cdd:PLN02224 345 SA--GLELPKMVFGHGFLTKDGMKMGKSLGntlepfelVQKFG---------PDAVRYFFLREVEFGNDGDYSEDRFIKI 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 640 NNSELLNNLGNFVNRA-GMFVQKFFNGCVPEMELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHGNQYIQ 718
Cdd:PLN02224 414 VNAHLANTIGNLLNRTlGLLKKNCESTLVEDSTVAAEGVPLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNTYMD 493
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 719 VNEPWKCIKGNQQEQKRAGTVTGVAVNMAALLSIMLHPYMPTISSVIQEQLLMPQE---SKVLTTDFCCCLQSGHQIGNV 795
Cdd:PLN02224 494 QRAPWFLFKQGGVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQLGYSEDqfnSITWSDTKWGGLKGGQVMEQA 573
                        570       580       590
                 ....*....|....*....|....*....|....*...
gi 147905173 796 SPLFQKLE-NDQIESLRKRFGGGQVKTESKVSPSQEAP 832
Cdd:PLN02224 574 SPVFARIElNPEKEEDEKKPKVGKKTGKAKVKVVEQTP 611
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
265-628 5.23e-31

catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.


Pssm-ID: 185674 [Multi-domain]  Cd Length: 312  Bit Score: 124.07  E-value: 5.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 265 LITSALPYVNNVPHLGNIIGSVLsADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGL-------------TPQQIC 331
Cdd:cd00668    3 YVTTPPPYANGSLHLGHALTHII-ADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEFV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 332 DKYNAIHTAIYQWFNISFDY--FGRTTTQHQTTISQDIFHRLLEREFLLTDTVeqlrcekcqrfladrfvegicpfcnye 409
Cdd:cd00668   82 EEMSGEHKEDFRRLGISYDWsdEYITTEPEYSKAVELIFSRLYEKGLIYRGTH--------------------------- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 410 eargdqcdkcgklinavelkkpqckickqsPVIKsSKHLFLDLPKLEKRLEQWLEQsfstGDWTSN---ARFitRSWIRD 486
Cdd:cd00668  135 ------------------------------PVRI-TEQWFFDMPKFKEKLLKALRR----GKIVPEhvkNRM--EAWLES 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 487 GLKpRCITRDLKWGTPVPldgfrDKVFYVWFDAPIGYISITAN--YTDQWEKWWKSpqqvqLYNFMAKDNVPFHSVVFPS 564
Cdd:cd00668  178 LLD-WAISRQRYWGTPLP-----EDVFDVWFDSGIGPLGSLGYpeEKEWFKDSYPA-----DWHLIGKDILRGWANFWIT 246
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147905173 565 CLLGAEDNYTLvNHLVATEYLNYEDG-KFSKSRG-VGVFGDMAKDTGipADIWRFYLLYVRPEGQD 628
Cdd:cd00668  247 MLVALFGEIPP-KNLLVHGFVLDEGGqKMSKSKGnVIDPSDVVEKYG--ADALRYYLTSLAPYGDD 309
GST_N_5 pfam18485
Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing ...
1-72 1.16e-24

Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing a thioredoxin fold. This domain found in methionyl-tRNA synthetase (MRS), a multi-tRNA synthetase complex (MSC) component.


Pssm-ID: 436537  Cd Length: 74  Bit Score: 97.85  E-value: 1.16e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147905173    1 MKLFVGEGNPQGVKVLAAAALWAQH--VQIDRLQQEEKIVPFMSQPRLPVLDLENGNYLFLSNAICRYFYLSSG 72
Cdd:pfam18485   1 MKLFVSEGNPHCLKVLAAAEATGVKcdVQVQFVNHEEKVVPFLTRPVLPTLELDSGQFLFSPNAICRYLFELSG 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-183 1.86e-11

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 64.15  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173   1 MKLFVGEGNPQGVKVLAAAAL----WaQHVQIDRLQQEEK------IVPFMsqpRLPVLdLENGNYLFLSNAICRYF--- 67
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEkglpY-ELVPVDLAKGEQKspeflaLNPLG---KVPVL-VDDGLVLTESLAILEYLaer 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  68 -----YLSSGHDMCDLSNQWLEWEAAELQPALSAAL--YAHVVQGKKKEDVMATISASLKHLDQSLAGKssPYLIKDALT 140
Cdd:COG0625   77 ypeppLLPADPAARARVRQWLAWADGDLHPALRNLLerLAPEKDPAAIARARAELARLLAVLEARLAGG--PYLAGDRFS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 147905173 141 VVDIVVWGSIYPLivDASNLP-EEMASLKRWFQNVSQLEQCQKA 183
Cdd:COG0625  155 IADIALAPVLRRL--DRLGLDlADYPNLAAWLARLAARPAFQRA 196
MetRS_RNA cd00939
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ...
848-877 1.67e-09

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: 54.02  E-value: 1.67e-09
                         10        20        30
                 ....*....|....*....|....*....|
gi 147905173 848 LMQELEKQGNHVRELKGKKAEKSVIDPEVQ 877
Cdd:cd00939    1 LEKEVAEQGNKVRKLKASKADKSVWQPEVN 30
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
271-524 2.21e-09

catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 185677 [Multi-domain]  Cd Length: 382  Bit Score: 60.34  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 271 PYVNNVPHLGNIIGSVLsADVFARYCRLRNWNTLYICGTDEYGTATETK----AMEEGLTPQQIC-DKYNAI-------- 337
Cdd:cd00817   10 PNVTGSLHMGHALNNTI-QDIIARYKRMKGYNVLWPPGTDHAGIATQVVvekkLGIEGKTRHDLGrEEFLEKcwewkees 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 338 HTAIYQWFN---ISFD----YFgrTTTQHQTTISQDIFHRLLEREFLLTDTVEQLRCEKCQRFLADRFVegicpfcnyee 410
Cdd:cd00817   89 GGKIREQLKrlgASVDwsreYF--TMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV----------- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 411 argdqCDKCGKLInavE-LKKPQ----CKICKQsPVIKSSKHLFLD-LPKL-EKRLEQWLEqsfSTGDWtsnarfitrsw 483
Cdd:cd00817  156 -----CSRSGDVI---EpLLKPQwfvkVKDLAK-KALEAVKEGDIKfVPERmEKRYENWLE---NIRDW----------- 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 147905173 484 irdglkprCITRDLKWGTPVPldgfrdkvfyVWFDAPIGYI 524
Cdd:cd00817  213 --------CISRQLWWGHRIP----------AWYCKDGGHW 235
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
445-769 7.62e-09

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: 59.69  E-value: 7.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  445 SKHLFLDLPKLEKRLEQWLEQSFStgDWTSNaRFITR--SWIRDgLKPRCITRDLKWGTPVPldgfrdkvfyVWfdapig 522
Cdd:TIGR00422 355 SKQWFVKVEKLADKALEAAEEGEI--KFVPK-RMEKRylNWLRN-IKDWCISRQLIWGHRIP----------VW------ 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  523 YISITANYTDQWEKWW-KSPQQVQL-YNFMAKDNVP---FHSVVFPSCLLGAEDN------------------------- 572
Cdd:TIGR00422 415 YCKECGEVYVAKEEPLpDDKTNTGPsVELEQDTDVLdtwFSSSLWPFSTLGWPDEtkdlkkfyptdllvtgydiiffwva 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  573 YTLVNHLVATEYLNY-----------EDG-KFSKSRGVGVFG-DMAKDTGipADIWRFYLLYVRPEGQDSAFSWSDlmLK 639
Cdd:TIGR00422 495 RMIFRSLALTGQVPFkevyihglvrdEQGrKMSKSLGNVIDPlDVIEKYG--ADALRFTLASLVTPGDDINFDWKR--VE 570
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  640 NNSELLNNLGNfvnrAGMFV------QKFFNGcvPEMELLSEDKRLLAQVAAELQQYNLLLEKVRIRDALRCILNISRHG 713
Cdd:TIGR00422 571 SARNFLNKLWN----ASRFVlmnlsdDLELSG--GEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALYEFIWND 644
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  714 --NQYIQV--NEPWkciKGNQQEQKRAGTVTGVAVNMAALLsimLHPYMPTISSVIQEQL 769
Cdd:TIGR00422 645 fcDWYIELvkYRLY---NGNEAEKKAARDTLYYVLDKALRL---LHPFMPFITEEIWQHF 698
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
81-176 3.03e-08

C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 2; composed of uncharacterized bacterial proteins, with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.


Pssm-ID: 198289 [Multi-domain]  Cd Length: 110  Bit Score: 52.67  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  81 QWLEWEAAELQPALSAALYAHVVQGKKKEDvMATISASL----KH---LDQSLAGKssPYLIKDALTVVDIVVWGSIYPL 153
Cdd:cd03180    8 RWMDWQTSTLNPAFRYAFWGLVRTPPEQRD-PAAIAASLaacnKLmaiLDAQLARQ--AYLAGDRFTLADIALGCSVYRW 84
                         90       100
                 ....*....|....*....|....*.
gi 147905173 154 IvdasNLPEEMAS---LKRWFQNVSQ 176
Cdd:cd03180   85 L----ELPIERPAlphLERWYARLSQ 106
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
266-633 2.14e-07

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: 53.79  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 266 ITSALPYVNNVPHLGNIIGSVLsADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQIcDKYNaIHTAIYQW- 344
Cdd:cd00812    4 ILVMFPYPSGALHVGHVRTYTI-GDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDW-TEYN-IKKMKEQLk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 345 -FNISFDYfgrtttqhqttisqdifhrllEREFLLTDtveqlrcEKCQRFLADRFVEgiCPFCNYeeargdqCDKCGKLI 423
Cdd:cd00812   81 rMGFSYDW---------------------RREFTTCD-------PEYYKFTQWLFLK--LYEKGL-------AYKKEAPV 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 424 NavelkkpQCKICKQspviksskhLFLDL------PKLEKRLEQWLeqsfstgDWTSNARFITRSWIRdglkprcITRDL 497
Cdd:cd00812  124 N-------WCKLLDQ---------WFLKYsetewkEKLLKDLEKLD-------GWPEEVRAMQENWIG-------CSRQR 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 498 KWGTPVP----LDGFRDKVFYvwfdaPIGYISitANYTDQ-WEKWWKSPQQVQLYnFM-------AKDNVP--------F 557
Cdd:cd00812  174 YWGTPIPwtdtMESLSDSTWY-----YARYTD--AHNLEQpYEGDLEFDREEFEY-WYpvdiyigGKEHAPnhllysrfN 245
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 147905173 558 HSVVFPSCLLGAEdnytLVNHLVATEYLNYEDGKFSKSRGVGV-FGDMAKDTGipADIWRFYLLYVRPegQDSAFSW 633
Cdd:cd00812  246 HKALFDEGLVTDE----PPKGLIVQGMVLLEGEKMSKSKGNVVtPDEAIKKYG--ADAARLYILFAAP--PDADFDW 314
WHEP-TRS pfam00458
WHEP-TRS domain;
848-878 2.15e-07

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 48.26  E-value: 2.15e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 147905173  848 LMQELEKQGNHVRELKGKKAEKSVIDPEVQK 878
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKK 31
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
108-175 9.19e-07

Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198322 [Multi-domain]  Cd Length: 82  Bit Score: 47.31  E-value: 9.19e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147905173 108 KEDVMATISASLKHLDQSLAgkSSPYLIKDALTVVDIVVWGSIYPLIVDASNL-PEEMASLKRWFQNVS 175
Cdd:cd10289   14 SLLKGKELEALLKSLNSYLA--SRTFLVGYSLTLADVAVFSALYPSGQKLSDKeKKKFPHVTRWFNHIQ 80
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
850-904 1.23e-06

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: 46.18  E-value: 1.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 147905173   850 QELEKQGNHVRELKGKKAEKSVIDPEVQKLLALKKELALAEGKSPDPPTQKGKKK 904
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDTP 56
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
81-183 1.65e-06

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 47.63  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  81 QWLEWEAAELQPALSAALYAH-----VVQGKKKEDVMATISASLKHLDQSLAGKssPYLIKDALTVVDI---VV--WGSI 150
Cdd:cd03188    8 EWLNFIASELHKAFGPLFYPArwaddALAEEVKAAARERLERRLAYLDAQLAGG--PYLLGDQFSVADAylfVVlrWARA 85
                         90       100       110
                 ....*....|....*....|....*....|...
gi 147905173 151 YPLivDASNLPeemaSLKRWFQNVSQLEQCQKA 183
Cdd:cd03188   86 VGL--DLSDWP----HLAAYLARVAARPAVQAA 112
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
849-878 4.44e-06

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: 44.07  E-value: 4.44e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 147905173 849 MQELEKQGNHVRELKGKKAEKSVIDPEVQK 878
Cdd:cd01200    1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKK 30
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
81-174 8.09e-06

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 45.18  E-value: 8.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  81 QWLEWEAAELQPALSAALYAHVVQGKKKEDVMAT----ISASLKHLDQSLAGKssPYLIKDALTVVDIVVWGSIYPLIV- 155
Cdd:cd00299    3 ALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAareeLPALLAALEQLLAGR--PYLAGDQFSLADVALAPVLARLEAl 80
                         90       100
                 ....*....|....*....|
gi 147905173 156 -DASNLPEEMASLKRWFQNV 174
Cdd:cd00299   81 gPYYDLLDEYPRLKAWYDRL 100
Anticodon_3 pfam19303
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ...
667-817 1.70e-05

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: 45.57  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  667 VPEM-ELLSEDKRLLAQVAAELQQYNLLLEKVRIRDA---LRCILNIsrhGNQYIQVNEPWKCIKgnqQEQKRAGTVTGV 742
Cdd:pfam19303   1 VPEGgAYGEAEAALIADLTTRLAAYEGHMEAMEVRKAaaeLRAIWVA---GNEYLQEAAPWTTFK---TDPEAAAAQVRL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  743 AVNMAALLSIMLHPYMPTISSVIQEQLLM-----PQE-SKVLTTdfcccLQSGHQIgnVSP--LFQKLENDQIESLRKRF 814
Cdd:pfam19303  75 ALNLIRLYAVLSAPFIPDAAAAMLAAMGTddaawPDDvAAALTA-----LPAGHAF--TVPevLFAKITDEQREEWQERF 147

                  ...
gi 147905173  815 GGG 817
Cdd:pfam19303 148 AGT 150
GST_C_AIMP3 cd10305
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
81-178 2.41e-05

Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging.


Pssm-ID: 198338 [Multi-domain]  Cd Length: 101  Bit Score: 43.82  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  81 QWLEWEAAELQPALSAAlyahvvqgkkkedvmaTISASLKHLDQSLAGKSspYLIKDALTVVDIVVWGSIYPLIVDASNL 160
Cdd:cd10305    9 QWLEYRVTQVAPASDKA----------------DAKSLLKELNSYLQDRT--YLVGHKLTLADVVLYYGLHPIMKDLSPQ 70
                         90
                 ....*....|....*....
gi 147905173 161 PEEMAS-LKRWFQNVSQLE 178
Cdd:cd10305   71 EKEQYLnVSRWFDHVQHLP 89
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
81-172 2.50e-05

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 43.82  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  81 QWLEWEAAELQPALSAALYAHVVQGKKKEDVMA----TISASLKHLDQSLAGKssPYLIKDALTVVDiVVWGSIYpLIVD 156
Cdd:cd03207    3 RWLFFAAGTVEPPLLNKALGRFFEPPWGEPAIAaaygDLDERLAALEAALAGR--PYLVGERFSAAD-LLLASVL-RWAR 78
                         90
                 ....*....|....*.
gi 147905173 157 ASNLPEEMASLKRWFQ 172
Cdd:cd03207   79 AFGLLPEYPALRAYVA 94
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
271-377 6.93e-05

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: 43.62  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173 271 PYVNNVPHLGNIIGSVLsADVFARYCRLRNWNTLYICGTDEYGTATETKAMEEGLTPQQICDKYNA-IHTAIYQWFNISF 349
Cdd:cd00802    6 ITPNGYLHIGHLRTIVT-FDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIErIKEDVEYMFLQAA 84
                         90       100       110
                 ....*....|....*....|....*....|
gi 147905173 350 DY--FGRTTTQHQTTISQDIFHRLLEREFL 377
Cdd:cd00802   85 DFllLYETECDIHLGGSDQLGHIELGLELL 114
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
848-877 7.57e-05

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: 41.07  E-value: 7.57e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 147905173 848 LMQELEKQGNHVRELKGKKAEKSVIDPEVQ 877
Cdd:cd00936    1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVK 30
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
2-67 1.05e-04

GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal TRX-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression.


Pssm-ID: 239342 [Multi-domain]  Cd Length: 75  Bit Score: 41.47  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147905173   2 KLFVGEGNPQGVKVLAAAALWAQHVQIDRLQQE--------EKIVPFMsqpRLPVLDLENGNYLFLSNAICRYF 67
Cdd:cd03044    2 TLYTYPGNPRSLKILAAAKYNGLDVEIVDFQPGkenktpefLKKFPLG---KVPAFEGADGFCLFESNAIAYYV 72
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
81-179 2.62e-04

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 41.39  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  81 QWLEWEAAELQPALSAA---LYAHVVQGKKKED-VMATISASLKHLDQSLAGKSspYLIKDALTVVDIVVWGSIYPL--- 153
Cdd:cd03181    7 QWISFANSELLPAAATWvlpLLGIAPYNKKAVDkAKEDLKRALGVLEEHLLTRT--YLVGERITLADIFVASALLRGfet 84
                         90       100
                 ....*....|....*....|....*.
gi 147905173 154 IVDASnLPEEMASLKRWFQNVSQLEQ 179
Cdd:cd03181   85 VLDPE-FRKKYPNVTRWFNTVVNQPK 109
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
80-183 3.58e-04

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.


Pssm-ID: 198324 [Multi-domain]  Cd Length: 110  Bit Score: 40.71  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905173  80 NQWLEWEAAELQPALSAA----LYA--HVVQGKKKedvMATISASLKH-LDQSLAGksSPYLIKDALTVVDIVVWGSIYP 152
Cdd:cd10291    6 LQWLMWQMGGLGPMQGQAhhfkRYApeKIPYAIKR---YTNETKRLYGvLDRRLAK--SKYLAGDEYSIADIAIWPWVAR 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 147905173 153 LI---VDASNLPEemasLKRWFQNVSQLEQCQKA 183
Cdd:cd10291   81 HEwqgIDLADFPN----LKRWFERLAARPAVQKG 110
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
271-319 4.51e-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: 40.86  E-value: 4.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 147905173  271 PYVNNVPHLGNIIGSVLSaDVFARYCRLRNWNTLYICGTDEYGTATETK 319
Cdd:pfam00133  32 PNATGSLHIGHALAKTLK-DIVIRYKRMKGYYVLWVPGWDHHGLPTEQV 79
GST_C_GluProRS_N cd10309
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ...
115-177 8.63e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198342 [Multi-domain]  Cd Length: 81  Bit Score: 36.14  E-value: 8.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 147905173 115 ISASLKHLDQSLAGKSspYLIKDALTVVDIVVWGSIYplivdASN----LPEEMASLKRWFQNVSQL 177
Cdd:cd10309   22 FSSALSYLDKALSLRT--YLVGNSLTLADFAVWAALR-----GNGewlaSKEKYVNVTRWFKFISSQ 81
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
106-179 9.99e-03

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 36.38  E-value: 9.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147905173  106 KKKEDVMATISASLKHLDQSLAGKSSPYLIKDALTVVDIVVWGSIYPLIV-DASNLPEEMASLKRWFQNVSQLEQ 179
Cdd:pfam14497  22 RRKEFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYpKAPDALDKYPKLKALHERVAARPN 96
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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