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Conserved domains on  [gi|544470873|ref|XP_005571393|]
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PREDICTED: methionine--tRNA ligase, cytoplasmic isoform X2 [Macaca fascicularis]

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
251-893 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: 859.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 251 RPQQNPVLPVTGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQ 330
Cdd:PLN02610   4 EGKSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 331 EICDKYHIIHADIYRWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPF--C 408
Cdd:PLN02610  84 EICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 409 GYEEARGDQCDKCGKLINAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRTLPGSDWTPNARFITRSWLRD 488
Cdd:PLN02610 164 NYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRD 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 489 GLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHGIVFPCSA 568
Cdd:PLN02610 244 GLKPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTL 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 569 LGAEDNYTLVSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLN 648
Cdd:PLN02610 324 LGTGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLN 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 649 NLGNFINRAGMFVSK----FFGGYVPEMV---LNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQV 721
Cdd:PLN02610 404 NLGNFINRVLSFIAKppgaGYGSVIPDAPgaeSHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQE 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 722 NEPWKRIKgseADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSilltnfLCT------------- 788
Cdd:PLN02610 484 SQFWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLS------LSDekgevarakrpwe 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 789 -LPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPTVIETVTTAGPQQIQALMDEVTKQGnivrELKAQKADKN 867
Cdd:PLN02610 555 lVPAGHKIGTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLAKQLKKKALSDGGKKKQ----GKKAGGGGKS 630
                        650       660       670
                 ....*....|....*....|....*....|
gi 544470873 868 QVAAE----VAKlLDLKKQLAVAEGKPPEA 893
Cdd:PLN02610 631 KAAAEreidVSR-LDIRVGLIVKAEKHPDA 659
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
77-179 3.94e-46

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: 160.36  E-value: 3.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  77 QDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLaGETESLADIVLWGALYPLL 156
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79
                         90       100
                 ....*....|....*....|...
gi 544470873 157 QDPAYLPEELSALHSWFQTLSTQ 179
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
GST_N_5 pfam18485
Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing ...
1-74 5.41e-29

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: 110.56  E-value: 5.41e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544470873    1 MRLFVSEGAPGCLPVLAAAGRARGRAELLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSG 74
Cdd:pfam18485   1 MKLFVSEGNPHCLKVLAAAEATGVKCDVQVQFVNHEEKVVPFLTRPVLPTLELDSGQFLFSPNAICRYLFELSG 74
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
251-893 0e+00

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 859.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 251 RPQQNPVLPVTGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQ 330
Cdd:PLN02610   4 EGKSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 331 EICDKYHIIHADIYRWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPF--C 408
Cdd:PLN02610  84 EICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 409 GYEEARGDQCDKCGKLINAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRTLPGSDWTPNARFITRSWLRD 488
Cdd:PLN02610 164 NYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRD 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 489 GLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHGIVFPCSA 568
Cdd:PLN02610 244 GLKPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTL 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 569 LGAEDNYTLVSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLN 648
Cdd:PLN02610 324 LGTGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLN 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 649 NLGNFINRAGMFVSK----FFGGYVPEMV---LNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQV 721
Cdd:PLN02610 404 NLGNFINRVLSFIAKppgaGYGSVIPDAPgaeSHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQE 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 722 NEPWKRIKgseADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSilltnfLCT------------- 788
Cdd:PLN02610 484 SQFWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLS------LSDekgevarakrpwe 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 789 -LPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPTVIETVTTAGPQQIQALMDEVTKQGnivrELKAQKADKN 867
Cdd:PLN02610 555 lVPAGHKIGTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLAKQLKKKALSDGGKKKQ----GKKAGGGGKS 630
                        650       660       670
                 ....*....|....*....|....*....|
gi 544470873 868 QVAAE----VAKlLDLKKQLAVAEGKPPEA 893
Cdd:PLN02610 631 KAAAEreidVSR-LDIRVGLIVKAEKHPDA 659
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
264-813 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: 647.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 264 RNVLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADI 343
Cdd:COG0143    1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 344 YRWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGK 423
Cdd:COG0143   80 FEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 424 LINAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLgRTLPgsDWTPNARFITRSWLRDGLKPRCITRDLKWGT 503
Cdd:COG0143  160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWI-EENP--DIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 504 PVPleGFEDKVFYVWFDATIGYLSITANYTDQ------WERWWKNPEqVDLYQFMAKDNVPFHGIVFPCSALGAedNYTL 577
Cdd:COG0143  237 PVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAPD-TELVHFIGKDIIRFHAIIWPAMLMAA--GLPL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 578 VSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRA 657
Cdd:COG0143  312 PKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRT 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 658 GMFVSKFFGGYVPEM-VLNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKgsEADRQ 736
Cdd:COG0143  391 LSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAK--DEDPE 468
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544470873 737 RAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSIllTNFLCTLPAGHQIGTVSPLFQKLENDQIESL 813
Cdd:COG0143  469 RLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTW--EDAGWPLPAGHKIGKPEPLFPRIEDEQIEAL 543
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
266-806 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: 585.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  266 VLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADIYR 345
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  346 WFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLI 425
Cdd:TIGR00398  80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  426 NAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRTLPGSDWTPNARFITRSWLRDGLKPRCITRDLK-WGTP 504
Cdd:TIGR00398 160 EPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVyWGIP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  505 VPLEgfEDKVFYVWFDATIGYLS---ITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHGIVFPCSALGAEdnYTLVSHL 581
Cdd:TIGR00398 240 VPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLG--LPLPTQV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  582 IATEYLNYEDGKFSKSRGVGVFGDMAQDtGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMFV 661
Cdd:TIGR00398 316 FSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  662 SKFFGGYVP-EMVLNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGSEADRQragt 740
Cdd:TIGR00398 395 KKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKE---- 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544470873  741 VTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPppacsiLLTNFLCTLPAGHQIGTVSPLFQKLE 806
Cdd:TIGR00398 471 LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE------LEWDFKLKLLEGHKLNKAEPLFSKIE 530
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
266-657 0e+00

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 561.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  266 VLITSALPYVNNVPHLGNIIGcVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADIYR 345
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLYS-YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  346 WFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLI 425
Cdd:pfam09334  80 KFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  426 NAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRTLPGsdWTPNARFITRSWLRDGLKPRCITRDLKWGTPV 505
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNPE--WPENVKNMVLEWLKEGLKDRAISRDLDWGIPV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  506 PleGFEDKVFYVWFDATIGYLSITANYTDQ---WERWWKNPEQVDLYQFMAKDNVPFHGIVFPCSALGAedNYTLVSHLI 582
Cdd:pfam09334 238 P--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGA--GYRLPTTVF 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544470873  583 ATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRA 657
Cdd:pfam09334 314 AHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
265-633 8.85e-170

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: 495.51  E-value: 8.85e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 265 NVLITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADIY 344
Cdd:cd00814    1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 345 RWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLadrfvegvcpfcgyeeargdqcdkcgkl 424
Cdd:cd00814   80 KWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL---------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 425 inavelkkpqckvcrscPVVQSTHHLFLDLPKLEKRLEEWLGRTlPGSDWTPNARFITRSWLRDGLKPRCITRDL-KWGT 503
Cdd:cd00814  132 -----------------PEWREEEHYFFRLSKFQDRLLEWLEKN-PDFIWPENARNEVLSWLKEGLKDLSITRDLfDWGI 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 504 PVPLegFEDKVFYVWFDATIGYLSITANYTDQWER-WWKNPEQVDLYQFMAKDNVPFHGIVFPCSALGAedNYTLVSHLI 582
Cdd:cd00814  194 PVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGA--GLPLPTRIV 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544470873 583 ATEYLNYEDGKFSKSRGVGVFGDMAQDTGiPADIWRFYLLYIRPEGQDSAF 633
Cdd:cd00814  270 AHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEGKDSDF 319
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
77-179 3.94e-46

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: 160.36  E-value: 3.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  77 QDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLaGETESLADIVLWGALYPLL 156
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79
                         90       100
                 ....*....|....*....|...
gi 544470873 157 QDPAYLPEELSALHSWFQTLSTQ 179
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
GST_N_5 pfam18485
Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing ...
1-74 5.41e-29

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: 110.56  E-value: 5.41e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544470873    1 MRLFVSEGAPGCLPVLAAAGRARGRAELLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSG 74
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 ...
847-899 4.74e-17

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 75.84  E-value: 4.74e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 544470873   847 DEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLAVAEGKP--PEAPKGKKK 899
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDykPGAPPGDTP 56
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
47-187 6.36e-13

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 68.38  E-value: 6.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  47 KVPVLQlDSGNYLFSTSAICRYF--------FLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQG--KKGEDVLGS 116
Cdd:COG0625   52 KVPVLV-DDGLVLTESLAILEYLaerypeppLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpAAIARARAE 130
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544470873 117 VRRALTHIDHSLSRQncPFLAGETESLADIVLWGALYPLLQDPAYLpEELSALHSWFQTLSTQEPCQRAAE 187
Cdd:COG0625  131 LARLLAVLEARLAGG--PYLAGDRFSIADIALAPVLRRLDRLGLDL-ADYPNLAAWLARLAARPAFQRALA 198
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
111-180 3.82e-05

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 43.04  E-value: 3.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544470873  111 EDVLGSVRRALTHIDHSLSrqNCPFLAGETESLADIVLWGAL-YPLLQDPAYLPEELSALHSWFQTLSTQE 180
Cdd:pfam00043  25 DEALEKVARVLSALEEVLK--GQTYLVGDKLTLADIALAPALlWLYELDPACLREKFPNLKAWFERVAARP 93
PLN02395 PLN02395
glutathione S-transferase
47-179 5.89e-03

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 39.08  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  47 KVPVLQldSGNY-LFSTSAICRYF----------FLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKG----E 111
Cdd:PLN02395  52 VVPVIV--DGDYkIFESRAIMRYYaekyrsqgpdLLGKTIEERGQVEQWLDVEATSYHPPLLNLTLHILFASKMGfpadE 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544470873 112 DVLGSVRRALTHI----DHSLSRQNcpFLAGETESLADIV-------LWGALypllqDPAYLPEELSALHSWFQTLSTQ 179
Cdd:PLN02395 130 KVIKESEEKLAKVldvyEARLSKSK--YLAGDFVSLADLAhlpfteyLVGPI-----GKAYLIKDRKHVSAWWDDISSR 201
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
251-893 0e+00

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 859.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 251 RPQQNPVLPVTGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQ 330
Cdd:PLN02610   4 EGKSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 331 EICDKYHIIHADIYRWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPF--C 408
Cdd:PLN02610  84 EICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 409 GYEEARGDQCDKCGKLINAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRTLPGSDWTPNARFITRSWLRD 488
Cdd:PLN02610 164 NYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRD 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 489 GLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHGIVFPCSA 568
Cdd:PLN02610 244 GLKPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTL 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 569 LGAEDNYTLVSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLN 648
Cdd:PLN02610 324 LGTGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLN 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 649 NLGNFINRAGMFVSK----FFGGYVPEMV---LNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQV 721
Cdd:PLN02610 404 NLGNFINRVLSFIAKppgaGYGSVIPDAPgaeSHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQE 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 722 NEPWKRIKgseADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSilltnfLCT------------- 788
Cdd:PLN02610 484 SQFWKLYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLS------LSDekgevarakrpwe 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 789 -LPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPTVIETVTTAGPQQIQALMDEVTKQGnivrELKAQKADKN 867
Cdd:PLN02610 555 lVPAGHKIGTPEPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLAKQLKKKALSDGGKKKQ----GKKAGGGGKS 630
                        650       660       670
                 ....*....|....*....|....*....|
gi 544470873 868 QVAAE----VAKlLDLKKQLAVAEGKPPEA 893
Cdd:PLN02610 631 KAAAEreidVSR-LDIRVGLIVKAEKHPDA 659
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
264-813 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: 647.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 264 RNVLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADI 343
Cdd:COG0143    1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 344 YRWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGK 423
Cdd:COG0143   80 FEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 424 LINAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLgRTLPgsDWTPNARFITRSWLRDGLKPRCITRDLKWGT 503
Cdd:COG0143  160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWI-EENP--DIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 504 PVPleGFEDKVFYVWFDATIGYLSITANYTDQ------WERWWKNPEqVDLYQFMAKDNVPFHGIVFPCSALGAedNYTL 577
Cdd:COG0143  237 PVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAPD-TELVHFIGKDIIRFHAIIWPAMLMAA--GLPL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 578 VSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRA 657
Cdd:COG0143  312 PKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRT 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 658 GMFVSKFFGGYVPEM-VLNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKgsEADRQ 736
Cdd:COG0143  391 LSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAK--DEDPE 468
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544470873 737 RAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSIllTNFLCTLPAGHQIGTVSPLFQKLENDQIESL 813
Cdd:COG0143  469 RLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTW--EDAGWPLPAGHKIGKPEPLFPRIEDEQIEAL 543
metG PRK00133
methionyl-tRNA synthetase; Reviewed
264-850 0e+00

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 635.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 264 RNVLITSALPYVNNVPHLGNIIGcVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADI 343
Cdd:PRK00133   2 RKILVTCALPYANGPIHLGHLVE-YIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 344 YRWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGK 423
Cdd:PRK00133  81 FAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 424 LINAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRTLpgsDWTPNARFITRSWLRDGLKPRCITRDLKW-G 502
Cdd:PRK00133 161 TYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRSG---ELQPNVANKMKEWLEEGLQDWDISRDAPYfG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 503 TPVPleGFEDKVFYVWFDATIGYLSITANYTDQ-----WERWWKNPEQVDLYQFMAKDNVPFHGIVFPCSALGAedNYTL 577
Cdd:PRK00133 238 FEIP--GAPGKVFYVWLDAPIGYISSTKNLCDKrggldWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGA--GYRL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 578 VSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEG-QDSAFSWTDLLLKNNSELLNNLGNFINR 656
Cdd:PRK00133 314 PTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDH-LDPDYLRYYLAAKLPETiDDLDFNWEDFQQRVNSELVGKVVNFASR 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 657 AGMFVSKFFGGYVPEMVLNPDdqrLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKgseADRQ 736
Cdd:PRK00133 393 TAGFINKRFDGKLPDALADPE---LLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAK---QDGE 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 737 RAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPpacsiLLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQR 816
Cdd:PRK00133 467 RLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEE-----LTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIEA 541
                        570       580       590
                 ....*....|....*....|....*....|....
gi 544470873 817 FGGGQAKTSPKPtvietvTTAGPQQIQALMDEVT 850
Cdd:PRK00133 542 SKEAAAAKAAAA------AAAAPLAEEPIAETIS 569
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
266-806 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: 585.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  266 VLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADIYR 345
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  346 WFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLI 425
Cdd:TIGR00398  80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  426 NAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRTLPGSDWTPNARFITRSWLRDGLKPRCITRDLK-WGTP 504
Cdd:TIGR00398 160 EPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVyWGIP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  505 VPLEgfEDKVFYVWFDATIGYLS---ITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHGIVFPCSALGAEdnYTLVSHL 581
Cdd:TIGR00398 240 VPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLG--LPLPTQV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  582 IATEYLNYEDGKFSKSRGVGVFGDMAQDtGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMFV 661
Cdd:TIGR00398 316 FSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  662 SKFFGGYVP-EMVLNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGSEADRQragt 740
Cdd:TIGR00398 395 KKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKE---- 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544470873  741 VTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPppacsiLLTNFLCTLPAGHQIGTVSPLFQKLE 806
Cdd:TIGR00398 471 LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE------LEWDFKLKLLEGHKLNKAEPLFSKIE 530
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
266-657 0e+00

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 561.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  266 VLITSALPYVNNVPHLGNIIGcVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADIYR 345
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLYS-YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  346 WFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLI 425
Cdd:pfam09334  80 KFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  426 NAVELKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRTLPGsdWTPNARFITRSWLRDGLKPRCITRDLKWGTPV 505
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNPE--WPENVKNMVLEWLKEGLKDRAISRDLDWGIPV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  506 PleGFEDKVFYVWFDATIGYLSITANYTDQ---WERWWKNPEQVDLYQFMAKDNVPFHGIVFPCSALGAedNYTLVSHLI 582
Cdd:pfam09334 238 P--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGA--GYRLPTTVF 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544470873  583 ATEYLNYEDGKFSKSRGVGVFGDMAQDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRA 657
Cdd:pfam09334 314 AHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
265-633 8.85e-170

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: 495.51  E-value: 8.85e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 265 NVLITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADIY 344
Cdd:cd00814    1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 345 RWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLadrfvegvcpfcgyeeargdqcdkcgkl 424
Cdd:cd00814   80 KWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL---------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 425 inavelkkpqckvcrscPVVQSTHHLFLDLPKLEKRLEEWLGRTlPGSDWTPNARFITRSWLRDGLKPRCITRDL-KWGT 503
Cdd:cd00814  132 -----------------PEWREEEHYFFRLSKFQDRLLEWLEKN-PDFIWPENARNEVLSWLKEGLKDLSITRDLfDWGI 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 504 PVPLegFEDKVFYVWFDATIGYLSITANYTDQWER-WWKNPEQVDLYQFMAKDNVPFHGIVFPCSALGAedNYTLVSHLI 582
Cdd:cd00814  194 PVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGA--GLPLPTRIV 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544470873 583 ATEYLNYEDGKFSKSRGVGVFGDMAQDTGiPADIWRFYLLYIRPEGQDSAF 633
Cdd:cd00814  270 AHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEGKDSDF 319
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
268-806 3.34e-95

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 308.73  E-value: 3.34e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 268 ITSALPYVNNVPHLGNIiGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHADIYRWF 347
Cdd:PRK11893   5 ITTPIYYPNGKPHIGHA-YTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEAL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 348 NISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFvegvcpfcgyeeargdqcdkcgkLINa 427
Cdd:PRK11893  84 NISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESE-----------------------LIE- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 428 velKKPQCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRtlpGSDW-TPNARF-ITRSWLRDGLKPRCITR-DLKWGTP 504
Cdd:PRK11893 140 ---DGYRCPPTGAPVEWVEEESYFFRLSKYQDKLLELYEA---NPDFiQPASRRnEVISFVKSGLKDLSISRtNFDWGIP 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 505 VPleGFEDKVFYVWFDATIGYLS------ITANYTDQWERWWknpeQVDLyQFMAKDNVPFHGIVFP--CSALGaednYT 576
Cdd:PRK11893 214 VP--GDPKHVIYVWFDALTNYLTalgypdDEELLAELFNKYW----PADV-HLIGKDILRFHAVYWPafLMAAG----LP 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 577 LVSHLIATEYLNYEDGKFSKSRG--VGVFgDMAQDTGipADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFI 654
Cdd:PRK11893 283 LPKRVFAHGFLTLDGEKMSKSLGnvIDPF-DLVDEYG--VDAVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNLA 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 655 NRAGMFVSKFFGGYVPEM-VLNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKgseA 733
Cdd:PRK11893 360 QRTLSMIAKNFDGKVPEPgALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAK---T 436
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544470873 734 DRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQIGTVSPLFQKLE 806
Cdd:PRK11893 437 DPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEEDENRDFAALSWGRLAPGTTLPKPEPIFPRLE 509
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
268-833 1.90e-84

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 284.00  E-value: 1.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 268 ITSALPYVNNVPHLGN----IIgcvlsADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKyhiIHADI 343
Cdd:PRK12267   8 ITTPIYYPNGKPHIGHayttIA-----ADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDE---ISAGF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 344 YR-W--FNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARF-----LADrfvEGVCPFCGYEearg 415
Cdd:PRK12267  80 KElWkkLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFftesqLVD---GGKCPDCGRE---- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 416 dqcdkcgklinaVELKKPQckvcrscpvvqsthHLFLDLPKLEKRLEEWLgrtlpgsdwTPNARFI---------TRSWL 486
Cdd:PRK12267 153 ------------VELVKEE--------------SYFFRMSKYQDRLLEYY---------EENPDFIqpesrknemINNFI 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 487 RDGLKPRCITRD-LKWGTPVPlegFEDK-VFYVWFDATIGYlsITA-NY----TDQWERWWknPEQVdlyQFMAKDNVPF 559
Cdd:PRK12267 198 KPGLEDLSISRTsFDWGIPVP---FDPKhVVYVWIDALLNY--ITAlGYgsddDELFKKFW--PADV---HLVGKDILRF 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 560 HGIVFPC--SALGAEdnytLVSHLIATEYLNYEDGKFSKSRGVGVFG-DMAQDTGIpaDIWRFYLLYIRPEGQDSAFSWT 636
Cdd:PRK12267 268 HAIYWPImlMALGLP----LPKKVFAHGWWLMKDGKMSKSKGNVVDPeELVDRYGL--DALRYYLLREVPFGSDGDFSPE 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 637 DLLLKNNSELLNNLGNFINRA-GMfVSKFFGGYVPEM-VLNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRH 714
Cdd:PRK12267 342 ALVERINSDLANDLGNLLNRTvAM-INKYFDGEIPAPgNVTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISR 420
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 715 GNQYIQVNEPWKRIKgSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQ 794
Cdd:PRK12267 421 ANKYIDETAPWVLAK-DEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLGLEEELTSWESLLEWGGLPAGTK 499
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|
gi 544470873 795 IGTVSPLFQKLENDQ-IESLRQRFGGGQAKTSPKPTVIET 833
Cdd:PRK12267 500 VAKGEPLFPRIDVEEeIAYIKEQMEGSAPKEPEEKEKKPE 539
Anticodon_Ia_Met cd07957
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ...
642-771 2.14e-46

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: 161.89  E-value: 2.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 642 NNSELLNNLGNFINRAGMFVSKFFGGYVPEM-VLNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQ 720
Cdd:cd07957    1 INSELANNLGNLVNRTLNMASKYFGGVVPEFgGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544470873 721 VNEPWKRIKgsEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQL 771
Cdd:cd07957   81 ETAPWKLAK--EEDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
77-179 3.94e-46

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: 160.36  E-value: 3.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  77 QDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLaGETESLADIVLWGALYPLL 156
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79
                         90       100
                 ....*....|....*....|...
gi 544470873 157 QDPAYLPEELSALHSWFQTLSTQ 179
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
PLN02224 PLN02224
methionine-tRNA ligase
262-836 3.17e-38

methionine-tRNA ligase


Pssm-ID: 177869 [Multi-domain]  Cd Length: 616  Bit Score: 151.79  E-value: 3.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 262 GERNVLiTSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKYHIIHA 341
Cdd:PLN02224  68 ADTFVL-TTPLYYVNAPPHMGSAY-TTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYR 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 342 DIYRWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADR-FVEGVCpfcgyeeargdqcdk 420
Cdd:PLN02224 146 TLWKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKeLLENNC--------------- 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 421 cgklinavelkkpqCKVCRSCPVVQSTHHLFLDLPKLEKRLEEWLGRtlpgsdwtpNARFI--------TRSWLRDGLKP 492
Cdd:PLN02224 211 --------------CPVHQMPCVARKEDNYFFALSKYQKPLEDILAQ---------NPRFVqpsyrlneVQSWIKSGLRD 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 493 RCITRDL-KWGTPVPLEgfEDKVFYVWFDATIGYLSITANYTDQwerwwKNPEQVDLY------QFMAKDNVPFHGIVFP 565
Cdd:PLN02224 268 FSISRALvDWGIPVPDD--DKQTIYVWFDALLGYISALTEDNKQ-----QNLETAVSFgwpaslHLIGKDILRFHAVYWP 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 566 CSALGAedNYTLVSHLIATEYLNYEDGKFSKSRGVGVFG-DMAQDTGipADIWRFYLLYIRPEGQDSAFSWTDLLLKNNS 644
Cdd:PLN02224 341 AMLMSA--GLELPKMVFGHGFLTKDGMKMGKSLGNTLEPfELVQKFG--PDAVRYFFLREVEFGNDGDYSEDRFIKIVNA 416
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 645 ELLNNLGNFINRA-GMFVSKFFGGYVPEMVLNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNE 723
Cdd:PLN02224 417 HLANTIGNLLNRTlGLLKKNCESTLVEDSTVAAEGVPLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNTYMDQRA 496
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 724 PWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPAC-SILLTNF-LCTLPAGHQIGTVSPL 801
Cdd:PLN02224 497 PWFLFKQGGVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQLGYSEDQFnSITWSDTkWGGLKGGQVMEQASPV 576
                        570       580       590
                 ....*....|....*....|....*....|....*.
gi 544470873 802 FQKLE-NDQIESLRQRFGGGQAKTSPKPTVIETVTT 836
Cdd:PLN02224 577 FARIElNPEKEEDEKKPKVGKKTGKAKVKVVEQTPT 612
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
267-630 7.09e-33

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: 129.46  E-value: 7.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 267 LITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGL-------------TPQEIC 333
Cdd:cd00668    3 YVTTPPPYANGSLHLGHALTHII-ADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEFV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 334 DKYHIIHADIYRWFNISFDT--FGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEqlrcehcarfladrfvegvcpfcgye 411
Cdd:cd00668   82 EEMSGEHKEDFRRLGISYDWsdEYITTEPEYSKAVELIFSRLYEKGLIYRGTHP-------------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 412 eargdqcdkcgklinavelkkpqckvcrscpvVQSTHHLFLDLPKLEKRLEEWLGRTlpgsDWTPN---ARFitRSWLRD 488
Cdd:cd00668  136 --------------------------------VRITEQWFFDMPKFKEKLLKALRRG----KIVPEhvkNRM--EAWLES 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 489 GLKpRCITRDLKWGTPVPlegfeDKVFYVWFDATIGYLSITANYTDqwERWWKNPEQVDLYqFMAKDNVPFHGIVFPCS- 567
Cdd:cd00668  178 LLD-WAISRQRYWGTPLP-----EDVFDVWFDSGIGPLGSLGYPEE--KEWFKDSYPADWH-LIGKDILRGWANFWITMl 248
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544470873 568 -ALGAEDNYtlvSHLIATEYLNYEDG-KFSKSRG-VGVFGDMAQDTGipADIWRFYLLYIRPEGQD 630
Cdd:cd00668  249 vALFGEIPP---KNLLVHGFVLDEGGqKMSKSKGnVIDPSDVVEKYG--ADALRYYLTSLAPYGDD 309
GST_N_5 pfam18485
Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing ...
1-74 5.41e-29

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: 110.56  E-value: 5.41e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544470873    1 MRLFVSEGAPGCLPVLAAAGRARGRAELLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSG 74
Cdd:pfam18485   1 MKLFVSEGNPHCLKVLAAAEATGVKCDVQVQFVNHEEKVVPFLTRPVLPTLELDSGQFLFSPNAICRYLFELSG 74
MetRS_RNA cd00939
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ...
845-889 2.90e-19

MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 81.75  E-value: 2.90e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 544470873 845 LMDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLAVAEGK 889
Cdd:cd00939    1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
WHEP-TRS pfam00458
WHEP-TRS domain;
845-895 4.47e-18

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 78.69  E-value: 4.47e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 544470873  845 LMDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLAVAEGKPPEAPK 895
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGA 51
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
847-899 4.74e-17

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 75.84  E-value: 4.74e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 544470873   847 DEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLAVAEGKP--PEAPKGKKK 899
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDykPGAPPGDTP 56
Anticodon_3 pfam19303
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ...
676-822 6.99e-16

Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ligase. The domain binds to the anticodon of the tRNA ligase.


Pssm-ID: 437135 [Multi-domain]  Cd Length: 152  Bit Score: 75.62  E-value: 6.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  676 PDDQRLLAHVTLELQHYHQLLEKVRIRDA---LRSILTIsrhGNQYIQVNEPWKRIKgseADRQRAGTVTGLAVNIAALL 752
Cdd:pfam19303   9 EAEAALIADLTTRLAAYEGHMEAMEVRKAaaeLRAIWVA---GNEYLQEAAPWTTFK---TDPEAAAAQVRLALNLIRLY 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544470873  753 SVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQIgTVSP-LFQKLENDQIESLRQRFGGGQA 822
Cdd:pfam19303  83 AVLSAPFIPDAAAAMLAAMGTDDAAWPDDVAAALTALPAGHAF-TVPEvLFAKITDEQREEWQERFAGTRA 152
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
846-887 9.73e-14

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: 66.02  E-value: 9.73e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 544470873 846 MDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLAVAE 887
Cdd:cd01200    1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
47-187 6.36e-13

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 68.38  E-value: 6.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  47 KVPVLQlDSGNYLFSTSAICRYF--------FLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQG--KKGEDVLGS 116
Cdd:COG0625   52 KVPVLV-DDGLVLTESLAILEYLaerypeppLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpAAIARARAE 130
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544470873 117 VRRALTHIDHSLSRQncPFLAGETESLADIVLWGALYPLLQDPAYLpEELSALHSWFQTLSTQEPCQRAAE 187
Cdd:COG0625  131 LARLLAVLEARLAGG--PYLAGDRFSIADIALAPVLRRLDRLGLDL-ADYPNLAAWLARLAARPAFQRALA 198
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
451-785 8.46e-13

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: 72.40  E-value: 8.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  451 FLDLPKLEKRLEEWLGRTLPgsDWTPNaRFITR--SWLRDgLKPRCITRDLKWGTPVP---------------------- 506
Cdd:TIGR00422 359 FVKVEKLADKALEAAEEGEI--KFVPK-RMEKRylNWLRN-IKDWCISRQLIWGHRIPvwyckecgevyvakeeplpddk 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  507 --------LEGFEDkVFYVWFDATIGYLSITAnytdqwerwWKNpEQVDLYQFMAKDNVPF-HGIVFPCSAlgaednYTL 577
Cdd:TIGR00422 435 tntgpsveLEQDTD-VLDTWFSSSLWPFSTLG---------WPD-ETKDLKKFYPTDLLVTgYDIIFFWVA------RMI 497
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  578 VSHLIATEYLNY-----------EDG-KFSKSRGVGVFG-DMAQDTGipADIWRFYLLYIRPEGQDSAFSWTDllLKNNS 644
Cdd:TIGR00422 498 FRSLALTGQVPFkevyihglvrdEQGrKMSKSLGNVIDPlDVIEKYG--ADALRFTLASLVTPGDDINFDWKR--VESAR 573
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  645 ELLNNLGNfinrAGMFVSKFFGGYV----PEMVLNPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHG--NQY 718
Cdd:TIGR00422 574 NFLNKLWN----ASRFVLMNLSDDLelsgGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALYEFIWNDfcDWY 649
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544470873  719 IQVNEPwkRIKGSEADRQRAGTVTGLAVNIAALlsVMLQPYMPTVSATIqAQlQLPPPACSILLTNF 785
Cdd:TIGR00422 650 IELVKY--RLYNGNEAEKKAARDTLYYVLDKAL--RLLHPFMPFITEEI-WQ-HFKEGADSIMLQSY 710
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
104-179 2.69e-11

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: 60.40  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 104 VVQGKKGEDVLGSV-----RRALTHIDHSLSRQNCpFLAGETESLADIVLWGALYPLLQDPAYL-PEELSALHSWFQTLS 177
Cdd:cd10289    2 AAQVDQWLDLAGSLlkgkeLEALLKSLNSYLASRT-FLVGYSLTLADVAVFSALYPSGQKLSDKeKKKFPHVTRWFNHIQ 80

                 ..
gi 544470873 178 TQ 179
Cdd:cd10289   81 NL 82
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
845-891 1.92e-10

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 56.86  E-value: 1.92e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 544470873 845 LMDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLK---KQLAVAEGKPP 891
Cdd:cd00936    1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKadyKEATGQDYKPG 50
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
273-526 1.54e-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: 60.72  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 273 PYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETK----AMEEGLTPQ--------EIC----DKY 336
Cdd:cd00817   10 PNVTGSLHMGHALNNTI-QDIIARYKRMKGYNVLWPPGTDHAGIATQVVvekkLGIEGKTRHdlgreeflEKCwewkEES 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 337 H--IIHADIYRWFNISFDTFGRTTTAQQTKITQDIFQRLLTRGFVLQDTVEQLRCEHCARFLADRFVegvcpfcgyeear 414
Cdd:cd00817   89 GgkIREQLKRLGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV------------- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 415 gdqCDKCGKLInavE-LKKPQckvcrscpvvqsthhLFLDLPKLEKRLEEWLGRTLPgsDWTPnARFITR--SWLrDGLK 491
Cdd:cd00817  156 ---CSRSGDVI---EpLLKPQ---------------WFVKVKDLAKKALEAVKEGDI--KFVP-ERMEKRyeNWL-ENIR 210
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 544470873 492 PRCITRDLKWGTPVPlegfedkvfyVWFDATIGYL 526
Cdd:cd00817  211 DWCISRQLWWGHRIP----------AWYCKDGGHW 235
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
844-883 2.17e-09

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 53.63  E-value: 2.17e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 544470873 844 ALMDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQL 883
Cdd:cd00938    2 KLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQL 41
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
83-186 3.31e-09

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: 55.36  E-value: 3.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  83 QWLEWEATELQPALSAALYYLVVQGKKGED---VLGSVRRALTHI---DHSLSRQncPFLAGETESLADIVLWGALYPLL 156
Cdd:cd03180    8 RWMDWQTSTLNPAFRYAFWGLVRTPPEQRDpaaIAASLAACNKLMailDAQLARQ--AYLAGDRFTLADIALGCSVYRWL 85
                         90       100       110
                 ....*....|....*....|....*....|
gi 544470873 157 QDPAYLPeELSALHSWFQTLStqepcQRAA 186
Cdd:cd03180   86 ELPIERP-ALPHLERWYARLS-----QRPA 109
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
268-635 2.91e-08

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: 56.49  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 268 ITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEIcDKYHI--IHADIYR 345
Cdd:cd00812    4 ILVMFPYPSGALHVGHVRTYTI-GDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDW-TEYNIkkMKEQLKR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 346 wFNISFDtFGR---TTTAQQTKITQDIFQRLltrgfvlqdtveqlrcehcarfladrfvegvcPFCGYeeargdqCDKCG 422
Cdd:cd00812   82 -MGFSYD-WRReftTCDPEYYKFTQWLFLKL--------------------------------YEKGL-------AYKKE 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 423 KLINavelkkpQCKVCRscpvvqsthHLFLDL------PKLEKRLEEWLGrtlpgsdWTPNARFITRSWLRdglkprcIT 496
Cdd:cd00812  121 APVN-------WCKLLD---------QWFLKYsetewkEKLLKDLEKLDG-------WPEEVRAMQENWIG-------CS 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873 497 RDLKWGTPVPlegFEDkVFYVWFDATIGYLSIT-ANYTDQ--WERWWKNPEQ------VDLYqFMAKDNVP--------F 559
Cdd:cd00812  171 RQRYWGTPIP---WTD-TMESLSDSTWYYARYTdAHNLEQpyEGDLEFDREEfeywypVDIY-IGGKEHAPnhllysrfN 245
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544470873 560 HGIVFPCSALGAEdnytLVSHLIATEYLNYEDGKFSKSRGVGV-FGDMAQDTGipADIWRFYLLYIRPegQDSAFSW 635
Cdd:cd00812  246 HKALFDEGLVTDE----PPKGLIVQGMVLLEGEKMSKSKGNVVtPDEAIKKYG--ADAARLYILFAAP--PDADFDW 314
PLN02734 PLN02734
glycyl-tRNA synthetase
840-896 2.18e-07

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 54.75  E-value: 2.18e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 544470873 840 QQIQALMDEVTKQGNIVRELKAQKADKNQVAAEVAKLLDLKKQLAVAEgKPPEAPKG 896
Cdd:PLN02734   7 DALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALE-KELQAAVG 62
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
81-176 3.10e-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: 46.34  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  81 TNQWLEWEATELQPALSAALYY----LVVQGKKGEDVLGSVRRALTHIDHSLSRQncPFLAGETESLADIVLWGALY--P 154
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLekvpLPKDEAAVEAAREELPALLAALEQLLAGR--PYLAGDQFSLADVALAPVLArlE 78
                         90       100
                 ....*....|....*....|..
gi 544470873 155 LLQDPAYLPEELSALHSWFQTL 176
Cdd:cd00299   79 ALGPYYDLLDEYPRLKAWYDRL 100
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
81-150 3.45e-06

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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.


Pssm-ID: 198288 [Multi-domain]  Cd Length: 110  Bit Score: 46.47  E-value: 3.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544470873  81 TNQWLEWEATELQPALSAALYYLVVQGKKG----EDVLGSVRRALTHIDHSLSRQncPFLAGETESLADIVLWG 150
Cdd:cd03178    5 VLQWLFFQMSGLGPMFGQAGHFLYFAPEKIpyaiERYTDEVKRLYGVLDKRLSDR--PYLAGEEYSIADIALYP 76
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
83-180 1.42e-05

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: 45.24  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  83 QWLEWEATELQPALSAALYYLVvqGKKG------EDVLGSVRRALTHIDHSLsrQNCPFLAGETESLADIVLWGALYPLL 156
Cdd:cd03181    7 QWISFANSELLPAAATWVLPLL--GIAPynkkavDKAKEDLKRALGVLEEHL--LTRTYLVGERITLADIFVASALLRGF 82
                         90       100
                 ....*....|....*....|....*..
gi 544470873 157 Q---DPAYLpEELSALHSWFQTLSTQE 180
Cdd:cd03181   83 EtvlDPEFR-KKYPNVTRWFNTVVNQP 108
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
111-180 3.82e-05

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 43.04  E-value: 3.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544470873  111 EDVLGSVRRALTHIDHSLSrqNCPFLAGETESLADIVLWGAL-YPLLQDPAYLPEELSALHSWFQTLSTQE 180
Cdd:pfam00043  25 DEALEKVARVLSALEEVLK--GQTYLVGDKLTLADIALAPALlWLYELDPACLREKFPNLKAWFERVAARP 93
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
116-177 1.09e-03

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 39.61  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544470873 116 SVRRALTHIDHSLSRQncPFLAGETESLADIVLWGAL---YPLLQDPaylPEELSALHSWFQTLS 177
Cdd:cd03182   52 RVIDFLPVLDKRLAES--PYVAGDRFSIADITAFVALdfaKNLKLPV---PEELTALRRWYERMA 111
GST_C_ValRS_N cd10294
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ...
77-179 1.23e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Valyl-tRNA synthetase (ValRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of human ValRS and its homologs from other vertebrates such as frog and zebrafish. 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. They typically form large stable complexes with other proteins. 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. The GST_C-like domain of ValRS 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. ValRSs from prokaryotes and lower eukaryotes, such as fungi and plants, do not appear to contain this GST_C-like domain.


Pssm-ID: 198327 [Multi-domain]  Cd Length: 123  Bit Score: 39.82  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  77 QDDLTNQWLEWEATELQPALSAALYYLV----VQGKKGEDVLGSVRRALTHIDHSLSRQNcpFLAGETESLADIVLWGAL 152
Cdd:cd10294    1 ACALVWQWVSFADNELTPAACAAAFPLLglsgSDKQNQQRSLAELQRVLKVLDCYLKLRT--YLVGEAITLADIAVACAL 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 544470873 153 ---YPLLQDPAyLPEELSALHSWFQTLSTQ 179
Cdd:cd10294   79 llpFKYVLDPA-RRESLLNVTRWFLTCVNQ 107
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
83-174 2.62e-03

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: 38.38  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  83 QWLEWEATELQPALSAALY---YLVVQGKKG--EDVLGSVRRALTHIDHSLSRQncPFLAGETESLADIVL-----WGAL 152
Cdd:cd03188    8 EWLNFIASELHKAFGPLFYparWADDALAEEvkAAARERLERRLAYLDAQLAGG--PYLLGDQFSVADAYLfvvlrWARA 85
                         90       100
                 ....*....|....*....|..
gi 544470873 153 YPLlqDPAYLPeelsALHSWFQ 174
Cdd:cd03188   86 VGL--DLSDWP----HLAAYLA 101
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
273-336 3.13e-03

catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173901 [Multi-domain]  Cd Length: 143  Bit Score: 39.00  E-value: 3.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544470873 273 PYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKAMEEGLTPQEICDKY 336
Cdd:cd00802    6 ITPNGYLHIGHLRTIVT-FDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERW 68
PLN02395 PLN02395
glutathione S-transferase
47-179 5.89e-03

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 39.08  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  47 KVPVLQldSGNY-LFSTSAICRYF----------FLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKG----E 111
Cdd:PLN02395  52 VVPVIV--DGDYkIFESRAIMRYYaekyrsqgpdLLGKTIEERGQVEQWLDVEATSYHPPLLNLTLHILFASKMGfpadE 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544470873 112 DVLGSVRRALTHI----DHSLSRQNcpFLAGETESLADIV-------LWGALypllqDPAYLPEELSALHSWFQTLSTQ 179
Cdd:PLN02395 130 KVIKESEEKLAKVldvyEARLSKSK--YLAGDFVSLADLAhlpfteyLVGPI-----GKAYLIKDRKHVSAWWDDISSR 201
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
83-164 6.39e-03

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: 36.89  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  83 QWLEWEATELQPAL----SAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQncPFLAGETESLADiVLWGALYPLLQD 158
Cdd:cd03207    3 RWLFFAAGTVEPPLlnkaLGRFFEPPWGEPAIAAAYGDLDERLAALEAALAGR--PYLVGERFSAAD-LLLASVLRWARA 79

                 ....*.
gi 544470873 159 PAYLPE 164
Cdd:cd03207   80 FGLLPE 85
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
273-321 6.94e-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: 40.09  E-value: 6.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 544470873  273 PYVNNVPHLGNIIGCVLSaDVFARYSRLRQWNTLYLCGTDEYGTATETK 321
Cdd:pfam00133  32 PNATGSLHIGHALAKTLK-DIVIRYKRMKGYYVLWVPGWDHHGLPTEQV 79
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
111-174 8.10e-03

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 35.76  E-value: 8.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544470873  111 EDVLGSVRRALTHIDHSLSRQncPFLAGETESLADIVLWGALYPLLQDPAYLP--EELSALHSWFQ 174
Cdd:pfam13410   3 ERAREQLRAALDALEARLADG--PGLLGDRPTLADIALAPVLARLDAAYPGLDlrEGYPRLRAWLE 66
ValS COG0525
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ...
292-332 9.34e-03

Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440291 [Multi-domain]  Cd Length: 877  Bit Score: 39.65  E-value: 9.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 544470873 292 DVFARYSRLRQWNTLYLCGTDEYGTATETK----AMEEGLTPQEI 332
Cdd:COG0525   62 DILIRYKRMQGYNTLWQPGTDHAGIATQAVverqLAEEGKSRHDL 106
GST_C_AIMP3 cd10305
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
80-176 9.37e-03

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: 36.50  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544470873  80 LTNQWLEWEATELQPALSAALyylvvqgkkgedvlgsVRRALTHIDHSLsrQNCPFLAGETESLADIVLWGALYPLLQDP 159
Cdd:cd10305    6 QVDQWLEYRVTQVAPASDKAD----------------AKSLLKELNSYL--QDRTYLVGHKLTLADVVLYYGLHPIMKDL 67
                         90
                 ....*....|....*...
gi 544470873 160 AYLPEE-LSALHSWFQTL 176
Cdd:cd10305   68 SPQEKEqYLNVSRWFDHV 85
 
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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