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Conserved domains on  [gi|284172357|ref|NP_001165053|]
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methionine--tRNA ligase, cytoplasmic isoform 1 [Mus musculus]

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
258-848 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: 877.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 258 PVLPVPGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDK 337
Cdd:PLN02610   9 PKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 338 YHAIHADIYRWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPF--CGYEEA 415
Cdd:PLN02610  89 YHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 416 RGDQCDRCGKLINAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKTVPGSDWTPNARFIIRSWLRDGLKPR 495
Cdd:PLN02610 169 RGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRDGLKPR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 496 CITRDLKWGTPVPLEGFEDKVFYVWFDATIGYVSITANYTDQWEKWWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAED 575
Cdd:PLN02610 249 CITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLGTGE 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 576 NYTLVKHIIATEYLNYEDGKFSKSRGIGVFGDMAKDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNF 655
Cdd:PLN02610 329 NWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNF 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 656 INRAGMFVSK----FFGGCVPEMA---LTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWK 728
Cdd:PLN02610 409 INRVLSFIAKppgaGYGSVIPDAPgaeSHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQFWK 488
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 729 RIKggeMDRQRAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPP---AACRILATSFICT-----LPAGHRIGTV 800
Cdd:PLN02610 489 LYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPeslSLSDEKGEVARAKrpwelVPAGHKIGTP 565
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 284172357 801 SPLFQKLENDQIENLRQRFGGGQLEESLELKAKGSPKPAAVEAVTAAG 848
Cdd:PLN02610 566 EPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLAKQLKKKALS 613
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
77-179 2.74e-41

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: 146.49  E-value: 2.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  77 QDDLTNQWLEWEATELQPVLSAALHCLVVQGKKGEDILGPLRRVLTHIDHSLSRQNCPFLaGDTESLADIVLWGALYPLL 156
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79
                         90       100
                 ....*....|....*....|...
gi 284172357 157 QDPAYLPEELGALQSWFQTLSTQ 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 1.52e-27

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: 106.32  E-value: 1.52e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284172357    1 MRLFVSEGSPGSLPVLAAAARARGRAELLISTVGPEECVVPFLTRPKVPVLQLDSGNYLFSASAICRYFFLLCG 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 ...
855-899 1.70e-18

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


:

Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 79.44  E-value: 1.70e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 284172357 855 LTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 899
Cdd:cd00939    1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
258-848 0e+00

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 877.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 258 PVLPVPGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDK 337
Cdd:PLN02610   9 PKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 338 YHAIHADIYRWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPF--CGYEEA 415
Cdd:PLN02610  89 YHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 416 RGDQCDRCGKLINAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKTVPGSDWTPNARFIIRSWLRDGLKPR 495
Cdd:PLN02610 169 RGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRDGLKPR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 496 CITRDLKWGTPVPLEGFEDKVFYVWFDATIGYVSITANYTDQWEKWWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAED 575
Cdd:PLN02610 249 CITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLGTGE 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 576 NYTLVKHIIATEYLNYEDGKFSKSRGIGVFGDMAKDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNF 655
Cdd:PLN02610 329 NWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNF 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 656 INRAGMFVSK----FFGGCVPEMA---LTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWK 728
Cdd:PLN02610 409 INRVLSFIAKppgaGYGSVIPDAPgaeSHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQFWK 488
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 729 RIKggeMDRQRAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPP---AACRILATSFICT-----LPAGHRIGTV 800
Cdd:PLN02610 489 LYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPeslSLSDEKGEVARAKrpwelVPAGHKIGTP 565
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 284172357 801 SPLFQKLENDQIENLRQRFGGGQLEESLELKAKGSPKPAAVEAVTAAG 848
Cdd:PLN02610 566 EPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLAKQLKKKALS 613
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
266-815 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: 656.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 266 RNVLITSALPYVNNVPHLGNIIgCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADI 345
Cdd:COG0143    1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 346 YRWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPFCGYEEARGDQCDRCGK 425
Cdd:COG0143   80 FEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 426 LINAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLgKTVPgsDWTPNARFIIRSWLRDGLKPRCITRDLKWGT 505
Cdd:COG0143  160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWI-EENP--DIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 506 PVPleGFEDKVFYVWFDATIGYVSITANYTDQ------WEKWWKNPEqVDLYQFMAKDNVPFHGLVFPCSVLGAedNYTL 579
Cdd:COG0143  237 PVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAPD-TELVHFIGKDIIRFHAIIWPAMLMAA--GLPL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 580 VKHIIATEYLNYEDGKFSKSRGIGVFGDMAKDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNFINRA 659
Cdd:COG0143  312 PKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRT 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 660 GMFVSKFFGGCVPEM-ALTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKggEMDRQ 738
Cdd:COG0143  391 LSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAK--DEDPE 468
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 284172357 739 RAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPPAACRILATSFIctLPAGHRIGTVSPLFQKLENDQIENL 815
Cdd:COG0143  469 RLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGWP--LPAGHKIGKPEPLFPRIEDEQIEAL 543
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
268-808 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: 580.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  268 VLITSALPYVNNVPHLGNIIgCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADIYR 347
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  348 WFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPFCGYEEARGDQCDRCGKLI 427
Cdd:TIGR00398  80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  428 NAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKTVPGSDWTPNARFIIRSWLRDGLKPRCITRDLK-WGTP 506
Cdd:TIGR00398 160 EPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVyWGIP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  507 VPLEgfEDKVFYVWFDATIGYVS---ITANYTDQWEKWWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAEdnYTLVKHI 583
Cdd:TIGR00398 240 VPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLG--LPLPTQV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  584 IATEYLNYEDGKFSKSRGIGVFGDMAKDtGIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNFINRAGMFV 663
Cdd:TIGR00398 316 FSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  664 SKFFGGCVP-EMALTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKggemDRQRAGT 742
Cdd:TIGR00398 395 KKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFK----QSPRLKE 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284172357  743 VTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPpaacriLATSFICTLPAGHRIGTVSPLFQKLE 808
Cdd:TIGR00398 471 LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE------LEWDFKLKLLEGHKLNKAEPLFSKIE 530
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
268-659 0e+00

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 568.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  268 VLITSALPYVNNVPHLGNIIGcVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADIYR 347
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLYS-YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  348 WFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPFCGYEEARGDQCDRCGKLI 427
Cdd:pfam09334  80 KFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  428 NAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKTVPGsdWTPNARFIIRSWLRDGLKPRCITRDLKWGTPV 507
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNPE--WPENVKNMVLEWLKEGLKDRAISRDLDWGIPV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  508 PleGFEDKVFYVWFDATIGYVSITANYTDQ---WEKWWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAedNYTLVKHII 584
Cdd:pfam09334 238 P--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGA--GYRLPTTVF 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284172357  585 ATEYLNYEDGKFSKSRGIGVFGDMAKDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNFINRA 659
Cdd:pfam09334 314 AHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
267-635 7.73e-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: 495.90  E-value: 7.73e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 267 NVLITSALPYVNNVPHLGNIIGCVLsADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADIY 346
Cdd:cd00814    1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 347 RWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLadrfvegvcpfcgyeeargdqcdrcgkl 426
Cdd:cd00814   80 KWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL---------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 427 inaielkkpqckicrscPVVRSSQHLFLDLPKLEKRLEDWLGKTvPGSDWTPNARFIIRSWLRDGLKPRCITRDL-KWGT 505
Cdd:cd00814  132 -----------------PEWREEEHYFFRLSKFQDRLLEWLEKN-PDFIWPENARNEVLSWLKEGLKDLSITRDLfDWGI 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 506 PVPLegFEDKVFYVWFDATIGYVSITANYTDQWEK-WWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAedNYTLVKHII 584
Cdd:cd00814  194 PVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGA--GLPLPTRIV 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 284172357 585 ATEYLNYEDGKFSKSRGIGVFGDMAKDTGiPADIWRFYLLYIRPEGQDSAF 635
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 2.74e-41

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: 146.49  E-value: 2.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  77 QDDLTNQWLEWEATELQPVLSAALHCLVVQGKKGEDILGPLRRVLTHIDHSLSRQNCPFLaGDTESLADIVLWGALYPLL 156
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79
                         90       100
                 ....*....|....*....|...
gi 284172357 157 QDPAYLPEELGALQSWFQTLSTQ 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 1.52e-27

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: 106.32  E-value: 1.52e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284172357    1 MRLFVSEGSPGSLPVLAAAARARGRAELLISTVGPEECVVPFLTRPKVPVLQLDSGNYLFSASAICRYFFLLCG 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 ...
855-899 1.70e-18

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


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 79.44  E-value: 1.70e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 284172357 855 LTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 899
Cdd:cd00939    1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
WHEP-TRS pfam00458
WHEP-TRS domain;
855-900 4.60e-18

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 78.69  E-value: 4.60e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 284172357  855 LTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGKP 900
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKD 46
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
857-899 1.03e-15

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


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 71.99  E-value: 1.03e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 284172357   857 DEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 899
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQ 44
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
47-187 1.32e-10

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 61.84  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  47 KVPVLQlDSGNYLFSASAICRYF--------FLLCGWEQDDLTNQWLEWEATELQPVLSAALHCLVVQG--KKGEDILGP 116
Cdd:COG0625   52 KVPVLV-DDGLVLTESLAILEYLaerypeppLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpAAIARARAE 130
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284172357 117 LRRVLTHIDHSLSRQncPFLAGDTESLADIVLWGALYPLLQDPAYLpEELGALQSWFQTLSTQEPCQRAAE 187
Cdd:COG0625  131 LARLLAVLEARLAGG--PYLAGDRFSIADIALAPVLRRLDRLGLDL-ADYPNLAAWLARLAARPAFQRALA 198
PLN02734 PLN02734
glycyl-tRNA synthetase
850-906 1.26e-06

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 52.44  E-value: 1.26e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 284172357 850 QHIQTLTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEgKPIETPKG 906
Cdd:PLN02734   7 DALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALE-KELQAAVG 62
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
117-180 4.80e-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: 4.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284172357  117 LRRVLTHIDHSLSrqNCPFLAGDTESLADIVLWGAL-YPLLQDPAYLPEELGALQSWFQTLSTQE 180
Cdd:pfam00043  31 VARVLSALEEVLK--GQTYLVGDKLTLADIALAPALlWLYELDPACLREKFPNLKAWFERVAARP 93
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
1-68 7.12e-04

GST_N family, unknown subfamily 3; 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 38.78  E-value: 7.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284172357   1 MRLFVSEGSPGS---LPVLAAAARARGRAELLISTVGPEECVVPFLTRPKVPVLQLDSGNYLFSASAICRY 68
Cdd:cd03049    1 MKLLYSPTSPYVrkvRVAAHETGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEY 71
PLN02395 PLN02395
glutathione S-transferase
47-179 3.43e-03

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 39.85  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  47 KVPVLQldSGNY-LFSASAICRYF----------FLLCGWEQDDLTNQWLEWEATELQP-VLSAALHCLV--VQG----- 107
Cdd:PLN02395  52 VVPVIV--DGDYkIFESRAIMRYYaekyrsqgpdLLGKTIEERGQVEQWLDVEATSYHPpLLNLTLHILFasKMGfpade 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 108 ---KKGEDILGplrRVLTHIDHSLSRQNcpFLAGDTESLADIV-------LWGALypllqDPAYLPEELGALQSWFQTLS 177
Cdd:PLN02395 130 kviKESEEKLA---KVLDVYEARLSKSK--YLAGDFVSLADLAhlpfteyLVGPI-----GKAYLIKDRKHVSAWWDDIS 199

                 ..
gi 284172357 178 TQ 179
Cdd:PLN02395 200 SR 201
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
258-848 0e+00

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 877.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 258 PVLPVPGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDK 337
Cdd:PLN02610   9 PKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 338 YHAIHADIYRWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPF--CGYEEA 415
Cdd:PLN02610  89 YHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 416 RGDQCDRCGKLINAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKTVPGSDWTPNARFIIRSWLRDGLKPR 495
Cdd:PLN02610 169 RGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRDGLKPR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 496 CITRDLKWGTPVPLEGFEDKVFYVWFDATIGYVSITANYTDQWEKWWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAED 575
Cdd:PLN02610 249 CITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLGTGE 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 576 NYTLVKHIIATEYLNYEDGKFSKSRGIGVFGDMAKDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNF 655
Cdd:PLN02610 329 NWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNF 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 656 INRAGMFVSK----FFGGCVPEMA---LTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWK 728
Cdd:PLN02610 409 INRVLSFIAKppgaGYGSVIPDAPgaeSHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQFWK 488
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 729 RIKggeMDRQRAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPP---AACRILATSFICT-----LPAGHRIGTV 800
Cdd:PLN02610 489 LYK---EDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPeslSLSDEKGEVARAKrpwelVPAGHKIGTP 565
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 284172357 801 SPLFQKLENDQIENLRQRFGGGQLEESLELKAKGSPKPAAVEAVTAAG 848
Cdd:PLN02610 566 EPLFKELKDEEVEAYREKFAGSQADRAARAEAAEAKKLAKQLKKKALS 613
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
266-815 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: 656.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 266 RNVLITSALPYVNNVPHLGNIIgCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADI 345
Cdd:COG0143    1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 346 YRWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPFCGYEEARGDQCDRCGK 425
Cdd:COG0143   80 FEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 426 LINAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLgKTVPgsDWTPNARFIIRSWLRDGLKPRCITRDLKWGT 505
Cdd:COG0143  160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWI-EENP--DIQPEVRNEVLSWLKEGLQDLSISRDFDWGI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 506 PVPleGFEDKVFYVWFDATIGYVSITANYTDQ------WEKWWKNPEqVDLYQFMAKDNVPFHGLVFPCSVLGAedNYTL 579
Cdd:COG0143  237 PVP--GDPGKVFYVWFDALIGYISATKGYADDrglpedFEKYWPAPD-TELVHFIGKDIIRFHAIIWPAMLMAA--GLPL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 580 VKHIIATEYLNYEDGKFSKSRGIGVFGDMAKDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNFINRA 659
Cdd:COG0143  312 PKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRT 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 660 GMFVSKFFGGCVPEM-ALTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKggEMDRQ 738
Cdd:COG0143  391 LSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAK--DEDPE 468
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 284172357 739 RAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPPAACRILATSFIctLPAGHRIGTVSPLFQKLENDQIENL 815
Cdd:COG0143  469 RLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGWP--LPAGHKIGKPEPLFPRIEDEQIEAL 543
metG PRK00133
methionyl-tRNA synthetase; Reviewed
266-847 0e+00

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 637.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 266 RNVLITSALPYVNNVPHLGNIIGcVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADI 345
Cdd:PRK00133   2 RKILVTCALPYANGPIHLGHLVE-YIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 346 YRWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPFCGYEEARGDQCDRCGK 425
Cdd:PRK00133  81 FAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 426 LINAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKtvpGSDWTPNARFIIRSWLRDGLKPRCITRDLKW-G 504
Cdd:PRK00133 161 TYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITR---SGELQPNVANKMKEWLEEGLQDWDISRDAPYfG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 505 TPVPleGFEDKVFYVWFDATIGYVSITANYTDQ-----WEKWWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAedNYTL 579
Cdd:PRK00133 238 FEIP--GAPGKVFYVWLDAPIGYISSTKNLCDKrggldWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGA--GYRL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 580 VKHIIATEYLNYEDGKFSKSRGIGVFGDMAKDTgIPADIWRFYLLYIRPEG-QDSAFSWTDLLIKNNSELLNNLGNFINR 658
Cdd:PRK00133 314 PTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDH-LDPDYLRYYLAAKLPETiDDLDFNWEDFQQRVNSELVGKVVNFASR 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 659 AGMFVSKFFGGCVPEMALTPDdrrLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGgemDRQ 738
Cdd:PRK00133 393 TAGFINKRFDGKLPDALADPE---LLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQ---DGE 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 739 RAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPPaacriLATSFICTLPAGHRIGTVSPLFQKLENDQIENLrqr 818
Cdd:PRK00133 467 RLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEE-----LTWDDAQQPLAGHPINKFKILFTRIEDKQIEAL--- 538
                        570       580
                 ....*....|....*....|....*....
gi 284172357 819 fgggqLEESLELKAKGSPKPAAVEAVTAA 847
Cdd:PRK00133 539 -----IEASKEAAAAKAAAAAAAAPLAEE 562
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
268-808 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: 580.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  268 VLITSALPYVNNVPHLGNIIgCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADIYR 347
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  348 WFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPFCGYEEARGDQCDRCGKLI 427
Cdd:TIGR00398  80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  428 NAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKTVPGSDWTPNARFIIRSWLRDGLKPRCITRDLK-WGTP 506
Cdd:TIGR00398 160 EPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVyWGIP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  507 VPLEgfEDKVFYVWFDATIGYVS---ITANYTDQWEKWWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAEdnYTLVKHI 583
Cdd:TIGR00398 240 VPND--PNKVVYVWFDALIGYISslgILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLG--LPLPTQV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  584 IATEYLNYEDGKFSKSRGIGVFGDMAKDtGIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNFINRAGMFV 663
Cdd:TIGR00398 316 FSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  664 SKFFGGCVP-EMALTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKggemDRQRAGT 742
Cdd:TIGR00398 395 KKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFK----QSPRLKE 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284172357  743 VTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPpaacriLATSFICTLPAGHRIGTVSPLFQKLE 808
Cdd:TIGR00398 471 LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFE------LEWDFKLKLLEGHKLNKAEPLFSKIE 530
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
268-659 0e+00

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 568.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  268 VLITSALPYVNNVPHLGNIIGcVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADIYR 347
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLYS-YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  348 WFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVEGVCPFCGYEEARGDQCDRCGKLI 427
Cdd:pfam09334  80 KFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  428 NAIELKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKTVPGsdWTPNARFIIRSWLRDGLKPRCITRDLKWGTPV 507
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNPE--WPENVKNMVLEWLKEGLKDRAISRDLDWGIPV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  508 PleGFEDKVFYVWFDATIGYVSITANYTDQ---WEKWWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAedNYTLVKHII 584
Cdd:pfam09334 238 P--GAEGKVFYVWLDAPIGYISATKELSGNeekWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGA--GYRLPTTVF 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284172357  585 ATEYLNYEDGKFSKSRGIGVFGDMAKDTgIPADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNFINRA 659
Cdd:pfam09334 314 AHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
267-635 7.73e-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: 495.90  E-value: 7.73e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 267 NVLITSALPYVNNVPHLGNIIGCVLsADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADIY 346
Cdd:cd00814    1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 347 RWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLadrfvegvcpfcgyeeargdqcdrcgkl 426
Cdd:cd00814   80 KWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL---------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 427 inaielkkpqckicrscPVVRSSQHLFLDLPKLEKRLEDWLGKTvPGSDWTPNARFIIRSWLRDGLKPRCITRDL-KWGT 505
Cdd:cd00814  132 -----------------PEWREEEHYFFRLSKFQDRLLEWLEKN-PDFIWPENARNEVLSWLKEGLKDLSITRDLfDWGI 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 506 PVPLegFEDKVFYVWFDATIGYVSITANYTDQWEK-WWKNPEQVDLYQFMAKDNVPFHGLVFPCSVLGAedNYTLVKHII 584
Cdd:cd00814  194 PVPL--DPGKVIYVWFDALIGYISATGYYNEEWGNsWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGA--GLPLPTRIV 269
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 284172357 585 ATEYLNYEDGKFSKSRGIGVFGDMAKDTGiPADIWRFYLLYIRPEGQDSAF 635
Cdd:cd00814  270 AHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEGKDSDF 319
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
270-808 2.49e-97

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 314.90  E-value: 2.49e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 270 ITSALPYVNNVPHLGNIiGCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADIYRWF 349
Cdd:PRK11893   5 ITTPIYYPNGKPHIGHA-YTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEAL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 350 GISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFvegvcpfcgyeeargdqcdrcgkLINa 429
Cdd:PRK11893  84 NISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESE-----------------------LIE- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 430 ielKKPQCKICRSCPVVRSSQHLFLDLPKLEKRLEDWLGKtvpGSDW-TPNARF-IIRSWLRDGLKPRCITR-DLKWGTP 506
Cdd:PRK11893 140 ---DGYRCPPTGAPVEWVEEESYFFRLSKYQDKLLELYEA---NPDFiQPASRRnEVISFVKSGLKDLSISRtNFDWGIP 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 507 VPleGFEDKVFYVWFDATIGYvsITA--------NYTDQWEKWWknpeQVDLyQFMAKDNVPFHGLVFPcSVLGAeDNYT 578
Cdd:PRK11893 214 VP--GDPKHVIYVWFDALTNY--LTAlgypddeeLLAELFNKYW----PADV-HLIGKDILRFHAVYWP-AFLMA-AGLP 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 579 LVKHIIATEYLNYEDGKFSKSRG--IGVFgDMAKDTGipADIWRFYLLYIRPEGQDSAFSWTDLLIKNNSELLNNLGNFI 656
Cdd:PRK11893 283 LPKRVFAHGFLTLDGEKMSKSLGnvIDPF-DLVDEYG--VDAVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNLA 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 657 NRAGMFVSKFFGGCVPEM-ALTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGgem 735
Cdd:PRK11893 360 QRTLSMIAKNFDGKVPEPgALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKT--- 436
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 284172357 736 DRQRAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPPAACRILATSFICTLPAGHRIGTVSPLFQKLE 808
Cdd:PRK11893 437 DPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEEDENRDFAALSWGRLAPGTTLPKPEPIFPRLE 509
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
270-843 8.09e-79

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 268.98  E-value: 8.09e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 270 ITSALPYVNNVPHLGN----IIgcvlsADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKyhaIHADI 345
Cdd:PRK12267   8 ITTPIYYPNGKPHIGHayttIA-----ADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDE---ISAGF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 346 YR-W--FGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARF-----LADrfvEGVCPFCGYEearg 417
Cdd:PRK12267  80 KElWkkLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFftesqLVD---GGKCPDCGRE---- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 418 dqcdrcgklinaielkkpqckicrscPVVRSSQHLFLDLPKLEKRLEDWLGKtvpgsdwtpNARFI---------IRSWL 488
Cdd:PRK12267 153 --------------------------VELVKEESYFFRMSKYQDRLLEYYEE---------NPDFIqpesrknemINNFI 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 489 RDGLKPRCITRD-LKWGTPVPlegFEDK-VFYVWFDATIGYvsITA-NY----TDQWEKWWknPEQVdlyQFMAKDNVPF 561
Cdd:PRK12267 198 KPGLEDLSISRTsFDWGIPVP---FDPKhVVYVWIDALLNY--ITAlGYgsddDELFKKFW--PADV---HLVGKDILRF 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 562 HGLVFPCsVLGAEDnYTLVKHIIATEYLNYEDGKFSKSRGIGVFG-DMAKDTGIpaDIWRFYLLYIRPEGQDSAFSWTDL 640
Cdd:PRK12267 268 HAIYWPI-MLMALG-LPLPKKVFAHGWWLMKDGKMSKSKGNVVDPeELVDRYGL--DALRYYLLREVPFGSDGDFSPEAL 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 641 LIKNNSELLNNLGNFINRA-GMfVSKFFGGCVPEMA-LTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGN 718
Cdd:PRK12267 344 VERINSDLANDLGNLLNRTvAM-INKYFDGEIPAPGnVTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISRAN 422
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 719 QYIQVNEPWKRIKGGEmDRQRAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPPAACRILATSFICTLPAGHRIG 798
Cdd:PRK12267 423 KYIDETAPWVLAKDEG-KKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLGLEEELTSWESLLEWGGLPAGTKVA 501
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 284172357 799 TVSPLFQKLENDqienlrqrfgggqlEESLELKAKGSPKPAAVEA 843
Cdd:PRK12267 502 KGEPLFPRIDVE--------------EEIAYIKEQMEGSAPKEPE 532
Anticodon_Ia_Met cd07957
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ...
644-773 8.82e-45

Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA synthetases (MetRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon (CAU). MetRS catalyzes the transfer of methionine to the 3'-end of its tRNA.


Pssm-ID: 153411 [Multi-domain]  Cd Length: 129  Bit Score: 157.27  E-value: 8.82e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 644 NNSELLNNLGNFINRAGMFVSKFFGGCVPEM-ALTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQ 722
Cdd:cd07957    1 INSELANNLGNLVNRTLNMASKYFGGVVPEFgGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 284172357 723 VNEPWKRIKggEMDRQRAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQL 773
Cdd:cd07957   81 ETAPWKLAK--EEDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
PLN02224 PLN02224
methionine-tRNA ligase
264-808 4.68e-42

methionine-tRNA ligase


Pssm-ID: 177869 [Multi-domain]  Cd Length: 616  Bit Score: 163.35  E-value: 4.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 264 GERNVLiTSALPYVNNVPHLGNIIgCVLSADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHA 343
Cdd:PLN02224  68 ADTFVL-TTPLYYVNAPPHMGSAY-TTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYR 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 344 DIYRWFGISFDTFGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCarfladrfvegvcpfcgyEEARGDQcdrc 423
Cdd:PLN02224 146 TLWKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNC------------------EEYKDEK---- 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 424 gklinaiELKKPQCKICRSCP-VVRSSQHLFLDLPKLEKRLEDWLGKtvpgsdwtpNARFI--------IRSWLRDGLKP 494
Cdd:PLN02224 204 -------ELLENNCCPVHQMPcVARKEDNYFFALSKYQKPLEDILAQ---------NPRFVqpsyrlneVQSWIKSGLRD 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 495 RCITRDL-KWGTPVPLEgfEDKVFYVWFDATIGYVSITANYTDQwekwwKNPEQVDLY------QFMAKDNVPFHGLVFP 567
Cdd:PLN02224 268 FSISRALvDWGIPVPDD--DKQTIYVWFDALLGYISALTEDNKQ-----QNLETAVSFgwpaslHLIGKDILRFHAVYWP 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 568 CSVLGAedNYTLVKHIIATEYLNYEDGKFSKSRG--IGVFgDMAKDTGipADIWRFYLLYIRPEGQDSAFSWTDLLIKNN 645
Cdd:PLN02224 341 AMLMSA--GLELPKMVFGHGFLTKDGMKMGKSLGntLEPF-ELVQKFG--PDAVRYFFLREVEFGNDGDYSEDRFIKIVN 415
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 646 SELLNNLGNFINRA-GMFVSKFFGGCVPEMALTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVN 724
Cdd:PLN02224 416 AHLANTIGNLLNRTlGLLKKNCESTLVEDSTVAAEGVPLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNTYMDQR 495
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 725 EPWKRIKGGEMDRQRAGTVTGMAVNMAALLSVMLQPYMPTVSSTIQTQLQLPPAACRILATSFI--CTLPAGHRIGTVSP 802
Cdd:PLN02224 496 APWFLFKQGGVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQLGYSEDQFNSITWSDTkwGGLKGGQVMEQASP 575

                 ....*.
gi 284172357 803 LFQKLE 808
Cdd:PLN02224 576 VFARIE 581
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
77-179 2.74e-41

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: 146.49  E-value: 2.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  77 QDDLTNQWLEWEATELQPVLSAALHCLVVQGKKGEDILGPLRRVLTHIDHSLSRQNCPFLaGDTESLADIVLWGALYPLL 156
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79
                         90       100
                 ....*....|....*....|...
gi 284172357 157 QDPAYLPEELGALQSWFQTLSTQ 179
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
269-632 1.14e-36

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: 140.63  E-value: 1.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 269 LITSALPYVNNVPHLGNIIGCVLsADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGL-------------TPREIC 335
Cdd:cd00668    3 YVTTPPPYANGSLHLGHALTHII-ADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEFV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 336 DKYHAIHADIYRWFGISFDT--FGRTTTPQQTKITQDIFQRLLTRGFVLRDTVEqlrcercarfladrfvegvcpfcgye 413
Cdd:cd00668   82 EEMSGEHKEDFRRLGISYDWsdEYITTEPEYSKAVELIFSRLYEKGLIYRGTHP-------------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 414 eargdqcdrcgklinaielkkpqckicrscpvVRSSQHLFLDLPKLEKRLEDWLGKTvpgsDWTPNA-RFIIRSWLRDGL 492
Cdd:cd00668  136 --------------------------------VRITEQWFFDMPKFKEKLLKALRRG----KIVPEHvKNRMEAWLESLL 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 493 KpRCITRDLKWGTPVPlegfeDKVFYVWFDATIGYVSITAN--YTDQWEKWWknPEqvdLYQFMAKDNVPFHGLVFPCSV 570
Cdd:cd00668  180 D-WAISRQRYWGTPLP-----EDVFDVWFDSGIGPLGSLGYpeEKEWFKDSY--PA---DWHLIGKDILRGWANFWITML 248
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284172357 571 LGAEDNYTLvKHIIATEYLNYEDG-KFSKSRG-IGVFGDMAKDTGipADIWRFYLLYIRPEGQD 632
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 1.52e-27

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: 106.32  E-value: 1.52e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284172357    1 MRLFVSEGSPGSLPVLAAAARARGRAELLISTVGPEECVVPFLTRPKVPVLQLDSGNYLFSASAICRYFFLLCG 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 ...
855-899 1.70e-18

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


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 79.44  E-value: 1.70e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 284172357 855 LTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 899
Cdd:cd00939    1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
WHEP-TRS pfam00458
WHEP-TRS domain;
855-900 4.60e-18

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 78.69  E-value: 4.60e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 284172357  855 LTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGKP 900
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKD 46
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
857-899 1.03e-15

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


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 71.99  E-value: 1.03e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 284172357   857 DEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 899
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQ 44
Anticodon_3 pfam19303
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ...
671-822 4.71e-14

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


Pssm-ID: 437135 [Multi-domain]  Cd Length: 152  Bit Score: 70.22  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  671 VPEM-ALTPDDRRLVAHVSWELQHYHQLLEKVRIRDA---LRSILTIsrhGNQYIQVNEPWKRIKggeMDRQRAGTVTGM 746
Cdd:pfam19303   1 VPEGgAYGEAEAALIADLTTRLAAYEGHMEAMEVRKAaaeLRAIWVA---GNEYLQEAAPWTTFK---TDPEAAAAQVRL 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 284172357  747 AVNMAALLSVMLQPYMPTVSSTIQTQLQLPPAACRILATSFICTLPAGHRIgTVSP-LFQKLENDQIENLRQRFGGG 822
Cdd:pfam19303  75 ALNLIRLYAVLSAPFIPDAAAAMLAAMGTDDAAWPDDVAAALTALPAGHAF-TVPEvLFAKITDEQREEWQERFAGT 150
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
857-897 5.07e-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: 66.79  E-value: 5.07e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 284172357 857 DEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAE 897
Cdd:cd01200    2 EKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
275-528 1.20e-13

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: 73.82  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 275 PYVNNVPHLGNIIGCVLsADVFARYCRLRQWNTLYLCGTDEYGTATETK----AMEEGLTPR--------EIC----DKY 338
Cdd:cd00817   10 PNVTGSLHMGHALNNTI-QDIIARYKRMKGYNVLWPPGTDHAGIATQVVvekkLGIEGKTRHdlgreeflEKCwewkEES 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 339 HAIHADIYRWFGISFDtFGR---TTTPQQTKITQDIFQRLLTRGFVLRDTVEQLRCERCARFLADRFVegvcpfcgyeea 415
Cdd:cd00817   89 GGKIREQLKRLGASVD-WSReyfTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV------------ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 416 rgdqCDRCGKLI----------NAIELKKPQCKicrscpVVRSSQHLFldLPKL-EKRLEDWLGKtvpgsdwtpnarfiI 484
Cdd:cd00817  156 ----CSRSGDVIepllkpqwfvKVKDLAKKALE------AVKEGDIKF--VPERmEKRYENWLEN--------------I 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 284172357 485 RSWlrdglkprCITRDLKWGTPVPlegfedkvfyVWFDATIGYV 528
Cdd:cd00817  210 RDW--------CISRQLWWGHRIP----------AWYCKDGGHW 235
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
275-773 1.05e-11

valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273070 [Multi-domain]  Cd Length: 861  Bit Score: 68.93  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  275 PYVNNVPHLGNIIGCVLSaDVFARYCRLRQWNTLYLCGTDEYGTATETK----AMEEGLT----PRE--------ICDKY 338
Cdd:TIGR00422  42 PNVTGSLHIGHALNWSIQ-DIIARYKRMKGYNVLWLPGTDHAGIATQVKvekkLGAEGKTkhdlGREefrekiweWKEES 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  339 HAIHADIYRWFGISFDtFGR---TTTPQQTKITQDIFQRLLTRGFVLRD------------------------------- 384
Cdd:TIGR00422 121 GGTIKNQIKRLGASLD-WSRerfTMDEGLSKAVKEAFVRLYEKGLIYRGeylvnwdpklntaisdieveykevkgklyyi 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  385 ------------TVEQLRCERCA------------RF-------------------LADRFVE--------GVCPFcgye 413
Cdd:TIGR00422 200 ryplangskdylVVATTRPETMFgdtavavhpedeRYkhligkkvilpltgrkipiIADEYVDmefgtgavKVTPA---- 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  414 earGDQCD-RCGK-----LINAIE--------------LKKPQC--KI----------------------CRSCPVVRS- 448
Cdd:TIGR00422 276 ---HDFNDyEWGKrhnleFINILDedgllnenagkyqgLTRFEArkKIvedlkeegllvkiephthnvgtCWRSGTVVEp 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  449 --SQHLFLDLPKLEKRLEDWLGKTVPgsDWTPNaRFIIR--SWLRDgLKPRCITRDLKWGTPVP---------------- 508
Cdd:TIGR00422 353 llSKQWFVKVEKLADKALEAAEEGEI--KFVPK-RMEKRylNWLRN-IKDWCISRQLIWGHRIPvwyckecgevyvakee 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  509 --------------LEGFEDkVFYVWFDAtigyvSITANYTDQWEKwwknpEQVDLYQFmakdnVPFHGLVFPCSVLGAE 574
Cdd:TIGR00422 429 plpddktntgpsveLEQDTD-VLDTWFSS-----SLWPFSTLGWPD-----ETKDLKKF-----YPTDLLVTGYDIIFFW 492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  575 DNYTLV-----------KHIIATEYLNYEDG-KFSKSRGIGVFG-DMAKDTGipADIWRFYLLYIRPEGQDSAFSWTDLl 641
Cdd:TIGR00422 493 VARMIFrslaltgqvpfKEVYIHGLVRDEQGrKMSKSLGNVIDPlDVIEKYG--ADALRFTLASLVTPGDDINFDWKRV- 569
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  642 iKNNSELLNNLGNFINRAGMFVSKFFGGCVPEMALTPDDRRLVAHVSWELQHYHQLLEKVRIRDALRSILTISRHG--NQ 719
Cdd:TIGR00422 570 -ESARNFLNKLWNASRFVLMNLSDDLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALYEFIWNDfcDW 648
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 284172357  720 YIQVNEPwkRIKGGEMDRQR-AGTVTGMAVNMAALLsvmLQPYMPTVSSTIQTQL 773
Cdd:TIGR00422 649 YIELVKY--RLYNGNEAEKKaARDTLYYVLDKALRL---LHPFMPFITEEIWQHF 698
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
855-899 4.88e-11

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: 58.40  E-value: 4.88e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 284172357 855 LTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEGK 899
Cdd:cd00936    1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQ 45
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
47-187 1.32e-10

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 61.84  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  47 KVPVLQlDSGNYLFSASAICRYF--------FLLCGWEQDDLTNQWLEWEATELQPVLSAALHCLVVQG--KKGEDILGP 116
Cdd:COG0625   52 KVPVLV-DDGLVLTESLAILEYLaerypeppLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpAAIARARAE 130
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284172357 117 LRRVLTHIDHSLSRQncPFLAGDTESLADIVLWGALYPLLQDPAYLpEELGALQSWFQTLSTQEPCQRAAE 187
Cdd:COG0625  131 LARLLAVLEARLAGG--PYLAGDRFSIADIALAPVLRRLDRLGLDL-ADYPNLAAWLARLAARPAFQRALA 198
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
270-637 3.01e-10

catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 173906 [Multi-domain]  Cd Length: 314  Bit Score: 62.65  E-value: 3.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 270 ITSALPYVNNVPHLGNIIGCVLsADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHA-IHADIYRw 348
Cdd:cd00812    4 ILVMFPYPSGALHVGHVRTYTI-GDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKkMKEQLKR- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 349 FGISFDtFGR---TTTPQQTKITQDIFQRLltrgfvlrdtveqlrcercarfladrfvegvcPFCGYeeargdqCDRCGK 425
Cdd:cd00812   82 MGFSYD-WRReftTCDPEYYKFTQWLFLKL--------------------------------YEKGL-------AYKKEA 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 426 LINaielkkpQCKICRscpvvrssqHLFLD--LPKLEKRLEDWLGKTvpgSDWTPNARFIIRSWLRdglkprcITRDLKW 503
Cdd:cd00812  122 PVN-------WCKLLD---------QWFLKysETEWKEKLLKDLEKL---DGWPEEVRAMQENWIG-------CSRQRYW 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 504 GTPVPlegFEDkVFYVWFDATIGYvsitANYTD-------QWEKWWKNPEQ------VDLYqFMAKDNVP--------FH 562
Cdd:cd00812  176 GTPIP---WTD-TMESLSDSTWYY----ARYTDahnleqpYEGDLEFDREEfeywypVDIY-IGGKEHAPnhllysrfNH 246
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284172357 563 GLVFPCSVLGAEdnytLVKHIIATEYLNYEDGKFSKSRGIGV-FGDMAKDTGipADIWRFYLLYIRPegQDSAFSW 637
Cdd:cd00812  247 KALFDEGLVTDE----PPKGLIVQGMVLLEGEKMSKSKGNVVtPDEAIKKYG--ADAARLYILFAAP--PDADFDW 314
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
854-893 1.22e-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: 54.40  E-value: 1.22e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 284172357 854 TLTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQL 893
Cdd:cd00938    2 KLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQL 41
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
121-179 6.77e-09

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: 53.47  E-value: 6.77e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 121 LTHIDHSLSRQNCpFLAGDTESLADIVLWGALYPLLQDPAYL-PEELGALQSWFQTLSTQ 179
Cdd:cd10289   24 LLKSLNSYLASRT-FLVGYSLTLADVAVFSALYPSGQKLSDKeKKKFPHVTRWFNHIQNL 82
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
83-186 1.06e-08

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


Pssm-ID: 198289 [Multi-domain]  Cd Length: 110  Bit Score: 53.82  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  83 QWLEWEATELQPVLSAALHCLV---------VQGKKGEDILGPLRRVLthiDHSLSRQncPFLAGDTESLADIVLWGALY 153
Cdd:cd03180    8 RWMDWQTSTLNPAFRYAFWGLVrtppeqrdpAAIAASLAACNKLMAIL---DAQLARQ--AYLAGDRFTLADIALGCSVY 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 284172357 154 PLLQDPAYLPeELGALQSWFQTLStqepcQRAA 186
Cdd:cd03180   83 RWLELPIERP-ALPHLERWYARLS-----QRPA 109
PLN02734 PLN02734
glycyl-tRNA synthetase
850-906 1.26e-06

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 52.44  E-value: 1.26e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 284172357 850 QHIQTLTDEVTKQGNVVRELKAQKADKNQVAAEVAKLLDLKKQLALAEgKPIETPKG 906
Cdd:PLN02734   7 DALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALE-KELQAAVG 62
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
81-176 3.54e-05

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: 43.64  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  81 TNQWLEWEATELQPVLSAALH----CLVVQGKKGEDILGPLRRVLTHIDHSLSRQncPFLAGDTESLADIVLWGALY--P 154
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYlekvPLPKDEAAVEAAREELPALLAALEQLLAGR--PYLAGDQFSLADVALAPVLArlE 78
                         90       100
                 ....*....|....*....|..
gi 284172357 155 LLQDPAYLPEELGALQSWFQTL 176
Cdd:cd00299   79 ALGPYYDLLDEYPRLKAWYDRL 100
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
117-180 4.80e-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: 4.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284172357  117 LRRVLTHIDHSLSrqNCPFLAGDTESLADIVLWGAL-YPLLQDPAYLPEELGALQSWFQTLSTQE 180
Cdd:pfam00043  31 VARVLSALEEVLK--GQTYLVGDKLTLADIALAPALlWLYELDPACLREKFPNLKAWFERVAARP 93
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
81-177 8.78e-05

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: 42.62  E-value: 8.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  81 TNQWLEWEATELQPVLSAALHCLVVQGKKG----EDILGPLRRVLTHIDHSLSRQncPFLAGDTESLADIVLWG-ALYPL 155
Cdd:cd03178    5 VLQWLFFQMSGLGPMFGQAGHFLYFAPEKIpyaiERYTDEVKRLYGVLDKRLSDR--PYLAGEEYSIADIALYPwTHYAD 82
                         90       100
                 ....*....|....*....|..
gi 284172357 156 LQDPAYLpEELGALQSWFQTLS 177
Cdd:cd03178   83 LGGFADL-SEYPNVKRWLERIA 103
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
275-383 1.00e-04

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: 45.86  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  275 PYVNNVPHLGNIIGCVLSaDVFARYCRLRQWNTLYLCGTDEYGTATETK-----AMEEGLTP------------REICDK 337
Cdd:pfam00133  32 PNATGSLHIGHALAKTLK-DIVIRYKRMKGYYVLWVPGWDHHGLPTEQVvekklGIKEKKTRhkygreefrekcREWKME 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 284172357  338 YHAIHADIYRWFGISFDtFGR---TTTPQQTKITQDIFQRLLTRGFVLR 383
Cdd:pfam00133 111 YADEIRKQFRRLGRSID-WDReyfTMDPELEAAVWEVFVRLHDKGLIYR 158
valS PRK14900
valyl-tRNA synthetase; Provisional
250-404 3.57e-04

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 44.60  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  250 PPLKLqqhpVLPVPGernvlITSALpyvnnvpHLGNIIGCVLSaDVFARYCRLRQWNTLYLCGTDEYGTAT------ETK 323
Cdd:PRK14900   48 PPFSI----VLPPPN-----VTGSL-------HLGHALTATLQ-DVLIRWKRMSGFNTLWLPGTDHAGIATqmivekELK 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  324 AME---------EGLTPR--EICDKYHAIHADIYRWFGISFDtFGR---TTTPQQTKITQDIFQRLLTRGFVLRDTVEQL 389
Cdd:PRK14900  111 KTEkksrhdlgrEAFLERvwAWKEQYGSRIGEQHKALGASLD-WQRerfTMDEGLSRAVREVFVRLHEEGLIYREKKLIN 189
                         170
                  ....*....|....*
gi 284172357  390 RCERCARFLADRFVE 404
Cdd:PRK14900  190 WCPDCRTALSDLEVE 204
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
1-68 7.12e-04

GST_N family, unknown subfamily 3; 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 38.78  E-value: 7.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284172357   1 MRLFVSEGSPGS---LPVLAAAARARGRAELLISTVGPEECVVPFLTRPKVPVLQLDSGNYLFSASAICRY 68
Cdd:cd03049    1 MKLLYSPTSPYVrkvRVAAHETGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEY 71
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
275-348 9.81e-04

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: 40.54  E-value: 9.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284172357 275 PYVNNVPHLGNIIGCVLsADVFARYCRLRQWNTLYLCGTDEYGTATETKAMEEGLTPREICDKYHAIHADIYRW 348
Cdd:cd00802    6 ITPNGYLHIGHLRTIVT-FDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVEY 78
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
134-177 1.04e-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: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 284172357 134 PFLAGDTESLADIVLWGAL---YPLLQDPaylPEELGALQSWFQTLS 177
Cdd:cd03182   68 PYVAGDRFSIADITAFVALdfaKNLKLPV---PEELTALRRWYERMA 111
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
83-180 1.06e-03

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: 39.85  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  83 QWLEWEATELQPVLSAALhcLVVQG-----KKGED--------ILGPLRRVLthidhslsrQNCPFLAGDTESLADIVLW 149
Cdd:cd03181    7 QWISFANSELLPAAATWV--LPLLGiapynKKAVDkakedlkrALGVLEEHL---------LTRTYLVGERITLADIFVA 75
                         90       100       110
                 ....*....|....*....|....*....|....
gi 284172357 150 GALYPLLQ---DPAYLpEELGALQSWFQTLSTQE 180
Cdd:cd03181   76 SALLRGFEtvlDPEFR-KKYPNVTRWFNTVVNQP 108
PLN02395 PLN02395
glutathione S-transferase
47-179 3.43e-03

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 39.85  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  47 KVPVLQldSGNY-LFSASAICRYF----------FLLCGWEQDDLTNQWLEWEATELQP-VLSAALHCLV--VQG----- 107
Cdd:PLN02395  52 VVPVIV--DGDYkIFESRAIMRYYaekyrsqgpdLLGKTIEERGQVEQWLDVEATSYHPpLLNLTLHILFasKMGfpade 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357 108 ---KKGEDILGplrRVLTHIDHSLSRQNcpFLAGDTESLADIV-------LWGALypllqDPAYLPEELGALQSWFQTLS 177
Cdd:PLN02395 130 kviKESEEKLA---KVLDVYEARLSKSK--YLAGDFVSLADLAhlpfteyLVGPI-----GKAYLIKDRKHVSAWWDDIS 199

                 ..
gi 284172357 178 TQ 179
Cdd:PLN02395 200 SR 201
GST_C_AIMP3 cd10305
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
80-176 4.15e-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: 37.65  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  80 LTNQWLEWEATELQPVLSAALhclvvqgkkgedilgpLRRVLTHIDHSLsrQNCPFLAGDTESLADIVLWGALYPLLQDP 159
Cdd:cd10305    6 QVDQWLEYRVTQVAPASDKAD----------------AKSLLKELNSYL--QDRTYLVGHKLTLADVVLYYGLHPIMKDL 67
                         90
                 ....*....|....*...
gi 284172357 160 AYLPEE-LGALQSWFQTL 176
Cdd:cd10305   68 SPQEKEqYLNVSRWFDHV 85
GST_C_ValRS_N cd10294
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ...
77-179 4.58e-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: 37.89  E-value: 4.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284172357  77 QDDLTNQWLEWEATELQPVLSAA----LHCLVVQGKKGEDILGPLRRVLTHIDHSLSRQNcpFLAGDTESLADIVLWGAL 152
Cdd:cd10294    1 ACALVWQWVSFADNELTPAACAAafplLGLSGSDKQNQQRSLAELQRVLKVLDCYLKLRT--YLVGEAITLADIAVACAL 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 284172357 153 ---YPLLQDPAyLPEELGALQSWFQTLSTQ 179
Cdd:cd10294   79 llpFKYVLDPA-RRESLLNVTRWFLTCVNQ 107
 
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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