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Conserved domains on  [gi|294856155|gb|ADF45015|]
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methionyl-tRNA synthetase, partial [Escherichia sp. TW09266]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metG super family cl35069
methionyl-tRNA synthetase; Reviewed
 1-175 2.06e-134

methionyl-tRNA synthetase; Reviewed


The actual alignment was detected with superfamily member PRK00133:

Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 390.28  E-value: 2.06e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:PRK00133  28 ADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAGFGISFDNYGSTHSEENRELAQEIY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHF 160
Cdd:PRK00133 108 LKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGATYSPTELINPKSAISGATPVLKESEHF 187

                        170
                 ....*....|....*
gi 294856155 161 FFDLPSFSEMLQAWT 175
Cdd:PRK00133 188 FFKLPRFEEFLKEWI 202
 
Name Accession Description Interval E-value
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 1-175 2.06e-134

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 390.28  E-value: 2.06e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:PRK00133  28 ADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAGFGISFDNYGSTHSEENRELAQEIY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHF 160
Cdd:PRK00133 108 LKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGATYSPTELINPKSAISGATPVLKESEHF 187

                        170
                 ....*....|....*
gi 294856155 161 FFDLPSFSEMLQAWT 175
Cdd:PRK00133 188 FFKLPRFEEFLKEWI 202
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 1-175 2.47e-110

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: 324.76  E-value: 2.47e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:COG0143   27 ADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFEKLGISFDNFIRTTSPEHKELVQEIF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHF 160
Cdd:COG0143  107 QRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGATLEPTELINPRSAISGAPPELREEEHY 186

                        170
                 ....*....|....*
gi 294856155 161 FFDLPSFSEMLQAWT 175
Cdd:COG0143  187 FFRLSKYQDRLLEWI 201
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 1-174 4.23e-100

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 293.43  E-value: 4.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155    1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:pfam09334  25 ADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKKFNISFDDYGRTTSERHHELVQEFF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHF 160
Cdd:pfam09334 105 LKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLEPTELINPKCVICGTTPEVKETEHY 184

                         170
                  ....*....|....
gi 294856155  161 FFDLPSFSEMLQAW 174
Cdd:pfam09334 185 FFDLSKFQDKLREW 198
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
 1-175 8.53e-94

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: 281.96  E-value: 8.53e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155    1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:TIGR00398  25 ADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKWLNISFDRFIRTTDEEHKEIVQKIF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHF 160
Cdd:TIGR00398 105 QKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLEPTELINPRCKICGAKPELRDSEHY 184

                         170
                  ....*....|....*
gi 294856155  161 FFDLPSFSEMLQAWT 175
Cdd:TIGR00398 185 FFRLSAFEKELEEWI 199
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 1-174 1.51e-52

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: 170.02  E-value: 1.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:cd00814   26 ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNISFDYFIRTTSPRHKEIVQEFF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYDPEKGMFLpdrfvkgtcpkckapdqygdncevcgatyspteliepksvvsgatPVMRDSEHF 160
Cdd:cd00814  106 KKLYENGYIYEGEYEGLYCVSCERFL---------------------------------------------PEWREEEHY 140

                        170
                 ....*....|....
gi 294856155 161 FFDLPSFSEMLQAW 174
Cdd:cd00814  141 FFRLSKFQDRLLEW 154
 
Name Accession Description Interval E-value
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 1-175 2.06e-134

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 390.28  E-value: 2.06e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:PRK00133  28 ADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAGFGISFDNYGSTHSEENRELAQEIY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHF 160
Cdd:PRK00133 108 LKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGATYSPTELINPKSAISGATPVLKESEHF 187

                        170
                 ....*....|....*
gi 294856155 161 FFDLPSFSEMLQAWT 175
Cdd:PRK00133 188 FFKLPRFEEFLKEWI 202
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 1-175 2.47e-110

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: 324.76  E-value: 2.47e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:COG0143   27 ADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFEKLGISFDNFIRTTSPEHKELVQEIF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHF 160
Cdd:COG0143  107 QRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGATLEPTELINPRSAISGAPPELREEEHY 186

                        170
                 ....*....|....*
gi 294856155 161 FFDLPSFSEMLQAWT 175
Cdd:COG0143  187 FFRLSKYQDRLLEWI 201
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 1-174 4.23e-100

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 293.43  E-value: 4.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155    1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:pfam09334  25 ADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKKFNISFDDYGRTTSERHHELVQEFF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHF 160
Cdd:pfam09334 105 LKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLEPTELINPKCVICGTTPEVKETEHY 184

                         170
                  ....*....|....
gi 294856155  161 FFDLPSFSEMLQAW 174
Cdd:pfam09334 185 FFDLSKFQDKLREW 198
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
 1-175 8.53e-94

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: 281.96  E-value: 8.53e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155    1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:TIGR00398  25 ADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKWLNISFDRFIRTTDEEHKEIVQKIF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHF 160
Cdd:TIGR00398 105 QKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLEPTELINPRCKICGAKPELRDSEHY 184

                         170
                  ....*....|....*
gi 294856155  161 FFDLPSFSEMLQAWT 175
Cdd:TIGR00398 185 FFRLSAFEKELEEWI 199
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 1-174 1.51e-52

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: 170.02  E-value: 1.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:cd00814   26 ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNISFDYFIRTTSPRHKEIVQEFF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYDPEKGMFLpdrfvkgtcpkckapdqygdncevcgatyspteliepksvvsgatPVMRDSEHF 160
Cdd:cd00814  106 KKLYENGYIYEGEYEGLYCVSCERFL---------------------------------------------PEWREEEHY 140

                        170
                 ....*....|....
gi 294856155 161 FFDLPSFSEMLQAW 174
Cdd:cd00814  141 FFRLSKFQDRLLEW 154
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 1-174 1.30e-43

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 153.78  E-value: 1.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:PLN02610  44 ADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIF 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPK--CKAPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSE 158
Cdd:PLN02610 124 KKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTD 203

                        170
                 ....*....|....*.
gi 294856155 159 HFFFDLPSFSEMLQAW 174
Cdd:PLN02610 204 HLFLELPLLKDKLVEY 219
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
 1-175 4.67e-42

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: 142.56  E-value: 4.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGI-------------TPEQMIGEMSQEHQTDFAGFNISYD--NYH 65
Cdd:cd00668   26 ADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEFVEEMSGEHKEDFRRLGISYDwsDEY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  66 STHSEENRQLSELIYTRLKENGFIKNRTISQlydpekgmflpdrfvkgtcpkckapdqygdncevcgatyspteliepks 145
Cdd:cd00668  106 ITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------------------------------- 136

                        170       180       190
                 ....*....|....*....|....*....|
gi 294856155 146 vvsgatpvmRDSEHFFFDLPSFSEMLQAWT 175
Cdd:cd00668  137 ---------RITEQWFFDMPKFKEKLLKAL 157
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
 1-173 1.38e-23

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 96.10  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:PRK11893  27 ADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEALNISYDDFIRTTDPRHKEAVQEIF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkckapdqygdnCEVCGATYSPTELIEPKSV--VSGATPVMRDSE 158
Cdd:PRK11893 107 QRLLANGDIYLGKYEGWY-----------------------------CVRCEEFYTESELIEDGYRcpPTGAPVEWVEEE 157

                        170
                 ....*....|....*
gi 294856155 159 HFFFDLPSFSEMLQA 173
Cdd:PRK11893 158 SYFFRLSKYQDKLLE 172
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 1-89 1.26e-12

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 64.82  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:PRK12267  30 ADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELWKKLDISYDKFIRTTDERHKKVVQKIF 109


                 ....*....
gi 294856155  81 TRLKENGFI 89
Cdd:PRK12267 110 EKLYEQGDI 118
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
 1-93 2.09e-09

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: 54.95  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQM----IGEMSQehQTDFAGFNISYDNYHSTHSEENRQLS 76
Cdd:cd00812   26 GDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWteynIKKMKE--QLKRMGFSYDWRREFTTCDPEYYKFT 103

                         90
                 ....*....|....*..
gi 294856155  77 ELIYTRLKENGFIKNRT 93
Cdd:cd00812  104 QWLFLKLYEKGLAYKKE 120
PLN02224 PLN02224
methionine-tRNA ligase
 1-172 1.15e-08

methionine-tRNA ligase


Pssm-ID: 177869 [Multi-domain]  Cd Length: 616  Bit Score: 53.18  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   1 ADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIY 80
Cdd:PLN02224  95 ADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKDLDIAYDKFIRTTDPKHEAIVKEFY 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155  81 TRLKENGFIKNRTISQLYdpekgmflpdrfvkgtCPKCkapDQYGDNcevcgatyspTELIEPKSVVSGATP-VMRDSEH 159
Cdd:PLN02224 175 ARVFANGDIYRADYEGLY----------------CVNC---EEYKDE----------KELLENNCCPVHQMPcVARKEDN 225

                        170
                 ....*....|...
gi 294856155 160 FFFDLPSFSEMLQ 172
Cdd:PLN02224 226 YFFALSKYQKPLE 238
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
 2-47 2.50e-06

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


Pssm-ID: 173909 [Multi-domain]  Cd Length: 338  Bit Score: 46.07  E-value: 2.50e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 294856155   2 DVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEMS 47
Cdd:cd00818   28 DIINRYKTMQGYYVPRRPGWDCHGLPIELKVeKELGISGKKDIEKMG 74
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
 2-89 8.14e-06

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: 45.05  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155    2 DVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGITPE-----------QMIGEMSQEH------QTDFAGFNISYDN 63
Cdd:TIGR00422  60 DIIARYKRMKGYNVLWLPGTDHAGIATQVKVEkKLGAEGKtkhdlgreefrEKIWEWKEESggtiknQIKRLGASLDWSR 139

                          90       100
                  ....*....|....*....|....*.
gi 294856155   64 YHSTHSEENRQLSELIYTRLKENGFI 89
Cdd:TIGR00422 140 ERFTMDEGLSKAVKEAFVRLYEKGLI 165
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
 2-49 1.93e-05

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


Pssm-ID: 439830 [Multi-domain]  Cd Length: 931  Bit Score: 43.92  E-value: 1.93e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 294856155   2 DVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITpEQMIGEMSQE 49
Cdd:COG0060   73 DIIVRYKTMRGFDVPYVPGWDCHGLPIELKVeKELGIK-KKDIEKVGIA 120
valS PRK13208
valyl-tRNA synthetase; Reviewed
 2-89 8.89e-05

valyl-tRNA synthetase; Reviewed


Pssm-ID: 237306 [Multi-domain]  Cd Length: 800  Bit Score: 42.10  E-value: 8.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   2 DVWVRYQRMRGHEVNF-ICADDaHGTPIMLKAQ-QLGITP----------------EQMIGEMSQEHQTdfAGFNISYDN 63
Cdd:PRK13208  65 DFIARYQRMRGYNVFFpQGWDD-NGLPTERKVEkYYGIRKddisreefielcreltDEDEKKFRELWRR--LGLSVDWSL 141

                         90       100
                 ....*....|....*....|....*.
gi 294856155  64 YHSTHSEENRQLSELIYTRLKENGFI 89
Cdd:PRK13208 142 EYQTISPEYRRISQKSFLDLYKKGLI 167
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
 2-89 1.64e-03

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: 38.00  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294856155   2 DVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGITPE-----------QMIGEMSQEHQTDFA------GFNISYDN 63
Cdd:cd00817   28 DIIARYKRMKGYNVLWPPGTDHAGIATQVVVEkKLGIEGKtrhdlgreeflEKCWEWKEESGGKIReqlkrlGASVDWSR 107

                         90       100
                 ....*....|....*....|....*.
gi 294856155  64 YHSTHSEENRQLSELIYTRLKENGFI 89
Cdd:cd00817  108 EYFTMDPGLSRAVQEAFVRLYEKGLI 133
 
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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