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Conserved domains on  [gi|610722335|gb|AHW82364|]
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methionyl-tRNA synthetase, partial [Aeromonas media]

Protein Classification

methionine--tRNA ligase( domain architecture ID 1001553)

methionine--tRNA ligase aminoacylates the 2'-OH of the nucleotide at the 3' of tRNA(Met); it is required for elongation of protein synthesis as well as for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation

CATH:  2.20.28.20|1.10.730.10
EC:  6.1.1.10
Gene Ontology:  GO:0046872|GO:0004825|GO:0005524|GO:0006431
SCOP:  4003662|4004390

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metG super family cl35069
methionyl-tRNA synthetase; Reviewed
 1-168 3.74e-126

methionyl-tRNA synthetase; Reviewed


The actual alignment was detected with superfamily member PRK00133:

Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 368.71  E-value: 3.74e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:PRK00133  28 ADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAGFGISFDNYGSTHSEENRELAQEIY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335  81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPKCKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSEHF 160
Cdd:PRK00133 108 LKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGATYSPTELINPKSAISGATPVLKESEHF 187


                 ....*...
gi 610722335 161 FFDLPQFE 168
Cdd:PRK00133 188 FFKLPRFE 195
 
Name Accession Description Interval E-value
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 1-168 3.74e-126

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 368.71  E-value: 3.74e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:PRK00133  28 ADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAGFGISFDNYGSTHSEENRELAQEIY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335  81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPKCKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSEHF 160
Cdd:PRK00133 108 LKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGATYSPTELINPKSAISGATPVLKESEHF 187


                 ....*...
gi 610722335 161 FFDLPQFE 168
Cdd:PRK00133 188 FFKLPRFE 195
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 1-168 4.93e-101

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: 300.49  E-value: 4.93e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:COG0143   27 ADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFEKLGISFDNFIRTTSPEHKELVQEIF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335  81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPKCKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSEHF 160
Cdd:COG0143  107 QRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGATLEPTELINPRSAISGAPPELREEEHY 186


                 ....*...
gi 610722335 161 FFDLPQFE 168
Cdd:COG0143  187 FFRLSKYQ 194
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 1-168 7.69e-94

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 277.25  E-value: 7.69e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335    1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:pfam09334  25 ADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKKFNISFDDYGRTTSERHHELVQEFF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPKCKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSEHF 160
Cdd:pfam09334 105 LKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLEPTELINPKCVICGTTPEVKETEHY 184


                  ....*...
gi 610722335  161 FFDLPQFE 168
Cdd:pfam09334 185 FFDLSKFQ 192
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
 1-168 1.45e-81

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: 250.37  E-value: 1.45e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335    1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:TIGR00398  25 ADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKWLNISFDRFIRTTDEEHKEIVQKIF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPKCKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSEHF 160
Cdd:TIGR00398 105 QKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLEPTELINPRCKICGAKPELRDSEHY 184


                  ....*...
gi 610722335  161 FFDLPQFE 168
Cdd:TIGR00398 185 FFRLSAFE 192
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 1-168 3.15e-43

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: 145.37  E-value: 3.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:cd00814   26 ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNISFDYFIRTTSPRHKEIVQEFF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335  81 GRLKESGKIKIRTISQLFDPEKFMFLpdrfvkgtcpkckspeqygdncdacgatysptelidpksavsgatPVMKDSEHF 160
Cdd:cd00814  106 KKLYENGYIYEGEYEGLYCVSCERFL---------------------------------------------PEWREEEHY 140


                 ....*...
gi 610722335 161 FFDLPQFE 168
Cdd:cd00814  141 FFRLSKFQ 148
 
Name Accession Description Interval E-value
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 1-168 3.74e-126

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 368.71  E-value: 3.74e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:PRK00133  28 ADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAGFGISFDNYGSTHSEENRELAQEIY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335  81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPKCKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSEHF 160
Cdd:PRK00133 108 LKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGATYSPTELINPKSAISGATPVLKESEHF 187


                 ....*...
gi 610722335 161 FFDLPQFE 168
Cdd:PRK00133 188 FFKLPRFE 195
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 1-168 4.93e-101

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: 300.49  E-value: 4.93e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:COG0143   27 ADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFEKLGISFDNFIRTTSPEHKELVQEIF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335  81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPKCKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSEHF 160
Cdd:COG0143  107 QRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGATLEPTELINPRSAISGAPPELREEEHY 186


                 ....*...
gi 610722335 161 FFDLPQFE 168
Cdd:COG0143  187 FFRLSKYQ 194
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 1-168 7.69e-94

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 277.25  E-value: 7.69e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335    1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:pfam09334  25 ADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKKFNISFDDYGRTTSERHHELVQEFF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPKCKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSEHF 160
Cdd:pfam09334 105 LKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLEPTELINPKCVICGTTPEVKETEHY 184


                  ....*...
gi 610722335  161 FFDLPQFE 168
Cdd:pfam09334 185 FFDLSKFQ 192
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
 1-168 1.45e-81

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: 250.37  E-value: 1.45e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335    1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:TIGR00398  25 ADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKWLNISFDRFIRTTDEEHKEIVQKIF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPKCKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSEHF 160
Cdd:TIGR00398 105 QKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLEPTELINPRCKICGAKPELRDSEHY 184


                  ....*...
gi 610722335  161 FFDLPQFE 168
Cdd:TIGR00398 185 FFRLSAFE 192
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 1-168 3.15e-43

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: 145.37  E-value: 3.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:cd00814   26 ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNISFDYFIRTTSPRHKEIVQEFF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335  81 GRLKESGKIKIRTISQLFDPEKFMFLpdrfvkgtcpkckspeqygdncdacgatysptelidpksavsgatPVMKDSEHF 160
Cdd:cd00814  106 KKLYENGYIYEGEYEGLYCVSCERFL---------------------------------------------PEWREEEHY 140


                 ....*...
gi 610722335 161 FFDLPQFE 168
Cdd:cd00814  141 FFRLSKFQ 148
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 1-168 1.12e-38

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 139.53  E-value: 1.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:PLN02610  44 ADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIF 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335  81 GRLKESGKIKIRTISQLFDPEKFMFLPDRFVKGTCPK--CKSPEQYGDNCDACGATYSPTELIDPKSAVSGATPVMKDSE 158
Cdd:PLN02610 124 KKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTD 203

                        170
                 ....*....|
gi 610722335 159 HFFFDLPQFE 168
Cdd:PLN02610 204 HLFLELPLLK 213
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
 1-103 3.77e-28

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: 105.96  E-value: 3.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGI-------------TPEEMIAAVSQEHQGDFAGFNISFD--NYH 65
Cdd:cd00668   26 ADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEFVEEMSGEHKEDFRRLGISYDwsDEY 105

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 610722335  66 STHSDENRELAGLIYGRLKESGKIKIRTISQLFDPEKF 103
Cdd:cd00668  106 ITTEPEYSKAVELIFSRLYEKGLIYRGTHPVRITEQWF 143
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
 1-167 6.80e-19

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 82.62  E-value: 6.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:PRK11893  27 ADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEALNISYDDFIRTTDPRHKEAVQEIF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335  81 GRLKESGKIkirtisqlfdpekfmflpdrfvkgtcpkCKSpEQYGDNCDACGATYSPTELIDPK--SAVSGATPVMKDSE 158
Cdd:PRK11893 107 QRLLANGDI----------------------------YLG-KYEGWYCVRCEEFYTESELIEDGyrCPPTGAPVEWVEEE 157


                 ....*....
gi 610722335 159 HFFFDLPQF 167
Cdd:PRK11893 158 SYFFRLSKY 166
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 1-89 4.01e-08

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 51.34  E-value: 4.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:PRK12267  30 ADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELWKKLDISYDKFIRTTDERHKKVVQKIF 109


                 ....*....
gi 610722335  81 GRLKESGKI 89
Cdd:PRK12267 110 EKLYEQGDI 118
PLN02224 PLN02224
methionine-tRNA ligase
 1-89 1.03e-06

methionine-tRNA ligase


Pssm-ID: 177869 [Multi-domain]  Cd Length: 616  Bit Score: 47.40  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFDNYHSTHSDENRELAGLIY 80
Cdd:PLN02224  95 ADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKDLDIAYDKFIRTTDPKHEAIVKEFY 174


                 ....*....
gi 610722335  81 GRLKESGKI 89
Cdd:PLN02224 175 ARVFANGDI 183
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
 2-47 8.63e-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: 44.53  E-value: 8.63e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 610722335   2 DIWVRYQRMRGNQVHFVCADDAHGTPIMLKA-QQMGITPEEMIAAVS 47
Cdd:cd00818   28 DIINRYKTMQGYYVPRRPGWDCHGLPIELKVeKELGISGKKDIEKMG 74
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
 1-62 9.18e-06

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: 44.55  E-value: 9.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 610722335   1 ADIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQMGITPEEMIAAVSQEHQGDFAGFNISFD 62
Cdd:cd00812   26 GDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMGFSYD 87
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
 2-38 1.86e-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: 1.86e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 610722335   2 DIWVRYQRMRGNQVHFVCADDAHGTPIMLKA-QQMGIT 38
Cdd:COG0060   73 DIIVRYKTMRGFDVPYVPGWDCHGLPIELKVeKELGIK 110
PLN02843 PLN02843
isoleucyl-tRNA synthetase
 2-34 4.40e-04

isoleucyl-tRNA synthetase


Pssm-ID: 215452 [Multi-domain]  Cd Length: 974  Bit Score: 39.75  E-value: 4.40e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 610722335   2 DIWVRYQRMRGNQVHFVCADDAHGTPIMLKAQQ 34
Cdd:PLN02843  59 DFINRYQLLQGKKVHYVPGWDCHGLPIELKVLQ 91
 
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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