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Conserved domains on  [gi|818897692|gb|KKW32008|]
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Methionine-tRNA ligase [Candidatus Uhrbacteria bacterium GW2011_GWA2_52_8d]

Protein Classification

methionine--tRNA ligase( domain architecture ID 1001758)

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 cl33774
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 5-212 5.42e-82

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


The actual alignment was detected with superfamily member COG0143:

Pssm-ID: 439913 [Multi-domain]  Cd Length: 544  Bit Score: 256.58  E-value: 5.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:COG0143    3 FLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQAE-ARGDQCDTCGKELN 163
Cdd:COG0143   83 LGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEdAYGDQCENCGATLE 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 818897692 164 PSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWVASQGHWRENA 212
Cdd:COG0143  163 PTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPDIQPEV 211
 
Name Accession Description Interval E-value
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 5-212 5.42e-82

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: 256.58  E-value: 5.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:COG0143    3 FLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQAE-ARGDQCDTCGKELN 163
Cdd:COG0143   83 LGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEdAYGDQCENCGATLE 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 818897692 164 PSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWVASQGHWRENA 212
Cdd:COG0143  163 PTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPDIQPEV 211
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 5-216 5.88e-81

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 249.13  E-value: 5.88e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692    5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQAE-ARGDQCDTCGKELN 163
Cdd:pfam09334  81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEdARGDQCENCGRHLE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 818897692  164 PSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWVAS-QGHWRENANRVS 216
Cdd:pfam09334 161 PTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEEnNPEWPENVKNMV 214
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 2-212 8.58e-74

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 238.13  E-value: 8.58e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   2 SRYIYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLT 81
Cdd:PRK00133   1 MRKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  82 FERLGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQAE-ARGDQCDTCGK 160
Cdd:PRK00133  81 FAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEdQYGDNCEVCGA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818897692 161 ELNPSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWVASQGHWRENA 212
Cdd:PRK00133 161 TYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRSGELQPNV 212
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
 5-215 1.02e-62

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: 206.07  E-value: 1.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692    5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQAE-ARGDQCDTCGKELN 163
Cdd:TIGR00398  81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEdARGDHCEVCGRHLE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 818897692  164 PSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWVASQ---GHWRENANRV 215
Cdd:TIGR00398 161 PTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNpesGSPASNVKNK 215
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 5-212 4.34e-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: 172.72  E-value: 4.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:cd00814    2 VLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFKW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRAdreingicpscqaeargdqcdtcgkelnp 164
Cdd:cd00814   82 LNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP----------------------------- 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 818897692 165 sellnpvcakcsskiTFETTRELFLNLPVLEERLREWVAS--QGHWRENA 212
Cdd:cd00814  133 ---------------EWREEEHYFFRLSKFQDRLLEWLEKnpDFIWPENA 167
 
Name Accession Description Interval E-value
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 5-212 5.42e-82

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: 256.58  E-value: 5.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:COG0143    3 FLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQAE-ARGDQCDTCGKELN 163
Cdd:COG0143   83 LGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEdAYGDQCENCGATLE 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 818897692 164 PSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWVASQGHWRENA 212
Cdd:COG0143  163 PTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPDIQPEV 211
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 5-216 5.88e-81

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 249.13  E-value: 5.88e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692    5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQAE-ARGDQCDTCGKELN 163
Cdd:pfam09334  81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEdARGDQCENCGRHLE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 818897692  164 PSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWVAS-QGHWRENANRVS 216
Cdd:pfam09334 161 PTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEEnNPEWPENVKNMV 214
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 2-212 8.58e-74

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 238.13  E-value: 8.58e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   2 SRYIYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLT 81
Cdd:PRK00133   1 MRKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  82 FERLGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQAE-ARGDQCDTCGK 160
Cdd:PRK00133  81 FAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEdQYGDNCEVCGA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818897692 161 ELNPSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWVASQGHWRENA 212
Cdd:PRK00133 161 TYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRSGELQPNV 212
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
 5-215 1.02e-62

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: 206.07  E-value: 1.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692    5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQAE-ARGDQCDTCGKELN 163
Cdd:TIGR00398  81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEdARGDHCEVCGRHLE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 818897692  164 PSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWVASQ---GHWRENANRV 215
Cdd:TIGR00398 161 PTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNpesGSPASNVKNK 215
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 5-212 4.34e-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: 172.72  E-value: 4.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:cd00814    2 VLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFKW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRAdreingicpscqaeargdqcdtcgkelnp 164
Cdd:cd00814   82 LNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP----------------------------- 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 818897692 165 sellnpvcakcsskiTFETTRELFLNLPVLEERLREWVAS--QGHWRENA 212
Cdd:cd00814  133 ---------------EWREEEHYFFRLSKFQDRLLEWLEKnpDFIWPENA 167
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 3-212 1.38e-48

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 171.89  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   3 RYIYVGSAWPYVNGPLHLGHVAGLV-SADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLT 81
Cdd:PLN02610  17 RNILITSALPYVNNVPHLGNIIGCVlSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  82 FERLGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREINGICPSCQ---AEARGDQCDTC 158
Cdd:PLN02610  97 YDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTEGcnyDSARGDQCEKC 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 818897692 159 GKELNPSELLNPVCAKCSSKITFETTRELFLNLPVLEERLREWV---ASQGHWRENA 212
Cdd:PLN02610 177 GKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYInetSVAGGWSQNA 233
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
 12-149 1.65e-30

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 119.22  E-value: 1.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFERLGFSYSL 91
Cdd:PRK11893  10 YYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEALNISYDD 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818897692  92 YWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREI---NGICPSCQAE 149
Cdd:PRK11893  90 FIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELiedGYRCPPTGAP 150
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
 5-122 6.94e-27

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: 106.35  E-value: 6.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   5 IYVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEG-------------RTAREVA 71
Cdd:cd00668    2 FYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGgrkkktiwieefrEDPKEFV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 818897692  72 QQYHGVVKLTFERLGFSY--SLYWATMEPEHHARVQESFSALYKAGYIMEGEY 122
Cdd:cd00668   82 EEMSGEHKEDFRRLGISYdwSDEYITTEPEYSKAVELIFSRLYEKGLIYRGTH 134
valS PRK13208
valyl-tRNA synthetase; Reviewed
 12-139 1.34e-23

valyl-tRNA synthetase; Reviewed


Pssm-ID: 237306 [Multi-domain]  Cd Length: 800  Bit Score: 100.27  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPiTER---------ARKEGR-----TAREVAQQYHGV 77
Cdd:PRK13208  47 PTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGLP-TERkvekyygirKDDISReefieLCRELTDEDEKK 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818897692  78 VKLTFERLGFS--YSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREI 139
Cdd:PRK13208 126 FRELWRRLGLSvdWSLEYQTISPEYRRISQKSFLDLYKKGLIYRAEAPVLWCPRCETAIAQAEV 189
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
 12-139 7.96e-23

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: 96.55  E-value: 7.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPiTER-----ARKEGRTAR------------EVAQQY 74
Cdd:cd00817   10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIA-TQVvvekkLGIEGKTRHdlgreeflekcwEWKEES 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818897692  75 HGVVKLTFERLGFSY--SLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREI 139
Cdd:cd00817   89 GGKIREQLKRLGASVdwSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV 155
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 5-149 4.28e-22

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 95.64  E-value: 4.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   5 IYvgsawpYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:PRK12267  12 IY------YPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELWKK 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818897692  85 LGFSYSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREI--NGICPSCQAE 149
Cdd:PRK12267  86 LDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLvdGGKCPDCGRE 152
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
 6-123 5.97e-22

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: 93.08  E-value: 5.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   6 YVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFERL 85
Cdd:cd00812    3 YILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRM 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 818897692  86 GFSYSlyW----ATMEPEHHARVQESFSALYKAGYIMEGEYK 123
Cdd:cd00812   83 GFSYD--WrrefTTCDPEYYKFTQWLFLKLYEKGLAYKKEAP 122
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
 12-139 7.80e-21

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: 92.04  E-value: 7.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTP----ITERARKEGRT------------AREVAQQYH 75
Cdd:TIGR00422  42 PNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIAtqvkVEKKLGAEGKTkhdlgreefrekIWEWKEESG 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818897692   76 GVVKLTFERLGFSYSlyWA----TMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREI 139
Cdd:TIGR00422 122 GTIKNQIKRLGASLD--WSrerfTMDEGLSKAVKEAFVRLYEKGLIYRGEYLVNWDPKLNTAISDIEV 187
PLN02224 PLN02224
methionine-tRNA ligase
 13-147 1.58e-18

methionine-tRNA ligase


Pssm-ID: 177869 [Multi-domain]  Cd Length: 616  Bit Score: 85.15  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  13 YVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTARE----VAQQYhgvvKLTFERLGFS 88
Cdd:PLN02224  79 YVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEhcdiISQSY----RTLWKDLDIA 154

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818897692  89 YSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREI--NGICPSCQ 147
Cdd:PLN02224 155 YDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKELleNNCCPVHQ 215
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
 12-140 5.25e-18

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: 83.61  E-value: 5.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKE------------GRTA-----REVAQQY 74
Cdd:pfam00133  32 PNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVEKKlgikekktrhkyGREEfrekcREWKMEY 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818897692   75 HGVVKLTFERLGFS--YSLYWATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADREIN 140
Cdd:pfam00133 112 ADEIRKQFRRLGRSidWDREYFTMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLEVE 179
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
 12-120 9.02e-13

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: 67.26  E-value: 9.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKE-GRT----------------AREVAQQY 74
Cdd:cd00818   10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKElGISgkkdiekmgiaefnakCREFALRY 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 818897692  75 HGVVKLTFERLGfsyslYWA-------TMEPEHHARVQESFSALYKAGYIMEG 120
Cdd:cd00818   90 VDEQEEQFQRLG-----VWVdwenpykTMDPEYMESVWWVFKQLHEKGLLYRG 137
PLN02563 PLN02563
aminoacyl-tRNA ligase
 6-142 7.27e-12

aminoacyl-tRNA ligase


Pssm-ID: 178177 [Multi-domain]  Cd Length: 963  Bit Score: 65.61  E-value: 7.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   6 YVGSAWPYVNGP-LHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFER 84
Cdd:PLN02563 113 YVLDMFPYPSGAgLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRSQLKS 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818897692  85 LGFSYSlyW----ATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCGESRADRE-INGI 142
Cdd:PLN02563 193 LGFSYD--WdreiSTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEvVDGL 253
PLN02843 PLN02843
isoleucyl-tRNA synthetase
 12-121 7.98e-12

isoleucyl-tRNA synthetase


Pssm-ID: 215452 [Multi-domain]  Cd Length: 974  Bit Score: 65.56  E-value: 7.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPIT--------ERARKE------GRTAREVAQQYHGV 77
Cdd:PLN02843  41 PYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIElkvlqsldQEARKEltpiklRAKAAKFAKKTVDT 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 818897692  78 VKLTFERLGFsyslyWA-------TMEPEHHARVQESFSALYKAGYIMEGE 121
Cdd:PLN02843 121 QRESFKRYGV-----WGdwenpylTLDPEYEAAQIEVFGQMFLNGYIYRGR 166
PTZ00419 PTZ00419
valyl-tRNA synthetase-like protein; Provisional
 12-117 6.59e-11

valyl-tRNA synthetase-like protein; Provisional


Pssm-ID: 240411 [Multi-domain]  Cd Length: 995  Bit Score: 62.72  E-value: 6.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHvaGLVSA--DVIARYHRLVGDEVLWTSGSDCHGTP---ITERA--RKEGRT----ARE-----VAQ--- 72
Cdd:PTZ00419  69 PNVTGYLHIGH--ALTGAiqDSLIRYHRMKGDETLWVPGTDHAGIAtqvVVEKKlmKEENKTrhdlGREeflkkVWEwkd 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 818897692  73 QYHGVVKLTFERLGFsySLYWA----TMEPEHHARVQESFSALYKAGYI 117
Cdd:PTZ00419 147 KHGNNICNQLRRLGS--SLDWSrevfTMDEQRSKAVKEAFVRLYEDGLI 193
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
 12-123 1.19e-10

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: 61.63  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPI-------------------TERARKEgrtAREVAQ 72
Cdd:COG0060   55 PYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLPIelkvekelgikkkdiekvgIAEFREK---CREYAL 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 818897692  73 QYHGVVKLTFERLGfsyslYWA-------TMEPEHHARVQESFSALYKAGYIMEGeYK 123
Cdd:COG0060  132 KYVDEQREDFKRLG-----VWGdwdnpylTMDPEYEESIWWALKKLYEKGLLYKG-LK 183
leuS PRK12300
leucyl-tRNA synthetase; Reviewed
 18-131 5.44e-10

leucyl-tRNA synthetase; Reviewed


Pssm-ID: 237049 [Multi-domain]  Cd Length: 897  Bit Score: 59.88  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  18 LHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPI---TER-ARKEGRTArEVAQQYHGV---------------- 77
Cdd:PRK12300   1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPIlgiAERiARGDPETI-ELYKSLYGIpeeelekfkdpeyive 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818897692  78 -----VKLTFERLGfsYSLYW----ATMEPEHHARVQESFSALYKAGYIMEGEYKHARCDHCG 131
Cdd:PRK12300  80 yfseeAKEDMKRIG--YSIDWrrefTTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDN 140
PLN02959 PLN02959
aminoacyl-tRNA ligase
 11-72 1.13e-09

aminoacyl-tRNA ligase


Pssm-ID: 215518 [Multi-domain]  Cd Length: 1084  Bit Score: 58.93  E-value: 1.13e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818897692   11 WPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKegrTAREVAQ 72
Cdd:PLN02959   53 YPYMNGLLHLGHAFSLSKLEFAAAYHRLRGANVLLPFAFHCTGMPIKASADK---LAREIQQ 111
PLN02943 PLN02943
aminoacyl-tRNA ligase
 12-122 1.28e-08

aminoacyl-tRNA ligase


Pssm-ID: 215509 [Multi-domain]  Cd Length: 958  Bit Score: 55.72  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSD---------------CHGTPITERARKE-GRTAREVAQQYH 75
Cdd:PLN02943  97 PNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDhagiatqlvvekmlaSEGIKRTDLGRDEfTKRVWEWKEKYG 176

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 818897692  76 GVVKLTFERLGFS--YSLYWATMEPEHHARVQESFSALYKAGYIMEGEY 122
Cdd:PLN02943 177 GTITNQIKRLGAScdWSRERFTLDEQLSRAVVEAFVRLHEKGLIYQGSY 225
valS PRK05729
valyl-tRNA synthetase; Reviewed
 12-122 1.20e-07

valyl-tRNA synthetase; Reviewed


Pssm-ID: 235582 [Multi-domain]  Cd Length: 874  Bit Score: 52.80  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHvaGLVSA--DVIARYHRLVGDEVLWTSGSDcH-GtpI-T----ERA-RKEGRTAREV------------ 70
Cdd:PRK05729  45 PNVTGSLHMGH--ALNNTlqDILIRYKRMQGYNTLWLPGTD-HaG--IaTqmvvERQlAAEGKSRHDLgrekflekvwew 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 818897692  71 AQQYHGVVKLTFERLGfsYSLYWA----TMEPEHHARVQESFSALYKAGYIMEGEY 122
Cdd:PRK05729 120 KEESGGTITNQLRRLG--ASCDWSrerfTMDEGLSKAVREVFVRLYEKGLIYRGKR 173
ValS COG0525
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ...
 12-122 4.44e-07

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


Pssm-ID: 440291 [Multi-domain]  Cd Length: 877  Bit Score: 50.82  E-value: 4.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  12 PYVNGPLHLGHvaglvsA------DVIARYHRLVGDEVLWTSGSDcH-GtpI-T----ERA-RKEGRTAREV-------- 70
Cdd:COG0525   44 PNVTGSLHMGH------AlnntlqDILIRYKRMQGYNTLWQPGTD-HaG--IaTqavvERQlAEEGKSRHDLgrekfler 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692  71 ----AQQYHGVVKLTFERLGFSYSlyWA----TMEPEHHARVQESFSALYKAGYIMEGEY 122
Cdd:COG0525  115 vwewKEESGGTITNQLRRLGASCD--WSrerfTMDEGLSKAVREVFVRLYEKGLIYRGKR 172
PLN02381 PLN02381
valyl-tRNA synthetase
 12-117 7.38e-07

valyl-tRNA synthetase


Pssm-ID: 215214 [Multi-domain]  Cd Length: 1066  Bit Score: 50.28  E-value: 7.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTP---ITERA--RKEGRTAREVAQ------------QY 74
Cdd:PLN02381  137 PNVTGALHIGHALTAAIEDTIIRWKRMSGYNALWVPGVDHAGIAtqvVVEKKlmRERHLTRHDIGReefvsevwkwkdEY 216

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 818897692   75 HGVVKLTFERLGfsYSLYWA----TMEPEHHARVQESFSALYKAGYI 117
Cdd:PLN02381  217 GGTILNQLRRLG--ASLDWSrecfTMDEQRSKAVTEAFVRLYKEGLI 261
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 12-83 1.96e-06

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: 46.32  E-value: 1.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818897692  12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKEGRTAREVAQQYHGVVKLTFE 83
Cdd:cd00802    6 ITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVE 77
PTZ00427 PTZ00427
isoleucine-tRNA ligase, putative; Provisional
 12-117 2.81e-06

isoleucine-tRNA ligase, putative; Provisional


Pssm-ID: 173617 [Multi-domain]  Cd Length: 1205  Bit Score: 48.42  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPITERARKE-----------------GRTAREVAQQY 74
Cdd:PTZ00427  111 PFATGLPHYGHLLAGIIKDCVTRYFYQCGFSVERKFGWDCHGLPIEYEIEKEnninkkedilkmgidvyNEKCRGIVLKY 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 818897692   75 HGVVKLTFERLG--FSYSLYWATMEPEHHARVQESFSALYKAGYI 117
Cdd:PTZ00427  191 SNEWVKTVERIGrwIDFKNDYKTMDKTFMESVWWVFSELYKNNYV 235
valS PRK14900
valyl-tRNA synthetase; Provisional
 12-147 5.47e-06

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 47.68  E-value: 5.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   12 PYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTP---ITERARKE---------GRTA-----REVAQQY 74
Cdd:PRK14900   57 PNVTGSLHLGHALTATLQDVLIRWKRMSGFNTLWLPGTDHAGIAtqmIVEKELKKtekksrhdlGREAflervWAWKEQY 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818897692   75 HGVVKLTFERLGfsYSLYWA----TMEPEHHARVQESFSALYKAGYIMegeykharcdhcgesRADREINGiCPSCQ 147
Cdd:PRK14900  137 GSRIGEQHKALG--ASLDWQrerfTMDEGLSRAVREVFVRLHEEGLIY---------------REKKLINW-CPDCR 195
LeuS COG0495
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ...
 6-115 1.52e-05

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


Pssm-ID: 440261 [Multi-domain]  Cd Length: 826  Bit Score: 46.20  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   6 YVGSAWPYVNGPLHLGHVAGLVSADVIARYHRLVGDEVLWTSGSDCHGTPiTER-ARKEGR-----TAREVAQQyhgvvK 79
Cdd:COG0495   36 YVLDMFPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNVLHPMGWDAFGLP-AENaAIKNGVhpaewTYENIANM-----R 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 818897692  80 LTFERLGFSYSlyW----ATMEPEHHARVQESFSALYKAG 115
Cdd:COG0495  110 RQLKRLGLSYD--WsreiATCDPEYYKWTQWIFLQLYEKG 147
PRK14714 PRK14714
DNA-directed DNA polymerase II large subunit;
115-190 4.76e-04

DNA-directed DNA polymerase II large subunit;


Pssm-ID: 237798 [Multi-domain]  Cd Length: 1337  Bit Score: 41.60  E-value: 4.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818897692  115 GYIMEGEYKHARCDHCGESradrEINGICPSCQAEARGD-QCDTCGKELNPSELLNPVCAKCSSKITFETTRELFLN 190
Cdd:PRK14714  658 GGVIEVEVGRRRCPSCGTE----TYENRCPDCGTHTEPVyVCPDCGAEVPPDESGRVECPRCDVELTPYQRRTINVK 730
PLN02882 PLN02882
aminoacyl-tRNA ligase
 12-120 3.00e-03

aminoacyl-tRNA ligase


Pssm-ID: 215477 [Multi-domain]  Cd Length: 1159  Bit Score: 38.94  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897692   12 PYVNGPLHLGHV-AGLVSaDVIARYHRLVGDEVLWTSGSDCHGTP----------ITERAR-------KEGRTAREVAQQ 73
Cdd:PLN02882   47 PFATGLPHYGHIlAGTIK-DIVTRYQSMTGHHVTRRFGWDCHGLPveyeidkklgIKRRDDvlkmgidKYNEECRSIVTR 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 818897692   74 YHGVVKLTFERLG--FSYSLYWATMEPEHHARVQESFSALYKAGYIMEG 120
Cdd:PLN02882  126 YSKEWEKTVTRTGrwIDFENDYKTMDPKFMESVWWVFKQLFEKGLVYKG 174
 
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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